P22818 (BIOD_LYSSH) 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

Organism

Lysinibacillus sphaericus (Bacillus sphaericus)

Taxonomic identifier

1421 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Lysinibacillus

Protein attributes

Sequence length	234 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.

Ontologies

Keywords
Biological process	Biotin biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
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 – 234	234	ATP-dependent dethiobiotin synthetase BioD HAMAP MF_00336		PRO_0000187948
Regions
	Nucleotide binding	115 – 118	4	ATP By similarity
Sites
	Metal binding	12	1	Magnesium 1 By similarity
	Metal binding	16	1	Magnesium 2 By similarity
	Metal binding	54	1	Magnesium 2 By similarity
	Metal binding	115	1	Magnesium 2 By similarity
	Binding site	41	1	Substrate By similarity
	Binding site	54	1	ATP By similarity
	Binding site	234	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P22818 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: 20EDA548021457E4	FASTA	234	26,488
	10 20 30 40 50 60 MQHFWVVGTD TDVGKTFVTT LLMRNLQKQG VRVTPYKPVQ TGEVYDGEQA YYFDTAMYEK 70 80 90 100 110 120 YSLQLLDREN LNGYSFKEAA SPHFAAQLEG QQIDTQQLLK QMQLLQQTWD VVICEGAGGL 130 140 150 160 170 180 FVPLDACGET TLLDVIVESK LPVVVVTRTA LGTINHTLLT LEALTTRKIE VLGLVFNGDM 190 200 210 220 230 GSRMEQDNIQ TILQYYTLPY MTIPKLEELS DINEYAITGT SLFERLIRRE TSIN

References

[1]	"Cloning and characterization of the Bacillus sphaericus genes controlling the bioconversion of pimelate into dethiobiotin." Gloeckler R., Ohsawa I., Speck D., Ledoux C., Bernard S., Zinsius M., Villeval D., Kisou T., Kamogawa K., Lemoine Y. Gene 87:63-70(1990) [PubMed: 2110099] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 10208 / NRS 966 / NCIB 11935 / 1911.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M29292 Genomic DNA. Translation: AAB02324.1.
PIR	JQ0506.
3D structure databases
ProteinModelPortal	P22818.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
HAMAP	MF_00336. BioD. [Tree]
InterPro	IPR002586. CbiA_P_synth. IPR004472. DTB_synth_BioD. [Graphical view]
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_LYSSH

Accession

Primary (citable) accession number: P22818

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	December 14, 2011
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program