Reviewed, UniProtKB/Swiss-Prot Q89WV5 (ACSA_BRAJA)

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:	blr0573

Organism

Bradyrhizobium japonicum [Complete proteome] [HAMAP]

Taxonomic identifier

375 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Bradyrhizobium

Protein attributes

Sequence length	648 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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.
Sequence caution	The sequence AAK95494.1 differs from that shown. Reason: Frameshift at position 479.

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 – 648	648	Acetyl-coenzyme A synthetase HAMAP MF_01123		PRO_0000208355
Sites
	Active site	514	1	By similarity
Amino acid modifications
	Modified residue	606	1	N6-acetyllysine By similarity
Experimental info
	Mutagenesis	263	1	G → I: Loss of activity. Ref.2
	Mutagenesis	266	1	G → I: Great decrease in activity. Ref.2
	Mutagenesis	269	1	K → G: Great decrease in activity. Ref.2
	Mutagenesis	414	1	E → Q: Great decrease in activity. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q89WV5-1 [UniParc]. Last modified September 26, 2003. Version 2. Checksum: 4D439C3AF01483B0	FASTA	648	72,030
	10 20 30 40 50 60 MSEKIYDVPA EWAKRAWVDQ AKYKEMYARS ISDPNGFWAE QAKRIDWMKA PTKIENVSFA 70 80 90 100 110 120 PGNVSIKWFE DGVLNVAHNC IDRHLHKRAN QTAIIWEGDD PSQSRHITYK ELHDEVCRMA 130 140 150 160 170 180 NILRTRNVKK GDRVTIYLPM IPEAAYAMLA CARIGAIHSV VFAGFSPDSL AQRINDCQSK 190 200 210 220 230 240 VIITADEGLR GGKKVPLKAN VDAALAKADG VDWVVVVKRT GGKIDMNPTR DLWYHEAAAM 250 260 270 280 290 300 VTTECPVEHM HAEDPLFILY TSGSTGQPKG VLHTSAGYLV YAAMTHQYVF DYHDGDIYWC 310 320 330 340 350 360 TADVGWVTGH SYILYGPLAN GATTLMFEGV PNYPDNSRFW NVIDKHKVNT FYTAPTAIRA 370 380 390 400 410 420 LMQGGDEPVK KTSRASLRLL GSVGEPINPE AWEWYHRVVG EDRCPIVDTW WQTETGGILI 430 440 450 460 470 480 TPLPGATKLK PGSATQPFFG VVPEIVDADG KVLEGETTGN LCLTRAWPGM MRTVYGDHAR 490 500 510 520 530 540 FEQTYFSTYK GKYFTGDGCR RDADGYYWIT GRVDDVINVS GHRMGTAEVE SALVAHEKVS 550 560 570 580 590 600 EAAVVGFPHD IKGQGIYAYV TLMAGVQPTE DLRKELVTWV RKEIGPIASP DQIQFAPGLP 610 620 630 640 KTRSGKIMRR ILRKIAEDEP GSLGDTSTLA DPAVVDDLVK NRQNKKSA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110." Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S. DNA Res. 9:189-197(2002) [PubMed: 12597275] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: USDA 110.
[2]	"Identification of active site residues in Bradyrhizobium japonicum acetyl-CoA synthetase." Lee H.Y., Na K.B., Koo H.M., Kim Y.S. J. Biochem. 130:807-813(2001) [PubMed: 11726281] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-605, MUTAGENESIS OF GLY-263; GLY-266; LYS-269 AND GLU-414. Strain: USDA 110.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000040 Genomic DNA. Translation: BAC45838.1. AF290478 Genomic DNA. Translation: AAK95494.1. Frameshift.
RefSeq	NP_767213.1.
3D structure databases
HSSP	HSSP built from PDB template 1PG4 based on UniProtKB Q8ZKF6.
ModBase	Search...
Genome annotation databases
GeneID	1049589.
GenomeReviews	Gene locus blr0573 in contig BA000040_GR.
KEGG	bja:blr0573.
NMPDR	fig|224911.1.peg.573.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q89WV5.
Enzyme and pathway databases
BioCyc	BJAP224911:BLR0573-MON.
BRENDA	6.2.1.1. 280.
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_BRAJA

Accession

Primary (citable) accession number: Q89WV5
Secondary accession number(s): Q93Q03

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2003
Last sequence update:	September 26, 2003
Last modified:	June 16, 2009
This is version 39 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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