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Q16B70 (Q16B70_ROSDO) 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

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 EMBL ABG30773.1
Ordered Locus Names:RD1_1117 EMBL ABG30773.1
OrganismRoseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp. (strain OCh 114)) (Roseobacter denitrificans) [Complete proteome] [HAMAP] EMBL ABG30773.1
Taxonomic identifier375451 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRoseobacter

Protein attributes

Sequence length640 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

Region398 – 4036Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5061 By similarity HAMAP-Rule MF_01123
Metal binding5261Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5281Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5311Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site2981Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3741Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site4891Substrate By similarity HAMAP-Rule MF_01123
Binding site5041Substrate By similarity HAMAP-Rule MF_01123
Binding site5121Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5151Substrate By similarity HAMAP-Rule MF_01123
Binding site5731Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue5981N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
Q16B70 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: 892116E2437F2578

FASTA64070,426
        10         20         30         40         50         60 
MTRTPHVTLS QYASLYSESV SDSEGFWRRE GGRVDWIKPF TKVRDVNFDL GSVSINWYGD 

        70         80         90        100        110        120 
GTLNVAANCV DRHLATRADQ TAIIWEPDDP KDAAKHITYK QLHVSVCKMA NVLESLGVRR 

       130        140        150        160        170        180 
GDRVVIYLPM IPEAAYAMLA CARIGAIHSI VFAGFSPDAL AARINGSDAK VVITADHAPR 

       190        200        210        220        230        240 
GGRATALKAN TDAALLHCKD SVKCLVVKRT GGQTTWIDGR DFDCGEMMLE ASDVSHPAEM 

       250        260        270        280        290        300 
NAEDPLFILY TSGSTGQPKG VVHTSGGYLT YAAMTHEIVF DYHDGDVFWC TADVGWVTGH 

       310        320        330        340        350        360 
SYIVYGPLAN GATTIMFEGV PTYPDASRFW QVCEKHKVNQ FYTAPTAIRA LMGQGKEFVE 

       370        380        390        400        410        420 
KCDLSDLKVL GTVGEPINPE AWNWYNDVVG KGKCPIVDTW WQTETGGHLM TPLPGAHTMK 

       430        440        450        460        470        480 
PGSAMKPFFG IKPMVLEPAS GEVLEGNDVE GVLVIADSWP GQMRTIWGDH ERFEKTYFSD 

       490        500        510        520        530        540 
YKGYYFTGDG CKRDADGDYW ITGRVDDVIN VSGHRMGTAE VESALVAHAK VAEAAVVGYP 

       550        560        570        580        590        600 
HDIKGQGIYC YVTLMNGEEP SDELYQELRK WVRAEIGPIA SPDLIQWAPG LPKTRSGKIM 

       610        620        630        640 
RRILRKIAED DFATLGDTST LADPTVVDDL IKNRMNKQDA 

« Hide

References

[1]"The complete genome sequence of Roseobacter denitrificans reveals a mixotrophic rather than photosynthetic metabolism."
Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H., Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K., O'huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T., Touchman J.W.
J. Bacteriol. 189:683-690(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33942 / OCh 114.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000362 Genomic DNA. Translation: ABG30773.1.
RefSeqYP_681459.1. NC_008209.1.

3D structure databases

ProteinModelPortalQ16B70.
SMRQ16B70. Positions 11-634.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING375451.RD1_1117.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG30773; ABG30773; RD1_1117.
GeneID4197563.
KEGGrde:RD1_1117.
PATRIC23360369. VBIRosDen86677_1079.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OrthoDBEOG68WR2H.

Enzyme and pathway databases

BioCycRDEN375451:GJIZ-1047-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 nameQ16B70_ROSDO
AccessionPrimary (citable) accession number: Q16B70
Entry history
Integrated into UniProtKB/TrEMBL: July 25, 2006
Last sequence update: July 25, 2006
Last modified: June 11, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)