ID   A0A165K0T3_XYLHT        Unreviewed;       808 AA.
AC   A0A165K0T3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=PLP-dependent transferase {ECO:0000313|EMBL:KZF26862.1};
GN   ORFNames=L228DRAFT_226683 {ECO:0000313|EMBL:KZF26862.1};
OS   Xylona heveae (strain CBS 132557 / TC161).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC   Xylonales; Xylonaceae; Xylona.
OX   NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF26862.1, ECO:0000313|Proteomes:UP000076632};
RN   [1] {ECO:0000313|EMBL:KZF26862.1, ECO:0000313|Proteomes:UP000076632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC161 {ECO:0000313|EMBL:KZF26862.1,
RC   ECO:0000313|Proteomes:UP000076632};
RX   PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA   Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA   Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The genome of Xylona heveae provides a window into fungal endophytism.";
RL   Fungal Biol. 120:26-42(2016).
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; KV407454; KZF26862.1; -; Genomic_DNA.
DR   RefSeq; XP_018192417.1; XM_018330431.1.
DR   AlphaFoldDB; A0A165K0T3; -.
DR   STRING; 1328760.A0A165K0T3; -.
DR   GeneID; 28895568; -.
DR   InParanoid; A0A165K0T3; -.
DR   OMA; KGWASRA; -.
DR   OrthoDB; 5487177at2759; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000076632; 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:UP000076632};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KZF26862.1}.
SQ   SEQUENCE   808 AA;  89058 MW;  D1F666EEF446E35D CRC64;
     MSQPIGSLLW RSLRAYQVYG ANTDVGKTIF STILAKASKK RRPAENVWFL KPVSTGPLDE
     ADDRHVSRFA QGVSTHCLHQ FEKPISPHLA ALSSAQETPS DSKVLRGIRD HFVECAQAGP
     GFAILETAGG VHSPGPSGAS QADLYRPLRL PVVLIADSRL GGISSSISAY ESLRIRGYDV
     ASVMLFHDAV YQNDDYLRTY FDKQNIPSLS LPFPPERKES LLEDEKSLAT YYEDVSSLPS
     MQDLLSRLDE QHENRINRLQ SMPSRALECI WYPFTQHQLL SPERITTIDS ASGDFFQTST
     LPVKAIDNYT EDSSAPLLKP SFDGSASWWT QGLGHANPEL VLAAAYAAGR YGHVMFAEAV
     HEPALSLAEM VLKYLNNPRM SRVFYTDNGS AGAEVAIKMG LRAARLRYGW SPSDNIEIIG
     LQGSYHGDTM GVMDCAEPSV YNEKVEWYQG RGFWFDYPKI KMANGSWVVE VPENLQQALG
     SGGVHSSLTD IFDVERREHG EEGQRYQQYI IDTLEKLQKQ GRKFGALVME PVILGAGGML
     FADPLFQRML VRVVRENPEL FGTRSNETTT IEGTSNDWSG LPVIFDEVFT GFYRLGRASS
     SAFLGVHPDV SIHAKLLTGG VVPLCVTVAS EPIFNAFDSA EKTDALLHGH SYTAHPIGCK
     VAEKSLQTMN ELDKTGHWDV FKLDWIAPSN IEAESGDIKL HTEECPTGVW SVWSKDFVTS
     LSLHDKVRGV FAIGSVLAIE LQDPSGGGYT STASKELQSA LMTGTLGDAG PRWDIHCRVL
     GNVLYLMASQ MSTPETVREI EALVRASL
//