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Q05599 (COBU_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Bifunctional adenosylcobalamin biosynthesis protein CobU
Alternative name(s):
Adenosylcobinamide kinase
EC=2.7.1.156
Adenosylcobinamide-phosphate guanylyltransferase
EC=2.7.7.62
Gene names
Name:cobU
Ordered Locus Names:STM2018
OrganismSalmonella typhimurium
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length181 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.

Catalytic activity

ATP or GTP + adenosylcobinamide = adenosylcobinamide phosphate + ADP or GDP.

GTP + adenosylcobinamide phosphate = diphosphate + adenosylcobinamide-GDP.

Pathway

Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.

Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 6/7.

Subunit structure

Homotrimer. Ref.3

Sequence caution

The sequence AAA27269.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 181181Bifunctional adenosylcobalamin biosynthesis protein CobU
PRO_0000089998

Regions

Nucleotide binding7 – 148GTP
Nucleotide binding31 – 333GTP
Nucleotide binding48 – 514GTP

Sites

Active site471GMP-histidine intermediate Ref.4
Binding site591GTP
Binding site811GTP; via carbonyl oxygen

Secondary structure

........................... 181
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q05599 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: F6F89892C6BEE091

FASTA18119,902
        10         20         30         40         50         60 
MMILVTGGAR SGKSRHAEAL IGDAPQVLYI ATSQILDDEM AARIQHHKDG RPAHWRTAEC 

        70         80         90        100        110        120 
WRHLDTLITA DLAPDDAILL ECITTMVTNL LFALGGENDP EQWDYAAMER AIDDEIQILI 

       130        140        150        160        170        180 
AACQRCPAKV VLVTNEVGMG IVPENRLARH FRDIAGRVNQ RLAAAADEVW LVVSGIGVKI 


K 

« Hide

References

« Hide 'large scale' references
[1]"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: 8501034] [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: 11677609] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"Three-dimensional structure of adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase from Salmonella typhimurium determined to 2.3-A resolution."
Thompson T.B., Thomas M.G., Escalante-Semerena J.C., Rayment I.
Biochemistry 37:7686-7695(1998) [PubMed: 9601028] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), SUBUNIT.
Strain: LT2.
[4]"Three-dimensional structure of adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase (CobU) complexed with GMP: evidence for a substrate-induced transferase active site."
Thompson T.B., Thomas M.G., Escalante-Semerena J.C., Rayment I.
Biochemistry 38:12995-13005(1999) [PubMed: 10529169] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH GMP AND PHOSPHATE, ACTIVE SITE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L12006 Genomic DNA. Translation: AAA27269.1. Different initiation.
AE006468 Genomic DNA. Translation: AAL20922.1.
RefSeqNP_460963.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C9KX-ray2.20A/B/C2-181[»]
1CBUX-ray2.30A/B/C2-181[»]
ProteinModelPortalQ05599.
SMRQ05599. Positions 2-181.
ModBaseSearch...

Proteomic databases

PRIDEQ05599.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1253539.
GenomeReviewsGene locus STM2018 in contig AE006468_GR.
KEGGstm:STM2018.
PATRIC32382619. VBISalEnt20916_2140.

Phylogenomic databases

HOGENOMHBG635321.
OMATLWLTNH.
ProtClustDBPRK05800.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13215.
STYP99287:STM2018-MONOMER.

Family and domain databases

InterProIPR003203. Cobinamide_kinase/P_G-Trfase.
[Graphical view]
KOK02231.
PfamPF02283. CobU. 1 hit.
[Graphical view]
PIRSFPIRSF006135. CobU. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCOBU_SALTY
AccessionPrimary (citable) accession number: Q05599
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: October 1, 1996
Last modified: January 25, 2012
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references