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O34899 (PDUO_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Cob(I)yrinic acid a,c-diamide adenosyltransferase

EC=2.5.1.17
Alternative name(s):
Cob(I)alamin adenosyltransferase
Gene names
Name:yvqK
Ordered Locus Names:BSU33150
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length193 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

ATP + cobinamide = triphosphate + adenosylcobinamide.

Pathway

Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.

Subunit structure

Homotrimer. Ref.4

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the Cob(I)alamin adenosyltransferase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 193193Cob(I)yrinic acid a,c-diamide adenosyltransferase
PRO_0000360832

Regions

Nucleotide binding5 – 139ATP By similarity
Nucleotide binding130 – 1356ATP By similarity

Sites

Binding site221ATP By similarity
Binding site1541ATP By similarity

Experimental info

Sequence conflict1631A → G in CAA11738. Ref.1

Secondary structure

............. 193
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O34899 [UniParc].

Last modified July 28, 2009. Version 2.
Checksum: 3FD1165F90E8526E

FASTA19321,504
        10         20         30         40         50         60 
MKLYTKTGDK GQTGLVGGRT DKDSLRVESY GTIDELNSFI GLALAELSGQ PGFEDLTAEL 

        70         80         90        100        110        120 
LTIQHELFDC GGDLAIVTER KDYKLTEESV SFLETRIDAY TAEAPELKKF ILPGGSKCAS 

       130        140        150        160        170        180 
LLHIARTITR RAERRVVALM KSEEIHETVL RYLNRLSDYF FAAARVVNAR SGIGDVEYER 

       190 
SAIVFRDRNS SES 

« Hide

References

« Hide 'large scale' references
[1]"The yvsA-yvqA (293 degrees - 289 degrees) region of the Bacillus subtilis chromosome containing genes involved in metal ion uptake and a putative sigma factor."
Wipat A., Brignell C.S., Guy J.B., Rose M., Emmerson P.T., Harwood C.R.
Microbiology 144:1593-1600(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 163.
[4]"Functional insights from structural genomics."
Forouhar F., Kuzin A., Seetharaman J., Lee I., Zhou W., Abashidze M., Chen Y., Yong W., Janjua H., Fang Y., Wang D., Cunningham K., Xiao R., Acton T.B., Pichersky E., Klessig D.F., Porter C.W., Montelione G.T., Tong L.
J. Struct. Funct. Genomics 8:37-44(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH PHOSPHATE, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ223978 Genomic DNA. Translation: CAA11738.1.
AL009126 Genomic DNA. Translation: CAB15305.2.
PIRD70046.
RefSeqNP_391195.2. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RTYX-ray2.40A/B/C1-193[»]
ProteinModelPortalO34899.
SMRO34899. Positions 23-180.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU33150.

Proteomic databases

PaxDbO34899.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15305; CAB15305; BSU33150.
GeneID935972.
KEGGbsu:BSU33150.
PATRIC18978620. VBIBacSub10457_3473.

Organism-specific databases

GenoListBSU33150.

Phylogenomic databases

eggNOGCOG2096.
HOGENOMHOG000291639.
OrthoDBEOG6SZ1P1.
ProtClustDBCLSK887861.

Enzyme and pathway databases

BioCycBSUB:BSU33150-MONOMER.
UniPathwayUPA00148; UER00233.

Family and domain databases

Gene3D1.20.1200.10. 1 hit.
InterProIPR016030. AdoCbl_synth_CblAdoTrfase-like.
[Graphical view]
PfamPF01923. Cob_adeno_trans. 1 hit.
[Graphical view]
ProDomPD007457. AdoCbl_syn_CblAdoTrfase_PduO_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF89028. SSF89028. 1 hit.
TIGRFAMsTIGR00636. PduO_Nterm. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO34899.

Entry information

Entry namePDUO_BACSU
AccessionPrimary (citable) accession number: O34899
Secondary accession number(s): Q7B2J8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: July 28, 2009
Last modified: November 13, 2013
This is version 82 of the entry and version 2 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

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList