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Database: UniProt
Entry: E3QTB3_COLGM
LinkDB: E3QTB3_COLGM
Original site: E3QTB3_COLGM 
ID   E3QTB3_COLGM            Unreviewed;       834 AA.
AC   E3QTB3;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:EFQ34101.1};
GN   ORFNames=GLRG_09245 {ECO:0000313|EMBL:EFQ34101.1};
OS   Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS   anthracnose fungus) (Glomerella graminicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN   [1] {ECO:0000313|Proteomes:UP000008782}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
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DR   EMBL; GG697376; EFQ34101.1; -; Genomic_DNA.
DR   RefSeq; XP_008098121.1; XM_008099930.1.
DR   AlphaFoldDB; E3QTB3; -.
DR   STRING; 645133.E3QTB3; -.
DR   EnsemblFungi; EFQ34101; EFQ34101; GLRG_09245.
DR   GeneID; 24414610; -.
DR   VEuPathDB; FungiDB:GLRG_09245; -.
DR   eggNOG; KOG2844; Eukaryota.
DR   HOGENOM; CLU_007884_11_2_1; -.
DR   OrthoDB; 1815533at2759; -.
DR   Proteomes; UP000008782; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1.
DR   Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR032503; FAO_M.
DR   InterPro; IPR013977; GCV_T_C.
DR   InterPro; IPR006222; GCV_T_N.
DR   InterPro; IPR029043; GcvT/YgfZ_C.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR13847:SF181; TRANSFERASE CAF17, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16350; FAO_M; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF103025; Folate-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008782}.
FT   DOMAIN          6..369
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          373..427
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          430..710
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          735..812
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   834 AA;  90405 MW;  26E6DD1BE4A48533 CRC64;
     MDRSQRVVII GAGIVGTNIA DELVSRGWTD ITVVEQGPLS MPGGSTSHAP GLVFQVTGSK
     TMSSFAKYTV QKLLSIGCFN QVGGLEVAET PQRLEELKRK HGYASSWGIP AHLLTADECK
     TLYPLLSTEV VLGGLHIPTD GLALAANAVQ LLIERTRKAG VRYLEHTPVT GIAQSGGRVT
     GVETRNGPVP ADLVLACAGL WGVEVGAMVG LPIPLLPVEH QYVKTTPVPV QKGKNLPVNG
     AQFPILRHQD RDLYYREHGE QYGIGYYGHR PLPVVAASLG ETPKHVDEHN MPSRRDFTPD
     DFAPAWELSK KLLPALAESE IEYGFNGIMS FTPDSGPLIG RAPNLEGFFV AEAVWVTHSA
     GVARAVAQLL TAGHSELDLS ECDISRFEQV QLAPEYVKEV STQNFIEVYD ILHPSQPRES
     PRNLRISPFH SRQQELGAYF LEAGGWERPQ WFEANANLLS QLPEKWKPRE RDAWSARYHS
     PIAAAEAWKT RTAVAMYDLT PIRRLEVSGP GAVELLQRLT TSDISKSPGT VTFTLLLDGH
     GGIRSDIFVA RLGNDLFQLA VNGPVDFAYL SREARIQAEA SPAKFVQVRD TTGGSGGIGL
     WGPRAADVIG GISSDNLKDM PPSRVKSAII AGIPVTVVSL SFVGEPGWEI YTSAENSLRL
     WDTLWQAGKP HGVIAAGRAA FSALRLETGF RTYGADVTSE HNPFEAGLES AVDPEKQGYV
     GHDAIKRLSK EKVSRRLRCL TIDDGRSVVL GKEPVFLDGK AVGYVTTAAF GYTIGKPIAY
     THLPSSVKEG AGVEIEYFGR RIKATVTAEP LHKASRGVSV AGPTPKRVAI RSRL
//
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