ID   A0A0D2JKT9_9EURO        Unreviewed;       851 AA.
AC   A0A0D2JKT9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Dethiobiotin synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Z520_10492 {ECO:0000313|EMBL:KIX93867.1};
OS   Fonsecaea multimorphosa CBS 102226.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX93867.1, ECO:0000313|Proteomes:UP000053411};
RN   [1] {ECO:0000313|EMBL:KIX93867.1, ECO:0000313|Proteomes:UP000053411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX93867.1,
RC   ECO:0000313|Proteomes:UP000053411};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004746}.
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DR   EMBL; KN848091; KIX93867.1; -; Genomic_DNA.
DR   RefSeq; XP_016627990.1; XM_016780984.1.
DR   AlphaFoldDB; A0A0D2JKT9; -.
DR   STRING; 1442371.A0A0D2JKT9; -.
DR   GeneID; 27716238; -.
DR   VEuPathDB; FungiDB:Z520_10492; -.
DR   OrthoDB; 5487177at2759; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000053411; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004141; F:dethiobiotin synthase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03109; DTBS; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_00336; BioD; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR004472; DTB_synth_BioD.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42684:SF21; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR   Pfam; PF13500; AAA_26; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053411};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          614..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..639
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   851 AA;  93318 MW;  2A5EC45597FCDD08 CRC64;
     MLWRDLKAWQ VFGANTNVGK TIVSTLLCRA LQTPDQRVLY LKPVSTGPRD EEDVGHIDTF
     VPGTVSKNIS QFSRPLSPHL AAQLDKDPSI PRSDASILSR VKAILGKHVE AGGRYAFVET
     AGGVLSPGPS GTVQADLYRP LRLPTILVGD SKLGGIATTI SAFESLHVRG FDVDSIVLFD
     DPEWGNFEYL DRYFRNHGIS TFALPKPPEK QQDGEQDKRA LSSYYSGWSK TGAARNLLDL
     LNQKHFSRIS KLTSMPSQAD AVIWHPFRQH GIPHNIIAID SAYNDHFQTY NQEADPALKE
     SSKTTSTMGL TPLAAQPTPK PLLTPLFDAS ASWWTQGLGH GNPNVALTAA HAAGRYGHVM
     FAHAVHEPAL DISYNLLSTL QNPRLSRVFF TDNGSTGMEV AVKMALRASS QRYGWTKDDD
     DDGGKTPVAI LGLKGSYHGD TIGVMNCSEP SVFNEKVDWH QPWGHWFDPP SVLMRKGVWE
     LTMPEEMYAT NQTQQFKSLH ALFDFDARTE DARRYESHIT ATLERLVRDQ GRRFGALILE
     PIIMGAGGMI FVDPLFQRTL IKTIRANPHL IAPKQFSEHD AADGQEGGSS VEWSGLPIIA
     DEVFTGLYRL GRSSSSSFLS SPSDFASTTA TSTSESPQPA LPPSIAPDIS AHAKLLTAGL
     LPLALTTASE SIFRTFLSDS KTDALLHGHS YTAHPIGCMV ANKALDEYRR MDSSKEGEGS
     WSRFKRAWSE ETSLLGEDAV PQKQTNPDIY SFFPPSLLQE LSHHPRLTGC FALGTVLVLK
     VAAPRGSTGG YTSTASAELQ SRLLTLLDED GCGIHSRVLG DMIYFMTSLT TTAEQVDRLG
     RTLLRALNME P
//