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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Methylobacterium extorquens (strain CM4 / NCIMB 13688) (Methylobacterium chloromethanicum)
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)DescriptionActionsGraphical viewLength
Binding sitei310Coenzyme AUniRule annotation1
Binding sitei499ATPUniRule annotation1
Binding sitei514ATPUniRule annotation1
Binding sitei522Coenzyme A; via carbonyl oxygenUniRule annotation1
Binding sitei525ATPUniRule annotation1
Metal bindingi536Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi538Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi541Magnesium; via carbonyl oxygenUniRule annotation1
Binding sitei583Coenzyme AUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi386 – 388ATPUniRule annotation3
Nucleotide bindingi410 – 415ATPUniRule annotation6

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:Mchl_2785
OrganismiMethylobacterium extorquens (strain CM4 / NCIMB 13688) (Methylobacterium chloromethanicum)
Taxonomic identifieri440085 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium
Proteomesi
  • UP000002385 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001640501 – 652Acetyl-coenzyme A synthetaseAdd BLAST652

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei608N6-acetyllysineUniRule annotation1

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Structurei

3D structure databases

ProteinModelPortaliB7KPN8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni190 – 193Coenzyme A bindingUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000229981.
KOiK01895.
OMAiEGAPNWP.
OrthoDBiPOG091H059D.

Family and domain databases

CDDicd05966. ACS. 1 hit.
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.

B7KPN8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEKVIDVQD AWRDRALIDE AKYKEMYEAS VSDPETFWGE HGKRIDWSTP
60 70 80 90 100
FSKVKNTSFA PGDVSIKWFE DGRTNVALNC IDRHLATRGD QTAIIWEGDD
110 120 130 140 150
PNESKHITYR QLHAEVCRMA NVLRNRGVGK GDRVTLYLPM IPEAAYAMLA
160 170 180 190 200
CARLGAIHAI VFGGFSPDSL ASRIKGCGSK LVITADEGLR GGRKVPLKAN
210 220 230 240 250
VDEAIKRLDK DLVDHVIVVK RTGGNVAMEP GRDVYYHEAA EQVTDECPAE
260 270 280 290 300
AVEAEHPLFI LYTSGSTGQP KGVVHTTGGY LVYASMTHQY VFDYHDGEVY
310 320 330 340 350
WCTADVGWVT GHSYIVYGPL ANGATTLMFE GIPTYPSNSR FWEVIDKHKV
360 370 380 390 400
NIFYTAPTAI RSLMGGGEGP VKKTSRQSLR VLGSVGEPIN PEAWDWYYRV
410 420 430 440 450
VGDSRCPIVD TWWQTETGGI LITPLPGATR LKPGSATLPF FGVQPVMVDA
460 470 480 490 500
EGKILDGACE GNLCIKDSWP GQMRTVYGDH ERFEQTYFST YKDLYFTGDG
510 520 530 540 550
ARRDADGYYW ITGRVDDVIN VSGHRMGTAE VESSLVAHPK VSEAAVVGYP
560 570 580 590 600
HNVKGQGIYA YVTLNEGEEG TDELRKELVT WVRKDIGPIA SPDLLQFAPG
610 620 630 640 650
LPKTRSGKIM RRILRKIAED DFGSLGDTST LAEPAVVDDL IENRQNRQNR

SA
Length:652
Mass (Da):72,190
Last modified:February 10, 2009 - v1
Checksum:i50BAC6E81B462479
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001298 Genomic DNA. Translation: ACK83624.1.
RefSeqiWP_015951093.1. NC_011757.1.

Genome annotation databases

EnsemblBacteriaiACK83624; ACK83624; Mchl_2785.
KEGGimch:Mchl_2785.
PATRICi22499839. VBIMetChl132133_2749.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001298 Genomic DNA. Translation: ACK83624.1.
RefSeqiWP_015951093.1. NC_011757.1.

3D structure databases

ProteinModelPortaliB7KPN8.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACK83624; ACK83624; Mchl_2785.
KEGGimch:Mchl_2785.
PATRICi22499839. VBIMetChl132133_2749.

Phylogenomic databases

HOGENOMiHOG000229981.
KOiK01895.
OMAiEGAPNWP.
OrthoDBiPOG091H059D.

Family and domain databases

CDDicd05966. ACS. 1 hit.
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_METC4
AccessioniPrimary (citable) accession number: B7KPN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: November 2, 2016
This is version 53 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

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.