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Database: UniProt
Entry: B1T191_9BURK
LinkDB: B1T191_9BURK
Original site: B1T191_9BURK 
ID   B1T191_9BURK            Unreviewed;       239 AA.
AC   B1T191;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   24-JAN-2024, entry version 78.
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   ORFNames=BamMEX5DRAFT_1557 {ECO:0000313|EMBL:EDT42674.1};
OS   Burkholderia ambifaria MEX-5.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=396597 {ECO:0000313|EMBL:EDT42674.1, ECO:0000313|Proteomes:UP000004814};
RN   [1] {ECO:0000313|EMBL:EDT42674.1, ECO:0000313|Proteomes:UP000004814}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MEX-5 {ECO:0000313|EMBL:EDT42674.1,
RC   ECO:0000313|Proteomes:UP000004814};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L.,
RA   Tiedje J., Richardson P.;
RT   "Sequencing of the draft genome and assembly of Burkholderia ambifaria MEX-
RT   5.";
RL   Submitted (MAR-2008) 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:EDT42674.1}.
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DR   EMBL; ABLK01000032; EDT42674.1; -; Genomic_DNA.
DR   RefSeq; WP_006757540.1; NZ_ABLK01000032.1.
DR   AlphaFoldDB; B1T191; -.
DR   PATRIC; fig|396597.7.peg.6748; -.
DR   UniPathway; UPA00078; UER00161.
DR   Proteomes; UP000004814; 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:SF5; ATP-DEPENDENT DETHIOBIOTIN SYNTHETASE BIOD 1; 1.
DR   PANTHER; PTHR43210; 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:EDT42674.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004814}.
FT   ACT_SITE        40
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         15..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         19
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         57
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         118..121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         118
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         178..179
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
SQ   SEQUENCE   239 AA;  25272 MW;  2921A549BF9E1CD5 CRC64;
     MTAPLSLFVT GTDTEIGKTF VSAAMLHGFA RHGLRAAALK PVAAGAYERD GVWRNEDADQ
     LDAAANVVLP PELRTPFLLK APAAPHIVAA HEGVTLDIDT IVASHREALT RADVVVVEGV
     GGFRVPLTDT QDTADLAVAL GLPVVLVVGV RLGCISHALL TADAIRQRGL TLAGWVANHV
     DPAMSYADEN VATIRDWLAR EHRAPLLGRI AHLRPAAPES AAAMLDIAAL VDTLRRAQH
//
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