Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
The new UniProt website is here! Take me to UniProt BETA

UniProtKB - Q03133 (ERYA3_SACER)

Entry version 153 (25 May 2022)
Sequence version 4 (23 Jan 2007)
Previous versions | rss
Add a publicationFeedback
Protein

6-deoxyerythronolide-B synthase EryA3, modules 5 and 6

Gene

eryA

Organism
Saccharopolyspora erythraea (Streptomyces erythraeus)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Involved in the biosynthesis of antibiotic erythromycin via the biosynthesis of its aglycone precursor, 6-deoxyerythronolide B (6-dEB).

1 Publication1 Publication

Miscellaneous

Type I modular polyketide synthases (PKSs) catalyze the step-wise condensation of simple carboxylic acid derivatives. Organizationally, type I PKSs are arranged into modules, wherein each module is comprised of a set of catalytic activities that is responsible for a single elongation of the polyketide chain and the appropriate reductive processing of the beta-keto functionality. A minimal elongation module contains an acyl transferase (AT) domain, an acyl-carrier protein (ACP) domain, and a ketosynthase (KS) domain. The AT domain is responsible for loading the methylmalonyl-CoA extender unit onto the phosphopantetheinylated ACP domain. Subsequently, the KS domain decarboxylates and then condenses the ACP-bound extender unit with the growing polyketide chain obtained from the preceding module to yield an ACP-bound beta-ketoacyl intermediate. In addition to the three core domains, each elongation module may contain up to three additional domains: a ketoreductase (KR), dehydratase (DH), and an enoyl reductase (ER) that are responsible for the reductive processing of the beta-keto functionality prior to the next extension step. The presence of a KR domain alone gives rise to a beta-hydroxyl functionality, the presence of both a KR and a DH domain generates an alkene, while the combination of KR, DH, and ER results in complete reduction to the alkane. Finally, a thioesterase (TE) domain, typically found at the terminus of the last elongation module, catalyzes the termination of polyketide biosynthesis. The activity of this domain results in cleavage of the acyl chain from the adjacent ACP and formation of the macrocyclic ring.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

pantetheine 4'-phosphate1 PublicationNote: Binds 2 phosphopantetheines covalently.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by diphenyl phosphonates derivatives such as diphenyl allylphosphonate.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: erythromycin biosynthesis

This protein is involved in the pathway erythromycin biosynthesis, which is part of Antibiotic biosynthesis.2 Publications
View all proteins of this organism that are known to be involved in the pathway erythromycin biosynthesis and in Antibiotic biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei199Acyl-thioester intermediate; for beta-ketoacyl synthase 1 activityPROSITE-ProRule annotation1 Publication1
Active sitei643Acyl-ester intermediate; for acyltransferase 1 activityPROSITE-ProRule annotation1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei644Important for discrimination between malonyl and methylmalonyl polyketide chain extension units1 Publication1
Sitei744Important for discrimination between malonyl and methylmalonyl polyketide chain extension units1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1229NADP 1By similarity1
Active sitei1264Acyl-ester intermediate; for beta-ketoacyl reductase 1 activityBy similarity1
Active sitei1661Acyl-thioester intermediate; for beta-ketoacyl synthase 2 activityPROSITE-ProRule annotation1
Active sitei2112Acyl-ester intermediate; for acyltransferase 2 activityPROSITE-ProRule annotation1
Binding sitei2666NADP 2Curated1
Active sitei2701Acyl-ester intermediate; for beta-ketoacyl reductase 2 activityCurated1
Binding sitei2965SubstrateBy similarity1
Active sitei3031Nucleophile; for thioesterase activityBy similarity2 Publications1
Binding sitei3032Substrate; via amide nitrogen1 Publication1
Binding sitei3058Substrate1 Publication1
Active sitei3148Proton acceptor; for thioesterase activityBy similarity2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1125 – 1128NADP 1By similarity4
Nucleotide bindingi1148 – 1151NADP 1By similarity4
Nucleotide bindingi1177 – 1178NADP 1By similarity2
Nucleotide bindingi1249 – 1250NADP 1By similarity2
Nucleotide bindingi2565 – 2568NADP 2Curated4
Nucleotide bindingi2588 – 2591NADP 2Curated4
Nucleotide bindingi2617 – 2618NADP 2Curated2
Nucleotide bindingi2686 – 2687NADP 2Curated2

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAcyltransferase, Multifunctional enzyme, Transferase
Biological processAntibiotic biosynthesis
LigandNADP

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.3.1.94, 5518

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00240

Protein family/group databases

ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

More...ESTHERi		sacer-ery3, Thioesterase

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
6-deoxyerythronolide-B synthase EryA3, modules 5 and 6Curated (EC:2.3.1.941 Publication)
Short name:
DEBS 31 Publication
Alternative name(s):
6-deoxyerythronolide B synthase III1 Publication
Erythronolide synthase
ORF C1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:eryA1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharopolyspora erythraea (Streptomyces erythraeus)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1836 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Actinobacteria › Pseudonocardiales › Pseudonocardiaceae › Saccharopolyspora

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001802952 – 31726-deoxyerythronolide-B synthase EryA3, modules 5 and 6Add BLAST3171

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1427O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei2854O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		Q03133

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:11752428, PubMed:12379102, PubMed:16844787). Erythronolide synthase is composed of EryAI, EryAII and EryAIII multimodular (2 modules) polypeptides each coding for a functional synthase subunit which participates in 2 of the six FAS-like elongation steps required for formation of the polyketide. Module 1, 2, 3, 4, 5, and 6 participating in biosynthesis steps 1, 2, 3, 4, 5, and 6, respectively.

3 Publications3 Publications

Protein-protein interaction databases

Database of interacting proteins

More...DIPi		DIP-61229N

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

13172
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q03133

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q03133

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1392 – 1467Carrier 1PROSITE-ProRule annotationAdd BLAST76
Domaini2819 – 2894Carrier 2PROSITE-ProRule annotationAdd BLAST76

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni41 – 1464Module 5CuratedAdd BLAST1424
Regioni41 – 455Beta-ketoacyl synthase 1CuratedAdd BLAST415
Regioni557 – 874Acyltransferase 1CuratedAdd BLAST318
Regioni1117 – 1294Beta-ketoacyl reductase 1CuratedAdd BLAST178
Regioni1492 – 2891Module 6CuratedAdd BLAST1400
Regioni1492 – 1919Beta-ketoacyl synthase 2CuratedAdd BLAST428
Regioni2022 – 2331Acyltransferase 2CuratedAdd BLAST310
Regioni2557 – 2731Beta-ketoacyl reductase 2CuratedAdd BLAST175
Regioni2960 – 3166ThioesteraseCuratedAdd BLAST207

Keywords - Domaini

Repeat

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.1200.10, 2 hits
3.40.366.10, 2 hits
3.40.47.10, 2 hits
3.40.50.1820, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR029058, AB_hydrolase
IPR001227, Ac_transferase_dom_sf
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR036291, NAD(P)-bd_dom_sf
IPR032821, PKS_assoc
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR013968, PKS_KR
IPR020806, PKS_PP-bd
IPR020802, PKS_thioesterase
IPR015083, Polyketide_synth_docking
IPR036299, Polyketide_synth_docking_sf
IPR009081, PP-bd_ACP
IPR006162, Ppantetheine_attach_site
IPR001031, Thioesterase
IPR016039, Thiolase-like

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00698, Acyl_transf_1, 2 hits
PF08990, Docking, 1 hit
PF16197, KAsynt_C_assoc, 2 hits
PF00109, ketoacyl-synt, 2 hits
PF02801, Ketoacyl-synt_C, 2 hits
PF08659, KR, 2 hits
PF00550, PP-binding, 2 hits
PF00975, Thioesterase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00827, PKS_AT, 2 hits
SM00825, PKS_KS, 2 hits
SM00823, PKS_PP, 2 hits
SM00824, PKS_TE, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF101173, SSF101173, 1 hit
SSF47336, SSF47336, 2 hits
SSF51735, SSF51735, 4 hits
SSF52151, SSF52151, 2 hits
SSF53474, SSF53474, 1 hit
SSF53901, SSF53901, 2 hits
SSF55048, SSF55048, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00606, B_KETOACYL_SYNTHASE, 2 hits
PS50075, CARRIER, 2 hits
PS00012, PHOSPHOPANTETHEINE, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q03133-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGDNGMTEE KLRRYLKRTV TELDSVTARL REVEHRAGEP IAIVGMACRF 
        60         70         80         90        100
PGDVDSPESF WEFVSGGGDA IAEAPADRGW EPDPDARLGG MLAAAGDFDA 
       110        120        130        140        150
GFFGISPREA LAMDPQQRIM LEISWEALER AGHDPVSLRG SATGVFTGVG 
       160        170        180        190        200
TVDYGPRPDE APDEVLGYVG TGTASSVASG RVAYCLGLEG PAMTVDTACS 
       210        220        230        240        250
SGLTALHLAM ESLRRDECGL ALAGGVTVMS SPGAFTEFRS QGGLAADGRC 
       260        270        280        290        300
KPFSKAADGF GLAEGAGVLV LQRLSAARRE GRPVLAVLAG SAVNQDGASN 
       310        320        330        340        350
GLTAPSGPAQ QRVIRRALEN AGVRAGDVDY VEAHGTGTRL GDPIEVHALL 
       360        370        380        390        400
STYGAERDPD DPLWIGSVKS NIGHTQAAAG VAGVMKAVLA LRHGEMPRTL 
       410        420        430        440        450
HFDEPSPQIE WDLGAVSVVS QARSWPAGER PRRAGVSSFG ISGTNAHVIV 
       460        470        480        490        500
EEAPEADEPE PAPDSGPVPL VLSGRDEQAM RAQAGRLADH LAPEPRNSLR 
       510        520        530        540        550
DTGFTLATRA SAMEHRAVVV GDRDEALAGL RAVADRRIAD RTATGQGPNS 
       560        570        580        590        600
PRRVAMVFPG QGAQWQGMAR DLLRESQVFA DSIRDCERAL APHVDWSLTD 
       610        620        630        640        650
LLSGARPLDR VDVVQPALFA VMVSLAALWR SHGVEPAAVV GHSQGEIAAA 
       660        670        680        690        700
HVAGALTLED AAKLVAVRSR VLRRLGGQGG MASFGLGTEQ AAERIGRFAG 
       710        720        730        740        750
ALSIASVNGP RSVVVVAGES GPLDELIAEC EAEAHKARRI PVDYASHSPQ 
       760        770        780        790        800
VESLREELLT ELAGISPVSA DVALYSTTTG QPIDTATMDT AYWYANLREQ 
       810        820        830        840        850
VRFQDATRQL AEAGFDAFVE VSPHPVLTVG IEATLDSALP ADAGACVVGT 
       860        870        880        890        900
LRRDRGGLAD FHTALGEAYA QGVEVDWSPA FADARPVELP VYPFQRYWLP 
       910        920        930        940        950
IPTGGRARDE DDDWRYQVVW REAEWESASL AGRVLLVTGP GVPSELSDAI 
       960        970        980        990       1000
RSGLEQSGAT VLTCDVESRS TIGTALEAAD TDALSTVGVA AVPHGEAVDP 
      1010       1020       1030       1040       1050
SLDALALVQA LGAAGVEAPL WVLTRNAVQV ADGELVDPAQ AMVGGLGRVV 
      1060       1070       1080       1090       1100
GIEQPGRWGG LVDLVDADAA SIRSLAAVLA DPRGEEQVAI RADGIKVARL 
      1110       1120       1130       1140       1150
VPAPARARTH PLEPLAGTVL VTGGTGGIGA HLARWLARSG AEHLVLLGRR 
      1160       1170       1180       1190       1200
GADAPGASEL REELTALGTG VTIAACDVAD RARLEAVLAA EAAAEGRTVS 
      1210       1220       1230       1240       1250
AVMHAAGVST STPLDDLTEA EFTEIADVKV RGTVNLDELC PDLDAFVLFS 
      1260       1270       1280       1290       1300
SNAGVWGSPG LASYAAANAF LDGFARAARS EGAPVTSIAW GLWAGQNMAG 
      1310       1320       1330       1340       1350
DEGGEYLRSQ GLRAMDPDRA VEELHITLDH GQTSVSVVDM DRRRFVELFT 
      1360       1370       1380       1390       1400
AARHRPLFDE IAGARAEARQ SEEGPALAQR LAALLCDGRE REHLAHLIRA 
      1410       1420       1430       1440       1450
EVAAVLGHGD DAAIDRDRAF RDLGFDSMTA VDLRNRLAAV TGVREAATVV 
      1460       1470       1480       1490       1500
FDHPTITRLA DHYLERLVGA AEAEQAPALV REVPPKDADD PIAIVGMACR 
      1510       1520       1530       1540       1550
FPGGVHNPGE LWEFIVGGGD AVTEMPTDRG WDLDALFDPD PQRHGTSYSR 
      1560       1570       1580       1590       1600
HGAFLDGAAD FDAAFFGISP REALAMDPQQ RQVLETTWEL FENAGIDPHS 
      1610       1620       1630       1640       1650
VRGSDTGVFL GAAYQGYGQD AVVPEDSEGY LLTGNSSAVV SGRVAYVLGL 
      1660       1670       1680       1690       1700
EGPAVTVDTA CSSSLVALHS ACGSLRDGDC GLAVAGGVSV MAGPEVFTEF 
      1710       1720       1730       1740       1750
SRQGGLAVDG RCKAFSAEAD GFGLPEGVAV VQLQRLSDGP AEGGRQVLGV 
      1760       1770       1780       1790       1800
VAGSAINQDG ATNGLAAPSG VAQQRVIRKA WARAGITGAD VAVVEAHGTG 
      1810       1820       1830       1840       1850
TRLGDPVEAS ALLATYGKSR GSSGPVLLGS VKSNIGHAQA AAGVAGVIKV 
      1860       1870       1880       1890       1900
VLGLNRGLVP PMLCRGERSP LIEWSSGGVE LAEAVSPWPP AADGVRRAGV 
      1910       1920       1930       1940       1950
SAFGVSGTNA HVIIAEPPEP EPLPEPGPVG VLAAANSVPV LLSARTETAL 
      1960       1970       1980       1990       2000
AAQARLLESA VDDSVPLTAL ASALATGRAH LPRRAALLAG DHEQLRGQLR 
      2010       2020       2030       2040       2050
AVAEGVAAPG ATTGTASAGG VVFVFPGQGA QWEGMARGLL SVPVFAESIA 
      2060       2070       2080       2090       2100
ECDAVLSEVA GFSASEVLEQ RPDAPSLERV DVVQPVLFSV MVSLARLWGA 
      2110       2120       2130       2140       2150
CGVSPSAVIG HSQGEIAAAV VAGVLSLEDG VRVVALRAKA LRALAGKGGM 
      2160       2170       2180       2190       2200
VSLAAPGERA RALIAPWEDR ISVAAVNSPS SVVVSGDPEA LAELVARCED 
      2210       2220       2230       2240       2250
EGVRAKTLPV DYASHSRHVE EIRETILADL DGISARRAAI PLYSTLHGER 
      2260       2270       2280       2290       2300
RDMGPRYWYD NLRSQVRFDE AVSAQSPDGH ATFVEMSPHP VLTAAVQEIA 
      2310       2320       2330       2340       2350
ADAVAIGSLH RDTAEEHLIA ELARAHVHGV AVDWRNVFPA APPVALPNYP 
      2360       2370       2380       2390       2400
FEPQRYWLAP EVSDQLADSR YRVDWRPLAT TPVDLEGGFL VHGSAPESLT 
      2410       2420       2430       2440       2450
SAVEKAGGVV PVASADREAL AAALREVPGE VAGVLSVHTG AANALALHQS 
      2460       2470       2480       2490       2500
LGEAGVRAPL WLVTSRAVAL GESEPVDPEQ AMVWGLGRVM GLETPERWGG 
      2510       2520       2530       2540       2550
LVDLPAEPAP GDGEAFVACL GADGHEDQVA IRDHARYGRR LVRAPLGTRE 
      2560       2570       2580       2590       2600
SSWEPAGTAL VTGGTGALGG HVARHLARCG VEDLVLVSRR GVDAPAAAEL 
      2610       2620       2630       2640       2650
EAELVALGPK TTITACDVAD REQLSKLLEE LRGQGRPVRT VVHTAGVPES 
      2660       2670       2680       2690       2700
RPLHEIGELE SVCAAKVTGA RLLDELCPDA ETFVLFSSGA GVWGSANLGA 
      2710       2720       2730       2740       2750
YSAANAYLDA LAHRRRAEGR AATSVAWGAW AGEGMATGDL EGLTRRGLRP 
      2760       2770       2780       2790       2800
MAPDRAIRAL HQALDNGDTC VSIADVDWEA FAVGFTAARP RPLLDELVTP 
      2810       2820       2830       2840       2850
AVGAVPAVQA APAREMTSQE LLEFTHSHVA AILGHSSPDA VGQDQPFTEL 
      2860       2870       2880       2890       2900
GFDSLTAVGL RNQLQQATGL ALPATLVFEH PTVRRLADHI GQQLDSGTPA 
      2910       2920       2930       2940       2950
REASSALRDG YRQAGVSGRV RSYLDLLAGL SDFREHFDGS DGFSLDLVDM 
      2960       2970       2980       2990       3000
ADGPGEVTVI CCAGTAAISG PHEFTRLAGA LRGIAPVRAV PQPGYEEGEP 
      3010       3020       3030       3040       3050
LPSSMAAVAA VQADAVIRTQ GDKPFVVAGH SAGALMAYAL ATELLDRGHP 
      3060       3070       3080       3090       3100
PRGVVLIDVY PPGHQDAMNA WLEELTATLF DRETVRMDDT RLTALGAYDR 
      3110       3120       3130       3140       3150
LTGQWRPRET GLPTLLVSAG EPMGPWPDDS WKPTWPFEHD TVAVPGDHFT 
      3160       3170 
MVQEHADAIA RHIDAWLGGG NS
Length:3,172
Mass (Da):331,479
Last modified:January 23, 2007 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iDBBD5094E77DDD5F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti289A → R in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti493 – 517PEPRN…MEHRA → ASRGTRCATPVSRWPPAAAP WEQ in CAA39583 (PubMed:2234082).CuratedAdd BLAST25
Sequence conflicti493P → R in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti510A → R in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti513M → W in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti525E → D in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti536R → G in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti547 – 551GPNSP → ARTR in AAA26495 (PubMed:2024119).Curated5
Sequence conflicti673R → A in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti716Missing in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti734 – 736AHK → GIT in AAA26495 (PubMed:2024119).Curated3
Sequence conflicti896R → RELPVYPFQRQR in CAA39583 (PubMed:2234082).Curated1
Sequence conflicti896R → RQR in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti988 – 994GVAAVPH → VSLLSRD in AAA26495 (PubMed:2024119).Curated7
Sequence conflicti1108 – 1116RTHPLEPLA → ARTRWSPR in AAA26495 (PubMed:2024119).Curated9
Sequence conflicti1123 – 1125Missing in CAA39583 (PubMed:2234082).Curated3
Sequence conflicti1132L → V in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti1192A → R in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti1194Missing in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti1277 – 1278AA → RR in AAA26495 (PubMed:2024119).Curated2
Sequence conflicti1385 – 1390LCDGRE → STAER in AAA26495 (PubMed:2024119).Curated6
Sequence conflicti1485Missing in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti1518G → R in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti1601V → L in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti1724 – 1725LP → FA in AAA26495 (PubMed:2024119).Curated2
Sequence conflicti1732Q → L in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti1739 – 1743GPAEG → ARRA in AAA26495 (PubMed:2024119).Curated5
Sequence conflicti1762T → S in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti2252D → DGAD in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti2275 – 2277QSP → AVA in AAA26495 (PubMed:2024119).Curated3
Sequence conflicti2408G → GR in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti2420 – 2421LA → S in AAA26495 (PubMed:2024119).Curated2
Sequence conflicti2443 – 2444NA → TH in AAA26495 (PubMed:2024119).Curated2
Sequence conflicti2596A → G in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti2609P → A in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti2715 – 2722RRAEGRAA → AVRKAVRR in CAA39583 (PubMed:2234082).Curated8
Sequence conflicti2754D → E in AAA26495 (PubMed:2024119).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
X56107 Genomic DNA Translation: CAA39583.1
M63677 Genomic DNA Translation: AAA26495.1
X62569 Genomic DNA Translation: CAA44449.1

Protein sequence database of the Protein Information Resource

More...PIRi		S13595
S22012

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56107 Genomic DNA Translation: CAA39583.1
M63677 Genomic DNA Translation: AAA26495.1
X62569 Genomic DNA Translation: CAA44449.1
PIRiS13595
S22012

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KEZX-ray2.80A/B/C2893-3172[»]
1MO2X-ray3.00A/B2893-3172[»]
1PZRNMR-A/B1-39[»]
2HG4X-ray2.73A/B/C/D/E/F1-917[»]
5D3KX-ray1.70A2904-3172[»]
5D3ZX-ray2.10A2904-3172[»]
6MLKX-ray2.45A2893-3172[»]
7M7Eelectron microscopy3.20A/B2896-3172[»]
7M7Felectron microscopy3.20A/B2896-3172[»]
7M7Gelectron microscopy4.10A/B2896-3172[»]
7M7Helectron microscopy4.10A/B2896-3172[»]
SMRiQ03133
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-61229N

Protein family/group databases

ESTHERisacer-ery3, Thioesterase

Proteomic databases

PRIDEiQ03133

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		Q03133, 1 sequenced antibody

Enzyme and pathway databases

UniPathwayiUPA00240
BRENDAi2.3.1.94, 5518

Miscellaneous databases

EvolutionaryTraceiQ03133

Family and domain databases

Gene3Di1.10.1200.10, 2 hits
3.40.366.10, 2 hits
3.40.47.10, 2 hits
3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058, AB_hydrolase
IPR001227, Ac_transferase_dom_sf
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR036291, NAD(P)-bd_dom_sf
IPR032821, PKS_assoc
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR013968, PKS_KR
IPR020806, PKS_PP-bd
IPR020802, PKS_thioesterase
IPR015083, Polyketide_synth_docking
IPR036299, Polyketide_synth_docking_sf
IPR009081, PP-bd_ACP
IPR006162, Ppantetheine_attach_site
IPR001031, Thioesterase
IPR016039, Thiolase-like
PfamiView protein in Pfam
PF00698, Acyl_transf_1, 2 hits
PF08990, Docking, 1 hit
PF16197, KAsynt_C_assoc, 2 hits
PF00109, ketoacyl-synt, 2 hits
PF02801, Ketoacyl-synt_C, 2 hits
PF08659, KR, 2 hits
PF00550, PP-binding, 2 hits
PF00975, Thioesterase, 1 hit
SMARTiView protein in SMART
SM00827, PKS_AT, 2 hits
SM00825, PKS_KS, 2 hits
SM00823, PKS_PP, 2 hits
SM00824, PKS_TE, 1 hit
SUPFAMiSSF101173, SSF101173, 1 hit
SSF47336, SSF47336, 2 hits
SSF51735, SSF51735, 4 hits
SSF52151, SSF52151, 2 hits
SSF53474, SSF53474, 1 hit
SSF53901, SSF53901, 2 hits
SSF55048, SSF55048, 2 hits
PROSITEiView protein in PROSITE
PS00606, B_KETOACYL_SYNTHASE, 2 hits
PS50075, CARRIER, 2 hits
PS00012, PHOSPHOPANTETHEINE, 2 hits

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiERYA3_SACER
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q03133
Secondary accession number(s): Q54097, Q99270
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: May 25, 2022
This is version 153 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again