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Protein

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

Gene

btuR

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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.

Catalytic activityi

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

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi36 – 427ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cob(I)yrinic acid a,c-diamide adenosyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. cobalamin biosynthetic process Source: UniProtKB-UniPathway
  2. porphyrin-containing compound biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Cobalamin biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13220.
SENT99287:GCTI-1727-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:STM1718
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 196196Cob(I)yrinic acid a,c-diamide adenosyltransferasePRO_0000065010Add
BLAST

Proteomic databases

PaxDbiP31570.
PRIDEiP31570.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi99287.STM1718.

Structurei

Secondary structure

1
196
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2317Combined sources
Beta strandi31 – 399Combined sources
Helixi41 – 5414Combined sources
Beta strandi59 – 657Combined sources
Helixi72 – 776Combined sources
Helixi78 – 803Combined sources
Beta strandi83 – 864Combined sources
Helixi95 – 973Combined sources
Helixi98 – 11518Combined sources
Beta strandi122 – 1276Combined sources
Helixi129 – 1346Combined sources
Helixi140 – 1489Combined sources
Beta strandi155 – 1595Combined sources
Helixi165 – 1706Combined sources
Beta strandi172 – 1765Combined sources
Helixi183 – 1864Combined sources
Turni192 – 1943Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G5RX-ray2.10A1-196[»]
1G5TX-ray1.80A1-196[»]
1G64X-ray2.10A/B1-196[»]
4HUTX-ray1.95A/B6-196[»]
ProteinModelPortaliP31570.
SMRiP31570. Positions 7-196.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31570.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2109.
HOGENOMiHOG000260311.
KOiK00798.
OMAiMTLVKHP.
OrthoDBiEOG6GN76J.
PhylomeDBiP31570.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003724. AdoCbl_synth_CblAdoTrfase_CobA.
IPR025826. Co_AT_N_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF12557. Co_AT_N. 1 hit.
PF02572. CobA_CobO_BtuR. 1 hit.
[Graphical view]
PIRSFiPIRSF015617. Adensltrnsf_CobA. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00708. cobA. 1 hit.

Sequencei

Sequence statusi: Complete.

P31570-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDERYQQRQ QKVKDRVDAR VAQAQEERGI IIVFTGNGKG KTTAAFGTAA
60 70 80 90 100
RAVGHGKNVG VVQFIKGTWP NGERNLLEPH GVEFQVMATG FTWETQNREA
110 120 130 140 150
DTAACMAVWQ HGKRMLADPL LDMVVLDELT YMVAYDYLPL EEVISALNAR
160 170 180 190
PGHQTVIITG RGCHRDILDL ADTVSELRPV KHAFDAGVKA QMGIDY
Length:196
Mass (Da):21,726
Last modified:July 1, 1993 - v1
Checksum:iAE02E11176513CC4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08890 Unassigned DNA. Translation: AAA71929.1.
AE006468 Genomic DNA. Translation: AAL20636.1.
PIRiJN0721.
RefSeqiNP_460677.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20636; AAL20636; STM1718.
GeneIDi1253237.
KEGGistm:STM1718.
PATRICi32381951. VBISalEnt20916_1815.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08890 Unassigned DNA. Translation: AAA71929.1.
AE006468 Genomic DNA. Translation: AAL20636.1.
PIRiJN0721.
RefSeqiNP_460677.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G5RX-ray2.10A1-196[»]
1G5TX-ray1.80A1-196[»]
1G64X-ray2.10A/B1-196[»]
4HUTX-ray1.95A/B6-196[»]
ProteinModelPortaliP31570.
SMRiP31570. Positions 7-196.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM1718.

Proteomic databases

PaxDbiP31570.
PRIDEiP31570.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL20636; AAL20636; STM1718.
GeneIDi1253237.
KEGGistm:STM1718.
PATRICi32381951. VBISalEnt20916_1815.

Phylogenomic databases

eggNOGiCOG2109.
HOGENOMiHOG000260311.
KOiK00798.
OMAiMTLVKHP.
OrthoDBiEOG6GN76J.
PhylomeDBiP31570.

Enzyme and pathway databases

UniPathwayiUPA00148; UER00233.
BioCyciMetaCyc:MONOMER-13220.
SENT99287:GCTI-1727-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP31570.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003724. AdoCbl_synth_CblAdoTrfase_CobA.
IPR025826. Co_AT_N_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF12557. Co_AT_N. 1 hit.
PF02572. CobA_CobO_BtuR. 1 hit.
[Graphical view]
PIRSFiPIRSF015617. Adensltrnsf_CobA. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00708. cobA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, sequencing and overexpression of cobA which encodes ATP:corrinoid adenosyltransferase in Salmonella typhimurium."
    Suh S.-J., Escalante-Semerena J.C.
    Gene 129:93-97(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: LT2.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  3. "Purification and initial characterization of the ATP:corrinoid adenosyltransferase encoded by the cobA gene of Salmonella typhimurium."
    Suh S.-J., Escalante-Semerena J.C.
    J. Bacteriol. 177:921-925(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-21, CHARACTERIZATION.
  4. "cobA function is required for both de novo cobalamin biosynthesis and assimilation of exogenous corrinoids in Salmonella typhimurium."
    Escalante-Semerena J.C., Suh S.-J., Roth J.R.
    J. Bacteriol. 172:273-280(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. "The ATP:Co(I)rrinoid adenosyltransferase (CobA) enzyme of Salmonella enterica requires the 2'-OH group of ATP for function and yields inorganic triphosphate as its reaction byproduct."
    Fonseca M.V., Buan N.R., Horswill A.R., Rayment I., Escalante-Semerena J.C.
    J. Biol. Chem. 277:33127-33131(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "Three-dimensional structure of ATP:corrinoid adenosyltransferase from Salmonella typhimurium in its free state, complexed with MgATP, or complexed with hydroxycobalamin and MgATP."
    Bauer C.B., Fonseca M.V., Holden H.M., Thoden J.B., Thompson T.B., Escalante-Semerena J.C., Rayment I.
    Biochemistry 40:361-374(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 27-183.

Entry informationi

Entry nameiBTUR_SALTY
AccessioniPrimary (citable) accession number: P31570
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: January 7, 2015
This is version 109 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.