ID   A0A066XXF9_COLSU        Unreviewed;       964 AA.
AC   A0A066XXF9;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Putative dethiobiotin synthase {ECO:0000313|EMBL:KDN72379.1};
GN   ORFNames=CSUB01_00062 {ECO:0000313|EMBL:KDN72379.1};
OS   Colletotrichum sublineola (Sorghum anthracnose fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN72379.1, ECO:0000313|Proteomes:UP000027238};
RN   [1] {ECO:0000313|Proteomes:UP000027238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX   PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA   Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT   "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT   of cultivated sorghum.";
RL   Genome Announc. 2:E0054014-E0054014(2014).
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:KDN72379.1}.
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DR   EMBL; JMSE01000001; KDN72379.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A066XXF9; -.
DR   STRING; 1173701.A0A066XXF9; -.
DR   eggNOG; KOG1401; Eukaryota.
DR   HOGENOM; CLU_010794_0_0_1; -.
DR   OMA; KGWASRA; -.
DR   OrthoDB; 5487177at2759; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000027238; 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; 3.40.50.300; 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; IPR049704; Aminotrans_3_PPA_site.
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   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; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027238};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          844..863
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..66
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   964 AA;  104972 MW;  3BBDAC274C8DBD44 CRC64;
     MQDPCRDEPA NRPNPTSSGP HRWEARRRDT PGFSARQIPH SPGSPPVYNA GEAAEEEEEG
     DEEATDGFLS EPNWAAIQAA YSYFKGHTAH LERQLDIAID QPTRPMAPVG ALLWRSLRTY
     QIYGANTDVG KTVFASVLCN AARTFWPREQ TAFLKPVSTG PAAEADDRCS VVVVLSLISR
     SLSSHIERFA PAVAKKTLFQ FEIPASPHLA AEASDQVNES PVLSPSHTVA GSFFANEHLP
     KPVPKNSQVL RSIYDYASRR AAEGPGWLFI ETAGGVHSPA PSGTPQADLY APLRVPVVLV
     GDAKLGGISQ TISAFESLQL RGYDVESILL FRDDYYQNHA YLSDYFARDR GIPVGVLHRP
     PSRAEDVEVD ADAMARYYRE TAPSRVVKNT LEHLHDRHLA RVSRLETMAR DAHGTIWYPF
     TQHKGLTPDK ITVIDSAHGD DFQTLVPAAS NSSSSSSSRA LLQPSFDGSS SWWTQGLGHA
     NPELTLAASY AAGRYGHVMF ASAVHEPALA LAQALLRGLR NPRLTRVFYS DNGSTGMEVA
     VKMGLRAARV RYGYGTAAAG DRLEVLGLRG SYHGDTMGAM DSTEPSVFND KVEWYDGKGF
     WFDYPSVVCK DGRWHVCVPE ALRGDLGGDD RAFGALSEVF DVVGREEAPR QEARLYEKYI
     VKTLRRLRDQ GRKFGALVME PVVLGAGGMI MADPLFQRTL VKVVRRHPEL FGTACHDPPS
     AETTDANGWT GLPVVFDEVF TGLGRLGRMS AASFLGVHPD VVVNAKLLTG GLVPLCTTTA
     SDSIFRAFES DEKSDALLHG HSYTAHPVGC QVALKSLQEL QRMDEAGGEW DWAKTGGWAV
     PVASDTRASQ SGSSSSSGST SPVWSVWSHS FVDWVSRQTG RVDGVWALGS VLAIHMRDSE
     GAGYSSTAAA DVQSGLLRGE DGPGGARWNV HSRVLGNVLY VMTSQTTRQE DVQRLETLLR
     RVLG
//