SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A6WXV8

- ACSA_OCHA4

UniProt

A6WXV8 - ACSA_OCHA4

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Acetyl-coenzyme A synthetase
Gene
acsA, Oant_1092
Organism
Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / NCTC 12168)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.UniRule annotation

Cofactori

Magnesium By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei311 – 3111Coenzyme A By similarity
Binding sitei335 – 3351Coenzyme A By similarity
Binding sitei387 – 3871Substrate; via amide nitrogen By similarity
Binding sitei500 – 5001Substrate By similarity
Binding sitei515 – 5151Substrate By similarity
Active sitei517 – 5171 By similarity
Binding sitei523 – 5231Coenzyme A By similarity
Binding sitei526 – 5261Substrate By similarity
Metal bindingi537 – 5371Magnesium; via carbonyl oxygen By similarity
Metal bindingi539 – 5391Magnesium; via carbonyl oxygen By similarity
Metal bindingi542 – 5421Magnesium; via carbonyl oxygen By similarity
Binding sitei586 – 5861Coenzyme A

GO - Molecular functioni

  1. AMP binding Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. acetate-CoA ligase activity Source: UniProtKB-HAMAP
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. acetyl-CoA biosynthetic process from acetate Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciOANT439375:GJIT-1108-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A synthetase (EC:6.2.1.1)
Short name:
AcCoA synthetase
Short name:
Acs
Alternative name(s):
Acetate--CoA ligase
Acyl-activating enzyme
Gene namesi
Name:acsA
Ordered Locus Names:Oant_1092
OrganismiOchrobactrum anthropi (strain ATCC 49188 / DSM 6882 / NCTC 12168)
Taxonomic identifieri439375 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeOchrobactrum
ProteomesiUP000002301: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 651651Acetyl-coenzyme A synthetaseUniRule annotation
PRO_1000065300Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei611 – 6111N6-acetyllysine By similarity

Post-translational modificationi

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity.UniRule annotation

Keywords - PTMi

Acetylation

Interactioni

Protein-protein interaction databases

STRINGi439375.Oant_1092.

Structurei

3D structure databases

ProteinModelPortaliA6WXV8.
SMRiA6WXV8. Positions 17-648.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni411 – 4166Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiAWIWYRD.
OrthoDBiEOG68WR2H.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth.
InterProiIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A6WXV8-1 [UniParc]FASTAAdd to Basket

« Hide

MSEKLYPVLA EAKRNTLIDN ATYLEWYQES VSDPDSFWAK HGRRIDWFKP    50
FTKVKNTDFN GDVSIKWYED GVTNVSYNCI DRHLKSRGDQ VAIIWEGDNP 100
YIDKKITYRE LHENVCRLAN VLKKHGVKKG DRVTIYLPMI PEAAYAMLAC 150
ARIGAVHSVV FAGFSPEALA GRIVDCESTF VITADEGVRG GKPVPLKENT 200
DTAIDIAAKQ YVMVNKVLTV RRTGGKVSWG PGRDLWYHQE VASVEPTCDP 250
EPMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYASMTHQ YVFDYHDGDI 300
YWCTADVGWV TGHSYIVYGP LANGATTLMF EGVPNFPDQG RFWEVVDKHH 350
VNIFYTAPTA IRALMGAGDE FVTRSSRSTL RLLGSVGEPI NPEAWEWYYN 400
VVGDQRSPIV DTWWQTETGG ILITPLPGAT DLKPGSATRP FFGIKPELVD 450
NEGAVIEGAV DGNLCIIDSW PGQMRTLYGD HKRFIEAYFS TYKGKYFTGD 500
GCRRDEDGYY WITGRVDDVL NISGHRLGTA EIESALVSHH SVSEAAVVGY 550
PHPIKGQGIY CYVTLMTGEA VQDEDALRKE LTQHVRKEIG PIATPDKIQF 600
SPGLPKTRSG KIMRRILRKI AEDEFGALGD TSTLADPGVV DDLIENRQNK 650
K 651
Length:651
Mass (Da):72,591
Last modified:August 21, 2007 - v1
Checksum:i6B8B09BA21A762B7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000758 Genomic DNA. Translation: ABS13812.1.
RefSeqiWP_010661479.1. NC_009667.1.
YP_001369641.1. NC_009667.1.

Genome annotation databases

EnsemblBacteriaiABS13812; ABS13812; Oant_1092.
GeneIDi5380140.
KEGGioan:Oant_1092.
PATRICi20467255. VBIOchAnt73124_1142.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000758 Genomic DNA. Translation: ABS13812.1 .
RefSeqi WP_010661479.1. NC_009667.1.
YP_001369641.1. NC_009667.1.

3D structure databases

ProteinModelPortali A6WXV8.
SMRi A6WXV8. Positions 17-648.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 439375.Oant_1092.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABS13812 ; ABS13812 ; Oant_1092 .
GeneIDi 5380140.
KEGGi oan:Oant_1092.
PATRICi 20467255. VBIOchAnt73124_1142.

Phylogenomic databases

eggNOGi COG0365.
HOGENOMi HOG000229981.
KOi K01895.
OMAi AWIWYRD.
OrthoDBi EOG68WR2H.

Enzyme and pathway databases

BioCyci OANT439375:GJIT-1108-MONOMER.

Family and domain databases

HAMAPi MF_01123. Ac_CoA_synth.
InterProi IPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiACSA_OCHA4
AccessioniPrimary (citable) accession number: A6WXV8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: August 21, 2007
Last modified: September 3, 2014
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi