Reviewed, UniProtKB/Swiss-Prot Q0VSR6 (ACSA_ALCBS)

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:	ABO_0334

Organism

Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]

Taxonomic identifier

393595 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax

Protein attributes

Sequence length	645 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
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 – 645	645	Acetyl-coenzyme A synthetase HAMAP MF_01123		PRO_1000065267
Sites
	Active site	514	1	By similarity
Amino acid modifications
	Modified residue	606	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0VSR6-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 797AF36619843BE5	FASTA	645	71,302
	10 20 30 40 50 60 MSQVHIHPVP ADYKKQTLMD RETYDRWYSQ SINDPGTFWA ERAEQLLDWK TPWDTVSEWD 70 80 90 100 110 120 FNEGRAAWFK GATLNACYNC VDRHLPERAN QTAIIWEGDE PDQDKHISYQ QLFEEVSKFG 130 140 150 160 170 180 NVLKNRGVKK GDRVVIYMPM IPEAAYAMLA CARIGAIHSV VFGGFSPEAL KDRILNAEAC 190 200 210 220 230 240 ALITADEGVR GGKTIPLKVN ADKALDGIDC VHTCLTVKRT GGDVDWQAPR DVWYHEAMAD 250 260 270 280 290 300 ASSDCEPEWV EAEDPLFTLY TSGSTGKPKG VVHTTAGYLL NTALTHKYVF DYQDGDIYWC 310 320 330 340 350 360 TADVGWITGH SYIVYGPLAN GATTLMFEGV PTYPDASRCW QVVDKHKVNI FYTAPTAIRA 370 380 390 400 410 420 LMGLGDAPVE QTSRASLKLL GTVGEPINPE AWEWYYRVVG DSRCPIVDTW WQTETGAIMI 430 440 450 460 470 480 APLPGAVDLK AGSATLPMFG VQPGLMDPDG NELDGAASGN LVLKASWPSQ IRTVYGDHQR 490 500 510 520 530 540 LIDTYFSAYK GCYFTGDGAR RDEDGYYWIT GRVDDVLNVS GHRLGTAEIE SALVLHPSIS 550 560 570 580 590 600 EAAVVGYQHD VKGQGIYAYV SLMAGKEGSE ELVKALRDLV TQEIGPIAKP DLIHFAPGLP 610 620 630 640 KTRSGKIMRR ILRKIAADEL DSLGDTSTLA DPSVVDQLID NRQNK

References

[1]

"Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis." Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., McHardy A.C., Meyer F. , Nechitaylo T., Puehler A., Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N. Nat. Biotechnol. 24:997-1004(2006) [PubMed: 16878126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM286690 Genomic DNA. Translation: CAL15782.1.
RefSeq	YP_692054.1.
3D structure databases
SMR	Q0VSR6. Positions 5-643.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0VSR6.
Genome annotation databases
GeneID	4211279.
GenomeReviews	Gene locus ABO_0334 in contig AM286690_GR.
KEGG	abo:ABO_0334.
NMPDR	fig|393595.12.peg.334.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0365.
HOGENOM	HBG547964.
OMA	SANEADQ.
PhylomeDB	Q0VSR6.
Enzyme and pathway databases
BioCyc	ABOR393595:ABO_0334-MONOMER.
Family and domain databases
HAMAP	MF_01123. Ac_CoA_synth. [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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACSA_ALCBS

Accession

Primary (citable) accession number: Q0VSR6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	September 5, 2006
Last modified:	February 9, 2010
This is version 29 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)