ID A0A1V6SR83_9EURO Unreviewed; 808 AA.
AC A0A1V6SR83;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Dethiobiotin synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENFLA_c028G10836 {ECO:0000313|EMBL:OQE16260.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE16260.1, ECO:0000313|Proteomes:UP000191342};
RN [1] {ECO:0000313|Proteomes:UP000191342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE16260.1}.
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DR EMBL; MLQL01000028; OQE16260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6SR83; -.
DR STRING; 254877.A0A1V6SR83; -.
DR OrthoDB; 5487177at2759; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000191342; 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:UP000191342};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 808 AA; 88549 MW; F7EEE65F3CAAFBAD CRC64;
MQVDSAEVSF GLHRDSLQLH HIMPPVGAAL WRSLRAHQVY GANTDVGKTI ISTVLCNAVQ
RQKQQAAFLK PVSTGALDDA DDRHLQRYGA GTLTKCLYQF DDPVSPHLAA KDKFVPRDDD
LLASIHSTLS GWARSNIDFA LVETAGGVHS PGPNGNSQAD LYRPLRLPIV LVADSRLGGI
SSSISAYESL LLRGYDISSV LLFRDEYYQN HEYLRDYFQK KSIPLVSLPA PPARPSQLDA
DSQLRDEEAM LSYYRKSAEE SEILQLLEEM SVNNTERVQR LEEMADRAQD LIWYPFTQHQ
GMKAKDITVI DSAHDDYFQT FGSTTSKDTQ SELRPTFDGS ASWWTQGLGH GNPELSLSAA
YAAGRYGHVM FAGAVHEPAL ALADNLLKTI ENPRLTKVFY TDNGSTGMEV AVKMGLRASC
DRYGWDASQE QIGILGLKGS YHGDTIGVMD CSEPSTFNKK VEWYRGRGHW FDFPLVKMVG
GSWKVEIPSE LQAELGEDVD FASLGSVFDL SQRLESATAQ RYKDYIRRTI EDLVQRQGAK
FGALILEPVI LGAGGMLFCD PLFQRCLTDV VRDHPELFST NAPAPKQSPS WSGLPVIFDE
VFTGLYRLGR RTSASFLGVH PDVAVNAKLL TGGLVPLCTT VASEEIFDAF SSTEKSDALL
HGHSYTAHAV GCTVAVDSLK TMAQLDTDGS WDAYRADWCS SSPTAAAAST PDVWSVWSHG
LLQDLSSADS VESVFAIGTV LSISLRDAAG GGYNSNASKG LQQKLAVGGD QFNVHSRVLG
NVLYLMSSVT SKPESLREME RLLRSALV
//
