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A6WXV8

- ACSA_OCHA4

UniProt

A6WXV8 - ACSA_OCHA4

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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / NCTC 12168)
Status
Reviewed - Annotation score: 3 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.UniRule annotation

Catalytic activityi

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

Cofactori

Magnesium.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei311 – 3111Coenzyme AUniRule annotation
Binding sitei335 – 3351Coenzyme AUniRule annotation
Binding sitei500 – 5001ATPUniRule annotation
Binding sitei515 – 5151ATPUniRule annotation
Binding sitei523 – 5231Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei526 – 5261ATPUniRule annotation
Metal bindingi537 – 5371Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi539 – 5391Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi542 – 5421Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei586 – 5861Coenzyme AUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi387 – 3893ATPUniRule annotation
Nucleotide bindingi411 – 4166ATPUniRule annotation

GO - Molecular functioni

  1. acetate-CoA ligase activity Source: UniProtKB-HAMAP
  2. AMP binding Source: InterPro
  3. ATP binding Source: UniProtKB-KW
  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 synthetaseUniRule annotation (EC:6.2.1.1UniRule annotation)
Short name:
AcCoA synthetaseUniRule annotation
Short name:
AcsUniRule annotation
Alternative name(s):
Acetate--CoA ligaseUniRule annotation
Acyl-activating enzymeUniRule annotation
Gene namesi
Name:acsAUniRule annotation
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 synthetasePRO_1000065300Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei611 – 6111N6-acetyllysineUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Interactioni

Protein-protein interaction databases

STRINGi439375.Oant_1092.

Structurei

3D structure databases

ProteinModelPortaliA6WXV8.
SMRiA6WXV8. Positions 17-648.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni189 – 1924Coenzyme A bindingUniRule annotation

Sequence similaritiesi

Belongs to the ATP-dependent AMP-binding enzyme family.UniRule annotation

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

        10         20         30         40         50
MSEKLYPVLA EAKRNTLIDN ATYLEWYQES VSDPDSFWAK HGRRIDWFKP
60 70 80 90 100
FTKVKNTDFN GDVSIKWYED GVTNVSYNCI DRHLKSRGDQ VAIIWEGDNP
110 120 130 140 150
YIDKKITYRE LHENVCRLAN VLKKHGVKKG DRVTIYLPMI PEAAYAMLAC
160 170 180 190 200
ARIGAVHSVV FAGFSPEALA GRIVDCESTF VITADEGVRG GKPVPLKENT
210 220 230 240 250
DTAIDIAAKQ YVMVNKVLTV RRTGGKVSWG PGRDLWYHQE VASVEPTCDP
260 270 280 290 300
EPMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYASMTHQ YVFDYHDGDI
310 320 330 340 350
YWCTADVGWV TGHSYIVYGP LANGATTLMF EGVPNFPDQG RFWEVVDKHH
360 370 380 390 400
VNIFYTAPTA IRALMGAGDE FVTRSSRSTL RLLGSVGEPI NPEAWEWYYN
410 420 430 440 450
VVGDQRSPIV DTWWQTETGG ILITPLPGAT DLKPGSATRP FFGIKPELVD
460 470 480 490 500
NEGAVIEGAV DGNLCIIDSW PGQMRTLYGD HKRFIEAYFS TYKGKYFTGD
510 520 530 540 550
GCRRDEDGYY WITGRVDDVL NISGHRLGTA EIESALVSHH SVSEAAVVGY
560 570 580 590 600
PHPIKGQGIY CYVTLMTGEA VQDEDALRKE LTQHVRKEIG PIATPDKIQF
610 620 630 640 650
SPGLPKTRSG KIMRRILRKI AEDEFGALGD TSTLADPGVV DDLIENRQNK

K
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.
RefSeqiYP_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 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: October 29, 2014
This is version 50 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3