Reviewed, UniProtKB/Swiss-Prot Q0AAW0 (ACSA_ALHEH)

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:	Mlg_0673

Organism

Alkalilimnicola ehrlichei (strain MLHE-1) [Complete proteome] [HAMAP]

Taxonomic identifier

187272 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Ectothiorhodospiraceae › Alkalilimnicola

Protein attributes

Sequence length	645 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)
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 – 645	645	Acetyl-coenzyme A synthetase HAMAP MF_01123		PRO_1000065268
Sites
	Active site	514	1	By similarity
Amino acid modifications
	Modified residue	606	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0AAW0-1 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: C56D61DCD4C81904	FASTA	645	71,429
	10 20 30 40 50 60 MSDTKVYPVP DYIREKAHIT KDTYEEMYRR SLDDPEGFWG EQAEKFLDWF SKWDKVYHSD 70 80 90 100 110 120 LKNGEIRFFE GGKLNVAHNC LDRHLEQRGD QTAIIWEGDD PNNSEHITYK DLHERVCRLA 130 140 150 160 170 180 NAMKARGVKK GDRVCIYLPM IPEAAVAMLA CARIGAIHSI VFGGFSPDAL KDRIQNADCE 190 200 210 220 230 240 TVITADEGVR GGRNVALKSN ADKALESCPD VKNVFVVKRT GGDIDWKEGR DIWYHEAVAD 250 260 270 280 290 300 VSADCPAEEL DAEDPLFILY TSGSTGKPKG VQHCSAGYLL GAAMTHKYVF DYQEGEVYWC 310 320 330 340 350 360 TADVGWVTGH SYIVYGPLAN GATTLMFEGV PTYPSAARCW EVVDKHNVSI FYTAPTAIRA 370 380 390 400 410 420 LMGQGNEHVT KTSRKSLRIL GTVGEPINPE AWEWYYNVVG DGRCPIVDTW WQTETGSILI 430 440 450 460 470 480 APLPGATDLK PGSATLPFFG VEPALVDPEG KELEGAASGN LVIKRAWPSM MRTVYGDHKR 490 500 510 520 530 540 FMETYLAAYP GMYFTGDGAR RDEDGYYWIT GRVDDVINVS GHRMGTAEVE SALVLHDAVA 550 560 570 580 590 600 EAAVVGYPHD IKGQGIYAYV TLMAGVEPSD ELKKELVKLV SNEIGPIAKP DVIQWAPGLP 610 620 630 640 KTRSGKIMRR ILRKVAANEL DSLGDTSTLA DPTVVDNLIE DRPNK

References

[1]

"Complete sequence of Alkalilimnicola ehrilichei MLHE-1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000453 Genomic DNA. Translation: ABI56027.1.
RefSeq	YP_741517.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q0AAW0.
Genome annotation databases
GeneID	4268468.
GenomeReviews	Gene locus Mlg_0673 in contig CP000453_GR.
KEGG	aeh:Mlg_0673.
NMPDR	fig|187272.6.peg.645.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0365.
HOGENOM	HBG547964.
OMA	HQRMVDT.
PhylomeDB	Q0AAW0.
Family and domain databases
HAMAP	MF_01123. Ac_CoA_synth. [Tree]
InterPro	IPR011904. Ac_CoA_lig_AcsA. IPR020845. AMP-binding_CS. 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_ALHEH

Accession

Primary (citable) accession number: Q0AAW0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 17, 2006
Last modified:	February 9, 2010
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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