O34899 (PDUO_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	193 AA.
Sequence status	Complete.
Protein existence	Evidence 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

Keywords
Biological process	Cobalamin biosynthesis Porphyrin biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cobalamin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway porphyrin-containing compound biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cob(I)yrinic acid a,c-diamide adenosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 193

193

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

PRO_0000360832

Regions

Nucleotide binding

5 – 13

9

ATP By similarity

Nucleotide binding

130 – 135

6

ATP By similarity

Sites

Binding site

22

1

ATP By similarity

Binding site

154

1

ATP By similarity

Experimental info

Sequence conflict

163

1

A → G in CAA11738. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

193

Helix Strand Turn

Details...

Helix

24 – 47

24

Beta strand

50 – 52

3

Helix

54 – 75

22

Helix

87 – 103

17

Helix

117 – 142

26

Helix

147 – 170

24

Sequences

	Sequence		Length	Mass (Da)
	O34899 [UniParc]. Last modified July 28, 2009. Version 2. Checksum: 3FD1165F90E8526E	FASTA	193	21,504
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

PIR

D70046.

RefSeq

NP_391195.2. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RTY	X-ray	2.40	A/B/C	1-193	[»]

ProteinModelPortal

O34899.

SMR

O34899. Positions 23-180.

ModBase

Search...

Protein-protein interaction databases

STRING

224308.BSU33150.

Proteomic databases

PaxDb

O34899.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB15305; CAB15305; BSU33150.

GeneID

935972.

KEGG

bsu:BSU33150.

PATRIC

18978620. VBIBacSub10457_3473.

Organism-specific databases

GenoList

BSU33150.

Phylogenomic databases

eggNOG

COG2096.

HOGENOM

HOG000291639.

ProtClustDB

CLSK887861.

Enzyme and pathway databases

BioCyc

BSUB:BSU33150-MONOMER.

UniPathway

UPA00148; UER00233.

Family and domain databases

Gene3D

1.20.1200.10. 1 hit.

InterPro

IPR016030. AdoCbl_synth_CblAdoTrfase-like.
[Graphical view]

Pfam

PF01923. Cob_adeno_trans. 1 hit.
[Graphical view]

ProDom

PD007457. AdoCbl_syn_CblAdoTrfase_PduO_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF89028. AdoCbl_synth_CblAdoTrfase-like. 1 hit.

TIGRFAMs

TIGR00636. PduO_Nterm. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

O34899.

Entry information

Entry name

PDUO_BACSU

Accession

Primary (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:	May 1, 2013
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program