Acetyl-coenzyme A synthetase - Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / NCTC 12168)

Preferred order of sections

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:	Oant_1092

Organism

Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / NCTC 12168) [Complete proteome] [HAMAP]

Taxonomic identifier

439375 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Ochrobactrum ›

Protein attributes

Sequence length	651 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 – 651

651

Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123

PRO_1000065300

Regions

Region

411 – 416

6

Substrate binding By similarity

Sites

Active site

517

1

By similarity

Metal binding

537

1

Magnesium; via carbonyl oxygen By similarity

Metal binding

539

1

Magnesium; via carbonyl oxygen By similarity

Metal binding

542

1

Magnesium; via carbonyl oxygen By similarity

Binding site

311

1

Coenzyme A By similarity

Binding site

335

1

Coenzyme A By similarity

Binding site

387

1

Substrate; via amide nitrogen By similarity

Binding site

500

1

Substrate By similarity

Binding site

515

1

Substrate By similarity

Binding site

523

1

Coenzyme A By similarity

Binding site

526

1

Substrate By similarity

Binding site

586

1

Coenzyme A

Amino acid modifications

Modified residue

611

1

N6-acetyllysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

A6WXV8 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 6B8B09BA21A762B7
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FASTA

651

72,591

        10         20         30         40         50         60 
MSEKLYPVLA EAKRNTLIDN ATYLEWYQES VSDPDSFWAK HGRRIDWFKP FTKVKNTDFN 

        70         80         90        100        110        120 
GDVSIKWYED GVTNVSYNCI DRHLKSRGDQ VAIIWEGDNP YIDKKITYRE LHENVCRLAN 

       130        140        150        160        170        180 
VLKKHGVKKG DRVTIYLPMI PEAAYAMLAC ARIGAVHSVV FAGFSPEALA GRIVDCESTF 

       190        200        210        220        230        240 
VITADEGVRG GKPVPLKENT DTAIDIAAKQ YVMVNKVLTV RRTGGKVSWG PGRDLWYHQE 

       250        260        270        280        290        300 
VASVEPTCDP EPMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYASMTHQ YVFDYHDGDI 

       310        320        330        340        350        360 
YWCTADVGWV TGHSYIVYGP LANGATTLMF EGVPNFPDQG RFWEVVDKHH VNIFYTAPTA 

       370        380        390        400        410        420 
IRALMGAGDE FVTRSSRSTL RLLGSVGEPI NPEAWEWYYN VVGDQRSPIV DTWWQTETGG 

       430        440        450        460        470        480 
ILITPLPGAT DLKPGSATRP FFGIKPELVD NEGAVIEGAV DGNLCIIDSW PGQMRTLYGD 

       490        500        510        520        530        540 
HKRFIEAYFS TYKGKYFTGD GCRRDEDGYY WITGRVDDVL NISGHRLGTA EIESALVSHH 

       550        560        570        580        590        600 
SVSEAAVVGY PHPIKGQGIY CYVTLMTGEA VQDEDALRKE LTQHVRKEIG PIATPDKIQF 

       610        620        630        640        650 
SPGLPKTRSG KIMRRILRKI AEDEFGALGD TSTLADPGVV DDLIENRQNK K

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References

[1]

"Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic pathogen and symbiont of several eukaryotic hosts."
Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M., Ugalde R.A., Garcia E., Tolmasky M.E.
J. Bacteriol. 193:4274-4275(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49188 / DSM 6882 / NCTC 12168.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000758 Genomic DNA. Translation: ABS13812.1.
RefSeq	YP_001369641.1. NC_009667.1.
3D structure databases
ProteinModelPortal	A6WXV8.
SMR	A6WXV8. Positions 17-648.
ModBase	Search...
Protein-protein interaction databases
STRING	439375.Oant_1092.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABS13812; ABS13812; Oant_1092.
GeneID	5380140.
KEGG	oan:Oant_1092.
PATRIC	20467255. VBIOchAnt73124_1142.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0365.
HOGENOM	HOG000229981.
KO	K01895.
OMA	AISKHEM.
ProtClustDB	PRK00174.
Enzyme and pathway databases
BioCyc	OANT439375:GJIT-1108-MONOMER.
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_OCHA4

Accession

Primary (citable) accession number: A6WXV8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	August 21, 2007
Last modified:	May 1, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents