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Q47X57 (Q47X57_COLP3) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 55. 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:acs EMBL AAZ26507.1
Synonyms:acsA HAMAP-Rule MF_01123
Ordered Locus Names:CPS_3955 EMBL AAZ26507.1
OrganismColwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus) [Complete proteome] [HAMAP] EMBL AAZ26507.1
Taxonomic identifier167879 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesColwelliaceaeColwellia

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 SAAS011904

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 site5151 By similarity HAMAP-Rule MF_01123
Metal binding5351Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5371Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5401Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3091Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3851Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site4981Substrate By similarity HAMAP-Rule MF_01123
Binding site5131Substrate By similarity HAMAP-Rule MF_01123
Binding site5211Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5241Substrate By similarity HAMAP-Rule MF_01123
Binding site5821Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6071N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
Q47X57 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 12B79CF080B776AB

FASTA64871,614
        10         20         30         40         50         60 
MKELKSCYPV SEKAKAHTHI DAATYDAMYK KSIEQPDEFW GEQAKEFIDW YKPWDSVSKV 

        70         80         90        100        110        120 
DLKNSEINWF SGGKLNVSYN CIDRHLATKA NDTAIIFEGD DPNDDSKVTY QELHDHVCRF 

       130        140        150        160        170        180 
ANLLKERGVK KGDRVCIYMP MIPEVGYAML ACARIGAIHS VVFGGFSTES IKARVLDADC 

       190        200        210        220        230        240 
KVVITADQSL RGGKRIPLKS NVDAAVIDCP NVHSVIVVAR TGGDVAWNDK VDINYEEAVA 

       250        260        270        280        290        300 
KQSAICEPEV MDAEDPLFVL YTSGSTGTPK GVVHTCGGYI LYAAMTHKYV FDYKEGEVYW 

       310        320        330        340        350        360 
CTADAGWITG HSYIFYGPLA NGATTLVFEG VPTYPDAGRF WQVCEKHKVN VFYTAPTAIR 

       370        380        390        400        410        420 
ALMSIGDDLV NQADLSSLRL LGTVGEPINP EAWHWYYEVV GKSNCPIVDT WWQTETGGIL 

       430        440        450        460        470        480 
ITSLPGAVDM KPGCAGKPFF GVQPALFDKD GNTLEGENAG LLVMTASWPG QLRTVYGDHN 

       490        500        510        520        530        540 
RFYQTYLGQY PGNYFTGDGA KRDEDGYYWI TGRVDDVLNV SGHRLGTAEI ESALVLHPAV 

       550        560        570        580        590        600 
AEAAVVGYPH EIKGQGVYCY VTLMGNATES DELNVELREF VAKELGRFAK PDYIQWSPGL 

       610        620        630        640 
PKTRSGKIMR RILRKIAEND VDSLGDTSTL ADPSVVENLI DKRIIHGA 

« Hide

References

[1]"The psychrophilic lifestyle as revealed by the genome sequence of Colwellia psychrerythraea 34H through genomic and proteomic analyses."
Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X., Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M., Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A., Zhou L., Davidsen T.M. expand/collapse author list , Wu M., Huston A.L., Lewis M., Weaver B., Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 34H / ATCC BAA-681.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000083 Genomic DNA. Translation: AAZ26507.1.
RefSeqYP_270613.1. NC_003910.7.

3D structure databases

ProteinModelPortalQ47X57.
SMRQ47X57. Positions 20-643.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167879.CPS_3955.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ26507; AAZ26507; CPS_3955.
GeneID3520759.
KEGGcps:CPS_3955.
PATRIC21470797. VBIColPsy94388_3583.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAHPPQKML.
OrthoDBEOG68WR2H.

Enzyme and pathway databases

BioCycCPSY167879:GI48-3955-MONOMER.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
InterProIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ47X57_COLP3
AccessionPrimary (citable) accession number: Q47X57
Entry history
Integrated into UniProtKB/TrEMBL: September 13, 2005
Last sequence update: September 13, 2005
Last modified: June 11, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)