NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=USDA 110;
DOI=10.1093/dnares/9.6.189; PubMed=12597275 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110.";
DNA Res. 9:189-197(2002).

[2]

NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-605, AND MUTAGENESIS OF GLY-263; GLY-266; LYS-269 AND GLU-414.
STRAIN=USDA 110;
PubMed=11726281 [NCBI, ExPASy, EBI, Israel, Japan]
Lee H.Y., Na K.B., Koo H.M., Kim Y.S.;
"Identification of active site residues in Bradyrhizobium japonicum acetyl-CoA synthetase.";
J. Biochem. 130:807-813(2001).

Comments

CATALYTIC ACTIVITY: ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.
PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme (By similarity).
SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
SEQUENCE CAUTION:
- Sequence=AAK95494.1; Type=Frameshift; Positions=479;

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BA000040; BAC45838.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF290478; AAK95494.1; ALT_FRAME; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_767213.1; -.

3D structure databases

HSSP

Q8ZKF6; 1PG4. [HSSP ENTRY / PDB]

ModBase

Q89WV5.

Enzyme and pathway databases

BioCyc

BJAP224911:BLR0573-MON; -.

Ontologies

GO:0003987;	Molecular function: acetate-CoA ligase activity (inferred from electronic annotation from HAMAP).
GO:0016208;	Molecular function: AMP binding (inferred from electronic annotation from InterPro).
GO:0008152;	Biological process: metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

HAMAP

MF_01123; -; 1.
PBIL [Tree]

InterPro

IPR011904; Ac_CoA_lig_AcsA.
IPR000873; AMP-dep_Synth/Lig.
Graphical view of domain structure.

Pfam

PF00501; AMP-binding; 1.
Pfam graphical view of domain structure.

PRINTS

PR00154; AMPBINDING.

TIGRFAMs

TIGR02188; Ac_CoA_lig_AcsA; 1.

PROSITE

PS00455; AMP_BINDING; 1.

Genome annotation databases

GeneID

1049589; -.

GenomeReviews

BA000040_GR; blr0573.

KEGG

bja:blr0573; -.

NMPDR

fig|224911.1.peg.573; -.

Phylogenomic databases

HOGENOM

Q89WV5; -.

Genome annotation databases

CMR

Q89WV5; blr0573.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Complete proteome; Ligase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 648`	`648`	`Acetyl-coenzyme A synthetase.`	`PRO_0000208355`
`ACT_SITE`	`514 514`		`By similarity.`
`MOD_RES`	`606 606`		`N6-acetyllysine (By similarity).`
`MUTAGEN`	`263 263`		`G->I: Loss of activity.`
`MUTAGEN`	`266 266`		`G->I: Great decrease in activity.`
`MUTAGEN`	`269 269`		`K->G: Great decrease in activity.`
`MUTAGEN`	`414 414`		`E->Q: Great decrease in activity.`

Sequence information

Length: 648 AA [This is the length of the unprocessed precursor]

Molecular weight: 72030 Da [This is the MW of the unprocessed precursor]

CRC64: 4D439C3AF01483B0 [This is a checksum on the sequence]

        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

Q89WV5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools