BIOD_YEAST
ID BIOD_YEAST Reviewed; 237 AA.
AC P53630; D6W1N2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Dethiobiotin synthetase {ECO:0000305};
DE Short=DTB synthetase {ECO:0000305};
DE EC=6.3.3.3 {ECO:0000305|PubMed:10333520};
DE AltName: Full=Dethiobiotin synthase {ECO:0000303|PubMed:10333520};
DE Short=DTBS {ECO:0000305};
GN Name=BIO4 {ECO:0000303|PubMed:10333520}; OrderedLocusNames=YNR057C;
GN ORFNames=N3506;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX PubMed=10333520; DOI=10.1016/s0378-1119(99)00117-1;
RA Phalip V., Kuhn I., Lemoine Y., Jeltsch J.-M.;
RT "Characterization of the biotin biosynthesis pathway in Saccharomyces
RT cerevisiae and evidence for a cluster containing BIO5, a novel gene
RT involved in vitamer uptake.";
RL Gene 232:43-51(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
CC -!- FUNCTION: Dethiobiotin synthetase involved in the biotin biosynthesis
CC pathway. {ECO:0000269|PubMed:10333520}.
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;
CC Evidence={ECO:0000305|PubMed:10333520};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P13000};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-
CC diaminononanoate: step 1/2. {ECO:0000305|PubMed:10333520}.
CC -!- SIMILARITY: Belongs to the dethiobiotin synthetase family.
CC {ECO:0000305}.
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DR EMBL; U53467; AAB63971.1; -; Genomic_DNA.
DR EMBL; Z71672; CAA96339.1; -; Genomic_DNA.
DR EMBL; AY558424; AAS56750.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10598.1; -; Genomic_DNA.
DR PIR; S63389; S63389.
DR RefSeq; NP_014455.1; NM_001183234.1.
DR AlphaFoldDB; P53630; -.
DR SMR; P53630; -.
DR BioGRID; 35883; 49.
DR IntAct; P53630; 2.
DR STRING; 4932.YNR057C; -.
DR MaxQB; P53630; -.
DR PaxDb; P53630; -.
DR PRIDE; P53630; -.
DR EnsemblFungi; YNR057C_mRNA; YNR057C; YNR057C.
DR GeneID; 855794; -.
DR KEGG; sce:YNR057C; -.
DR SGD; S000005340; BIO4.
DR VEuPathDB; FungiDB:YNR057C; -.
DR eggNOG; ENOG502RXZU; Eukaryota.
DR HOGENOM; CLU_072551_2_0_1; -.
DR InParanoid; P53630; -.
DR OMA; SPHWAAE; -.
DR BioCyc; YEAST:YNR057C-MON; -.
DR UniPathway; UPA00078; UER00161.
DR PRO; PR:P53630; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53630; protein.
DR GO; GO:0005737; C:cytoplasm; ISS:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004141; F:dethiobiotin synthase activity; IDA:SGD.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0009102; P:biotin biosynthetic process; IDA:SGD.
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 PANTHER; PTHR43210; PTHR43210; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00347; bioD; 1.
PE 3: Inferred from homology;
KW ATP-binding; Biotin biosynthesis; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..237
FT /note="Dethiobiotin synthetase"
FT /id="PRO_0000188006"
FT ACT_SITE 42
FT /evidence="ECO:0000250|UniProtKB:P13000"
FT BINDING 22..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P13000"
FT BINDING 26
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P13000"
FT BINDING 117..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P13000"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P13000"
FT BINDING 184..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P13000"
FT BINDING 213..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P13000"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P13000"
SQ SEQUENCE 237 AA; 26257 MW; F1147BF18DA40735 CRC64;
MNSKSQQQEQ QPIVFVTGTD TDVGKTFVST LLVHKWKAAY WKPVQTGIES DQGDSETLKN
FKIAASTWQP PIFTPTYALQ KPLSPLQAME YEPNVDIRLL DFVVPEEWSA ENPLVVEGAG
GVCVPITRKL EITTDLIKHL IETSGHPVYV VVVARSGLGT LNHTLLTWNH LCDNGLRSHL
FGVILNGEPN EGNVQALKKF GVNIMAQVAQ CTTAHDQDME LHELPSVESL MTQQDVE
