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A5F3Q8

- A5F3Q8_VIBC3

UniProt

A5F3Q8 - A5F3Q8_VIBC3

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Protein
Acetyl-coenzyme A synthetase
Gene
acs-1, acsA, VC0395_A2691, VC395_0342
Organism
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
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 sitei328 – 3281Coenzyme A By similarityUniRule annotation
Binding sitei352 – 3521Coenzyme A By similarityUniRule annotation
Binding sitei404 – 4041Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei517 – 5171Substrate By similarityUniRule annotation
Binding sitei532 – 5321Substrate By similarityUniRule annotation
Active sitei534 – 5341 By similarityUniRule annotation
Binding sitei540 – 5401Coenzyme A By similarityUniRule annotation
Binding sitei543 – 5431Substrate By similarityUniRule annotation
Metal bindingi554 – 5541Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi556 – 5561Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi559 – 5591Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei601 – 6011Coenzyme 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

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:acs-1Imported
Synonyms:acsAUniRule annotation
Ordered Locus Names:VC0395_A2691Imported, VC395_0342Imported
OrganismiVibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)Imported
Taxonomic identifieri345073 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000001630: Chromosome I, UP000000249: Chromosome 2

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei626 – 6261N6-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

STRINGi345073.VC0395_A2691.

Structurei

3D structure databases

ProteinModelPortaliA5F3Q8.
SMRiA5F3Q8. Positions 22-662.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni428 – 4336Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiAWIWYRD.

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.

A5F3Q8-1 [UniParc]FASTAAdd to Basket

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MKRALSGNLP NSQGEPVMSE AHIYPVKQNI KAHTHADNDT YLAMYQQSIK    50
DPEGFWSEHG KIVDWIKPFT KVKHTSFDPG HIDIRWFEDG TLNVSANCID 100
RHLATRGDQV AIIWEGDDPT QDKTLTYKQL HQEVCRFANA LKEQGVRKGD 150
VVCIYMPMVP EAAVAMLACT RIGAVHTIVF GGFSPEALAG RIIDSNAKLV 200
ITADEGVRGG RAVPLKKNVD EALCNPEVKN ISKVMVLKRT GGNVAWHEHR 250
DIWWHEATAK ASDNCPPEEM KAEDPLFILY TSGSTGKPKG VLHTTGGYLV 300
YATMTFKYVF DYQPNEVFWC TADVGWITGH SYLVYGPLAN GAKTILFEGV 350
PNYPTTARMS EVVDKHKVNI LYTAPTAIRA LMAKGDEAIK GTSRDSLRIM 400
GSVGEPINPE AWEWYYRTIG NEESPIVDTW WQTETGGILI TPLPGATALK 450
PGSATRPFFG VQPALVDNMG EIVEGATEGN LVLLDSWPGQ MRTVYGDHDR 500
FEQTYFSTFK GMYFTGDGAR RDEDGYYWIT GRVDDVLNVS GHRMGTAEIE 550
SALVAFNKIA EAAVVGVPHD IKGQAIYAYI TLNDGVYPSA ELHKEVKDWV 600
RKEIGAIATP DVLHWTDALP KTRSGKIMRR ILRKIATGDT SNLGDTSTLA 650
DPSVVDRLIA EKAQLK 666
Length:666
Mass (Da):73,676
Last modified:June 12, 2007 - v1
Checksum:iF88F13DB61BB7BE2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000627 Genomic DNA. Translation: ABQ21501.1.
CP001235 Genomic DNA. Translation: ACP08367.1.
RefSeqiYP_002818603.1. NC_012582.1.

Genome annotation databases

EnsemblBacteriaiABQ21501; ABQ21501; VC0395_A2691.
ACP08367; ACP08367; VC395_0342.
GeneIDi7774414.
KEGGivcr:VC395_0342.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000627 Genomic DNA. Translation: ABQ21501.1 .
CP001235 Genomic DNA. Translation: ACP08367.1 .
RefSeqi YP_002818603.1. NC_012582.1.

3D structure databases

ProteinModelPortali A5F3Q8.
SMRi A5F3Q8. Positions 22-662.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 345073.VC0395_A2691.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABQ21501 ; ABQ21501 ; VC0395_A2691 .
ACP08367 ; ACP08367 ; VC395_0342 .
GeneIDi 7774414.
KEGGi vcr:VC395_0342.

Phylogenomic databases

eggNOGi COG0365.
HOGENOMi HOG000229981.
KOi K01895.
OMAi AWIWYRD.

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. Heidelberg J.
    Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 39541 / Classical Ogawa 395 / O395 and O395Imported.
  2. "A recalibrated molecular clock and independent origins for the cholera pandemic clones."
    Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.
    PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 39541 / Classical Ogawa 395 / O395 and O395Imported.

Entry informationi

Entry nameiA5F3Q8_VIBC3
AccessioniPrimary (citable) accession number: A5F3Q8
Entry historyi
Integrated into UniProtKB/TrEMBL: June 12, 2007
Last sequence update: June 12, 2007
Last modified: September 3, 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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