ID   R7Z2K3_CONA1            Unreviewed;       833 AA.
AC   R7Z2K3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=N,N-dimethylglycine oxidase {ECO:0000313|EMBL:EON68397.1};
GN   ORFNames=W97_07721 {ECO:0000313|EMBL:EON68397.1};
OS   Coniosporium apollinis (strain CBS 100218) (Rock-inhabiting black yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Coniosporium.
OX   NCBI_TaxID=1168221 {ECO:0000313|EMBL:EON68397.1, ECO:0000313|Proteomes:UP000016924};
RN   [1] {ECO:0000313|Proteomes:UP000016924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 100218 {ECO:0000313|Proteomes:UP000016924};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Gorbushina A., Noack S., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The genome sequence of Coniosporium apollinis CBS 100218.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
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DR   EMBL; JH767596; EON68397.1; -; Genomic_DNA.
DR   RefSeq; XP_007783714.1; XM_007785524.1.
DR   AlphaFoldDB; R7Z2K3; -.
DR   STRING; 1168221.R7Z2K3; -.
DR   GeneID; 19905032; -.
DR   eggNOG; KOG2844; Eukaryota.
DR   HOGENOM; CLU_007884_11_2_1; -.
DR   OMA; PMKHAYI; -.
DR   OrthoDB; 1815533at2759; -.
DR   Proteomes; UP000016924; 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; IPR028896; GCST/YgfZ/DmdA.
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; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 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:UP000016924}.
FT   DOMAIN          11..378
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          382..437
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          440..723
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          748..825
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   833 AA;  90929 MW;  14D2E3B061CA1686 CRC64;
     MGSIAAPSPP RVVIIGAGIV GTNLADELVS RGWTDISVID QGPLDMPGGS TSHAPGLVFQ
     TNPSKTMTLF AKYTVEKLLS LEWDGESCFN QVGGLEVATT PARLEELKRK HGYAASWGVD
     ARLIGAEECL KIYPNLNKDM VLGGLHIPSD GLALAASAVQ RLIARTREAG VRYLGSTPVT
     GIERAEGHVT GVMTPNGTVP ADIVVSCAGF WGVEVGAMVN LPIPLLPLAH QYVKTTAVPA
     LAGRNPRPNG ASLPILRHQD QDLYYREHGD QYGIGYYGHK PMPVVAASLG LTPEHVDGKN
     MPSRLEFTPE DFDPAWKESQ KFLPALQGTE IADGFNGIFS FTPDGGPLVG QAPHLDGFYV
     AEAVWVTHSA GVARALAEVL TTGRSKIDLA DCELSRFEEV QLAPEYVKET AQQNFVEVYD
     ILHPLQPRES PRGLRVSPFH ARQHELGAFF LEAGAWERPY WYEANERLVK DLPMEWQPVE
     RDAWSSRYYS PIAAVEAWKT RTAVAMYDMT PLRRLEVSGP GAVDLLQRLC TGDVSKKPGA
     VTYTLFLNEH GGVRSDLTVA RIEDELFQVG VNGPVDTAYV TRAARLQSRQ TPNRWVQVRD
     ITGGTCCIGL WGPRARDVIT SVSADDFTNK GLRFFRCNKA NIAGIPVTAM RLSYVGELGW
     EIYTSADRGQ ALWDVLWKAG QPHGMVAAGR SAFNALRLEK GYRSWGADMT TEHDPYEAGV
     GFAVKAGKEG YVGRVALEGR SEKTAAQRLR CLTVDDSRSV VLGKEPVFHN GKSIGYVTSA
     AFGYTIRKPV AYAYLPSTVV EGDSVEIEYF GRRIPATVTP EPLYDPDMSR LRG
//