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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Caulobacter sp. (strain K31)
Status
Unreviewed-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 sitei309 – 3091Coenzyme AUniRule annotation
Binding sitei333 – 3331Coenzyme AUniRule annotation
Binding sitei498 – 4981ATPUniRule annotation
Binding sitei513 – 5131ATPUniRule annotation
Binding sitei521 – 5211Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei524 – 5241ATPUniRule annotation
Metal bindingi535 – 5351Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi537 – 5371Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi540 – 5401Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei582 – 5821Coenzyme AUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi385 – 3873ATPUniRule annotation
Nucleotide bindingi409 – 4146ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotationImported

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotation, Metal-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

BioCyciCSP366602:GH0Y-112-MONOMER.

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:Caul_0111Imported
OrganismiCaulobacter sp. (strain K31)Imported
Taxonomic identifieri366602 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter
ProteomesiUP000001316 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei607 – 6071N6-acetyllysineUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi366602.Caul_0111.

Structurei

3D structure databases

ProteinModelPortaliB0T280.
SMRiB0T280. Positions 9-643.
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.
HOGENOMiHOG000229981.
KOiK01895.
OMAiTANEGPR.
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.

B0T280-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDGQVFPIP DDWAGKAHID AAGYEAALAR VEADPEGYWR DLAGRLDWIR
60 70 80 90 100
APTQIKDVSF AKDDFRIHWY ADGVLNVSAN CIDRHLPHRK DEVALIFEGD
110 120 130 140 150
EPGVSSTLTY GQLHEEVCRM ANVLKVQGVR KGDRVTIYLP MIPIAAVAML
160 170 180 190 200
ACARIGAVHS VVFGGFSPDS IAGRIQDCGS HFVITADEGR RGGKRVPLKA
210 220 230 240 250
NIDKALEHCP WVSKVLMVRW TGAETTLVRH RDVVWEDVKD SVSADCPPEP
260 270 280 290 300
MNAEDPLFIL YTSGSTGKPK GVLHTTGGYL AWAAWTHEAV FDYRPGEVFW
310 320 330 340 350
CTADVGWVTG HSYVVYGPLA NGGTSLIFEG VPNYPTPARF WEVVDKHQVE
360 370 380 390 400
IFYTAPTALR ALMREGDDWV TKNDLSSLRL LGSVGEPINP EAWLWYHRVV
410 420 430 440 450
GKDRLPIVDT WWQTETGGVL VSPLPGATAL KPGSATKPLP GVKLQLVDAE
460 470 480 490 500
GHVLEGATEG NLLITDSWPG QMRTVYGDHG RFFDTYFSAY PGKYFTGDGC
510 520 530 540 550
RRDADGYYWI TGRVDDVINV SGHRLGTAEI ESALVAHDTV AEAAVVGYPH
560 570 580 590 600
DIKGQGVYAY VTLRAGVEPT DSLRKDLMLW VRQEIGPFAA PDVLQWAPGL
610 620 630 640
PKTRSGKIMR RILRKIAENE LGSLGDISTL ADPSVVDDLV KNRANS
Length:646
Mass (Da):70,982
Last modified:April 8, 2008 - v1
Checksum:i1AA950EAE622162D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000927 Genomic DNA. Translation: ABZ69249.1.
RefSeqiWP_012284207.1. NC_010338.1.

Genome annotation databases

EnsemblBacteriaiABZ69249; ABZ69249; Caul_0111.
KEGGicak:Caul_0111.
PATRICi21313238. VBICauSp18104_0493.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000927 Genomic DNA. Translation: ABZ69249.1.
RefSeqiWP_012284207.1. NC_010338.1.

3D structure databases

ProteinModelPortaliB0T280.
SMRiB0T280. Positions 9-643.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi366602.Caul_0111.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABZ69249; ABZ69249; Caul_0111.
KEGGicak:Caul_0111.
PATRICi21313238. VBICauSp18104_0493.

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiTANEGPR.
OrthoDBiEOG68WR2H.

Enzyme and pathway databases

BioCyciCSP366602:GH0Y-112-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K31Imported.

Entry informationi

Entry nameiB0T280_CAUSK
AccessioniPrimary (citable) accession number: B0T280
Entry historyi
Integrated into UniProtKB/TrEMBL: April 8, 2008
Last sequence update: April 8, 2008
Last modified: July 22, 2015
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.