Q635G3 (BIOD_BACCZ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-dependent dethiobiotin synthetase BioD
EC=6.3.3.3

Alternative name(s):
DTB synthetase
Short name=DTBS
Dethiobiotin synthase

Gene names

Name:	bioD
Ordered Locus Names:	BCE33L3874

Organism

Bacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP]

Taxonomic identifier

288681 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	242 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA) to form an ureido ring By similarity. HAMAP MF_00336
Catalytic activity	ATP + 7,8-diaminononanoate + CO2 = ADP + phosphate + dethiobiotin. HAMAP MF_00336
Cofactor	Magnesium By similarity. HAMAP MF_00336
Pathway	Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2. HAMAP MF_00336
Subcellular location	Cytoplasm By similarity HAMAP MF_00336.
Sequence similarities	Belongs to the dethiobiotin synthetase family.

Ontologies

Keywords
Biological process	Biotin biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	biotin 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 dethiobiotin synthase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 242	242	ATP-dependent dethiobiotin synthetase BioD HAMAP MF_00336		PRO_0000302477
Regions
	Nucleotide binding	12 – 17	6	ATP By similarity
	Nucleotide binding	112 – 115	4	ATP By similarity
Sites
	Metal binding	12	1	Magnesium 1 By similarity
	Metal binding	16	1	Magnesium 2 By similarity
	Metal binding	51	1	Magnesium 2 By similarity
	Metal binding	112	1	Magnesium 2 By similarity
	Binding site	41	1	Substrate By similarity
	Binding site	51	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q635G3 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 6D5C2D1D1AAAF5C0	FASTA	242	26,265
	10 20 30 40 50 60 MSGFFITATD TEVGKTVVAG ALAGVFRELG YNIGVYKPLQ SGHVASNPEG DAARLKALSG 70 80 90 100 110 120 VPTKEDEICP YSIEEPLAPR LAMKRAGRTV TLKDIIHHYN ERLKEFNSLF VEGAGGLAVP 130 140 150 160 170 180 YTEDALVIDF AKELQLPLIV VARPTLGTVN HTVLTIAYAK AHGLTVAGVI LSGCKECEME 190 200 210 220 230 240 RVQENKVMIE ELSGVPVLGL LPFFEGEFTK KEVLESAKEY IMISKLEECI RNESTVAHTS SN

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ZK / E33L.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000001 Genomic DNA. Translation: AAU16395.1.
RefSeq	YP_085454.1. NC_006274.1.
3D structure databases
HSSP	HSSP built from PDB template 1DAI based on UniProtKB P13000.
ProteinModelPortal	Q635G3.
ModBase	Search...
Protein-protein interaction databases
STRING	Q635G3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000042136; EBBACP00000041037; EBBACG00000042127.
GeneID	3026496.
GenomeReviews	Gene locus BCE33L3874 in contig CP000001_GR.
KEGG	bcz:BCZK3874.
PATRIC	18891526. VBIBacCer95304_4101.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0132.
GeneTree	EBGT00050000001962.
HOGENOM	HBG650065.
OMA	ANCVDPN.
ProtClustDB	PRK00090.
Enzyme and pathway databases
BioCyc	BCER288681:BCE33L3874-MONOMER.
Family and domain databases
HAMAP	MF_00336. BioD. [Tree]
InterPro	IPR002586. CbiA_P_synth. IPR004472. DTB_synth_BioD. [Graphical view]
KO	K01935.
Pfam	PF01656. CbiA. 1 hit. [Graphical view]
PIRSF	PIRSF006755. DTB_synth. 1 hit.
TIGRFAMs	TIGR00347. BioD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

BIOD_BACCZ

Accession

Primary (citable) accession number: Q635G3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program