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Entry version 143 (05 Dec 2018)
Sequence version 4 (23 Jan 2007)
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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_section">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 ‘Function’ 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_section">'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 ‘Function’ 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 ‘Function’ 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 ‘Function’ 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

GO - Biological processi

<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

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:MONOMER-17079

BRENDA Comprehensive Enzyme Information System

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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

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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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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 lineageiBacteriaActinobacteriaPseudonocardialesPseudonocardiaceaeSaccharopolyspora

<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_processing_section">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.<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_section">'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_section">'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

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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

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q03133

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

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SMRi
Q03133

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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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_and_domains_section">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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4107SQU Bacteria
COG3321 LUCA

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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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
IPR032821 KAsynt_C_assoc
IPR018201 Ketoacyl_synth_AS
IPR014031 Ketoacyl_synth_C
IPR014030 Ketoacyl_synth_N
IPR016036 Malonyl_transacylase_ACP-bd
IPR036291 NAD(P)-bd_dom_sf
IPR020801 PKS_acyl_transferase
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

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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

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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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliQ03133
SMRiQ03133
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61229N

Protein family/group databases

ESTHERisacer-ery3 Thioesterase

Proteomic databases

PRIDEiQ03133

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107SQU Bacteria
COG3321 LUCA

Enzyme and pathway databases

UniPathwayi
UPA00240

BioCyciMetaCyc:MONOMER-17079
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
IPR032821 KAsynt_C_assoc
IPR018201 Ketoacyl_synth_AS
IPR014031 Ketoacyl_synth_C
IPR014030 Ketoacyl_synth_N
IPR016036 Malonyl_transacylase_ACP-bd
IPR036291 NAD(P)-bd_dom_sf
IPR020801 PKS_acyl_transferase
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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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_and_isoforms">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: December 5, 2018
This is version 143 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
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