Reviewed, UniProtKB/Swiss-Prot Q2T3N9 (ACSA_BURTA)

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:	BTH_II2017

Organism

Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]

Taxonomic identifier

271848 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	660 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. HAMAP MF_01123
Post-translational modification	Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity.
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
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: HAMAP
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_1000065286
Sites
	Active site	530	1	By similarity
Amino acid modifications
	Modified residue	625	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2T3N9-1 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: 79A3CEB29447DD7D	FASTA	660	72,217
	10 20 30 40 50 60 MSAIESVLHE RRQFAPPAAV EKAAAISGMA AYRALAEEAE RDYEGFWARL ARETLEWRKP 70 80 90 100 110 120 FGKALDETNA PFYKWFDDGE LNASYNCLDR HVAAGLGERI AVIFEADDGT VARVTYADLL 130 140 150 160 170 180 ARVSRFANAL KKRGIGRGDR VVIYIPMSVE GIVAMQACAR IGATHSVVFG GFSSKSLHER 190 200 210 220 230 240 IVDVGATALV TADEQMRGGK TLPLKSIADE ALAMGGCDAV KTVVVYRRTG GNVDWHAGRD 250 260 270 280 290 300 VWMHEIVANE SDACEPEWVG AEHPLFILYT SGSTGKPKGV QHSTAGYLLW VAQTMKWTFD 310 320 330 340 350 360 WKPDDVFWCT ADIGWVTGHS YITYGPLAVG ATQVVFEGVP TYPNAGRFWK MIGDHKVSVF 370 380 390 400 410 420 YTAPTAIRSL IKAAEADEHV HPKSYDLSSL RIIGTVGEPI NPEAWIWYHK NVGQERCPIV 430 440 450 460 470 480 DTWWQTETGG HMITPLPGAT PTVPGSCTLP LPGIMAAVVD ETGQDVPNGQ GGILVVKRPW 490 500 510 520 530 540 PAMARTIWGD PERFKKSYFP DELGGRLYLA 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]

Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R., Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. , Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D., Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F., Roberts K., Hatch B., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000085 Genomic DNA. Translation: ABC35414.1.
RefSeq	YP_440210.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3846624.
GenomeReviews	Gene locus BTH_II2017 in contig CP000085_GR.
KEGG	bte:BTH_II2017.
TIGR	BTH_II2017.
Phylogenomic databases
HOGENOM	Q2T3N9.
OMA	Q2T3N9. ETASEHC.
Enzyme and pathway databases
BioCyc	BTHA271848:BTH_II2017-MON.
Family and domain databases
HAMAP	MF_01123. [Tree]
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

ACSA_BURTA

Accession

Primary (citable) accession number: Q2T3N9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	January 24, 2006
Last modified:	June 16, 2009
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)