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O34899

- PDUO_BACSU

UniProt

O34899 - PDUO_BACSU

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Protein

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

Gene

yvqK

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei22 – 221ATPBy similarity
Binding sitei154 – 1541ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi5 – 139ATPBy similarity
Nucleotide bindingi130 – 1356ATPBy 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

BioCyciBSUB:BSU33150-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
Gene namesi
Name:yvqK
Ordered Locus Names:BSU33150
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU33150.

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 193193Cob(I)yrinic acid a,c-diamide adenosyltransferasePRO_0000360832Add
BLAST

Proteomic databases

PaxDbiO34899.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

STRINGi224308.BSU33150.

Structurei

Secondary structure

1
193
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 4724
Beta strandi50 – 523
Helixi54 – 7522
Helixi87 – 10317
Helixi117 – 14226
Helixi147 – 17024

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RTYX-ray2.40A/B/C1-193[»]
ProteinModelPortaliO34899.
SMRiO34899. Positions 23-180.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO34899.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2096.
HOGENOMiHOG000291639.
InParanoidiO34899.
OrthoDBiEOG6SZ1P1.
PhylomeDBiO34899.

Family and domain databases

Gene3Di1.20.1200.10. 1 hit.
InterProiIPR016030. AdoCbl_synth_CblAdoTrfase-like.
IPR029499. PduO-typ.
[Graphical view]
PfamiPF01923. Cob_adeno_trans. 1 hit.
[Graphical view]
ProDomiPD007457. AdoCbl_syn_CblAdoTrfase_PduO_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF89028. SSF89028. 1 hit.
TIGRFAMsiTIGR00636. PduO_Nterm. 1 hit.

Sequencei

Sequence statusi: Complete.

O34899-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLYTKTGDK GQTGLVGGRT DKDSLRVESY GTIDELNSFI GLALAELSGQ
60 70 80 90 100
PGFEDLTAEL LTIQHELFDC GGDLAIVTER KDYKLTEESV SFLETRIDAY
110 120 130 140 150
TAEAPELKKF ILPGGSKCAS LLHIARTITR RAERRVVALM KSEEIHETVL
160 170 180 190
RYLNRLSDYF FAAARVVNAR SGIGDVEYER SAIVFRDRNS SES
Length:193
Mass (Da):21,504
Last modified:July 28, 2009 - v2
Checksum:i3FD1165F90E8526E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti163 – 1631A → G in CAA11738. (PubMed:9639930)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ223978 Genomic DNA. Translation: CAA11738.1.
AL009126 Genomic DNA. Translation: CAB15305.2.
PIRiD70046.
RefSeqiNP_391195.2. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB15305; CAB15305; BSU33150.
GeneIDi935972.
KEGGibsu:BSU33150.
PATRICi18978620. VBIBacSub10457_3473.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ223978 Genomic DNA. Translation: CAA11738.1 .
AL009126 Genomic DNA. Translation: CAB15305.2 .
PIRi D70046.
RefSeqi NP_391195.2. NC_000964.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RTY X-ray 2.40 A/B/C 1-193 [» ]
ProteinModelPortali O34899.
SMRi O34899. Positions 23-180.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU33150.

Proteomic databases

PaxDbi O34899.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB15305 ; CAB15305 ; BSU33150 .
GeneIDi 935972.
KEGGi bsu:BSU33150.
PATRICi 18978620. VBIBacSub10457_3473.

Organism-specific databases

GenoListi BSU33150.

Phylogenomic databases

eggNOGi COG2096.
HOGENOMi HOG000291639.
InParanoidi O34899.
OrthoDBi EOG6SZ1P1.
PhylomeDBi O34899.

Enzyme and pathway databases

UniPathwayi UPA00148 ; UER00233 .
BioCyci BSUB:BSU33150-MONOMER.

Miscellaneous databases

EvolutionaryTracei O34899.

Family and domain databases

Gene3Di 1.20.1200.10. 1 hit.
InterProi IPR016030. AdoCbl_synth_CblAdoTrfase-like.
IPR029499. PduO-typ.
[Graphical view ]
Pfami PF01923. Cob_adeno_trans. 1 hit.
[Graphical view ]
ProDomi PD007457. AdoCbl_syn_CblAdoTrfase_PduO_N. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF89028. SSF89028. 1 hit.
TIGRFAMsi TIGR00636. PduO_Nterm. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH PHOSPHATE, SUBUNIT.

Entry informationi

Entry nameiPDUO_BACSU
AccessioniPrimary (citable) accession number: O34899
Secondary accession number(s): Q7B2J8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: July 28, 2009
Last modified: October 29, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3