Q63NC4 (ACSA_BURPS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetyl-coenzyme A synthetase
EC=6.2.1.1

Alternative name(s):
Acetate--CoA ligase
Acyl-activating enzyme

Gene names

Name:	acsA
Ordered Locus Names:	BPSS0375

Organism

Burkholderia pseudomallei (Pseudomonas pseudomallei)

Taxonomic identifier

28450 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	660 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP MF_01123
Post-translational modification	Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity. HAMAP MF_01123
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
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 – 660	660	Acetyl-coenzyme A synthetase HAMAP MF_01123		PRO_1000065284
Sites
	Active site	530	1	By similarity
Amino acid modifications
	Modified residue	625	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q63NC4 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: B067B10A94777DF9	FASTA	660	72,282
	10 20 30 40 50 60 MSAIESVLHE RRQFAPPAAV EKAAAISGMA AYRALAEEAE RDYEGFWARL ARETLEWRKP 70 80 90 100 110 120 FGKVLDETNA PFYKWFEDGE LNASYNCLDR HVAAGLGERV AVIFEADDGT VTRVTYADLL 130 140 150 160 170 180 ARVSRFANAL KKRGVGRGDR VVIYIPMSVE GIVAMQACAR IGATHSVVFG GFSSKSLHER 190 200 210 220 230 240 IVDVGATALV TADEQMRGGK TLPLKSIADE ALAMGGCDAV KTVVVYRRTG GNVDWHAGRD 250 260 270 280 290 300 VWMHEMVANE SDACEPEWVG AEHPLFILYT SGSTGKPKGV QHSTAGYLLW VAQTMKWTFD 310 320 330 340 350 360 WKPDDVFWCT ADIGWVTGHS YITYGPLAVG ATQVVFEGVP TYPNAGRFWK MIGDHKVTVF 370 380 390 400 410 420 YTAPTAIRSL IKAAEADDRV HPRSYDLSSL RIIGTVGEPI NPEAWIWYHK NVGQARCPIV 430 440 450 460 470 480 DTWWQTETGG HMITPLPGAT PTVPGSCTLP LPGIMAAVVD ETGQDVPNGQ GGILVVKRPW 490 500 510 520 530 540 PAMARTIWGD PERFKKSYFP EELGGRLYLA GDGTVRDKET GYFTIMGRID DVLNVSGHRL 550 560 570 580 590 600 GTMEIESALV SHELVAEAAV VGRPDDTTGE AVVAFVVLKR SRPEGEEAAA LAKTLRDWVG 610 620 630 640 650 660 KEIGPIAKPK DIRFGDNLPK TRSGKIMRRL LRSLAKGEAI TQDTSTLENP AILEQLAEVR

References

[1]

"Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei." Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F., Challis G.L. , Cherevach I., Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004) [PubMed: 15377794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K96243.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571966 Genomic DNA. Translation: CAH37823.1.
RefSeq	YP_110395.1. NC_006351.1.
3D structure databases
HSSP	HSSP built from PDB template 1RY2 based on UniProtKB Q01574.
ProteinModelPortal	Q63NC4.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3095797.
GenomeReviews	Gene locus BPSS0375 in contig BX571966_GR.
KEGG	bps:BPSS0375.
PATRIC	19268394. VBIBurPse99623_4369.
Phylogenomic databases
HOGENOM	HBG547964.
OMA	TRGTEES.
PhylomeDB	Q63NC4.
ProtClustDB	PRK00174.
Enzyme and pathway databases
BioCyc	BPSE272560:BPSS0375-MONOMER.
Family and domain databases
HAMAP	MF_01123. Ac_CoA_synth. [Tree]
InterPro	IPR011904. Ac_CoA_lig. IPR024597. Acyl-CoA_synth_DUF3448. IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. [Graphical view]
KO	K01895.
PANTHER	PTHR24095:SF42. PTHR24095:SF42. 1 hit.
Pfam	PF00501. AMP-binding. 1 hit. PF11930. DUF3448. 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

ACSA_BURPS

Accession

Primary (citable) accession number: Q63NC4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program