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Database: UniProt
Entry: A0A1S8W5P9_9FUNG
LinkDB: A0A1S8W5P9_9FUNG
Original site: A0A1S8W5P9_9FUNG 
ID   A0A1S8W5P9_9FUNG        Unreviewed;       717 AA.
AC   A0A1S8W5P9;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Dethiobiotin synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BSLG_01244 {ECO:0000313|EMBL:OON09792.1};
OS   Batrachochytrium salamandrivorans.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC   Rhizophydiales incertae sedis; Batrachochytrium.
OX   NCBI_TaxID=1357716 {ECO:0000313|EMBL:OON09792.1, ECO:0000313|Proteomes:UP000189906};
RN   [1] {ECO:0000313|EMBL:OON09792.1, ECO:0000313|Proteomes:UP000189906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS {ECO:0000313|EMBL:OON09792.1,
RC   ECO:0000313|Proteomes:UP000189906};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) 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:OON09792.1}.
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DR   EMBL; LYON01000113; OON09792.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S8W5P9; -.
DR   VEuPathDB; FungiDB:BSLG_01244; -.
DR   OrthoDB; 5487177at2759; -.
DR   Proteomes; UP000189906; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
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   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
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   4: Predicted;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189906};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   717 AA;  78932 MW;  F5B4A6018491DEC4 CRC64;
     MPLHHCNRHV RMFCPSAIAE TLVTYTEPAS PHLTAIQEKR WITDDELRQR IVSALEKYSG
     ILNGRAGFSI IETAGGVHSP SMSGSLQSDV YRTFRFPIVL IGDSQLGGIS TTLTAYESLR
     MRGYDIPCVV MLDNPRYKNQ DIIQKHLDKE TAVFVIPAPP PLPVNMGMPE SDLDKTQMAA
     YYESIDALSS EMAVYVHDSH MARLNRINSM AMTGESKLWW PFTQHGTIKS TLVIDSAFGD
     DLTVFNPALQ QSQQLFDACG SWWTQGVGHG HVRLAKAASY AAGRYGHVIF PESVHEPAMK
     LAERLLDTSG KGWASRVFYT DDGSTAIEVA LKMAFKTTVT AQKLDKPKLD IVGVRGSYHG
     DTIGAMNASD PNVYNQQVDW YTGRGVWFDP PTVVLKNGQY HIRLPESISA HVKKVANASN
     VNNLETTQIH SRDDVFDICR NGSPLALAYR SYIETVLDQG ERQGRVFGAL LIEPILMGAG
     GMLWVDPLFQ RELVLTVRQR SPQAPMPVIF DEIFVGMYRL GFASPGCSLL HVYPDIACYA
     KCLTGIVPLA ATLARESVFG AFRGESKIDA LLHGHSFTAH PVGCQVAVES INLLEGLVSK
     AATIDKRLPD GSVQSKQVVP CVWDGEILTR ISALKCVDGV VPIGTVLAIE LSASEKGYAS
     HVSSDIVQKL RSDTNINIFT RPLGNVIYFM ATHETPAESI QHVLKHLHQQ LLKQSQS
//
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