P27095 (ACSA_METSO) 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
Synonyms:	acs

Organism

Methanothrix soehngenii

Taxonomic identifier

2223 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosaetaceae › Methanosaeta

Protein attributes

Sequence length	672 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP MF_01123
Subunit structure	Homodimer.
Post-translational modification	The N-terminus is blocked. HAMAP MF_01123 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
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 – 672	672	Acetyl-coenzyme A synthetase HAMAP MF_01123		PRO_0000208401
Sites
	Active site	546	1	By similarity
Amino acid modifications
	Modified residue	638	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P27095 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: D3CB6AC88BAEAF65	FASTA	672	75,527
	10 20 30 40 50 60 MLKLAGKEDK KLKTTVFQDE TRIFNPPKEL VEKSIVMQWM KKKGFKTEKE MRAWCSSDEH 70 80 90 100 110 120 YLEFWDEMAK TYVDWHKPYT KVMDDSEMPY FHWFTGGEIN ITYNAVDRHA KGAKKDKVAY 130 140 150 160 170 180 IWIPEPTDQP VQKITYGDLY KEVNKFANGL KSLGLKKGDR VSIYMPMIPQ LPIAMLACAK 190 200 210 220 230 240 LGVSHIVVFS GFSSKGLMDR AAHCGSRAII TVDGFYRRGK PVPLKPNADE AAGGAPSVEK 250 260 270 280 290 300 IIVYKRAGVD VSMKEGRDVW WHDLVKGQSE ECEPVWVDPE HRLYILYTSG TTGKPKGIEH 310 320 330 340 350 360 ATGGNAVGPA QTLHWVFDLK DDDVWWCTAD IGWVTGHSYI VYAPLILGMT SLMYEGAADY 370 380 390 400 410 420 PDFGRWWKNI QDHKVTVLYT APTAVRMFMK QGAEWPDKYD LSSLRLLGSV GEPINPEAWM 430 440 450 460 470 480 WYREHIGRGE LQIMDTWWQT ETGTFLNSPL PITPLKPGSC TFPLPGYDIS ILDEEGNEVP 490 500 510 520 530 540 LGSGGNIVAL KPYPSMLRAF WGDKERFMKE YWQFYWDVPG RRGVYLAGDK AQRDKDGYFF 550 560 570 580 590 600 IQGRIDDVLS VAGHRIANAE VESALVAHPK IAEAAVVGKP DEVKGESIVA FVILRVGNEP 610 620 630 640 650 660 SPELAKDAIA FVRKTLGPVA APTEVHFVND LPKTRSGKIM RRVVKARALG NPVGDISTLM 670 NPEAVDGIPK IV

References

[1]	"Cloning, sequence analysis, and functional expression of the acetyl coenzyme A synthetase gene from Methanothrix soehngenii in Escherichia coli." Eggen R.I.L., Geerling A.C.M., Boshoven A.B.P., de Vos W.M. J. Bacteriol. 173:6383-6389(1991) [PubMed: 1680850] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Opfikon / DSM 2139.
[2]	"Isolation and characterization of acetyl-coenzyme A synthetase from Methanothrix soehngenii." Jetten M.S., Stams A.J., Zehnder A.J. J. Bacteriol. 171:5430-5435(1989) [PubMed: 2571608] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M63968 Genomic DNA. Translation: AAA73007.1.
PIR	A41043.
3D structure databases
ProteinModelPortal	P27095.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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]
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_METSO

Accession

Primary (citable) accession number: P27095

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	October 19, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program