P53558 (BIOD_BACSU) 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:	BSU30210

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	231 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.
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.
Sequence caution	The sequence AAC00264.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Biotin biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference 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 – 231	231	ATP-dependent dethiobiotin synthetase BioD HAMAP MF_00336		PRO_0000187949
Regions
	Nucleotide binding	12 – 17	6	ATP By similarity
	Nucleotide binding	112 – 115	4	ATP By similarity
	Nucleotide binding	202 – 204	3	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)
	P53558 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 8C51EB667BC4E96A	FASTA	231	25,160
	10 20 30 40 50 60 MRGFFVTGTD TEVGKTVISS GLAALLKDNN RHVGVYKPFL SGISRHHPDS DTSLLKDMSQ 70 80 90 100 110 120 TSLSHEDITP FAFKAPLAPY VAGKLEGKTV TMEEVLSHWG RIREKHECFI VEGAGGISVP 130 140 150 160 170 180 LGEDYLVSHV IKALQLPMII VARPRLGTIN HTFLTVKYAE SMGLPIAGII INGISDSPDE 190 200 210 220 230 DEKTNPEMIE RLCGVPILGV TPKLANVTKE TVLHMVKDHI NLSLLMNQVG V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, sequencing, and characterization of the Bacillus subtilis biotin biosynthetic operon." Bower S., Perkins J.B., Yocum R.R., Howitt C.L., Rahaim P., Pero J. J. Bacteriol. 178:4122-4130(1996) [PubMed: 8763940] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region." Lapidus A., Galleron N., Sorokin A., Ehrlich S.D. Microbiology 143:3431-3441(1997) [PubMed: 9387221] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"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: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U51868 Genomic DNA. Translation: AAB17460.1. AF008220 Genomic DNA. Translation: AAC00264.1. Different initiation. AL009126 Genomic DNA. Translation: CAB14999.1.
PIR	E69594.
RefSeq	NP_390899.1. NC_000964.3.
3D structure databases
ProteinModelPortal	P53558.
SMR	P53558. Positions 2-225.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000000731; EBBACP00000000731; EBBACG00000000729.
GeneID	937264.
GenomeReviews	Gene locus BSU30210 in contig AL009126_GR.
KEGG	bsu:BSU30210.
NMPDR	fig|224308.1.peg.3024.
PATRIC	18977944. VBIBacSub10457_3160.
Organism-specific databases
GenoList	BSU30210. [Micado]
Phylogenomic databases
GeneTree	EBGT00050000001962.
HOGENOM	HBG650065.
OMA	TRTNEDV.
PhylomeDB	P53558.
ProtClustDB	PRK00090.
Enzyme and pathway databases
BioCyc	BSUB:BSU30210-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_BACSU

Accession

Primary (citable) accession number: P53558
Secondary accession number(s): O30501

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program