Q2NXE2 (ACSA_XANOM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetyl-coenzyme A synthetase
Short name=AcCoA synthetase
Short name=Acs
EC=6.2.1.1

Alternative name(s):
Acetate--CoA ligase
Acyl-activating enzyme

Gene names

Name:	acsA
Ordered Locus Names:	XOO4280

Organism

Xanthomonas oryzae pv. oryzae (strain MAFF 311018) [Complete proteome] [HAMAP]

Taxonomic identifier

342109 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas › Xanthomonas oryzae › Xanthomonas oryzae pv. oryzae

Protein attributes

Sequence length	647 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA By similarity. HAMAP-Rule MF_01123
Catalytic activity	ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP-Rule MF_01123
Cofactor	Magnesium By similarity.
Post-translational modification	Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity. HAMAP-Rule MF_01123
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA biosynthetic process from acetate 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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 647	647	Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123		PRO_1000085008
Regions
	Region	410 – 415	6	Substrate binding By similarity
Sites
	Active site	516	1	By similarity
	Metal binding	536	1	Magnesium; via carbonyl oxygen By similarity
	Metal binding	538	1	Magnesium; via carbonyl oxygen By similarity
	Metal binding	541	1	Magnesium; via carbonyl oxygen By similarity
	Binding site	310	1	Coenzyme A By similarity
	Binding site	334	1	Coenzyme A By similarity
	Binding site	386	1	Substrate; via amide nitrogen By similarity
	Binding site	499	1	Substrate By similarity
	Binding site	514	1	Substrate By similarity
	Binding site	522	1	Coenzyme A By similarity
	Binding site	525	1	Substrate By similarity
	Binding site	583	1	Coenzyme A
Amino acid modifications
	Modified residue	608	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2NXE2 [UniParc]. Last modified February 7, 2006. Version 1. Checksum: 33558E37802A2523	FASTA	647	71,366
	10 20 30 40 50 60 MADVYPVDPA FAADARVTRE QYAALYRESI EHPEQFWGKA AQRLEWFKQP TQVKDVSYAL 70 80 90 100 110 120 DDFHIRWFGD GELNASVNCL DRQLATRGDK TALLFEPDSP DAASYPVTYR QLYERVCKLG 130 140 150 160 170 180 NALRNLGVKK GDRVTIYLPM IVDAAVAMLA CARIGAVHSV VFGGFAANSI ADRVIDCQSK 190 200 210 220 230 240 LIITADEGLR GGKKIPLKAN VDAALKIPGT NTIETVLVVR HTGGAVEMQA PRDRWFHDVV 250 260 270 280 290 300 DGQPAECEPE RMNAEDPLFI LYTSGSTGKP KGVLHTTAGY LLFASYTHEV VFDLREDDIY 310 320 330 340 350 360 WCTADVGWVT GHSYIVYGPL ANGATAVMFE GVPNYPNVSR FWEVIDKHQV TIFYTAPTAI 370 380 390 400 410 420 RALMRDGAEP VKKTSRKSLR LLGSVGEPIN PEAWRWYYDV VGDSRCPIVD TWWQTETGGI 430 440 450 460 470 480 LISPLAGAVD LKPGSATLPF FGVQPALVDA EGKILEGATE GNLVLLDSWP GQMRSVYGDH 490 500 510 520 530 540 QRFIDTYFRT YPGSYFTGDG CRRDADGYYW ITGRVDDVIN VSGHRIGTAE VESALVSHPK 550 560 570 580 590 600 VAEAAVVGFP HDVKGQGIYA YVTLIAGETP SDELHKELVS WVRKEIGPIA SPDHLQWAPG 610 620 630 640 LPKTRSGKIM RRILRKIAEN APDQLGDTST LADPSVVDSL VNERLTR

References

[1]

"Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of large numbers of effector genes and insertion sequences to its race diversity." Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H. Jpn. Agric. Res. Q. 39:275-287(2005) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MAFF 311018.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP008229 Genomic DNA. Translation: BAE71035.1.
RefSeq	YP_453309.1. NC_007705.1.
3D structure databases
ProteinModelPortal	Q2NXE2.
SMR	Q2NXE2. Positions 9-644.
ModBase	Search...
Protein-protein interaction databases
STRING	342109.XOO_4280.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAE71035; BAE71035; BAE71035.
GeneID	3859446.
KEGG	xom:XOO_4280.
PATRIC	24119017. VBIXanOry49434_4911.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0365.
HOGENOM	HOG000128470.
KO	K01895.
OMA	GHAGKPF.
ProtClustDB	PRK00174.
Family and domain databases
HAMAP	MF_01123. Ac_CoA_synth.
InterPro	IPR011904. Ac_CoA_lig. IPR024597. Acyl-CoA_synth_DUF3448. IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. IPR025110. DUF4009. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. PF11930. DUF3448. 1 hit. PF13193. DUF4009. 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_XANOM

Accession

Primary (citable) accession number: Q2NXE2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 7, 2006
Last modified:	May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program