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UniProtKB/Swiss-Prot entry Q9Y7B5


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

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Entry information
Entry name ACS2_KLULA
Primary accession number Q9Y7B5
Secondary accession number Q6CQG2
Integrated into Swiss-Prot on April 27, 2001
Sequence was last modified on September 27, 2004 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 37)
Name and origin of the protein
Protein name Acetyl-coenzyme A synthetase 2
Synonyms EC 6.2.1.1
Acetate--CoA ligase 2
Acyl-activating enzyme 2
Gene name
Name: ACS2
OrderedLocusNames: KLLA0D17336g
From
Kluyveromyces lactis (Yeast) (Candida sphaerica) [TaxID: 28985] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC MYA-539 / JBD100;
DOI=10.1002/yea.936; PubMed=12489122 [NCBI, ExPASy, EBI, Israel, Japan]
Zeeman A.M., Steensma H.Y.;
"The acetyl co-enzyme A synthetase genes of Kluyveromyces lactis.";
Yeast 20:13-23(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37;
DOI=10.1038/nature02579; PubMed=15229592 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
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
AF134491; AAD30108.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR382124; CAH00923.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq XP_453827.1; -.
3D structure databases
HSSP Q8ZKF6; 1PG4. [HSSP ENTRY / PDB]
ModBase Q9Y7B5.
Ontologies
GO
GO:0003987; Molecular function: acetate-CoA ligase activity (inferred from electronic annotation from InterPro).
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
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 Q9Y7B5.
Genome annotation databases
GeneID 2893299; -.
KEGG kla:KLLA0D17336g; -.
Phylogenomic databases
HOGENOM Q9Y7B5; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Ligase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   684  684     Acetyl-coenzyme A synthetase 2. PRO_0000208415
CONFLICT   491   491        A -> D (in Ref. 1; AAD30108). 
Sequence information
Length: 684 AA [This is the length of the unprocessed precursor] Molecular weight: 75105 Da [This is the MW of the unprocessed precursor] CRC64: 9B62655F72CFAA8E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSSDKLHKVV HEAHDVEARH APEHFYNSQP GKSYCTDEEH YREMYTQSIE DPAGFFGPLA 

        70         80         90        100        110        120 
KEYLDWDRPF TQVQSGSLEH GDIAWFLNGE LNASYNCVDR HAFANPDKPA LIYEADDESE 

       130        140        150        160        170        180 
NKVITFGELL RQVSEVAGVL QSWGVKKGDT VAVYLPMIPA AVVAMLAVAR LGAIHSVIFA 

       190        200        210        220        230        240 
GFSAGSLKER VVDAGCKVVI TCDEGKRGGK TVHTKKIVDE GLAGVDSVSK ILVFQRTGTQ 

       250        260        270        280        290        300 
GIPMKPARDF WWHEECVKQR GYLPPVPVNS EDPLFLLYTS GSTGSPKGVV HSTAGYLLGS 

       310        320        330        340        350        360 
ALTTRFVFDI HPEDVLFTAG DVGWITGHTY ALYGPLTLGT ATIIFESTPA YPDYGRYWRI 

       370        380        390        400        410        420 
IERHRATHFY VAPTALRLIK RVGEEEIAKY DTSSLRVLGS VGEPISPDLW EWYHEKVGKN 

       430        440        450        460        470        480 
NCVICDTMWQ TESGSHLIAP LAGAVPTKPG SATVPFFGIN ACIIDPVSGE ELKGNDVEGV 

       490        500        510        520        530        540 
LAVKSPWPSM ARSVWNNHAR YFETYLKPYP GYYFTGDGAG RDHDGYYWIR GRVDDVVNVS 

       550        560        570        580        590        600 
GHRLSTAEIE AALAEHEGVS EAAVVGITDE LTGQAVIAFV SLKDGYLSEN AVEGDSTHIS 

       610        620        630        640        650        660 
PDNLRRELIL QVRGEIGPFA APKTVVVVND LPKTRSGKIM RRVLRKVASK EADQLGDLST 

       670        680 
LANADVVPSI ISAVENQFFS QQKK 

Q9Y7B5 in FASTA format

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