ID   W9XFC7_9EURO            Unreviewed;       851 AA.
AC   W9XFC7;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Dethiobiotin synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A1O3_08713 {ECO:0000313|EMBL:EXJ79212.1};
OS   Capronia epimyces CBS 606.96.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX   NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ79212.1, ECO:0000313|Proteomes:UP000019478};
RN   [1] {ECO:0000313|EMBL:EXJ79212.1, ECO:0000313|Proteomes:UP000019478}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ79212.1,
RC   ECO:0000313|Proteomes:UP000019478};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL   Submitted (MAR-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXJ79212.1}.
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DR   EMBL; AMGY01000008; EXJ79212.1; -; Genomic_DNA.
DR   RefSeq; XP_007737000.1; XM_007738810.1.
DR   AlphaFoldDB; W9XFC7; -.
DR   STRING; 1182542.W9XFC7; -.
DR   GeneID; 19172800; -.
DR   eggNOG; KOG1401; Eukaryota.
DR   HOGENOM; CLU_010794_0_0_1; -.
DR   OrthoDB; 5487177at2759; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000019478; 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:UP000019478};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          570..596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          621..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..643
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   851 AA;  92353 MW;  30B6E6BFA225348F CRC64;
     MLWRDLKAWQ VYGANTDVGK TIVSTILCRV LQRRAPPNGL LYLKPVSTGP QAEADDRHIT
     RYVPGIKSRC ISQFSQPLSP HLAAQLDGPS SIPTSDASIV AQVKDLLSQH SQAGGRYAVL
     ETAGGVLSPA PSGSVQADLY RPLRLPTLLV GDSKLGGIST TVAAFESLHV RGYDLDSVVL
     FDDPKWANHG YLEAHFARHG IPTLALPPPP ARRDDPKDDE AVLADYYQAC SESASLTDLV
     DSLQRRHFAR VSKLTSMPSQ AEAVIWHPFR QHGIPHNIIA IDSAYGDHFQ AYNQESDLGL
     GTPTASALTG LTPLAAQPPA KPLLTPLFDA SASWWTQGLG HGNPELALTA AHAAGRYGHV
     MFAHAVHEPA LDIAYNLLST LQNPRLGRVF FSDNGSTGME VAVKMALRAS SQRYGWNKDD
     DRGQTPVAIL GLKGSYHGDT IGVMNCSEPN VYNEKVDWHQ PWGHWFDPPT LLLRNGVWEL
     SLPDEMRPAC AVQKFPSLDA LFDFPARADD AARYEEHIKT TLDTLVRHQG RRFGALILEP
     LLMGAGGMFF VDPLFQRSLI TVVRSNPELV GSTIHPGSQG EGESKTKREP NNQDWSGLPV
     IADEVFTGLY RLGRASSSSF LASPTDVVPS TSTSTQQSTS QLQPQPQPPL PAAIAPDISV
     HAKLLTAGLL PLALTTASEA IFQTFLSSSK TDALLHGHSY TAHPIGCMVA NKALDEYRRM
     DTDGSWDGFR HSWPSSSPSE SDPSSSTPPS ANVYSFWPLP FVTALSHHPR LRGCFALGTV
     LVLKLASEGS GYTSTATSSL QSRLLTLLDS DGCGIHSRVL GDIIYFMTSL TTTQKQVERL
     TKTIMEALNE E
//