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G4REV1 (G4REV1_PELHB) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 10. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123
Short name=AcCoA synthetase HAMAP-Rule MF_01123
Short name=Acs HAMAP-Rule MF_01123
EC=6.2.1.1 HAMAP-Rule MF_01123
Alternative name(s):
Acetate--CoA ligase HAMAP-Rule MF_01123
Acyl-activating enzyme HAMAP-Rule MF_01123
Gene names
Name:acsA HAMAP-Rule MF_01123
Ordered Locus Names:KKY_1911 EMBL AEQ51922.1
OrganismPelagibacterium halotolerans (strain JCM 15775 / CGMCC 1.7692 / B2) [Complete proteome] [HAMAP]
Taxonomic identifier1082931 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Hyphomicrobiaceae › Pelagibacterium ›

Protein attributes

Sequence length648 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_01123

Catalytic activity

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP-Rule MF_01123

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01123 SAAS SAAS020845

Post-translational modification

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity. HAMAP-Rule MF_01123

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family. HAMAP-Rule MF_01123

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region409 – 4146Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5171 By similarity HAMAP-Rule MF_01123
Metal binding5371Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5391Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5421Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3091Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3331Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3851Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5001Substrate By similarity HAMAP-Rule MF_01123
Binding site5151Substrate By similarity HAMAP-Rule MF_01123
Binding site5231Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5261Substrate By similarity HAMAP-Rule MF_01123
Binding site5841Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6091N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
G4REV1 [UniParc].

Last modified December 14, 2011. Version 1.
Checksum: 1940E68026A1A373

FASTA64871,561
        10         20         30         40         50         60 
MSSEVFAPSD EVVAKTRVTA EQYDRMYRRS VSDPDGFWGE QAQRIDWIKP FTKVKNTSFE 

        70         80         90        100        110        120 
WPDVSIKWFE DGQLNVAANC IDRHLKEHGD TVAIIFEPDD PEAETRHITY RLLHGEVCRF 

       130        140        150        160        170        180 
ANVLKELGVQ KGERVTIYMP MIPEAAYAML ACARIGAVHS VVFGGFSPDA LAGRVNDCDS 

       190        200        210        220        230        240 
RVVITADEGC RGGKKVPLKV NVDKALEDCP GVEKVLVVRN TGSDIAMTSG RDVWLHEAEA 

       250        260        270        280        290        300 
GVEAVCEPEP MNAEDPLFIL YTSGSTGKPK GVLHTTGGYL VYASLTHELT FDYRQGEVFW 

       310        320        330        340        350        360 
CTADVGWVTG HSYIVYGPLA NGATTLMFEG VPNYPDAGRF WEVVDKHKVN IFYTAPTAIR 

       370        380        390        400        410        420 
ALMGAGNQFV ERADLSSLRL LGSVGEPINP EAWMWYHKQV GRERCIVVDT WWQTETGGFM 

       430        440        450        460        470        480 
ITPLPGAIPT KPGSATKPFF GVQPVVLEPE SGKVIEETEA AGVLAIADSW PGQMRTVYGD 

       490        500        510        520        530        540 
HQRFKETYFQ QYKGYYFTGD GCRRDEDGYY WITGRVDDVL NVSGHRLGTA EVESALVAHP 

       550        560        570        580        590        600 
KVSEAAVVGF PHDVKGQGIY CYVTLMAGEA ASDDLAGELR NWVRKEIGPI ASPDHIQFAP 

       610        620        630        640 
GLPKTRSGKI MRRILRKVAE NDYGALGDTS TLADPGVVDD LIANRKNR

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References

[1]"Complete genome sequence of Pelagibacterium halotolerans B2T."
Huo Y.Y., Cheng H., Han X.F., Jiang X.W., Sun C., Zhang X.Q., Zhu X.F., Liu Y.F., Li P.F., Ni P.X., Wu M.
J. Bacteriol. 194:197-198(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 15775 / CGMCC 1.7692 / B2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP003075 Genomic DNA. Translation: AEQ51922.1.
RefSeqYP_004899672.1. NC_016078.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEQ51922; AEQ51922; KKY_1911.
GeneID11342874.
KEGGphl:KKY_1911.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01895.

Enzyme and pathway databases

BioCycPHAL1082931:GJXT-1906-MONOMER.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
InterProIPR011904. Ac_CoA_lig.
IPR024597. Acyl-CoA_synth_DUF3448.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR025110. DUF4009.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF11930. DUF3448. 1 hit.
PF13193. DUF4009. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG4REV1_PELHB
AccessionPrimary (citable) accession number: G4REV1
Entry history
Integrated into UniProtKB/TrEMBL: December 14, 2011
Last sequence update: December 14, 2011
Last modified: April 3, 2013
This is version 10 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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