AC   MF_00336;
DC   Protein; auto
TR   HAMAP; MF_00336; -; 1; level=0
XX
Names: BioD
XX
ID   BIOD
DE   RecName: Full=ATP-dependent dethiobiotin synthetase BioD;
DE            EC=6.3.3.3;
DE   AltName: Full=DTB synthetase;
DE            Short=DTBS;
DE   AltName: Full=Dethiobiotin synthase;
GN   Name=bioD;
XX
CC   -!- FUNCTION: Catalyzes a mechanistically unusual reaction, the ATP-
CC       dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-
CC       diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to
CC       form a ureido ring.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-
CC         dethiobiotin + ADP + 3 H(+) + phosphate; Xref=Rhea:RHEA:15805,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:149469, ChEBI:CHEBI:149473,
CC         ChEBI:CHEBI:456216; EC=6.3.3.3;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-
CC       diaminononanoate: step 1/2.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the dethiobiotin synthetase family.
XX
DR   NCBIfam; TIGR00347; BioD; 1; trigger=no
DR   PIRSF; PIRSF006755; DTB_synth; 1; trigger=no
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KW   ATP-binding
KW   Biotin biosynthesis
KW   Cytoplasm
KW   Ligase
KW   Magnesium
KW   Metal-binding
KW   Nucleotide-binding
XX
GO   GO:0005524; F:ATP binding
GO   GO:0004141; F:dethiobiotin synthase activity
GO   GO:0000287; F:magnesium ion binding
GO   GO:0009102; P:biotin biosynthetic process
XX
FT   From: BIOD1_ECOLI (P13000)
FT   BINDING         13..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [EDNSG]-[VAILSC]-G-K-[TS]-[VLTIYFH]
FT   BINDING         116..119
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: E-x-x-G
FT   BINDING         176..177
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [NSMVILG]-[DEHRQTNCSMK]
FT   BINDING         205..207
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [PA]-x-[LIVSTG]
FT   ACT_SITE        38
FT   Condition: K
FT   BINDING         17
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: [TS]
FT   BINDING         55
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: [DNCRHK]
FT   BINDING         116
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: E
FT   BINDING         42
FT                   /ligand="substrate"
FT   Condition: [ST]
FT   BINDING         55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [DN]
FT   BINDING         212
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [ENQ]
XX
Size: 191-278;
Related: None;
Template: P13000; P22818; P9WPQ5; O24872;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: MF_00835 (BioC)
 Cter: None
Duplicate: in ECO57, ECOLI, HAEDU, HAEIN, PASMU, SALTI, SALTY, YERPE
Plasmid: None
Comments: None
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# Revision 1.43 2023/06/01
//