ID A0A0W0STU0_9GAMM Unreviewed; 219 AA.
AC A0A0W0STU0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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:KTC86807.1};
GN ORFNames=Lbru_0748 {ECO:0000313|EMBL:KTC86807.1};
OS Legionella brunensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=29422 {ECO:0000313|EMBL:KTC86807.1, ECO:0000313|Proteomes:UP000054742};
RN [1] {ECO:0000313|EMBL:KTC86807.1, ECO:0000313|Proteomes:UP000054742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43878 {ECO:0000313|EMBL:KTC86807.1,
RC ECO:0000313|Proteomes:UP000054742};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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:KTC86807.1}.
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DR EMBL; LNXV01000004; KTC86807.1; -; Genomic_DNA.
DR RefSeq; WP_058440827.1; NZ_LNXV01000004.1.
DR AlphaFoldDB; A0A0W0STU0; -.
DR STRING; 29422.Lbru_0748; -.
DR PATRIC; fig|29422.6.peg.783; -.
DR OrthoDB; 9802097at2; -.
DR UniPathway; UPA00078; UER00161.
DR Proteomes; UP000054742; 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:SF5; 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|ARBA:ARBA00022756, ECO:0000256|HAMAP-
KW Rule:MF_00336}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00336};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00336, ECO:0000313|EMBL:KTC86807.1};
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 37
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT BINDING 12..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT BINDING 54
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT BINDING 114..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT BINDING 174..175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
SQ SEQUENCE 219 AA; 24487 MW; 0C72F12663534026 CRC64;
MKPFFITGTD TDCGKTYVTC QLLDYLKNFE KKILAIKPVA SGCIEINGQL LSEDVNHLQQ
YNLNSDYTVN CWQFRSPISP HLAAKEEGCS LSVKEIAAFC QHEQYKNLDC LLIEGAGGLL
VPLNEEETWL DFLRLTRIPT ILVVGMKLGC INHALLTASV LQNHKIPYVG WVANCLDKNM
LVLNENITTL SQKMPMPLLA TVPFQGKLIP HSSFYGVIN
//