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Entry version 125 (05 Dec 2018)
Sequence version 1 (01 Oct 1993)
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Protein

6-deoxyerythronolide-B synthase EryA1, modules 1 and 2

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 Publication2 Publications

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. KR controls the stereochemistry of the beta-hydroxyl group of a polyketide (PubMed:16564177).1 Publication1 Publication

<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 3 phosphopantetheines covalently.Curated

<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 sitei145Acyl-ester intermediate; for acyltransferase 1 activityCurated1
Active sitei677Acyl-thioester intermediate; for beta-ketoacyl synthase 1 activityPROSITE-ProRule annotation1
Active sitei1128Acyl-ester intermediate; for acyltransferase 2 activityPROSITE-ProRule annotationBy similarity1
<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 sitei1723NADP 11 Publication1
<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>Sitei1748Could be the principal determinant of stereospecificity1 Publication1
Active sitei1760For beta-ketoacyl reductase 1 activityBy similarity1 Publication1
Active sitei2148Acyl-thioester intermediate; for beta-ketoacyl synthase 2 activityPROSITE-ProRule annotation1
Active sitei2598Acyl-ester intermediate; for acyltransferase 3 activityPROSITE-ProRule annotationBy similarity1
Binding sitei3168NADP 2Curated1
Active sitei3203For beta-ketoacyl reductase 2 activityCurated1

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 bindingi1621 – 1624NADP 11 Publication4
Nucleotide bindingi1644 – 1647NADP 11 Publication4
Nucleotide bindingi1673 – 1674NADP 11 Publication2
Nucleotide bindingi1745 – 1746NADP 11 Publication2
Nucleotide bindingi3065 – 3068NADP 2Curated4
Nucleotide bindingi3088 – 3091NADP 2Curated4
Nucleotide bindingi3117 – 3118NADP 2Curated2
Nucleotide bindingi3188 – 3189NADP 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

  • erythronolide synthase activity Source: UniProtKB
  • phosphopantetheine binding Source: UniProtKB

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-17077

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

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UniPathwayi
UPA00240

<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 EryA1, modules 1 and 2Curated (EC:2.3.1.941 Publication)
Short name:
DEBS 11 Publication
Alternative name(s):
6-deoxyerythronolide B synthase I1 Publication
Erythronolide synthase
ORF CCurated
<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:eryA
<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 provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1705D → A: Still able to produce the triketide lactone (TKL), albeit at reduced titer (40%) compared to the wild-type. Still able to produce the triketide lactone (TKL), albeit at reduced titer (10%) compared to the wild-type; when associated with G-1748. 1 Publication1
Mutagenesisi1748F → G: Still able to produce the triketide lactone (TKL), albeit at reduced titer (10%) compared to the wild-type; when associated with A-1705. 1 Publication1

<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 ‘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_00001802931 – 34916-deoxyerythronolide-B synthase EryA1, modules 1 and 2Add BLAST3491

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 residuei447O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei1921O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei3367O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q03131

<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:16564177). 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.2 Publications1 Publication

<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

13491
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
2FR0X-ray1.81A1391-1872[»]
2FR1X-ray1.79A1391-1872[»]
2JU1NMR-A3318-3408[»]
2JU2NMR-A3318-3408[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q03131

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

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SMRi
Q03131

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
Q03131

<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>Domaini412 – 487Carrier 1PROSITE-ProRule annotationAdd BLAST76
Domaini1886 – 1961Carrier 2PROSITE-ProRule annotationAdd BLAST76
Domaini3329 – 3407Carrier 3PROSITE-ProRule annotationAdd BLAST79

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>Regioni1 – 484Loading domainCuratedAdd BLAST484
Regioni57 – 372Acyltransferase 1CuratedAdd BLAST316
Regioni507 – 1958Module 1CuratedAdd BLAST1452
Regioni507 – 931Beta-ketoacyl synthase 1CuratedAdd BLAST425
Regioni1031 – 1352Acyltransferase 2CuratedAdd BLAST322
Regioni1613 – 1790Beta-ketoacyl reductase 1CuratedAdd BLAST178
Regioni1982 – 3404Module 2CuratedAdd BLAST1423
Regioni1982 – 2405Beta-ketoacyl synthase 2CuratedAdd BLAST424
Regioni2508 – 2827Acyltransferase 3CuratedAdd BLAST320
Regioni3057 – 3233Beta-ketoacyl reductase 2CuratedAdd BLAST177

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG4107EEY Bacteria
COG3321 LUCA

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.1200.10, 3 hits
3.40.366.10, 3 hits
3.40.47.10, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
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
IPR009081 PP-bd_ACP
IPR006162 Ppantetheine_attach_site
IPR016039 Thiolase-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00698 Acyl_transf_1, 3 hits
PF16197 KAsynt_C_assoc, 2 hits
PF00109 ketoacyl-synt, 2 hits
PF02801 Ketoacyl-synt_C, 2 hits
PF08659 KR, 2 hits
PF00550 PP-binding, 3 hits

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00827 PKS_AT, 3 hits
SM00825 PKS_KS, 2 hits
SM00823 PKS_PP, 3 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47336 SSF47336, 3 hits
SSF51735 SSF51735, 4 hits
SSF52151 SSF52151, 3 hits
SSF53901 SSF53901, 2 hits
SSF55048 SSF55048, 3 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, 3 hits
PS00012 PHOSPHOPANTETHEINE, 3 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.

Q03131-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGPRSRTTS RRTPVRIGAV VVASSTSELL DGLAAVADGR PHASVVRGVA
60 70 80 90 100
RPSAPVVFVF PGQGAQWAGM AGELLGESRV FAAAMDACAR AFEPVTDWTL
110 120 130 140 150
AQVLDSPEQS RRVEVVQPAL FAVQTSLAAL WRSFGVTPDA VVGHSIGELA
160 170 180 190 200
AAHVCGAAGA ADAARAAALW SREMIPLVGN GDMAAVALSA DEIEPRIARW
210 220 230 240 250
DDDVVLAGVN GPRSVLLTGS PEPVARRVQE LSAEGVRAQV INVSMAAHSA
260 270 280 290 300
QVDDIAEGMR SALAWFAPGG SEVPFYASLT GGAVDTRELV ADYWRRSFRL
310 320 330 340 350
PVRFDEAIRS ALEVGPGTFV EASPHPVLAA ALQQTLDAEG SSAAVVPTLQ
360 370 380 390 400
RGQGGMRRFL LAAAQAFTGG VAVDWTAAYD DVGPNPALCR SSRRPRRKTS
410 420 430 440 450
RPSPASTGTR HRTCCERLLA VVNGETAALA GREADAEATF RELGLDSVLA
460 470 480 490 500
AQLRAKVSAA IGREVNIALL YDHPTPRALA EALAAGTEVA QRETRARTNE
510 520 530 540 550
AAPGEPVAVV AMACRLPGGV STPEEFWELL SEGRDAVAGL PTDRGWDLDS
560 570 580 590 600
LFHPDPTRSG TAHQRGGGFL TEATAFDPAF FGMSPREALA VDPQQRLMLE
610 620 630 640 650
LSWEVLERAG IPPTSLQASP TGVFVGLIPQ EYGPRLAEGG EGVEGYLMTG
660 670 680 690 700
TTTSVASGRI AYTLGLEGPA ISVDTACSSS LVAVHLACQS LRRGESSLAM
710 720 730 740 750
AGGVTVMPTP GMLVDFSRMN SLAPDGRCKA FSAGANGFGM AEGAGMLLLE
760 770 780 790 800
RLSDARRNGH PVLAVLRGTA VNSDGASNGL SAPNGRAQVR VIQQALAESG
810 820 830 840 850
LGPADIDAVE AHGTGTRLGD PIEARALFEA YGRDREQPLH LGSVKSNLGH
860 870 880 890 900
TQAAAGVAGV IKMVLAMRAG TLPRTLHASE RSKEIDWSSG AISLLDEPEP
910 920 930 940 950
WPAGARPRRA GVSSFGISGT NAHAIIEEAP QVVEGERVEA GDVVAPWVLS
960 970 980 990 1000
ASSAEGLRAQ AARLAAHLRE HPGQDPRDIA YSLATGRAAL PHRAAFAPVD
1010 1020 1030 1040 1050
ESAALRVLDG LATGNADGAA VGTSRAQQRA VFVFPGQGWQ WAGMAVDLLD
1060 1070 1080 1090 1100
TSPVFAAALR ECADALEPHL DFEVIPFLRA EAARREQDAA LSTERVDVVQ
1110 1120 1130 1140 1150
PVMFAVMVSL ASMWRAHGVE PAAVIGHSQG EIAAACVAGA LSLDDAARVV
1160 1170 1180 1190 1200
ALRSRVIATM PGNKGMASIA APAGEVRARI GDRVEIAAVN GPRSVVVAGD
1210 1220 1230 1240 1250
SDELDRLVAS CTTECIRAKR LAVDYASHSS HVETIRDALH AELGEDFHPL
1260 1270 1280 1290 1300
PGFVPFFSTV TGRWTQPDEL DAGYWYRNLR RTVRFADAVR ALAEQGYRTF
1310 1320 1330 1340 1350
LEVSAHPILT AAIEEIGDGS GADLSAIHSL RRGDGSLADF GEALSRAFAA
1360 1370 1380 1390 1400
GVAVDWESVH LGTGARRVPL PTYPFQRERV WLEPKPVARR STEVDEVSAL
1410 1420 1430 1440 1450
RYRIEWRPTG AGEPARLDGT WLVAKYAGTA DETSTAAREA LESAGARVRE
1460 1470 1480 1490 1500
LVVDARCGRD ELAERLRSVG EVAGVLSLLA VDEAEPEEAP LALASLADTL
1510 1520 1530 1540 1550
SLVQAMVSAE LGCPLWTVTE SAVATGPFER VRNAAHGALW GVGRVIALEN
1560 1570 1580 1590 1600
PAVWGGLVDV PAGSVAELAR HLAAVVSGGA GEDQLALRAD GVYGRRWVRA
1610 1620 1630 1640 1650
AAPATDDEWK PTGTVLVTGG TGGVGGQIAR WLARRGAPHL LLVSRSGPDA
1660 1670 1680 1690 1700
DGAGELVAEL EALGARTTVA ACDVTDRESV RELLGGIGDD VPLSAVFHAA
1710 1720 1730 1740 1750
ATLDDGTVDT LTGERIERAS RAKVLGARNL HELTRELDLT AFVLFSSFAS
1760 1770 1780 1790 1800
AFGAPGLGGY APGNAYLDGL AQQRRSDGLP ATAVAWGTWA GSGMAEGAVA
1810 1820 1830 1840 1850
DRFRRHGVIE MPPETACRAL QNALDRAEVC PIVIDVRWDR FLLAYTAQRP
1860 1870 1880 1890 1900
TRLFDEIDDA RRAAPQAPAE PRVGALASLP APEREEALFE LVRSHAAAVL
1910 1920 1930 1940 1950
GHASAERVPA DQAFAELGVD SLSALELRNR LGAATGVRLP TTTVFDHPDV
1960 1970 1980 1990 2000
RTLAAHLAAE LGGATGAEQA APATTAPVDE PIAIVGMACR LPGEVDSPER
2010 2020 2030 2040 2050
LWELITSGRD SAAEVPDDRG WVPDELMASD AAGTRAHGNF MAGAGDFDAA
2060 2070 2080 2090 2100
FFGISPREAL AMDPQQRQAL ETTWEALESA GIPPETLRGS DTGVFVGMSH
2110 2120 2130 2140 2150
QGYATGRPRP EDGVDGYLLT GNTASVASGR IAYVLGLEGP ALTVDTACSS
2160 2170 2180 2190 2200
SLVALHTACG SLRDGDCGLA VAGGVSVMAG PEVFTEFSRQ GALSPDGRCK
2210 2220 2230 2240 2250
PFSDEADGFG LGEGSAFVVL QRLSDARREG RRVLGVVAGS AVNQDGASNG
2260 2270 2280 2290 2300
LSAPSGVAQQ RVIRRAWARA GITGADVAVV EAHGTGTRLG DPVEASALLA
2310 2320 2330 2340 2350
TYGKSRGSSG PVLLGSVKSN IGHAQAAAGV AGVIKVLLGL ERGVVPPMLC
2360 2370 2380 2390 2400
RGERSGLIDW SSGEIELADG VREWSPAADG VRRAGVSAFG VSGTNAHVII
2410 2420 2430 2440 2450
AEPPEPEPVP QPRRMLPATG VVPVVLSART GAALRAQAGR LADHLAAHPG
2460 2470 2480 2490 2500
IAPADVSWTM ARARQHFEER AAVLAADTAE AVHRLRAVAD GAVVPGVVTG
2510 2520 2530 2540 2550
SASDGGSVFV FPGQGAQWEG MARELLPVPV FAESIAECDA VLSEVAGFSV
2560 2570 2580 2590 2600
SEVLEPRPDA PSLERVDVVQ PVLFAVMVSL ARLWRACGAV PSAVIGHSQG
2610 2620 2630 2640 2650
EIAAAVVAGA LSLEDGMRVV ARRSRAVRAV AGRGSMLSVR GGRSDVEKLL
2660 2670 2680 2690 2700
ADDSWTGRLE VAAVNGPDAV VVAGDAQAAR EFLEYCEGVG IRARAIPVDY
2710 2720 2730 2740 2750
ASHTAHVEPV RDELVQALAG ITPRRAEVPF FSTLTGDFLD GTELDAGYWY
2760 2770 2780 2790 2800
RNLRHPVEFH SAVQALTDQG YATFIEVSPH PVLASSVQET LDDAESDAAV
2810 2820 2830 2840 2850
LGTLERDAGD ADRFLTALAD AHTRGVAVDW EAVLGRAGLV DLPGYPFQGK
2860 2870 2880 2890 2900
RFWLLPDRTT PRDELDGWFY RVDWTEVPRS EPAALRGRWL VVVPEGHEED
2910 2920 2930 2940 2950
GWTVEVRSAL AEAGAEPEVT RGVGGLVGDC AGVVSLLALE GDGAVQTLVL
2960 2970 2980 2990 3000
VRELDAEGID APLWTVTFGA VDAGSPVARP DQAKLWGLGQ VASLERGPRW
3010 3020 3030 3040 3050
TGLVDLPHMP DPELRGRLTA VLAGSEDQVA VRADAVRARR LSPAHVTATS
3060 3070 3080 3090 3100
EYAVPGGTIL VTGGTAGLGA EVARWLAGRG AEHLALVSRR GPDTEGVGDL
3110 3120 3130 3140 3150
TAELTRLGAR VSVHACDVSS REPVRELVHG LIEQGDVVRG VVHAAGLPQQ
3160 3170 3180 3190 3200
VAINDMDEAA FDEVVAAKAG GAVHLDELCS DAELFLLFSS GAGVWGSARQ
3210 3220 3230 3240 3250
GAYAAGNAFL DAFARHRRGR GLPATSVAWG LWAAGGMTGD EEAVSFLRER
3260 3270 3280 3290 3300
GVRAMPVPRA LAALDRVLAS GETAVVVTDV DWPAFAESYT AARPRPLLDR
3310 3320 3330 3340 3350
IVTTAPSERA GEPETESLRD RLAGLPRAER TAELVRLVRT STATVLGHDD
3360 3370 3380 3390 3400
PKAVRATTPF KELGFDSLAA VRLRNLLNAA TGLRLPSTLV FDHPNASAVA
3410 3420 3430 3440 3450
GFLDAELGTE VRGEAPSALA GLDALEGALP EVPATEREEL VQRLERMLAA
3460 3470 3480 3490
LRPVAQAADA SGTGANPSGD DLGEAGVDEL LEALGRELDG D
Length:3,491
Mass (Da):365,029
Last modified:October 1, 1993 - v1
<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:i682BFC32C90FA8C4
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M63676 Genomic DNA Translation: AAA26493.2
L07626 Genomic DNA Translation: AAA26504.1

Protein sequence database of the Protein Information Resource

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PIRi
T43231

<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
M63676 Genomic DNA Translation: AAA26493.2
L07626 Genomic DNA Translation: AAA26504.1
PIRiT43231

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FR0X-ray1.81A1391-1872[»]
2FR1X-ray1.79A1391-1872[»]
2JU1NMR-A3318-3408[»]
2JU2NMR-A3318-3408[»]
ProteinModelPortaliQ03131
SMRiQ03131
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ03131

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107EEY Bacteria
COG3321 LUCA

Enzyme and pathway databases

UniPathwayi
UPA00240

BioCyciMetaCyc:MONOMER-17077
BRENDAi2.3.1.94 5518

Miscellaneous databases

EvolutionaryTraceiQ03131

Family and domain databases

Gene3Di1.10.1200.10, 3 hits
3.40.366.10, 3 hits
3.40.47.10, 2 hits
InterProiView protein in InterPro
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
IPR009081 PP-bd_ACP
IPR006162 Ppantetheine_attach_site
IPR016039 Thiolase-like
PfamiView protein in Pfam
PF00698 Acyl_transf_1, 3 hits
PF16197 KAsynt_C_assoc, 2 hits
PF00109 ketoacyl-synt, 2 hits
PF02801 Ketoacyl-synt_C, 2 hits
PF08659 KR, 2 hits
PF00550 PP-binding, 3 hits
SMARTiView protein in SMART
SM00827 PKS_AT, 3 hits
SM00825 PKS_KS, 2 hits
SM00823 PKS_PP, 3 hits
SUPFAMiSSF47336 SSF47336, 3 hits
SSF51735 SSF51735, 4 hits
SSF52151 SSF52151, 3 hits
SSF53901 SSF53901, 2 hits
SSF55048 SSF55048, 3 hits
PROSITEiView protein in PROSITE
PS00606 B_KETOACYL_SYNTHASE, 2 hits
PS50075 CARRIER, 3 hits
PS00012 PHOSPHOPANTETHEINE, 3 hits

ProtoNet; Automatic hierarchical classification of proteins

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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 nameiERYA1_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: Q03131
<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: October 1, 1993
Last modified: December 5, 2018
This is version 125 of the entry and version 1 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

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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