Reviewed, UniProtKB/Swiss-Prot Q9Y7B5 (ACS2_KLULA)

Names and origin

Protein names

Recommended name:
    Acetyl-coenzyme A synthetase 2
    EC=6.2.1.1
Alternative name(s):
    Acetate--CoA ligase 2
    Acyl-activating enzyme 2

Gene names

Name:	ACS2
Ordered Locus Names:	KLLA0D17336g

Organism

Kluyveromyces lactis (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

28985 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces

Protein attributes

Sequence length	684 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	AMP binding Inferred from electronic annotation. Source: InterPro ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetate-CoA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 684	684	Acetyl-coenzyme A synthetase 2		PRO_0000208415
Experimental info
	Sequence conflict	491	1	A → D in AAD30108. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9Y7B5-1 [UniParc]. Last modified September 27, 2004. Version 2. Checksum: 9B62655F72CFAA8E	FASTA	684	75,105
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The acetyl co-enzyme A synthetase genes of Kluyveromyces lactis." Zeeman A.-M., Steensma H.Y. Yeast 20:13-23(2003) [PubMed: 12489122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC MYA-539 / JBD100.
[2]	"Genome evolution in yeasts." 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. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF134491 Genomic DNA. Translation: AAD30108.1. CR382124 Genomic DNA. Translation: CAH00923.1.
RefSeq	XP_453827.1.
3D structure databases
HSSP	HSSP built from PDB template 1PG4 based on UniProtKB Q8ZKF6.
ModBase	Search...
Genome annotation databases
GeneID	2893299.
KEGG	kla:KLLA0D17336g.
Phylogenomic databases
HOGENOM	Q9Y7B5.
OMA	Q9Y7B5. DSSVINE.
Enzyme and pathway databases
BRENDA	6.2.1.1. 74088.
Family and domain databases
InterPro	IPR011904. Ac_CoA_lig_AcsA. IPR000873. AMP-dep_Synth/Lig. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
TIGRFAMs	TIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACS2_KLULA

Accession

Primary (citable) accession number: Q9Y7B5
Secondary accession number(s): Q6CQG2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	September 27, 2004
Last modified:	June 16, 2009
This is version 42 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)