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A5F3Q8

- A5F3Q8_VIBC3

UniProt

A5F3Q8 - A5F3Q8_VIBC3

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Protein

Acetyl-coenzyme A synthetase

Gene

acs-1

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.UniRule annotation

Catalytic activityi

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

Cofactori

Magnesium.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei328 – 3281Coenzyme AUniRule annotation
Binding sitei352 – 3521Coenzyme AUniRule annotation
Binding sitei517 – 5171ATPUniRule annotation
Binding sitei532 – 5321ATPUniRule annotation
Binding sitei540 – 5401Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei543 – 5431ATPUniRule annotation
Metal bindingi554 – 5541Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi556 – 5561Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi559 – 5591Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei601 – 6011Coenzyme AUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi404 – 4063ATPUniRule annotation
Nucleotide bindingi428 – 4336ATPUniRule annotation

GO - Molecular functioni

  1. acetate-CoA ligase activity Source: UniProtKB-HAMAP
  2. AMP binding Source: InterPro
  3. ATP binding Source: UniProtKB-KW
  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 ligaseUniRule annotation
Acyl-activating enzymeUniRule annotation
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
ProteomesiUP000000249: Chromosome 2, UP000001630: Chromosome I

PTM / Processingi

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi345073.VC0395_A2691.

Structurei

3D structure databases

ProteinModelPortaliA5F3Q8.
SMRiA5F3Q8. Positions 22-662.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni208 – 2114Coenzyme A bindingUniRule annotation

Sequence similaritiesi

Belongs to the ATP-dependent AMP-binding enzyme family.UniRule annotation

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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKRALSGNLP NSQGEPVMSE AHIYPVKQNI KAHTHADNDT YLAMYQQSIK
60 70 80 90 100
DPEGFWSEHG KIVDWIKPFT KVKHTSFDPG HIDIRWFEDG TLNVSANCID
110 120 130 140 150
RHLATRGDQV AIIWEGDDPT QDKTLTYKQL HQEVCRFANA LKEQGVRKGD
160 170 180 190 200
VVCIYMPMVP EAAVAMLACT RIGAVHTIVF GGFSPEALAG RIIDSNAKLV
210 220 230 240 250
ITADEGVRGG RAVPLKKNVD EALCNPEVKN ISKVMVLKRT GGNVAWHEHR
260 270 280 290 300
DIWWHEATAK ASDNCPPEEM KAEDPLFILY TSGSTGKPKG VLHTTGGYLV
310 320 330 340 350
YATMTFKYVF DYQPNEVFWC TADVGWITGH SYLVYGPLAN GAKTILFEGV
360 370 380 390 400
PNYPTTARMS EVVDKHKVNI LYTAPTAIRA LMAKGDEAIK GTSRDSLRIM
410 420 430 440 450
GSVGEPINPE AWEWYYRTIG NEESPIVDTW WQTETGGILI TPLPGATALK
460 470 480 490 500
PGSATRPFFG VQPALVDNMG EIVEGATEGN LVLLDSWPGQ MRTVYGDHDR
510 520 530 540 550
FEQTYFSTFK GMYFTGDGAR RDEDGYYWIT GRVDDVLNVS GHRMGTAEIE
560 570 580 590 600
SALVAFNKIA EAAVVGVPHD IKGQAIYAYI TLNDGVYPSA ELHKEVKDWV
610 620 630 640 650
RKEIGAIATP DVLHWTDALP KTRSGKIMRR ILRKIATGDT SNLGDTSTLA
660
DPSVVDRLIA EKAQLK
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 / O395Imported 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: October 29, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3