ID   C1DWK1_SULAA            Unreviewed;       217 AA.
AC   C1DWK1;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   04-MAR-2015, entry version 51.
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   AltName: Full=Dethiobiotin synthase {ECO:0000256|HAMAP-Rule:MF_00336};
GN   Name=bioD {ECO:0000256|HAMAP-Rule:MF_00336,
GN   ECO:0000313|EMBL:ACN98244.1};
GN   OrderedLocusNames=SULAZ_1522 {ECO:0000313|EMBL:ACN98244.1};
OS   Sulfurihydrogenibium azorense (strain Az-Fu1 / DSM 15241 / OCM 825).
OC   Bacteria; Aquificae; Aquificales; Hydrogenothermaceae;
OC   Sulfurihydrogenibium.
OX   NCBI_TaxID=204536 {ECO:0000313|EMBL:ACN98244.1, ECO:0000313|Proteomes:UP000001369};
RN   [1] {ECO:0000313|EMBL:ACN98244.1, ECO:0000313|Proteomes:UP000001369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Az-Fu1 / DSM 15241 / OCM 825
RC   {ECO:0000313|Proteomes:UP000001369};
RX   PubMed=19136599; DOI=10.1128/JB.01645-08;
RA   Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA   Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA   Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT   "Complete and draft genome sequences of six members of the
RT   Aquificales.";
RL   J. Bacteriol. 191:1992-1993(2009).
CC   -!- FUNCTION: Catalyzes a mechanistically unusual reaction, the ATP-
CC       dependent insertion of CO2 between the N7 and N8 nitrogen atoms of
CC       7,8-diaminopelargonic acid (DAPA) to form an ureido ring.
CC       {ECO:0000256|HAMAP-Rule:MF_00336, ECO:0000256|SAAS:SAAS00089824}.
CC   -!- CATALYTIC ACTIVITY: ATP + 7,8-diaminononanoate + CO(2) = ADP +
CC       phosphate + dethiobiotin. {ECO:0000256|HAMAP-Rule:MF_00336,
CC       ECO:0000256|SAAS:SAAS00089820}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00336,
CC         ECO:0000256|SAAS:SAAS00173485};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from
CC       7,8-diaminononanoate: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00336,
CC       ECO:0000256|SAAS:SAAS00089826}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00336,
CC       ECO:0000256|SAAS:SAAS00089828}.
CC   -!- SIMILARITY: Belongs to the dethiobiotin synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00336}.
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DR   EMBL; CP001229; ACN98244.1; -; Genomic_DNA.
DR   RefSeq; YP_002729488.1; NC_012438.1.
DR   STRING; 204536.SULAZ_1522; -.
DR   EnsemblBacteria; ACN98244; ACN98244; SULAZ_1522.
DR   GeneID; 7673620; -.
DR   KEGG; saf:SULAZ_1522; -.
DR   PATRIC; 23764160; VBISulAzo123226_1479.
DR   eggNOG; COG0132; -.
DR   HOGENOM; HOG000275033; -.
DR   KO; K01935; -.
DR   OMA; CINHAVL; -.
DR   OrthoDB; EOG66B3XT; -.
DR   BioCyc; SAZO204536:GHRE-1518-MONOMER; -.
DR   UniPathway; UPA00078; UER00161.
DR   Proteomes; UP000001369; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004141; F:dethiobiotin synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00336; BioD; 1.
DR   InterPro; IPR004472; DTB_synth_BioD.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PIRSF; PIRSF006755; DTB_synth; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00347; bioD; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00336,
KW   ECO:0000256|SAAS:SAAS00089817};
KW   Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00336,
KW   ECO:0000256|SAAS:SAAS00089830};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001369};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00336,
KW   ECO:0000256|SAAS:SAAS00089815};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00336,
KW   ECO:0000256|SAAS:SAAS00089835};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00336,
KW   ECO:0000256|SAAS:SAAS00089822};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00336,
KW   ECO:0000256|SAAS:SAAS00089802};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00336,
KW   ECO:0000256|SAAS:SAAS00089817}.
FT   METAL        17     17       Magnesium 2. {ECO:0000256|HAMAP-
FT                                Rule:MF_00336}.
FT   METAL        50     50       Magnesium 2. {ECO:0000256|HAMAP-
FT                                Rule:MF_00336}.
FT   METAL       109    109       Magnesium 2. {ECO:0000256|HAMAP-
FT                                Rule:MF_00336}.
FT   BINDING      42     42       Substrate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00336}.
FT   BINDING      50     50       ATP. {ECO:0000256|HAMAP-Rule:MF_00336}.
FT   BINDING     203    203       ATP. {ECO:0000256|HAMAP-Rule:MF_00336}.
SQ   SEQUENCE   217 AA;  23912 MW;  B321397B96C4E2E2 CRC64;
     MLNSLFITAT DTGVGKTTVS AAICKLLKEK GVNVAYFKPA ETGCQPIPQD AYTISKITGQ
     PLEEVVIYTF ENPVAPYTAT VLEGKEIDIQ KIIKHYKYLK TKYDFVIVEG AGGLLVPIKK
     NYTYLNLIED LNIPVLIVSR ASLGTINHTA LTIRALEGKQ IVGIVMNGFS GEDISEETNP
     QIIQEMTGVK VLAKCKKSQQ PVEECYSKLM DFVKTFV
//