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Q9KV59

- ACSA_VIBCH

UniProt

Q9KV59 - ACSA_VIBCH

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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed - 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 sitei311 – 3111Coenzyme AUniRule annotation
Binding sitei335 – 3351Coenzyme AUniRule annotation
Binding sitei500 – 5001ATPUniRule annotation
Binding sitei515 – 5151ATPUniRule annotation
Binding sitei523 – 5231Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei526 – 5261ATPUniRule annotation
Metal bindingi537 – 5371Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi539 – 5391Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi542 – 5421Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei584 – 5841Coenzyme AUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi387 – 3893ATPUniRule annotation
Nucleotide bindingi411 – 4166ATPUniRule annotation

GO - Molecular functioni

  1. acetate-CoA ligase activity Source: TIGR
  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: 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 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:acsAUniRule annotation
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 synthetasePRO_0000208392Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei609 – 6091N6-acetyllysineUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Interactioni

Protein-protein interaction databases

STRINGi243277.VC0298.

Structurei

3D structure databases

ProteinModelPortaliQ9KV59.
SMRiQ9KV59. Positions 5-645.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni191 – 1944Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEAHIYPVK QNIKAHTHAD NDTYLAMYQQ SIKDPEGFWS EHGKIVDWIK
60 70 80 90 100
PFTKVKHTSF DPGHIDIRWF EDGTLNVSAN CIDRHLATRG DQVAIIWEGD
110 120 130 140 150
DPTQDKTLTY KQLHQEVCRF ANALKEQGVR KGDVVCIYMP MVPEAAVAML
160 170 180 190 200
ACTRIGAVHT IVFGGFSPEA LAGRIIDSNA KLVITADEGV RGGRAVPLKK
210 220 230 240 250
NVDEALCNPE VKNISKVMVL KRTGGNVAWH EHRDIWWHEA TAKASDNCPP
260 270 280 290 300
EEMKAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYATMTFK YVFDYQPNEV
310 320 330 340 350
FWCTADVGWI TGHSYLVYGP LANGAKTILF EGVPNYPTTA RMSEVVDKHK
360 370 380 390 400
VNILYTAPTA IRALMAKGDE AIKGTSRDSL RIMGSVGEPI NPEAWEWYYR
410 420 430 440 450
TIGNEKSPIV DTWWQTETGG ILITPLPGAT ALKPGSATRP FFGVQPALVD
460 470 480 490 500
NMGEIVEGAT EGNLVLLDSW PGQMRTVYGD HDRFEQTYFS TFKGMYFTGD
510 520 530 540 550
GARRDEDGYY WITGRVDDVL NVSGHRMGTA EIESALVAFN KIAEAAVVGV
560 570 580 590 600
PHDIKGQAIY AYITLNDGVY PSAELHKEVK DWVRKEIGAI ATPDVLHWTD
610 620 630 640
ALPKTRSGKI MRRILRKIAT GDTSNLGDTS TLADPSVVDR LIAEKAQLK
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: October 1, 2014
This is version 77 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