(data stored in ACNUC7421 zone)

SWISSPROT: BIOD_PSEAB

ID   BIOD_PSEAB              Reviewed;         228 AA.
AC   Q02TR2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   07-JUN-2017, entry version 69.
DE   RecName: Full=ATP-dependent dethiobiotin synthetase BioD {ECO:0000255|HAMAP-Rule:MF_00336};
DE            EC=6.3.3.3 {ECO:0000255|HAMAP-Rule:MF_00336};
DE   AltName: Full=DTB synthetase {ECO:0000255|HAMAP-Rule:MF_00336};
DE            Short=DTBS {ECO:0000255|HAMAP-Rule:MF_00336};
DE   AltName: Full=Dethiobiotin synthase {ECO:0000255|HAMAP-Rule:MF_00336};
GN   Name=bioD {ECO:0000255|HAMAP-Rule:MF_00336};
GN   OrderedLocusNames=PA14_06570;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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:0000255|HAMAP-Rule:MF_00336}.
CC   -!- CATALYTIC ACTIVITY: ATP + 7,8-diaminononanoate + CO(2) = ADP +
CC       phosphate + dethiobiotin. {ECO:0000255|HAMAP-Rule:MF_00336}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00336};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from
CC       7,8-diaminononanoate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00336}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00336}.
CC   -!- SIMILARITY: Belongs to the dethiobiotin synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00336}.
DR   EMBL; CP000438; ABJ15466.1; -; Genomic_DNA.
DR   RefSeq; WP_003111241.1; NC_008463.1.
DR   ProteinModelPortal; Q02TR2; -.
DR   SMR; Q02TR2; -.
DR   EnsemblBacteria; ABJ15466; ABJ15466; PA14_06570.
DR   KEGG; pau:PA14_06570; -.
DR   HOGENOM; HOG000275032; -.
DR   KO; K01935; -.
DR   OMA; DYWKPIQ; -.
DR   UniPathway; UPA00078; UER00161.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004141; F:dethiobiotin synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00336; BioD; 1.
DR   InterPro; IPR004472; DTB_synth_BioD.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR43210; PTHR43210; 1.
DR   PIRSF; PIRSF006755; DTB_synth; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00347; bioD; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q02TR2.
DR   SWISS-2DPAGE; Q02TR2.
KW   ATP-binding; Biotin biosynthesis; Complete proteome; Cytoplasm;
KW   Ligase; Magnesium; Metal-binding; Nucleotide-binding.
FT   CHAIN         1    228       ATP-dependent dethiobiotin synthetase
FT                                BioD.
FT                                /FTId=PRO_0000302541.
FT   NP_BIND      12     17       ATP. {ECO:0000255|HAMAP-Rule:MF_00336}.
FT   NP_BIND     116    119       ATP. {ECO:0000255|HAMAP-Rule:MF_00336}.
FT   NP_BIND     205    207       ATP. {ECO:0000255|HAMAP-Rule:MF_00336}.
FT   METAL        12     12       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00336}.
FT   METAL        16     16       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00336}.
FT   METAL        54     54       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00336}.
FT   METAL       116    116       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00336}.
FT   BINDING      41     41       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00336}.
FT   BINDING      54     54       ATP. {ECO:0000255|HAMAP-Rule:MF_00336}.
SQ   SEQUENCE   228 AA;  23359 MW;  D7E54E62332CA0A4 CRC64;
     MPAFFVTGTD TEIGKTTIAA GLLHAARRAG LSTAAAKPVA SGCEPTAQGL RNGDALALLG
     QCSLALAYEQ VNPLAFAPAI APHLAAREAG VELSAARLHE AVREVLALQA DLTLVEGAGG
     WRVPLQGREN LSDLARLLAL PVVLVVGVRL GCINHALLSA EAILGDGLAL AGWVANVVDP
     ATSRLEENLA TLAERLPAPC LGRVPRLEEA TPAAVAAHLD LRPLGIGL
//

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