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Q05603 (COBT_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase

Short name=NN:DBI PRT
EC=2.4.2.21
Alternative name(s):
N(1)-alpha-phosphoribosyltransferase
Gene names
Name:cobT
Ordered Locus Names:STM2016
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB). HAMAP-Rule MF_00230

Catalytic activity

Beta-nicotinate D-ribonucleotide + 5,6-dimethylbenzimidazole = nicotinate + alpha-ribazole 5'-phosphate. HAMAP-Rule MF_00230

Pathway

Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-ribazole from 5,6-dimethylbenzimidazole: step 1/2. HAMAP-Rule MF_00230

Subunit structure

Homodimer.

Sequence similarities

Belongs to the CobT family.

Sequence caution

The sequence AAA27271.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAA69297.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 356356Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase HAMAP-Rule MF_00230
PRO_0000167069

Sites

Active site3171Proton acceptor

Amino acid modifications

Disulfide bond160 ↔ 256 HAMAP-Rule MF_00230

Experimental info

Sequence conflict221A → T Ref.1
Sequence conflict221A → T Ref.3
Sequence conflict158 – 1592YT → CA Ref.1
Sequence conflict158 – 1592YT → CA Ref.3

Secondary structure

.......................................................... 356
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q05603 [UniParc].

Last modified January 23, 2002. Version 5.
Checksum: 3665FD3BB1B8A44C

FASTA35636,613
        10         20         30         40         50         60 
MQTLHALLRD IPAPDAEAMA RAQQHIDGLL KPPGSLGRLE TLAVQLAGMP GLNGTPQVGE 

        70         80         90        100        110        120 
KAVLVMCADH GVWDEGVAVS PKIVTAIQAA NMTRGTTGVC VLAAQAGAKV HVIDVGIDAE 

       130        140        150        160        170        180 
PIPGVVNMRV ARGCGNIAVG PAMSRLQAEA LLLEVSRYTC DLAQRGVTLF GVGELGMANT 

       190        200        210        220        230        240 
TPAAAMVSVF TGSDAKEVVG IGANLPPSRI DNKVDVVRRA IAINQPNPRD GIDVLSKVGG 

       250        260        270        280        290        300 
FDLVGMTGVM LGAARCGLPV LLDGFLSYSA ALAACQIAPA VRPYLIPSHF SAEKGARIAL 

       310        320        330        340        350 
AHLSMEPYLH MAMRLGEGSG AALAMPIVEA ACAMFHNMGE LAASNIVLPE GNANAT 

« Hide

References

« Hide 'large scale' references
[1]"The end of the cob operon: evidence that the last gene (cobT) catalyzes synthesis of the lower ligand of vitamin B12, dimethylbenzimidazole."
Chen P., Ailion M., Weyand N., Roth J.R.
J. Bacteriol. 177:1461-1469(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LT2.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"Characterization of the cobalamin (vitamin B12) biosynthetic genes of Salmonella typhimurium."
Roth J.R., Lawrence J.G., Rubenfield M., Kieffer-Higgins S., Church G.M.
J. Bacteriol. 175:3303-3316(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-242.
Strain: LT2.
[4]"The three-dimensional structures of nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase (CobT) from Salmonella typhimurium complexed with 5,6-dimethybenzimidazole and its reaction products determined to 1.9-A resolution."
Cheong C.-G., Escalante-Semerena J.C., Rayment I.
Biochemistry 38:16125-16135(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SEQUENCE REVISION TO 158.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L35477 Genomic DNA. Translation: AAA69297.1. Different initiation.
AE006468 Genomic DNA. Translation: AAL20920.1.
L12006 Genomic DNA. Translation: AAA27271.1. Different initiation.
RefSeqNP_460961.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D0SX-ray1.90A1-356[»]
1D0VX-ray1.90A1-356[»]
1JH8X-ray1.80A1-356[»]
1JHAX-ray2.00A1-356[»]
1JHMX-ray2.20A1-356[»]
1JHOX-ray2.00A1-356[»]
1JHPX-ray2.20A1-356[»]
1JHQX-ray2.00A1-356[»]
1JHRX-ray2.00A1-356[»]
1JHUX-ray2.00A1-356[»]
1JHVX-ray2.00A1-356[»]
1JHXX-ray2.00A1-356[»]
1JHYX-ray2.00A1-356[»]
1L4BX-ray1.70A1-356[»]
1L4EX-ray2.00A1-356[»]
1L4FX-ray2.10A1-356[»]
1L4GX-ray2.10A1-356[»]
1L4HX-ray2.10A1-356[»]
1L4KX-ray2.20A1-356[»]
1L4LX-ray2.00A1-356[»]
1L4MX-ray2.00A1-356[»]
1L4NX-ray2.00A1-356[»]
1L5FX-ray1.90A1-356[»]
1L5KX-ray2.00A1-356[»]
1L5LX-ray2.00A1-356[»]
1L5MX-ray2.00A1-356[»]
1L5NX-ray1.90A1-356[»]
1L5OX-ray1.60A1-356[»]
ProteinModelPortalQ05603.
SMRQ05603. Positions 3-350.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM2016.

Chemistry

DrugBankDB00173. Adenine.

Proteomic databases

PaxDbQ05603.
PRIDEQ05603.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL20920; AAL20920; STM2016.
GeneID1253537.
KEGGstm:STM2016.
PATRIC32382615. VBISalEnt20916_2138.

Phylogenomic databases

eggNOGCOG2038.
HOGENOMHOG000263499.
KOK00768.
OMAPAMSRSQ.
OrthoDBEOG6HF61K.
ProtClustDBPRK00105.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13214.
SENT99287:GCTI-2028-MONOMER.
UniPathwayUPA00061; UER00516.

Family and domain databases

Gene3D1.10.1610.10. 1 hit.
HAMAPMF_00230. CobT.
InterProIPR003200. Nict_dMeBzImd_PRibTrfase-like.
IPR023195. Nict_dMeBzImd_PRibTrfase_N.
IPR017846. Nict_dMeBzImd_PRibTrfase_pro.
[Graphical view]
PfamPF02277. DBI_PRT. 1 hit.
[Graphical view]
SUPFAMSSF52733. SSF52733. 1 hit.
TIGRFAMsTIGR03160. cobT_DBIPRT. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ05603.

Entry information

Entry nameCOBT_SALTY
AccessionPrimary (citable) accession number: Q05603
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2002
Last modified: April 16, 2014
This is version 118 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways