Q72LY9 (ACSA_LEPIC) 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:	LIC_13404

Organism

Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130) [Complete proteome] [HAMAP]

Taxonomic identifier

267671 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Leptospiraceae › Leptospira

Protein attributes

Sequence length	661 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)
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 – 661	661	Acetyl-coenzyme A synthetase HAMAP MF_01123		PRO_0000208366
Sites
	Active site	528	1	By similarity
Amino acid modifications
	Modified residue	620	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q72LY9 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: CADEA253EA654C42	FASTA	661	74,063
	10 20 30 40 50 60 MPNSEEVMAK ERVVSPSAEF KKNANISLKN YKSLYKESIE NPNKFWAREA NRLIWFKKWT 70 80 90 100 110 120 KVLSHDFKNA KVEWFKGGKL NVSYNCLDRH ISTPLKNKAA LIWEGDNPTE SRVLTYYDVY 130 140 150 160 170 180 REVNRFANIL KKFGVKKGDR VLVYLPMIPE LAITILACTR IGAIHSVVFG GFSPEALQSR 190 200 210 220 230 240 IDDCKPKLVV TADGGFRGGK PIELKKNVDL ALEKSKEKVK TVIVVRRTGN ESGLTWKDGQ 250 260 270 280 290 300 DYWYHFLMND PELSAYCKPE EMDAEDPLFI LYTSGSTGKP KGVLHTTGGY LLGANLTFHY 310 320 330 340 350 360 VFDIKPEDTY WCTADIGWVT GHSYLVYGPL SNGASSVMFE GVPSYPDAGR FWDVIDKYGV 370 380 390 400 410 420 NIFYTAPTAI RALMREGLNH IQKRDLSSLR LLGSVGEPIN PEAWEWYFKN IGKGKCPIVD 430 440 450 460 470 480 TWWQTETGSI MITALPGAIP QKPGSATLPF FGVQPVLVDN DGKEITDKGE VSGNLCIKGP 490 500 510 520 530 540 WPSMMRGVYG DPKRFFETYF SQFKGYYFTG DGARRDKDGY FWITGRVDDV INVSGHRIGS 550 560 570 580 590 600 AEVESALVEN KSVAEAAVVG FPHDIKGQGI YAYVTVKEGV TTNDVLKKEL ISTVEKMIGK 610 620 630 640 650 660 IARPDVIHWA PGLPKTRSGK IMRRILRKIA SGEFEGLGDT STLADPSVVQ KLIEDKKKFH S

References

[1]

"Comparative genomics of two Leptospira interrogans serovars reveals novel insights into physiology and pathogenesis." Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B., Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V., Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L., Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S. , Ferro M.I.T., Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H., Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M., Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L., Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A., Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A. J. Bacteriol. 186:2164-2172(2004) [PubMed: 15028702] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Fiocruz L1-130.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016823 Genomic DNA. Translation: AAS71944.1.
RefSeq	YP_003307.1. NC_005823.1.
3D structure databases
ProteinModelPortal	Q72LY9.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2769882.
GenomeReviews	Gene locus LIC_13404 in contig AE016823_GR.
KEGG	lic:LIC13404.
NMPDR	fig|267671.1.peg.3307.
PATRIC	22379945. VBILepInt6257_4120.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG547964.
OMA	VISVSGH.
PhylomeDB	Q72LY9.
ProtClustDB	PRK00174.
Enzyme and pathway databases
BioCyc	LINT267671:LIC_13404-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_LEPIC

Accession

Primary (citable) accession number: Q72LY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program