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A3PBZ3

- A3PBZ3_PROM0

UniProt

A3PBZ3 - A3PBZ3_PROM0

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Protein
Acetyl-coenzyme A synthetase
Gene
acs, acsA, P9301_06451
Organism
Prochlorococcus marinus (strain MIT 9301)
Status
Unreviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA By similarity.UniRule annotation

Catalytic activityi

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.UniRule annotation

Cofactori

Magnesium By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei322 – 3221Coenzyme A By similarityUniRule annotation
Binding sitei398 – 3981Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei516 – 5161Substrate By similarityUniRule annotation
Binding sitei531 – 5311Substrate By similarityUniRule annotation
Active sitei533 – 5331 By similarityUniRule annotation
Binding sitei539 – 5391Coenzyme A By similarityUniRule annotation
Binding sitei542 – 5421Substrate By similarityUniRule annotation
Metal bindingi553 – 5531Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi555 – 5551Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi558 – 5581Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei600 – 6001Coenzyme A By similarityUniRule annotation

GO - Molecular functioni

  1. AMP binding Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. acetate-CoA ligase activity Source: UniProtKB-HAMAP
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. acetyl-CoA biosynthetic process from acetate Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotationImported

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotation, Metal-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

BioCyciPMAR167546:GH1Y-665-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A synthetaseUniRule annotation (EC:6.2.1.1UniRule annotation)
Short name:
AcCoA synthetaseUniRule annotation
Short name:
AcsUniRule annotation
Alternative name(s):
Acetate--CoA ligase
Acyl-activating enzyme
Gene namesi
Name:acsImported
Synonyms:acsAUniRule annotation
Ordered Locus Names:P9301_06451Imported
OrganismiProchlorococcus marinus (strain MIT 9301)Imported
Taxonomic identifieri167546 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000001430: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei625 – 6251N6-acetyllysine By similarityUniRule annotation

Post-translational modificationi

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity.UniRule annotation

Keywords - PTMi

AcetylationUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi167546.P9301_06451.

Structurei

3D structure databases

ProteinModelPortaliA3PBZ3.
SMRiA3PBZ3. Positions 21-658.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni422 – 4276Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiAGCAVFV.
OrthoDBiEOG68WR2H.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth.
InterProiIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A3PBZ3-1 [UniParc]FASTAAdd to Basket

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MTLDKKNSIN NILEEKRIFP PSKKFAENSN ISTQEELLSL KKQASDNPIQ    50
FWESFAKSEL DWFEPFQTVL DNENAPFFKW FKEGKLNITY NCLDRHIKRG 100
LGGKTALIWE GEPGDSKKYT YEELLKEVCR AANALKAIGV KKGDLVCIYM 150
PMIPEAMFAM LACARIGAPH SVVFGGFSSE ALKDRLIDGN ARYVITADGG 200
FRKDKVIELK QAVDAAIENG ADKVVEKVVV VQRTKKNISM VDDRDLWWHE 250
LVKDQKDQCE PEIMSSEDRL FILYTSGSTG KPKGVVHTTG GYNLWSHLTF 300
KWIFDLKDDD IYWCTADVGW ITGHSYIVYG PLSNGATTLM YEGVPRRSNL 350
GAFWEIVQKY KVSIFYTAPT AIRAFMKSGR EIPDKYNLES LRLLGTVGEP 400
INPEAWMWYK DVIGKDKCPI VDTWWQTETG GVMISPLPGV VATKPGSATF 450
PLPGIEVEIV DKDGDKVKEN EGGYLIIKKP WPGMMRTIHG NSKRYLESYW 500
EYISFKGEKN VYFAGDGARI DEDGYIWIMG RVDDVISVSG HRLGTMEIES 550
ALVSHKSVAE SAVVGKKDDL KGEVIVAFVS LEKDVNGSSE LVEDLKKHVV 600
NEIGIIAKPE KIIISDSLPK TRSGKIMRRI LRSLAGGEKI SGDISTLEDS 650
SVLEKLKELS 660
Length:660
Mass (Da):74,035
Last modified:April 3, 2007 - v1
Checksum:i8EC977BFDFF2C40D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000576 Genomic DNA. Translation: ABO17268.1.
RefSeqiYP_001090869.1. NC_009091.1.

Genome annotation databases

EnsemblBacteriaiABO17268; ABO17268; P9301_06451.
GeneIDi4911088.
KEGGipmg:P9301_06451.
PATRICi22994885. VBIProMar103344_0631.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000576 Genomic DNA. Translation: ABO17268.1 .
RefSeqi YP_001090869.1. NC_009091.1.

3D structure databases

ProteinModelPortali A3PBZ3.
SMRi A3PBZ3. Positions 21-658.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 167546.P9301_06451.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABO17268 ; ABO17268 ; P9301_06451 .
GeneIDi 4911088.
KEGGi pmg:P9301_06451.
PATRICi 22994885. VBIProMar103344_0631.

Phylogenomic databases

eggNOGi COG0365.
HOGENOMi HOG000229981.
KOi K01895.
OMAi AGCAVFV.
OrthoDBi EOG68WR2H.

Enzyme and pathway databases

BioCyci PMAR167546:GH1Y-665-MONOMER.

Family and domain databases

HAMAPi MF_01123. Ac_CoA_synth.
InterProi IPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MIT 9301Imported.

Entry informationi

Entry nameiA3PBZ3_PROM0
AccessioniPrimary (citable) accession number: A3PBZ3
Entry historyi
Integrated into UniProtKB/TrEMBL: April 3, 2007
Last sequence update: April 3, 2007
Last modified: June 11, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

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