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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Pasteurella multocida (strain Pm70)
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 sitei314Coenzyme AUniRule annotation1
Binding sitei505ATPUniRule annotation1
Binding sitei520ATPUniRule annotation1
Binding sitei528Coenzyme A; via carbonyl oxygenUniRule annotation1
Binding sitei531ATPUniRule annotation1
Metal bindingi542Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi547Magnesium; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi390 – 392ATPUniRule annotation3
Nucleotide bindingi414 – 419ATPUniRule 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:PM0692
OrganismiPasteurella multocida (strain Pm70)
Taxonomic identifieri272843 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella
Proteomesi
  • UP000000809 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002083721 – 653Acetyl-coenzyme A synthetaseAdd BLAST653

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei617N6-acetyllysineUniRule annotation1

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiQ9CMW1.

Interactioni

Protein-protein interaction databases

STRINGi272843.PM0692.

Structurei

3D structure databases

ProteinModelPortaliQ9CMW1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni195 – 198Coenzyme A bindingUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiEGAPNWP.

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.
IPR019758. Pept_S26A_signal_pept_1_CS.
[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.

Q9CMW1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPHNSMLKEN RLFKPTDEFR RQANISGLET YQALWEFADK DYLTYWSDLA
60 70 80 90 100
RELITWKKPF MHIFDDSEAP FYKWFSDGTL NVSYNCLDRH LPDKADKTAL
110 120 130 140 150
IFESDFGQVQ LYTYAKLHNR VCRFANALRE LGIKKGDRVI IYLPMLVEAV
160 170 180 190 200
IAMQACARIG AVHSVVFGGF SASALRDRIE DAEAKLVITA NAGLRGGKII
210 220 230 240 250
PLKETVDEAL EMGCKTIENV IVFHRVNIDT PWKKGRDLWW NELTANQPAF
260 270 280 290 300
CEPEWMNAED PLFILYTSGS TGKPKGIVHS TGGYLLGALN SFRNVFDNKP
310 320 330 340 350
NDIFWCTADV GWITGHSYVC YGPLANGATQ VIFEGVPTYP DPGRIWRMIQ
360 370 380 390 400
RHKINVFYTS PTLIRSLTRL GDHIPNKYDL SSLRLLGSVG EPINPSAWMW
410 420 430 440 450
FYEVVGKSRC PIVDTWWQTE TGSIMLAPIP GVTATKPGSC TLPLPGIMAE
460 470 480 490 500
VLDENGQKCA VEQGGALAIK RPFPSMLRTI WNDPERYKST YFPAEYGGKY
510 520 530 540 550
YIAGDNAHRD KDGYFWILGR TDDVLNVSGH RLGTMEIESA LVASPKVAEA
560 570 580 590 600
AVVGKPDEIK GEAIVAFVVL NDFRPEGEEA RQLAEELKAW VSNEIGKIAR
610 620 630 640 650
PEDIRFADNL PKTRSGKIMR RLLRSIAKNE MITQDISTLE NPQIIGQLQQ

QWL
Length:653
Mass (Da):73,616
Last modified:June 1, 2001 - v1
Checksum:i67FEB2721E4BF899
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004439 Genomic DNA. Translation: AAK02776.1.
RefSeqiWP_005754110.1. NC_002663.1.

Genome annotation databases

EnsemblBacteriaiAAK02776; AAK02776; PM0692.
GeneIDi1244039.
KEGGipmu:PM0692.
PATRICi22870578. VBIPasMul88067_0700.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004439 Genomic DNA. Translation: AAK02776.1.
RefSeqiWP_005754110.1. NC_002663.1.

3D structure databases

ProteinModelPortaliQ9CMW1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272843.PM0692.

Proteomic databases

PRIDEiQ9CMW1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK02776; AAK02776; PM0692.
GeneIDi1244039.
KEGGipmu:PM0692.
PATRICi22870578. VBIPasMul88067_0700.

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiEGAPNWP.

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.
IPR019758. Pept_S26A_signal_pept_1_CS.
[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_PASMU
AccessioniPrimary (citable) accession number: Q9CMW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: June 1, 2001
Last modified: November 2, 2016
This is version 82 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.