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E7B6B6

- E7B6B6_YERE1

UniProt

E7B6B6 - E7B6B6_YERE1

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Protein

Acetyl-coenzyme A synthetase

Gene

acs

Organism
Yersinia enterocolitica subsp. palearctica serotype O:3 (strain DSM 13030 / CIP 106945 / Y11)
Status
Unreviewed - 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. Acs undergoes a two-step reaction. In the first half reaction, Acs 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
Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis.UniRule annotation

Catalytic activityi

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

Cofactori

Note: Magnesium.UniRule annotationSAAS annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei312 – 3121Coenzyme AUniRule annotation
Binding sitei336 – 3361Coenzyme AUniRule annotation
Binding sitei501 – 5011ATPUniRule annotation
Binding sitei516 – 5161ATPUniRule annotation
Binding sitei524 – 5241Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei527 – 5271ATPUniRule annotation
Metal bindingi538 – 5381Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi540 – 5401Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi543 – 5431Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei585 – 5851Coenzyme AUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi388 – 3903ATPUniRule annotation
Nucleotide bindingi412 – 4176ATPUniRule 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: UniProtKB-HAMAP
  2. chemotaxis Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotationImported

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation, Nucleotide-binding

Enzyme and pathway databases

BioCyciYENT930944:GLMU-3592-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:acsUniRule annotation
Ordered Locus Names:Y11_35151Imported
OrganismiYersinia enterocolitica subsp. palearctica serotype O:3 (strain DSM 13030 / CIP 106945 / Y11)Imported
Taxonomic identifieri930944 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
ProteomesiUP000008084: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei610 – 6101N6-acetyllysineUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliE7B6B6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni192 – 1954Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

KOiK01895.

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.

E7B6B6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMSQIHKHPI PTAIAEHALI NPEQYHQYYQ QSVQNPDEFW GEHGKIIDWI
60 70 80 90 100
KPYKTVKNTS FDPGHVSIRW FEDGTLNLAA NCLDRHLAER SDQTAIIWEG
110 120 130 140 150
DDPNQSKTVT YKQLHHDVCQ FANVLKKLGI KKGDVVAIYM PMVPEAAVAM
160 170 180 190 200
LACARIGAVH SVIFGGFSPD AVAGRIIDSN SKLVITADEG IRAGRAIPLK
210 220 230 240 250
KNVDEALKNP AITSIKNVVV FQRTGNASYW KDGRDVWWHD LIENASADCP
260 270 280 290 300
PEEMNAEDPL FILYTSGSTG KPKGVLHTTG GYLVYAALTF KYVFDYHPGD
310 320 330 340 350
IYWCTADVGW VTGHSYLLYG PLACGAITLM FEGVPNYPGV NRLGQVIDKH
360 370 380 390 400
QVNILYTAPT AIRALMAEGD KAIEDTKRTS LRIMGSVGEP INPEAWEWYY
410 420 430 440 450
NKIGNSKCPI VDTWWQTETG GFMITPLPGA TELKAGSATR PFFGVQPALV
460 470 480 490 500
DNLGNPQEGA AEGNLVITDS WPGQARTLFG DHDRFEQTYF STFKGMYFSG
510 520 530 540 550
DGARRDEDGY YWITGRVDDV LNVSGHRLGT AEIESALVSH PKIAEAAVVG
560 570 580 590 600
VPHNIKGQAI YAYITLNHGE EPTPELYTEV RNWVRKEIGP IATPDILHWT
610 620 630 640 650
DSLPKTRSGK IMRRILRKIA AGDTSNLGDT STLADPGVVD KLLEEKQSMQ

APS
Length:653
Mass (Da):72,214
Last modified:March 8, 2011 - v1
Checksum:i07271790E643740E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FR729477 Genomic DNA. Translation: CBY29015.1.
RefSeqiWP_014609328.1. NC_017564.1.
YP_006007014.1. NC_017564.1.

Genome annotation databases

EnsemblBacteriaiCBY29015; CBY29015; Y11_35151.
GeneIDi12602229.
KEGGiyey:Y11_35151.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FR729477 Genomic DNA. Translation: CBY29015.1 .
RefSeqi WP_014609328.1. NC_017564.1.
YP_006007014.1. NC_017564.1.

3D structure databases

ProteinModelPortali E7B6B6.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CBY29015 ; CBY29015 ; Y11_35151 .
GeneIDi 12602229.
KEGGi yey:Y11_35151.

Phylogenomic databases

KOi K01895.

Enzyme and pathway databases

BioCyci YENT930944:GLMU-3592-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

« Hide 'large scale' publications
  1. "Complete genome sequence of Y. enterocolitica subsp. palearctica serogroup O:3."
    Batzilla J., Hoeper D., Heesemann J., Rakin A.
    Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Y11.
  2. "Complete genome sequence of Yersinia enterocolitica subsp. palearctica serogroup O:3."
    Batzilla J., Hoper D., Antonenka U., Heesemann J., Rakin A.
    J. Bacteriol. 193:2067-2067(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 13030 / CIP 106945 / Y11Imported.

Entry informationi

Entry nameiE7B6B6_YERE1
AccessioniPrimary (citable) accession number: E7B6B6
Entry historyi
Integrated into UniProtKB/TrEMBL: March 8, 2011
Last sequence update: March 8, 2011
Last modified: November 26, 2014
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3