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Entry version 151 (11 Dec 2019)
Sequence version 3 (23 Jan 2007)
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Protein

6-deoxyerythronolide-B synthase EryA2, modules 3 and 4

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).2 Publications4 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.2 Publications
C2-type beta-ketoacyl reductase 1 is unable to bind NADP and seems to act as a racemase.1 Publication

<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 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 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>Sitei155Important for substrate specificity of the beta-ketoacyl synthase 11 Publication1
Sitei156Important for substrate specificity of the beta-ketoacyl synthase 11 Publication1
<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 sitei202Acyl-thioester intermediate; for beta-ketoacyl synthase 1 activityPROSITE-ProRule annotation1 Publication1
Active sitei651Acyl-ester intermediate; for acyltransferase 1 activityPROSITE-ProRule annotation1
Active sitei1267For C2-type beta-ketoacyl reductase 1 and probable racemase activityBy similarity1 Publication1
Active sitei1661Acyl-thioester intermediate; for beta-ketoacyl synthase 2 activityPROSITE-ProRule annotation1
Active sitei2105Acyl-ester intermediate; for acyltransferase 2 activityPROSITE-ProRule annotation1
Active sitei2409Proton acceptor, for dehydratase activity1 Publication1
Active sitei2571Proton donor; for dehydratase activity1 Publication1
Active sitei2874For enoyl reductase activity1 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 sitei3250NADP 2By similarity1
Active sitei3287For beta-ketoacyl reductase 2 activityCurated1

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 bindingi2964 – 2973NADP 11 Publication10
Nucleotide bindingi3149 – 3152NADP 2Curated4
Nucleotide bindingi3173 – 3176NADP 2Curated4
Nucleotide bindingi3202 – 3203NADP 2Curated2
Nucleotide bindingi3272 – 3273NADP 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
  • oxidoreductase activity Source: InterPro
  • phosphopantetheine binding Source: UniProtKB

GO - Biological processi

  • macrolide biosynthetic process Source: UniProtKB

<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

More...
BioCyci
MetaCyc:MONOMER-17078

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

<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 EryA2, modules 3 and 4Curated (EC:2.3.1.941 Publication)
Short name:
DEBS 21 Publication
Alternative name(s):
6-deoxyerythronolide B synthase II1 Publication
Erythronolide synthase
ORF B1 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 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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Cells lacking this gene are unable to produce 6-deoxyerythronolide (6-dEB), however a tetraketide lactone shunt is produced.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi1254S → F: Produces tetraketide lactone shunt and also 6-deoxyerythronolide (6-dEB). 1 Publication1
Mutagenesisi1267Y → F: Produces tetraketide lactone shunt and also 6-deoxyerythronolide (6-dEB). 1 Publication1
Mutagenesisi2640R → D: Decreased production of the erythromycin precursor 6-deoxyerythronolide B (6-dEB). 1 Publication1
Mutagenesisi2874Y → V: Switches the configuration of the C-2 methyl group of the product. 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 <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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001802942 – 35676-deoxyerythronolide-B synthase EryA2, modules 3 and 4Add BLAST3566

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 residuei1430O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei3448O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

<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:12954331, PubMed:17719492, PubMed:18952099). 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

<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

13567
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

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SMRi
Q03132

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q03132

<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>Domaini1395 – 1470Carrier 1PROSITE-ProRule annotationAdd BLAST76
Domaini3413 – 3488Carrier 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>Regioni33 – 1467Module 3CuratedAdd BLAST1435
Regioni33 – 458Beta-ketoacyl synthase 1CuratedAdd BLAST426
Regioni560 – 880Acyltransferase 1CuratedAdd BLAST321
Regioni1132 – 1297C2-type beta-ketoacyl reductase 1CuratedAdd BLAST166
Regioni1491 – 3485Module 4CuratedAdd BLAST1995
Regioni1491 – 1915Beta-ketoacyl synthase 2CuratedAdd BLAST425
Regioni2015 – 2331Acyltransferase 2CuratedAdd BLAST317
Regioni2377 – 2645DehydrataseCuratedAdd BLAST269
Regioni2831 – 3131Enoyl reductaseCuratedAdd BLAST301
Regioni3141 – 3317Beta-ketoacyl reductase 2CuratedAdd BLAST177

Keywords - Domaini

Repeat

Family and domain databases

Database of protein disorder

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DisProti
DP01272

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.1200.10, 2 hits
3.10.129.110, 1 hit
3.40.366.10, 2 hits
3.40.47.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001227 Ac_transferase_dom_sf
IPR036736 ACP-like_sf
IPR014043 Acyl_transferase
IPR016035 Acyl_Trfase/lysoPLipase
IPR013154 ADH_N
IPR036347 DEBS_docking_sf
IPR015357 Erythronolide_synth_docking
IPR011032 GroES-like_sf
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
IPR020807 PKS_dehydratase
IPR042104 PKS_dehydratase_sf
IPR020843 PKS_ER
IPR013968 PKS_KR
IPR020806 PKS_PP-bd
IPR015083 Polyketide_synth_docking
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, 2 hits
PF08240 ADH_N, 1 hit
PF08990 Docking, 1 hit
PF09277 Erythro-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
PF14765 PS-DH, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00827 PKS_AT, 2 hits
SM00826 PKS_DH, 1 hit
SM00829 PKS_ER, 1 hit
SM00825 PKS_KS, 2 hits
SM00823 PKS_PP, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF101166 SSF101166, 1 hit
SSF47336 SSF47336, 2 hits
SSF50129 SSF50129, 1 hit
SSF51735 SSF51735, 5 hits
SSF52151 SSF52151, 2 hits
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.

Q03132-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTDSEKVAEY LRRATLDLRA ARQRIRELES DPIAIVSMAC RLPGGVNTPQ
60 70 80 90 100
RLWELLREGG ETLSGFPTDR GWDLARLHHP DPDNPGTSYV DKGGFLDDAA
110 120 130 140 150
GFDAEFFGVS PREAAAMDPQ QRLLLETSWE LVENAGIDPH SLRGTATGVF
160 170 180 190 200
LGVAKFGYGE DTAAAEDVEG YSVTGVAPAV ASGRISYTMG LEGPSISVDT
210 220 230 240 250
ACSSSLVALH LAVESLRKGE SSMAVVGGAA VMATPGVFVD FSRQRALAAD
260 270 280 290 300
GRSKAFGAGA DGFGFSEGVT LVLLERLSEA RRNGHEVLAV VRGSALNQDG
310 320 330 340 350
ASNGLSAPSG PAQRRVIRQA LESCGLEPGD VDAVEAHGTG TALGDPIEAN
360 370 380 390 400
ALLDTYGRDR DADRPLWLGS VKSNIGHTQA AAGVTGLLKV VLALRNGELP
410 420 430 440 450
ATLHVEEPTP HVDWSSGGVA LLAGNQPWRR GERTRRARVS AFGISGTNAH
460 470 480 490 500
VIVEEAPERE HRETTAHDGR PVPLVVSART TAALRAQAAQ IAELLERPDA
510 520 530 540 550
DLAGVGLGLA TTRARHEHRA AVVASTREEA VRGLREIAAG AATADAVVEG
560 570 580 590 600
VTEVDGRNVV FLFPGQGSQW AGMGAELLSS SPVFAGKIRA CDESMAPMQD
610 620 630 640 650
WKVSDVLRQA PGAPGLDRVD VVQPVLFAVM VSLAELWRSY GVEPAAVVGH
660 670 680 690 700
SQGEIAAAHV AGALTLEDAA KLVVGRSRLM RSLSGEGGMA AVALGEAAVR
710 720 730 740 750
ERLRPWQDRL SVAAVNGPRS VVVSGEPGAL RAFSEDCAAE GIRVRDIDVD
760 770 780 790 800
YASHSPQIER VREELLETTG DIAPRPARVT FHSTVESRSM DGTELDARYW
810 820 830 840 850
YRNLRETVRF ADAVTRLAES GYDAFIEVSP HPVVVQAVEE AVEEADGAED
860 870 880 890 900
AVVVGSLHRD GGDLSAFLRS MATAHVSGVD IRWDVALPGA APFALPTYPF
910 920 930 940 950
QRKRYWLQPA APAAASDELA YRVSWTPIEK PESGNLDGDW LVVTPLISPE
960 970 980 990 1000
WTEMLCEAIN ANGGRALRCE VDTSASRTEM AQAVAQAGTG FRGVLSLLSS
1010 1020 1030 1040 1050
DESACRPGVP AGAVGLLTLV QALGDAGVDA PVWCLTQGAV RTPADDDLAR
1060 1070 1080 1090 1100
PAQTTAHGFA QVAGLELPGR WGGVVDLPES VDDAALRLLV AVLRGGGRAE
1110 1120 1130 1140 1150
DHLAVRDGRL HGRRVVRASL PQSGSRSWTP HGTVLVTGAA SPVGDQLVRW
1160 1170 1180 1190 1200
LADRGAERLV LAGACPGDDL LAAVEEAGAS AVVCAQDAAA LREALGDEPV
1210 1220 1230 1240 1250
TALVHAGTLT NFGSISEVAP EEFAETIAAK TALLAVLDEV LGDRAVEREV
1260 1270 1280 1290 1300
YCSSVAGIWG GAGMAAYAAG SAYLDALAEH HRARGRSCTS VAWTPWALPG
1310 1320 1330 1340 1350
GAVDDGYLRE RGLRSLSADR AMRTWERVLA AGPVSVAVAD VDWPVLSEGF
1360 1370 1380 1390 1400
AATRPTALFA ELAGRGGQAE AEPDSGPTGE PAQRLAGLSP DEQQENLLEL
1410 1420 1430 1440 1450
VANAVAEVLG HESAAEINVR RAFSELGLDS LNAMALRKRL SASTGLRLPA
1460 1470 1480 1490 1500
SLVFDHPTVT ALAQHLRARL VGDADQAAVR VVGAADESEP IAIVGIGCRF
1510 1520 1530 1540 1550
PGGIGSPEQL WRVLAEGANL TTGFPADRGW DIGRLYHPDP DNPGTSYVDK
1560 1570 1580 1590 1600
GGFLTDAADF DPGFFGITPR EALAMDPQQR LMLETAWEAV ERAGIDPDAL
1610 1620 1630 1640 1650
RGTDTGVFVG MNGQSYMQLL AGEAERVDGY QGLGNSASVL SGRIAYTFGW
1660 1670 1680 1690 1700
EGPALTVDTA CSSSLVGIHL AMQALRRGEC SLALAGGVTV MSDPYTFVDF
1710 1720 1730 1740 1750
STQRGLASDG RCKAFSARAD GFALSEGVAA LVLEPLSRAR ANGHQVLAVL
1760 1770 1780 1790 1800
RGSAVNQDGA SNGLAAPNGP SQERVIRQAL AASGVPAADV DVVEAHGTGT
1810 1820 1830 1840 1850
ELGDPIEAGA LIATYGQDRD RPLRLGSVKT NIGHTQAAAG AAGVIKVVLA
1860 1870 1880 1890 1900
MRHGMLPRSL HADELSPHID WESGAVEVLR EEVPWPAGER PRRAGVSSFG
1910 1920 1930 1940 1950
VSGTNAHVIV EEAPAEQEAA RTERGPLPFV LSGRSEAVVA AQARALAEHL
1960 1970 1980 1990 2000
RDTPELGLTD AAWTLATGRA RFDVRAAVLG DDRAGVCAEL DALAEGRPSA
2010 2020 2030 2040 2050
DAVAPVTSAP RKPVLVFPGQ GAQWVGMARD LLESSEVFAE SMSRCAEALS
2060 2070 2080 2090 2100
PHTDWKLLDV VRGDGGPDPH ERVDVLQPVL FSIMVSLAEL WRAHGVTPAA
2110 2120 2130 2140 2150
VVGHSQGEIA AAHVAGALSL EAAAKVVALR SQVLRELDDQ GGMVSVGASR
2160 2170 2180 2190 2200
DELETVLARW DGRVAVAAVN GPGTSVVAGP TAELDEFFAE AEAREMKPRR
2210 2220 2230 2240 2250
IAVRYASHSP EVARIEDRLA AELGTITAVR GSVPLHSTVT GEVIDTSAMD
2260 2270 2280 2290 2300
ASYWYRNLRR PVLFEQAVRG LVEQGFDTFV EVSPHPVLLM AVEETAEHAG
2310 2320 2330 2340 2350
AEVTCVPTLR REQSGPHEFL RNLLRAHVHG VGADLRPAVA GGRPAELPTY
2360 2370 2380 2390 2400
PFEHQRFWPR PHRPADVSAL GVRGAEHPLL LAAVDVPGHG GAVFTGRLST
2410 2420 2430 2440 2450
DEQPWLAEHV VGGRTLVPGS VLVDLALAAG EDVGLPVLEE LVLQRPLVLA
2460 2470 2480 2490 2500
GAGALLRMSV GAPDESGRRT IDVHAAEDVA DLADAQWSQH ATGTLAQGVA
2510 2520 2530 2540 2550
AGPRDTEQWP PEDAVRIPLD DHYDGLAEQG YEYGPSFQAL RAAWRKDDSV
2560 2570 2580 2590 2600
YAEVSIAADE EGYAFHPVLL DAVAQTLSLG ALGEPGGGKL PFAWNTVTLH
2610 2620 2630 2640 2650
ASGATSVRVV ATPAGADAMA LRVTDPAGHL VATVDSLVVR STGEKWEQPE
2660 2670 2680 2690 2700
PRGGEGELHA LDWGRLAEPG STGRVVAADA SDLDAVLRSG EPEPDAVLVR
2710 2720 2730 2740 2750
YEPEGDDPRA AARHGVLWAA ALVRRWLEQE ELPGATLVIA TSGAVTVSDD
2760 2770 2780 2790 2800
DSVPEPGAAA MWGVIRCAQA ESPDRFVLLD TDAEPGMLPA VPDNPQLALR
2810 2820 2830 2840 2850
GDDVFVPRLS PLAPSALTLP AGTQRLVPGD GAIDSVAFEP APDVEQPLRA
2860 2870 2880 2890 2900
GEVRVDVRAT GVNFRDVLLA LGMYPQKADM GTEAAGVVTA VGPDVDAFAP
2910 2920 2930 2940 2950
GDRVLGLFQG AFAPIAVTDH RLLARVPDGW SDADAAAVPI AYTTAHYALH
2960 2970 2980 2990 3000
DLAGLRAGQS VLIHAAAGGV GMAAVALARR AGAEVLATAG PAKHGTLRAL
3010 3020 3030 3040 3050
GLDDEHIASS RETGFARKFR ERTGGRGVDV VLNSLTGELL DESADLLAED
3060 3070 3080 3090 3100
GVFVEMGKTD LRDAGDFRGR YAPFDLGEAG DDRLGEILRE VVGLLGAGEL
3110 3120 3130 3140 3150
DRLPVSAWEL GSAPAALQHM SRGRHVGKLV LTQPAPVDPD GTVLITGGTG
3160 3170 3180 3190 3200
TLGRLLARHL VTEHGVRHLL LVSRRGADAP GSDELRAEIE DLGASAEIAA
3210 3220 3230 3240 3250
CDTADRDALS ALLDGLPRPL TGVVHAAGVL ADGLVTSIDE PAVEQVLRAK
3260 3270 3280 3290 3300
VDAAWNLHEL TANTGLSFFV LFSSAASVLA GPGQGVYAAA NESLNALAAL
3310 3320 3330 3340 3350
RRTRGLPAKA LGWGLWAQAS EMTSGLGDRI ARTGVAALPT ERALALFDSA
3360 3370 3380 3390 3400
LRRGGEVVFP LSINRSALRR AEFVPEVLRG MVRAKLRAAG QAEAAGPNVV
3410 3420 3430 3440 3450
DRLAGRSESD QVAGLAELVR SHAAAVSGYG SADQLPERKA FKDLGFDSLA
3460 3470 3480 3490 3500
AVELRNRLGT ATGVRLPSTL VFDHPTPLAV AEHLRDRLFA ASPAVDIGDR
3510 3520 3530 3540 3550
LDELEKALEA LSAEDGHDDV GQRLESLLRR WNSRRADAPS TSAISEDASD
3560
DELFSMLDQR FGGGEDL
Length:3,567
Mass (Da):374,421
Last modified:January 23, 2007 - v3
<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:iEE6284F4738AA0C0
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 conflicti438R → A in CAA44448 (PubMed:1740151).Curated1
Sequence conflicti480T → S in CAA44448 (PubMed:1740151).Curated1
Sequence conflicti1241L → F in CAA44448 (PubMed:1740151).Curated1
Sequence conflicti2664G → V in CAA44448 (PubMed:1740151).Curated1

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

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DDBJi
Links Updated
M63677 Genomic DNA Translation: AAA26494.1
X62569 Genomic DNA Translation: CAA44448.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S23070

<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
M63677 Genomic DNA Translation: AAA26494.1
X62569 Genomic DNA Translation: CAA44448.1
PIRiS23070

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
1PZQNMR-A/B3490-3547[»]
1PZRNMR-A/B3548-3567[»]
2QO3X-ray2.59A/B27-922[»]
3EL6X-ray1.85A2362-2653[»]
6C9UX-ray2.09A2-922[»]
SMRiQ03132
ModBaseiSearch...
PDBe-KBiSearch...

Enzyme and pathway databases

UniPathwayiUPA00240
BioCyciMetaCyc:MONOMER-17078
BRENDAi2.3.1.94 5518

Miscellaneous databases

EvolutionaryTraceiQ03132

Family and domain databases

DisProtiDP01272
Gene3Di1.10.1200.10, 2 hits
3.10.129.110, 1 hit
3.40.366.10, 2 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
IPR013154 ADH_N
IPR036347 DEBS_docking_sf
IPR015357 Erythronolide_synth_docking
IPR011032 GroES-like_sf
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
IPR020807 PKS_dehydratase
IPR042104 PKS_dehydratase_sf
IPR020843 PKS_ER
IPR013968 PKS_KR
IPR020806 PKS_PP-bd
IPR015083 Polyketide_synth_docking
IPR009081 PP-bd_ACP
IPR006162 Ppantetheine_attach_site
IPR016039 Thiolase-like
PfamiView protein in Pfam
PF00698 Acyl_transf_1, 2 hits
PF08240 ADH_N, 1 hit
PF08990 Docking, 1 hit
PF09277 Erythro-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
PF14765 PS-DH, 1 hit
SMARTiView protein in SMART
SM00827 PKS_AT, 2 hits
SM00826 PKS_DH, 1 hit
SM00829 PKS_ER, 1 hit
SM00825 PKS_KS, 2 hits
SM00823 PKS_PP, 2 hits
SUPFAMiSSF101166 SSF101166, 1 hit
SSF47336 SSF47336, 2 hits
SSF50129 SSF50129, 1 hit
SSF51735 SSF51735, 5 hits
SSF52151 SSF52151, 2 hits
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

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ProtoNeti
Search...

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 nameiERYA2_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: Q03132
Secondary accession number(s): Q54096
<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: December 11, 2019
This is version 151 of the entry and version 3 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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