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E1RZ77

- E1RZ77_ECOUM

UniProt

E1RZ77 - E1RZ77_ECOUM

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Protein

Acetyl-coenzyme A synthetase

Gene

acs

Organism
Escherichia coli (strain UM146)
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 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 sitei584 – 5841Coenzyme 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: 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

BioCyciECOL869729:GI9Z-4103-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:UM146_20540Imported
OrganismiEscherichia coli (strain UM146)Imported
Taxonomic identifieri869729 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000006682: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei609 – 6091N6-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

ProteinModelPortaliE1RZ77.
SMRiE1RZ77. Positions 5-647.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni191 – 1944Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000229981.
KOiK01895.
OMAiAWIWYRD.

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.

E1RZ77-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSQIHKHTIP ANIADRCLIN PQQYEAMYQQ SINAPDTFWG EQGKILDWIT
60 70 80 90 100
PYQKVKNTSF APGNVSIKWY EDGTLNLAAN CLDRHLQENG DRTAIIWEGD
110 120 130 140 150
DASQSKHISY KELHRDVCRF ANTLLELGIK KGDVVAIYMP MVPEAAVAML
160 170 180 190 200
ACARIGAVHS VIFGGFSPEA VAGRIIDSSS RLVITSDEGV RAGRSIPLKK
210 220 230 240 250
NVDDALKNPN VTSVEHVVVL KRTGGKIDWQ EGRDLWWHDL VEQASDQHQA
260 270 280 290 300
EEMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAALTFK YVFDYHPGDI
310 320 330 340 350
YWCTADVGWV TGHSYLLYGP LACGATTLMF EGVPNWPTPA RMAQVVDKHQ
360 370 380 390 400
VNILYTAPTA IRALMAEGDK AIEGTDRSSL RILGSVGEPI NPEAWEWYWK
410 420 430 440 450
KIGNEKCPVV DTWWQTETGG FMITPLPGAT ELKAGSATRP FFGVQPALVD
460 470 480 490 500
NEGNPLEGAT EGSLVITDSW PGQARTLFGD HERFEQTYFS TFKNMYFSGD
510 520 530 540 550
GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVAHP KIAEAAVVGI
560 570 580 590 600
PHNIKGQAIY AYVTLNHGEE PSPELYAEVR NWVRKEIGPL ATPDVLHWTD
610 620 630 640 650
SLPKTRSGKI MRRILRKIAA GDTSNLGDTS TLADPGVVEK LLEEKQAIAM

PS
Length:652
Mass (Da):72,011
Last modified:November 30, 2010 - v1
Checksum:i3332DC71328CE507
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002167 Genomic DNA. Translation: ADN73438.1.
RefSeqiYP_006112950.1. NC_017632.1.

Genome annotation databases

EnsemblBacteriaiADN73438; ADN73438; UM146_20540.
GeneIDi12702614.
KEGGielu:UM146_20540.
PATRICi42975248. VBIEscCol167775_4412.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002167 Genomic DNA. Translation: ADN73438.1 .
RefSeqi YP_006112950.1. NC_017632.1.

3D structure databases

ProteinModelPortali E1RZ77.
SMRi E1RZ77. Positions 5-647.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADN73438 ; ADN73438 ; UM146_20540 .
GeneIDi 12702614.
KEGGi elu:UM146_20540.
PATRICi 42975248. VBIEscCol167775_4412.

Phylogenomic databases

HOGENOMi HOG000229981.
KOi K01895.
OMAi AWIWYRD.

Enzyme and pathway databases

BioCyci ECOL869729:GI9Z-4103-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 adherent invasive Escherichia coli UM146 isolated from ileal Crohn's disease biopsy tissue."
    Krause D.O., Little A.C., Dowd S.E., Bernstein C.N.
    Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: UM146.
  2. "Complete genome sequence of adherent invasive Escherichia coli UM146 isolated from ileal Crohn's disease biopsy tissue."
    Krause D.O., Little A.C., Dowd S.E., Bernstein C.N.
    J. Bacteriol. 193:583-583(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: UM146Imported.

Entry informationi

Entry nameiE1RZ77_ECOUM
AccessioniPrimary (citable) accession number: E1RZ77
Entry historyi
Integrated into UniProtKB/TrEMBL: November 30, 2010
Last sequence update: November 30, 2010
Last modified: November 26, 2014
This is version 29 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