ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q8KBY0

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ACSA_CHLTE
Primary accession number Q8KBY0
Secondary accession numbers None
Integrated into Swiss-Prot on September 26, 2003
Sequence was last modified on September 26, 2003 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 35)
Name and origin of the protein
Protein name Acetyl-coenzyme A synthetase
Synonyms EC 6.2.1.1
Acetate--CoA ligase
Acyl-activating enzyme
Gene name
Name: acsA
Synonyms: acs
OrderedLocusNames: CT1652
From
Chlorobium tepidum [TaxID: 1097] [HAMAP proteome]
Taxonomy Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 49652 / DSM 12025 / TLS;
DOI=10.1073/pnas.132181499; PubMed=12093901 [NCBI, ExPASy, EBI, Israel, Japan]
Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.;
"The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium.";
Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE006470; AAM72877.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_662535.1; -.
3D structure databases
HSSP Q8ZKF6; 1PG4. [HSSP ENTRY / PDB]
ModBase Q8KBY0.
Enzyme and pathway databases
BioCyc CTEP194439:CT_1652-MON; -.
Ontologies
GO
GO:0003987; Molecular function: acetate-CoA ligase activity (inferred from electronic annotation from HAMAP).
GO:0016208; Molecular function: AMP binding (inferred from electronic annotation from InterPro).
GO:0008152; Biological process: metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
HAMAP MF_01123; -; 1.
PBIL [Tree]
InterPro IPR011904; Ac_CoA_lig_AcsA.
IPR000873; AMP-dep_Synth/Lig.
Graphical view of domain structure.
Pfam PF00501; AMP-binding; 1.
Pfam graphical view of domain structure.
PRINTS PR00154; AMPBINDING.
TIGRFAMs TIGR02188; Ac_CoA_lig_AcsA; 1.
PROSITE PS00455; AMP_BINDING; 1.
ProtoNet Q8KBY0.
Genome annotation databases
GeneID 1006138; -.
GenomeReviews AE006470_GR; CT1652.
KEGG cte:CT1652; -.
NMPDR fig|194439.1.peg.1629; -.
TIGR CT1652; -.
Phylogenomic databases
HOGENOM Q8KBY0; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Complete proteome; Ligase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   659  659     Acetyl-coenzyme A synthetase. PRO_0000208360
ACT_SITE   529   529        By similarity. 
MOD_RES   621   621        N6-acetyllysine (By similarity). 
Sequence information
Length: 659 AA [This is the length of the unprocessed precursor] Molecular weight: 73576 Da [This is the MW of the unprocessed precursor] CRC64: 2BB84C9AB13EA034 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MATEQTKGQS SESISSVLSE RRKFPPPEAF SSQSHISSME QYEKLYADAA ADPDKYWGDL 

        70         80         90        100        110        120 
AEQFHWFKKW DSVLEWNAPY AKWFNGGTTN IAYNCLDVHV GSWRKNKAAI IWEGEEGNER 

       130        140        150        160        170        180 
ILTYGELHRQ VSKFANVLKI AGIKPGDKVA IYMGMVPELV IAVLACARVG AVHNVIFAGF 

       190        200        210        220        230        240 
AAHAITERVN DSRAKIVICA DGTRRRGSTI NLKNIVDEAI INTPSVKNVI VLKVTGEEIH 

       250        260        270        280        290        300 
MHDGMDHWWH DLMGLAVDEC EPAQVDSEHP LFLLYTSGST GKPKGILHTT AGYMVHAASS 

       310        320        330        340        350        360 
FKYVFDIKDE DIYFCTADIG WITGHTYIIY GPLLNGATVF MYEGAPNYPQ WDRFWDIINR 

       370        380        390        400        410        420 
HKITILYTAP TAIRAFIRAG NEWVTKHDLS SLRLLGTVGE PINPEAWMWY HKYVGQEKCP 

       430        440        450        460        470        480 
IVDTWWQTET GGIMISPMPG ATPTKPGTAT RPLPGIMVDV VRKDGTPCNA NEGGYLVVKR 

       490        500        510        520        530        540 
PWPSMLRTIY GDNERYEKTY WSEFPGMYFT GDGARKDDDG YIWIMGRVDD VVNVSGHRLG 

       550        560        570        580        590        600 
TSEVESALVS HEAVAEAAVV SRPDEIKGNA LVAFVTLKDG YEGDAKLRDS LGKHVAKEIG 

       610        620        630        640        650 
AIAKPDEIRW AKGLPKTRSG KIMRRLLREL ATSNEIKGDV TTLEDLGVIE NLREQEDEG
Q8KBY0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!