Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W) (Vibrio succinogenes)
Status
Reviewed-Annotation score: 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

Mg2+UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei313 – 3131Coenzyme AUniRule annotation
Binding sitei506 – 5061ATPUniRule annotation
Binding sitei521 – 5211ATPUniRule annotation
Binding sitei529 – 5291Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei532 – 5321ATPUniRule annotation
Metal bindingi545 – 5451Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi548 – 5481Magnesium; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi389 – 3913ATPUniRule annotation
Nucleotide bindingi413 – 4186ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

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:WS0595
OrganismiWolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W) (Vibrio succinogenes)
Taxonomic identifieri273121 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeWolinella
Proteomesi
  • UP000000422 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 654654Acetyl-coenzyme A synthetasePRO_1000065331Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei619 – 6191N6-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

STRINGi273121.WS0595.

Structurei

3D structure databases

ProteinModelPortaliQ7M9Y2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni193 – 1964Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiIKNMCEY.
OrthoDBiPOG091H059D.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth. 1 hit.
InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. 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.

Q7M9Y2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQTHSTELF KPNRAFAKTA RIKNLCEYED LRLDAEEDFE GFWGKLAKEK
60 70 80 90 100
IDWMEPFSKV LDESEAPFYK WFVGGKLNVC AQCLDRHLDT RKNKAAIIFE
110 120 130 140 150
GELGDSRIIT YRELFYEVKR TANLLKNKFN VKKGDRVVIY MPMIPEAAFM
160 170 180 190 200
MLACARIGAI HSVVFGGFSA EALRDRIIDA EAKLVITADG AYRRGKPYML
210 220 230 240 250
KPVVDDALAE GACPSIEKVL IVIRNKEEIN YVPGRDYIYN EMIGLESAHC
260 270 280 290 300
PPEPMDAEDP LFLLYTSGST GKPKGVQHNQ AGYILWAQTT MEWVFDVKEN
310 320 330 340 350
DTYWCTADVG WITGHTYIVY GPLAMGATTV MYEGVPIYPD TGRWWKMIEH
360 370 380 390 400
YRVNQFYTAP TAIRLLHKEG KEEPKKYNLS NLKVLGTVGE PINPDAWNWY
410 420 430 440 450
YNEIGGGQCP IVDTWWQTET GGHMISPLPG ATPIKPGCAT LPLPGIFAEV
460 470 480 490 500
IDEEGNPKPA GEQGYLCITK PWPSMIRNIW GDPKRYESSY FSTCKKNGKP
510 520 530 540 550
VYFAGDGAIR DERGYITITG RMDDVINVSG HRLGTAEIES AIAKHPGVAE
560 570 580 590 600
TAVVSRLDEI KGESVYAFIV LKPGYEDNVA EELQLLKEIN AVITREIGPL
610 620 630 640 650
AKADTMLFVP GLPKTRSGKI MRRILRSIAR GEEITQDTST LEDPAIVQKI

QQLA
Length:654
Mass (Da):73,456
Last modified:December 15, 2003 - v1
Checksum:i5BE112983A35FFC8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571658 Genomic DNA. Translation: CAE09727.1.
RefSeqiWP_011138527.1. NC_005090.1.

Genome annotation databases

EnsemblBacteriaiCAE09727; CAE09727; WS0595.
KEGGiwsu:WS0595.
PATRICi24038270. VBIWolSuc63014_0566.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571658 Genomic DNA. Translation: CAE09727.1.
RefSeqiWP_011138527.1. NC_005090.1.

3D structure databases

ProteinModelPortaliQ7M9Y2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273121.WS0595.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAE09727; CAE09727; WS0595.
KEGGiwsu:WS0595.
PATRICi24038270. VBIWolSuc63014_0566.

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiIKNMCEY.
OrthoDBiPOG091H059D.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth. 1 hit.
InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiACSA_WOLSU
AccessioniPrimary (citable) accession number: Q7M9Y2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 15, 2003
Last modified: September 7, 2016
This is version 72 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.