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Database: UniProt
Entry: E1L5T4_9FIRM
LinkDB: E1L5T4_9FIRM
Original site: E1L5T4_9FIRM 
ID   E1L5T4_9FIRM            Unreviewed;       250 AA.
AC   E1L5T4;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=ATP-dependent dethiobiotin synthetase BioD {ECO:0000256|HAMAP-Rule:MF_00336};
DE            EC=6.3.3.3 {ECO:0000256|HAMAP-Rule:MF_00336};
DE   AltName: Full=DTB synthetase {ECO:0000256|HAMAP-Rule:MF_00336};
DE            Short=DTBS {ECO:0000256|HAMAP-Rule:MF_00336};
DE   AltName: Full=Dethiobiotin synthase {ECO:0000256|HAMAP-Rule:MF_00336};
GN   Name=bioD {ECO:0000256|HAMAP-Rule:MF_00336,
GN   ECO:0000313|EMBL:EFL56282.1};
GN   ORFNames=HMPREF9321_1613 {ECO:0000313|EMBL:EFL56282.1};
OS   Veillonella atypica ACS-049-V-Sch6.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Veillonella.
OX   NCBI_TaxID=866776 {ECO:0000313|EMBL:EFL56282.1, ECO:0000313|Proteomes:UP000004211};
RN   [1] {ECO:0000313|EMBL:EFL56282.1, ECO:0000313|Proteomes:UP000004211}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-049-V-Sch6 {ECO:0000313|EMBL:EFL56282.1,
RC   ECO:0000313|Proteomes:UP000004211};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-Rule:MF_00336}.
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00336};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00336};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-
CC       diaminononanoate: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00336}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00336}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00336}.
CC   -!- SIMILARITY: Belongs to the dethiobiotin synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00336}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00336}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFL56282.1}.
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DR   EMBL; AEDR01000024; EFL56282.1; -; Genomic_DNA.
DR   RefSeq; WP_005376648.1; NZ_AEDR01000024.1.
DR   AlphaFoldDB; E1L5T4; -.
DR   eggNOG; COG0132; Bacteria.
DR   UniPathway; UPA00078; UER00161.
DR   Proteomes; UP000004211; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004141; F:dethiobiotin synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03109; DTBS; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00336; BioD; 1.
DR   InterPro; IPR004472; DTB_synth_BioD.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00347; bioD; 1.
DR   PANTHER; PTHR43210; DETHIOBIOTIN SYNTHETASE; 1.
DR   PANTHER; PTHR43210:SF2; DETHIOBIOTIN SYNTHETASE; 1.
DR   Pfam; PF13500; AAA_26; 1.
DR   PIRSF; PIRSF006755; DTB_synth; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00336};
KW   Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00336};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00336};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00336, ECO:0000313|EMBL:EFL56282.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00336};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00336};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00336}.
FT   ACT_SITE        39
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         14..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         18
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         43
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         67
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         129..132
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         129
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         189..190
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
SQ   SEQUENCE   250 AA;  27209 MW;  04370A87BC055F35 CRC64;
     MRQLGVSIIG TDTDVGKTFV TGLLGALAVD DGFDVGMVKP VSSSAVPFSQ CETMDEDEIC
     MGLESKDATY LMQSVGIPES RRREVNPIAL AGDYSPRLAA ELAGVDIDYP EIVSHVKRVV
     NQHDITFVEG AGGITTPLTK DITFTNLMTD IAYPAILVAD GRLGSINRVV LTYEYAKQHH
     IDVKGIIVND TTVVDPFLLK TNIEDMERYT GIPVLGVLPP YQGPNQAHIK LGWGRSFLDS
     AKIWQTVWGV
//
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