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Database: UniProt
Entry: A0A0L1JGU8_ASPNO
LinkDB: A0A0L1JGU8_ASPNO
Original site: A0A0L1JGU8_ASPNO 
ID   A0A0L1JGU8_ASPNO        Unreviewed;       770 AA.
AC   A0A0L1JGU8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Onanonoxo-7-onima-8-eninoihtemlysoneda {ECO:0000313|EMBL:KNG90976.1};
GN   ORFNames=ANOM_000669 {ECO:0000313|EMBL:KNG90976.1};
OS   Aspergillus nomiae NRRL 13137.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG90976.1, ECO:0000313|Proteomes:UP000037505};
RN   [1] {ECO:0000313|EMBL:KNG90976.1, ECO:0000313|Proteomes:UP000037505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG90976.1,
RC   ECO:0000313|Proteomes:UP000037505};
RA   Moore M.G., Shannon B.M., Brian M.M.;
RT   "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL   Submitted (JUN-2014) 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:KNG90976.1}.
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DR   EMBL; JNOM01000007; KNG90976.1; -; Genomic_DNA.
DR   RefSeq; XP_015411899.1; XM_015545927.1.
DR   AlphaFoldDB; A0A0L1JGU8; -.
DR   STRING; 1509407.A0A0L1JGU8; -.
DR   GeneID; 26802473; -.
DR   OrthoDB; 5487177at2759; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000037505; 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; 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   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; 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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037505};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   770 AA;  84725 MW;  C363DC81676B29F7 CRC64;
     MSPVGAALWR SLRAHQVYGA NTDVGKTIVS TVLCNAVQRQ KSQDQAAFLK PVSTGPLDDA
     DDRHIQRHAA GTLTKCLYQF DEPVSPHIAA QQKKFTVPRD DDILASVHKT LSDWAGSGVN
     FALVETAGGV HSPGPNGNSQ ADLYRPLRLP IVLVADSRLG GISSSISAYE SLLLRGYDIH
     SVLLFRDEYY KNHEYLLNYF QKKSIPLVPL PSPPPKPSVQ DVDSLARDEE AMTTYYGRVA
     QETDVASLLE QLSAKNAERI DRLESMASRA HDTIWYPFTQ HHAWRPRISH RLTLPMMTTF
     KRLGHGNPSL ALSAAYAAGR YGHVMFPGNI HEPALSLAEL LLESIGNPRL RKVFYTDNGS
     TGMEVAVKMG LRAACDRYGW DASQEQISIL GLKGSYHGDT IGVMDCSEPS TYNKKVEWYR
     GRGYWFDFPQ VKMSQGMWKV EIPENLRESL GSGFEFSSLD DIFDMEERLQ SAAGKRYTEY
     IRNTIQDLVQ QEGMKFGSLI MEPIILGAGG MLFCDPLFQR CLVEVVRGYP ELFGASGAKS
     TKDHPVATSW SGLPVIFDEV FTGLYRLGRK SSASFLQVDS DIAVNAKLLT GGLLPLCTTM
     ASDEIFQAFS SPEKSDALLH GHSYTAHAVG CQVAVDSLQT MMRMENSGSW DGYRQDWTTL
     SDTPVTLGAR DSSNIWSVWS HGLVSDLSHA PSVDGVFAIG TVLSISLKDV QGGGYTSTAA
     RGLQQRLSTS DGKFNVHSRV LGNVLYLMSS VTSQPQALRS IEGVLREALL
//
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