(data stored in ACNUC7421 zone)

SWISSPROT: BIOD_ANADE

ID   BIOD_ANADE              Reviewed;         223 AA.
AC   Q2IM14;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   11-DEC-2019, entry version 81.
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}; OrderedLocusNames=Adeh_0070;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA   Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA   Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) 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) to form an ureido ring.
CC       {ECO:0000255|HAMAP-Rule:MF_00336}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7,8-diaminononanoate + ATP + CO2 = ADP + dethiobiotin + 3 H(+)
CC         + phosphate; Xref=Rhea:RHEA:15805, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57861, ChEBI:CHEBI:58500, ChEBI:CHEBI:456216; EC=6.3.3.3;
CC         Evidence={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 7,8-
CC       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; CP000251; ABC79848.1; -; Genomic_DNA.
DR   RefSeq; WP_011419131.1; NC_007760.1.
DR   SMR; Q2IM14; -.
DR   STRING; 290397.Adeh_0070; -.
DR   PRIDE; Q2IM14; -.
DR   EnsemblBacteria; ABC79848; ABC79848; Adeh_0070.
DR   KEGG; ade:Adeh_0070; -.
DR   eggNOG; ENOG4105E78; Bacteria.
DR   eggNOG; COG0132; LUCA.
DR   HOGENOM; HOG000275033; -.
DR   KO; K01935; -.
DR   OMA; SPHWAAE; -.
DR   BioCyc; ADEH290397:G1G5W-73-MONOMER; -.
DR   UniPathway; UPA00078; UER00161.
DR   Proteomes; UP000001935; Chromosome.
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   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; Q2IM14.
DR   SWISS-2DPAGE; Q2IM14.
KW   ATP-binding; Biotin biosynthesis; Cytoplasm; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..223
FT                   /note="ATP-dependent dethiobiotin synthetase BioD"
FT                   /id="PRO_0000302473"
FT   NP_BIND         111..114
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00336"
FT   NP_BIND         171..172
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00336"
FT   METAL           16
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00336"
FT   METAL           50
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00336"
FT   METAL           111
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00336"
FT   BINDING         41
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00336"
FT   BINDING         50
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00336"
SQ   SEQUENCE   223 AA;  22788 MW;  19276B658DB1EE8C CRC64;
     MRGLFVTGTD TGVGKTEVAC ALVRAARAAG LDAVGMKPAQ SGHVAGEPSD AERLREASGG
     VEPLEAICPY TFAAPLAPAA AARAEGREVS LARVVEAARA LAARHAAVVV EGAGGLLVPL
     TARETHADLA AALGLPVLVV ARAGLGTVNH TALTVEALER RGLPIAGIVL NRTGPEDDPS
     VPLNAAEIAR LTHREPLALL PWEPDIARRA RALGSVLAAK IQF
//

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