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Protein

Cob(I)yrinic acid a,c-diamide adenosyltransferase

Gene

btuR

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Required for both de novo synthesis of the corrin ring for the assimilation of exogenous corrinoids. Participates in the adenosylation of a variety of incomplete and complete corrinoids (By similarity).By similarity

Catalytic activityi

ATP + cob(I)yrinic acid a,c-diamide = triphosphate + adenosylcob(III)yrinic acid a,c-diamide.
ATP + cobinamide = triphosphate + adenosylcobinamide.

Pathwayi: adenosylcobalamin biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes adenosylcobalamin from cob(II)yrinate a,c-diamide.
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Cob(I)yrinic acid a,c-diamide adenosyltransferase (btuR)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. Bifunctional adenosylcobalamin biosynthesis protein CobU (cobU)
  6. Bifunctional adenosylcobalamin biosynthesis protein CobU (cobU)
  7. Adenosylcobinamide-GDP ribazoletransferase (cobS)
This subpathway is part of the pathway adenosylcobalamin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes adenosylcobalamin from cob(II)yrinate a,c-diamide, the pathway adenosylcobalamin biosynthesis and in Cofactor biosynthesis.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi36 – 42ATPBy similarity7

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cob(I)yrinic acid a,c-diamide adenosyltransferase activity Source: EcoCyc

GO - Biological processi

  • aerobic cobalamin biosynthetic process Source: EcoCyc
  • cobalamin biosynthetic process Source: EcoCyc
  • porphyrin-containing compound biosynthetic process Source: UniProtKB-KW

Keywordsi

Molecular functionTransferase
Biological processCobalamin biosynthesis, Porphyrin biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:COBALADENOSYLTRANS-MONOMER
UniPathwayiUPA00148; UER00233

Names & Taxonomyi

Protein namesi
Recommended name:
Cob(I)yrinic acid a,c-diamide adenosyltransferase (EC:2.5.1.17)
Alternative name(s):
Cob(I)alamin adenosyltransferase
Corrinoid adenosyltransferase
Gene namesi
Name:btuR
Synonyms:cobA
Ordered Locus Names:b1270, JW1262
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10130 btuR

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000650091 – 196Cob(I)yrinic acid a,c-diamide adenosyltransferaseAdd BLAST196

Proteomic databases

EPDiP0A9H5
PaxDbiP0A9H5
PRIDEiP0A9H5

Interactioni

Protein-protein interaction databases

BioGridi4259575, 12 interactors
IntActiP0A9H5, 14 interactors
STRINGi316385.ECDH10B_1385

Structurei

3D structure databases

ProteinModelPortaliP0A9H5
SMRiP0A9H5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG41068B1 Bacteria
COG2109 LUCA
HOGENOMiHOG000260311
InParanoidiP0A9H5
KOiK19221
OMAiLVTEMTL
PhylomeDBiP0A9H5

Family and domain databases

CDDicd00561 CobA_CobO_BtuR, 1 hit
InterProiView protein in InterPro
IPR003724 CblAdoTrfase_CobA
IPR025826 Co_AT_N_dom
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF12557 Co_AT_N, 1 hit
PF02572 CobA_CobO_BtuR, 1 hit
PIRSFiPIRSF015617 Adensltrnsf_CobA, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00708 cobA, 1 hit

Sequencei

Sequence statusi: Complete.

P0A9H5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDERYQQRQ QRVKEKVDAR VAQAQDERGI IIVFTGNGKG KTTAAFGTAT
60 70 80 90 100
RAVGHGKKVG VVQFIKGTWP NGERNLLEPH GVEFQVMATG FTWDTQNRES
110 120 130 140 150
DTAACREVWQ HAKRMLADSS LDMVLLDELT YMVAYDYLPL EEVVQALNER
160 170 180 190
PHQQTVIITG RGCHRDILEL ADTVSELRPV KHAFDAGVKA QIGIDY
Length:196
Mass (Da):21,999
Last modified:July 19, 2005 - v1
Checksum:i4EE2FDD9C74FE8AE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21528 Genomic DNA Translation: AAA23530.1
U00096 Genomic DNA Translation: AAC74352.1
AP009048 Genomic DNA Translation: BAA14807.1
PIRiA64875
RefSeqiNP_415786.1, NC_000913.3
WP_001278906.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC74352; AAC74352; b1270
BAA14807; BAA14807; BAA14807
GeneIDi945839
KEGGiecj:JW1262
eco:b1270
PATRICifig|1411691.4.peg.1014

Similar proteinsi

Entry informationi

Entry nameiBTUR_ECOLI
AccessioniPrimary (citable) accession number: P0A9H5
Secondary accession number(s): P13040
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: March 28, 2018
This is version 96 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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