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Database: UniProt
Entry: F9XNC5_ZYMTI
LinkDB: F9XNC5_ZYMTI
Original site: F9XNC5_ZYMTI 
ID   F9XNC5_ZYMTI            Unreviewed;       791 AA.
AC   F9XNC5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGP83538.1};
GN   ORFNames=MYCGRDRAFT_111308 {ECO:0000313|EMBL:EGP83538.1};
OS   Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS   fungus) (Septoria tritici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP83538.1, ECO:0000313|Proteomes:UP000008062};
RN   [1] {ECO:0000313|EMBL:EGP83538.1, ECO:0000313|Proteomes:UP000008062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX   PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA   Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA   Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA   Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA   Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA   Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA   van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA   Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA   Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA   Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA   Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA   de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA   Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT   "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT   reveals dispensome structure, chromosome plasticity, and stealth
RT   pathogenesis.";
RL   PLoS Genet. 7:E1002070-E1002070(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; CM001206; EGP83538.1; -; Genomic_DNA.
DR   RefSeq; XP_003848562.1; XM_003848514.1.
DR   AlphaFoldDB; F9XNC5; -.
DR   STRING; 336722.F9XNC5; -.
DR   EnsemblFungi; Mycgr3T111308; Mycgr3P111308; Mycgr3G111308.
DR   GeneID; 13396252; -.
DR   KEGG; ztr:MYCGRDRAFT_111308; -.
DR   VEuPathDB; FungiDB:ZTRI_11.366; -.
DR   eggNOG; KOG1401; Eukaryota.
DR   HOGENOM; CLU_010794_0_0_1; -.
DR   InParanoid; F9XNC5; -.
DR   OMA; KGWASRA; -.
DR   OrthoDB; 5487177at2759; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000008062; Chromosome 11.
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   NCBIfam; TIGR00347; bioD; 1.
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:UP000008062};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   791 AA;  86912 MW;  79CF5F4A6953CB12 CRC64;
     MRHVGSVLWP KLRVLQVYGA NTGVGKTIFS SVLIRAFKKR LQNVNYLKPV STGPLDEADD
     HHIARLGSNV SSRCLFQFDD PVSPHLAVRS AGKPISDAAV LEAVYGELNG YADGKDRIAI
     VETAGGVLSP APSGSSQADL YRPLRLPTIL IGDHNLGGIG TTISAWESLH IRGYDVTSVA
     LFSGDRYENH VYLKDYFKER GVASFSIPPP PERHADAEED LKAMQYYYDK SSGDAGVADF
     TRDFIEAHDK RIAYLRSMPE QADKVIWHPF LQHTERSKYT ITAWDSAYGD HFQSYTIKSD
     QAKLDSAEQE QSLLKPAFDG SASWWTQGLG HGNPKLALTA ANAAGRYGHV MFGGAVHQPA
     LELAKTVVKE SSNPRLSKVF YSDNGSTGME VAVKMALRAM MVRHKPREPR KTELSILGLK
     NSYHGDTIGT MDCSEPSIFN EKVEWYRGRG LWLDFPTVKM RKGQWIVEPF DSSRETRQFD
     SLNDVFDFSN READCKQYKK YILDTISETV KKERLNLGAL IIEPILLGAG GMMFADPLYQ
     KCLVEVAREL QFARQDGPKA GSHGGSSGSP LDWQGLPVIF DEVFTGLYRL GRFSSGSFLG
     VEPDIVVNAK LLTGGLLPLC TTTASESIFE AFLSEDKTDA LLHGHSYTAH PMGCSVANES
     LRTLMTLDRG GSWTDYKKDW SPTTSTNSPN NQHAWSMWSL SFVSAISHKE QVDNVFAIGS
     VLAITVKDPA GSGYASTAAT GLRDRLLAGN GNDEAVIHSR VLGNVLYLMS APTTPAETIA
     DIEKTVTEAL E
//
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