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Q9KV59

- ACSA_VIBCH

UniProt

Q9KV59 - ACSA_VIBCH

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Protein
Acetyl-coenzyme A synthetase
Gene
acsA, VC_0298
Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed - Annotation score: 4 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 sitei311 – 3111Coenzyme A By similarity
Binding sitei335 – 3351Coenzyme A By similarity
Binding sitei387 – 3871Substrate; via amide nitrogen By similarity
Binding sitei500 – 5001Substrate By similarity
Binding sitei515 – 5151Substrate By similarity
Active sitei517 – 5171 By similarity
Binding sitei523 – 5231Coenzyme A By similarity
Binding sitei526 – 5261Substrate By similarity
Metal bindingi537 – 5371Magnesium; via carbonyl oxygen By similarity
Metal bindingi539 – 5391Magnesium; via carbonyl oxygen By similarity
Metal bindingi542 – 5421Magnesium; via carbonyl oxygen By similarity
Binding sitei584 – 5841Coenzyme A

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A synthetase (EC:6.2.1.1)
Short name:
AcCoA synthetase
Short name:
Acs
Alternative name(s):
Acetate--CoA ligase
Acyl-activating enzyme
Gene namesi
Name:acsA
Ordered Locus Names:VC_0298
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000000584: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 649649Acetyl-coenzyme A synthetaseUniRule annotation
PRO_0000208392Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei609 – 6091N6-acetyllysine By similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Interactioni

Protein-protein interaction databases

STRINGi243277.VC0298.

Structurei

3D structure databases

ProteinModelPortaliQ9KV59.
SMRiQ9KV59. Positions 5-645.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni411 – 4166Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
KOiK01895.
OMAiAWIWYRD.
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.

Q9KV59-1 [UniParc]FASTAAdd to Basket

« Hide

MSEAHIYPVK QNIKAHTHAD NDTYLAMYQQ SIKDPEGFWS EHGKIVDWIK    50
PFTKVKHTSF DPGHIDIRWF EDGTLNVSAN CIDRHLATRG DQVAIIWEGD 100
DPTQDKTLTY KQLHQEVCRF ANALKEQGVR KGDVVCIYMP MVPEAAVAML 150
ACTRIGAVHT IVFGGFSPEA LAGRIIDSNA KLVITADEGV RGGRAVPLKK 200
NVDEALCNPE VKNISKVMVL KRTGGNVAWH EHRDIWWHEA TAKASDNCPP 250
EEMKAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYATMTFK YVFDYQPNEV 300
FWCTADVGWI TGHSYLVYGP LANGAKTILF EGVPNYPTTA RMSEVVDKHK 350
VNILYTAPTA IRALMAKGDE AIKGTSRDSL RIMGSVGEPI NPEAWEWYYR 400
TIGNEKSPIV DTWWQTETGG ILITPLPGAT ALKPGSATRP FFGVQPALVD 450
NMGEIVEGAT EGNLVLLDSW PGQMRTVYGD HDRFEQTYFS TFKGMYFTGD 500
GARRDEDGYY WITGRVDDVL NVSGHRMGTA EIESALVAFN KIAEAAVVGV 550
PHDIKGQAIY AYITLNDGVY PSAELHKEVK DWVRKEIGAI ATPDVLHWTD 600
ALPKTRSGKI MRRILRKIAT GDTSNLGDTS TLADPSVVDR LIAEKAQLK 649
Length:649
Mass (Da):71,895
Last modified:September 26, 2003 - v2
Checksum:iA0C7282B14806B6E
GO

Sequence cautioni

The sequence AAF93472.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE003852 Genomic DNA. Translation: AAF93472.1. Different initiation.
PIRiD82339.
RefSeqiNP_229953.2. NC_002505.1.

Genome annotation databases

EnsemblBacteriaiAAF93472; AAF93472; VC_0298.
GeneIDi2614968.
KEGGivch:VC0298.
PATRICi20079643. VBIVibCho83274_0280.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE003852 Genomic DNA. Translation: AAF93472.1 . Different initiation.
PIRi D82339.
RefSeqi NP_229953.2. NC_002505.1.

3D structure databases

ProteinModelPortali Q9KV59.
SMRi Q9KV59. Positions 5-645.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243277.VC0298.

Protocols and materials databases

DNASUi 2614968.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF93472 ; AAF93472 ; VC_0298 .
GeneIDi 2614968.
KEGGi vch:VC0298.
PATRICi 20079643. VBIVibCho83274_0280.

Phylogenomic databases

eggNOGi COG0365.
KOi K01895.
OMAi AWIWYRD.
OrthoDBi EOG68WR2H.

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: ATCC 39315 / El Tor Inaba N16961.

Entry informationi

Entry nameiACSA_VIBCH
AccessioniPrimary (citable) accession number: Q9KV59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: September 26, 2003
Last modified: May 14, 2014
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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