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Q3APY8 (Q3APY8_CHLCH) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 57. 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:Cag_1685 EMBL ABB28937.1
OrganismChlorobium chlorochromatii (strain CaD3) [Complete proteome] [HAMAP] EMBL ABB28937.1
Taxonomic identifier340177 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupChlorobium

Protein attributes

Sequence length666 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

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

Region431 – 4366Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5371 By similarity HAMAP-Rule MF_01123
Metal binding5571Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5591Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5621Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3311Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3551Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site4071Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5201Substrate By similarity HAMAP-Rule MF_01123
Binding site5351Substrate By similarity HAMAP-Rule MF_01123
Binding site5431Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5461Substrate By similarity HAMAP-Rule MF_01123
Binding site6041Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6291N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
Q3APY8 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: BAC348AF52226EDF

FASTA66674,565
        10         20         30         40         50         60 
MATETPSSSQ QEAAANPAED SISSVLTEKR KFPPPASFSE QAHLSTMEQY EKLYADAAAD 

        70         80         90        100        110        120 
PEGYWAGIAE QFHWFKKWDS VLEWNSPYAK WFNGGKTNIC YNALDVHVKS WRKNKAAVIW 

       130        140        150        160        170        180 
EGEQGDQRIL TYGELHRQVC KFANVLKIAG IKPGDRIAIY MGMVPELMIA VLACARVGAV 

       190        200        210        220        230        240 
HNVIFAGFSA HAITERVNDS RAKMVICADG TRRRGSTINL KNIVDEAIVN TPSVRNVIVL 

       250        260        270        280        290        300 
KTTGETIKMH DGMDHWWHDL MGLAVDESEA VELDAEHPLF VLYTSGSTGK PKGILHTTAG 

       310        320        330        340        350        360 
YMVHAASSFR YVFDIKDEDI YFCTADIGWI TGHSYMVYGP LLNGATLLMY EGAPNYPQWD 

       370        380        390        400        410        420 
RFWDIINRHK VTILYTAPTA IRAFIRAGNE WVTKHNLNSL RLLGTVGEPI NPEAWMWYHK 

       430        440        450        460        470        480 
VVGQEKCPIV DTWWQTETGG IMVSPMPGAT PTKPGTATRP LPGIMVDVVH KDGTPCGANE 

       490        500        510        520        530        540 
GGYLVIKKPW PSMLRTIYGD NERYEKTYWS EFKDMYFTGD GARKDDDGYI WIMGRVDDVV 

       550        560        570        580        590        600 
NVSGHRLGTS EVESALVSHE AVAEAAVVSR PDDIKGNSLV AFVTLKDEYE GDMKLRESLR 

       610        620        630        640        650        660 
NHVAREIGPI AKPDEIRWAK ALPKTRSGKI MRRLLRELAT SNEIKGDVTT LEDFGVLENL 


RDQENE 

« Hide

References

[1]"Complete sequence of Chlorobium chlorochromatii CaD3."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CaD3 EMBL ABB28937.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000108 Genomic DNA. Translation: ABB28937.1.
RefSeqYP_379980.1. NC_007514.1.

3D structure databases

ProteinModelPortalQ3APY8.
SMRQ3APY8. Positions 31-664.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING340177.Cag_1685.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB28937; ABB28937; Cag_1685.
GeneID3746375.
KEGGcch:Cag_1685.
PATRIC21371113. VBIChlChl46571_1751.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAYNNDERF.
OrthoDBEOG68WR2H.

Enzyme and pathway databases

BioCycCCHL340177:GHBW-1701-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 nameQ3APY8_CHLCH
AccessionPrimary (citable) accession number: Q3APY8
Entry history
Integrated into UniProtKB/TrEMBL: November 22, 2005
Last sequence update: November 22, 2005
Last modified: June 11, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)