Q056J9 (ACSA_LEPBL) 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:	LBL_0125

Organism

Leptospira borgpetersenii serovar Hardjo-bovis (strain L550) [Complete proteome] [HAMAP]

Taxonomic identifier

355276 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Leptospiraceae › Leptospira

Protein attributes

Sequence length	654 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 – 654	654	Acetyl-coenzyme A synthetase HAMAP MF_01123		PRO_1000085002
Sites
	Active site	521	1	By similarity
Amino acid modifications
	Modified residue	613	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q056J9 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 2A51CC717429B00A	FASTA	654	73,402
	10 20 30 40 50 60 MAKERIVLPS AEFKKNSNIT LKDYKSLYKE SIENPNKFWA KEANRLTWFK KWTKVLNHDF 70 80 90 100 110 120 KNAKVEWFKG GKLNVSYNCL DRHISTPLKN KAALIWEGDN PSESKVLTYY DVYREVNRFA 130 140 150 160 170 180 NVLKKYGVKK GDRVLVYLPM IPELAITILA CTRIGAIHSV VFGGFSPEAL QSRIDDCKPK 190 200 210 220 230 240 LIVTADGGFR GGKPIELKRN VDIALEKSKE DVKTVIVVRR TGNESGLVWK DGRDYWYHFL 250 260 270 280 290 300 ISDPDLSPYC KPESMDAEDP LFILYTSGST GKPKGVLHTT GGYLLGVNLT FHYVFDIKPE 310 320 330 340 350 360 DTYWCTADIG WVTGHSYLVY GPLSNGASSV MFEGVPSYPD AGRFWDVIDK YGVNIFYTAP 370 380 390 400 410 420 TAIRALMREG LTHVQKRNLS SLRLLGSVGE PINPEAWEWY FKIIGKEKCP IVDTWWQTET 430 440 450 460 470 480 GSIMITALPG AIPQKPGSAT LPFFGVQPVL VDNDGKEIND KGEVSGNLCI KSPWPSMMRG 490 500 510 520 530 540 VYGDSKRFFD TYFSQFKGYY FTGDGARRDK DGYYWITGRV DDVINVSGHR IGSAEVESAL 550 560 570 580 590 600 VENRSVAEAA VVGFPHDIKG QGIYAYVTVK EGIATNDTLK KELVAIVEKV IGKIARPDVI 610 620 630 640 650 HWAPSLPKTR SGKIMRRILR KIASGEFEGL GDTSTLADPS VVQKLIEDKR KFHS

References

[1]

"Genome reduction in Leptospira borgpetersenii reflects limited transmission potential." Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B. Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006) [PubMed: 16973745] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: L550.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000348 Genomic DNA. Translation: ABJ77746.1.
RefSeq	YP_796679.1. NC_008508.1.
3D structure databases
ProteinModelPortal	Q056J9.
SMR	Q056J9. Positions 10-650.
ModBase	Search...
Protein-protein interaction databases
STRING	Q056J9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4408535.
GenomeReviews	Gene locus LBL_0125 in contig CP000348_GR.
KEGG	lbl:LBL_0125.
PATRIC	22363334. VBILepBor75619_0146.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0365.
HOGENOM	HBG547964.
OMA	VISVSGH.
ProtClustDB	PRK00174.
Enzyme and pathway databases
BioCyc	LBOR355276:LBL_0125-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_LEPBL

Accession

Primary (citable) accession number: Q056J9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	November 14, 2006
Last modified:	January 25, 2012
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program