ID Q5K7Y0_CRYNJ Unreviewed; 867 AA.
AC Q5K7Y0; Q55IE1;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN OrderedLocusNames=CNM00900 {ECO:0000313|EMBL:AAW46800.1};
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684 {ECO:0000313|EMBL:AAW46800.1, ECO:0000313|Proteomes:UP000002149};
RN [1] {ECO:0000313|EMBL:AAW46800.1, ECO:0000313|Proteomes:UP000002149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565 {ECO:0000313|Proteomes:UP000002149};
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J., Koo H.L., Krzywinski M.I., Kwon-Chung J.K.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017353; AAW46800.1; -; Genomic_DNA.
DR RefSeq; XP_568317.1; XM_568317.1.
DR AlphaFoldDB; Q5K7Y0; -.
DR STRING; 214684.Q5K7Y0; -.
DR PaxDb; 214684-Q5K7Y0; -.
DR EnsemblFungi; AAW46800; AAW46800; CNM00900.
DR GeneID; 3255288; -.
DR KEGG; cne:CNM00900; -.
DR VEuPathDB; FungiDB:CNM00900; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_6_0_1; -.
DR InParanoid; Q5K7Y0; -.
DR OMA; WTYVNEA; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000002149; Chromosome 13.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 4.10.450.10; Glucose Oxidase, domain 2; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR027424; Glucose_Oxidase_domain_2.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF218; GMC_OXRDTASE_N DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968}; Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002149};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..867
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004258133"
FT TRANSMEM 706..729
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 135..158
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 332..346
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 810..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 867 AA; 92172 MW; F5B086A12FA3E294 CRC64;
MLAPLALLPL LSLMLPQASA DTRPGSLPHN LHHPYRRSLK RSITSDASSI NGESFDFVIA
GGGVAGLTLA ARLSEWSNVT VLCIEAGGDG SNYEDQIDIP GYSYLNSLTG TAYDWAYNTV
PQTDALDLTK YWPRGKGLGG SGAINGLFWG RASSIEYDAW ATLNPNGNET WNWEEVNKYI
KKSENLTAPP TDIQEKFGIV VNASAHGDDG PIQIGFSEYI FDEVAKWIPT WETLGLSGKD
LAGGSTHGAM ISTSTINMRN QTRSDSKAGY IDPLPPRSNL VILTEQQVTG VIFNGSTDAS
GNIVASGVTF QANSNSANYS VQANKEVLLA GGTVGSPQIL QLSGIGPKDL LSSLGIDTKI
DLPVGYNLQD HVSYSMYWST PQGTLTWSNL SASSTLQSEQ LAQYKSNFTG MWTYVNEAVG
YPSMSDIMQS SSSASTYAST VSSAIDGMVT NVTSWLDLPD TVATGLTSQY QIQQQWLTED
IGQLEIVLTL LGNGGNELGI QVALQHPFSR GTIFINSTDP FTQPNINPDY FGVGYDIDIM
AYGSEFARRL AAASPLSDVM ITETAPGSSV TGDSLATYTK QNCGTEYHPL GTCSMLPKNS
GGVVDTTLTV YGTSNLRVID TSIAPLQLSA HLMATTYGIA EKGADIIKKK YWYVDPVTSS
SATVAAATTS TEATTAAVGD ATDTAVTNIN QNNAESGSTL SSGAKIGIGV GVGVGAAAVL
AGLLLFFVMR KRNQKEDEKG WYGDRQEGWN PDAGDAYKEP GSAYPMADFD SHNSYASPTP
AFIGNHSRNQ SINTIATADL ASRTPMRNSS SFSYAAGGPG VGRTASPYRD DMSDDGNGQG
HVYQAPEAPA GQQATRGEQR YQPVNIR
//
