ID C1GMH0_PARBD Unreviewed; 834 AA.
AC C1GMH0;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Dethiobiotin synthase {ECO:0000313|EMBL:EEH43636.2};
GN ORFNames=PADG_08456 {ECO:0000313|EMBL:EEH43636.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH43636.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH43636.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH43636.2,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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; KN275974; EEH43636.2; -; Genomic_DNA.
DR RefSeq; XP_010763778.1; XM_010765476.1.
DR AlphaFoldDB; C1GMH0; -.
DR STRING; 502780.C1GMH0; -.
DR GeneID; 22586742; -.
DR KEGG; pbn:PADG_08456; -.
DR VEuPathDB; FungiDB:PADG_08456; -.
DR eggNOG; KOG1401; Eukaryota.
DR HOGENOM; CLU_010794_0_0_1; -.
DR InParanoid; C1GMH0; -.
DR OMA; KGWASRA; -.
DR OrthoDB; 5487177at2759; -.
DR Proteomes; UP000001628; 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; 3.90.1150.10; 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 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 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 4: Predicted;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000001628};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 834 AA; 92305 MW; A634F293BEA00B46 CRC64;
MARAGAFLSR HLLTYQVYGA NTNVGKTIFS SLLYRAHTVS NPKANHWYLK PVSTGPDCER
DDRHISRFAR HVSCKCLYTF DRPVSPHIAA IGKKCPNDRE IIEAVSQTLN GWAQHGQGLA
LVETAGGVLS PGPNGTPQSD VYRPLRLPVI LIADSKLGGI SSSIAAYESL VLRGYDIDAV
AVLEDNYYQN HEYLEDFFAS KKSIPVLVFS QPPEKKLTSN GYPAENDEEA MSKYYEQQVE
KLVTENHSPL SGFLDGLSEK HHSRISELEA MPSKAHSSLW YPFTQHKSIT SGDIMVIDSA
YGDCFQTLKG NSTNLCSNST TSNITPAQTD TPNLLRPTFD GSASWWTQCL GHGNPELSLE
AAYAAGRYGH VIFPSAVHKP ALSLAEALIK MMDNPRLTRV FYSDNGSTGM EVAVKMALRA
ACKRYQWDSS KDDIEILGLR GSYHGDTIGT MDLSEPSIYN KRVEWYRGRG HWFDFPTVKM
VRGRWIVQTP AGLKEALGPD AEFSTLQSIF DLDQRRSSEA SGRYKIYIKK IIENLTLRDG
RKFGALIMEP VILGAGGMLF VDPLFQQSMV DVVRENPALF GQGQTTQRSR HHNTWSGLPV
IFDEVFTGLY RLGRVSSSSF LDTHPDISVH AKLLTGGLLP LCVTLAGQDV FEAFCSPHKA
DALLHGHSYT AHPVGCKVAE ASLRMLSTAD AERHRKIQQR NQKHGDPLTA AGDMDRALNR
VIDQMTDPQG QQQQSRQVWS SWSEELVRDL SHSEQVEGVF AIGTVISISL RNQDGGGYDS
NAASGLQRRL SETNPDGFNI HCRVLGNVLY LMCDLTSDLD ELAMVNKALR SALL
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