ID   D2VZR5_NAEGR            Unreviewed;       538 AA.
AC   D2VZR5;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC37745.1};
GN   ORFNames=NAEGRDRAFT_74589 {ECO:0000313|EMBL:EFC37745.1};
OS   Naegleria gruberi (Amoeba).
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN   [1] {ECO:0000313|EMBL:EFC37745.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC37745.1,
RC   ECO:0000313|Proteomes:UP000006671};
RX   PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA   Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA   Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA   Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA   Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT   "The genome of Naegleria gruberi illuminates early eukaryotic
RT   versatility.";
RL   Cell 140:631-642(2010).
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}.
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DR   EMBL; GG738915; EFC37745.1; -; Genomic_DNA.
DR   RefSeq; XP_002670489.1; XM_002670443.1.
DR   AlphaFoldDB; D2VZR5; -.
DR   STRING; 5762.D2VZR5; -.
DR   EnsemblProtists; EFC37745; EFC37745; NAEGRDRAFT_74589.
DR   GeneID; 8857622; -.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_74589; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   InParanoid; D2VZR5; -.
DR   OrthoDB; 3382025at2759; -.
DR   Proteomes; UP000006671; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 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   Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          132..155
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          330..344
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
SQ   SEQUENCE   538 AA;  61179 MW;  8815DDB80588FB68 CRC64;
     MSILGTLFRT TLFLLFSLFL IFTFLYSHVW FPDRLSEQHE RFQNHQDPKE FDFIIVGSGS
     AGSVLANRLS QNVNHSVLLL EAGKSDNTPL AKFTPLYLFM LKSVHDWQYY TIGEESEINP
     KHLLKKMFWP RGKILGGSSS MNAMIYMRGS PQDYDTWNEC EFGGKSKIWN FEHVLKYFKK
     SEAQQGPAEI FSDEYHGRNG EWIVKEQGET FSIIEPVVKA MSQVLSIPIV RDLNNPKITH
     SKDNSQSDFV EYGAVGTTQI HSLHGRRFST ADAFLNDTVL KRPNLFVRTE ALATNILFEG
     NKAVGVRYFD RRKKAYVEKR VRKEVILSGG AINSPQLLML SGIGDSKELS KHNITTIVDN
     KNVGKHLHDH LAIHVPYYIS WDYDSVLSVL FKPNEIYKVL FEGSGVLGTN GIGLNGLLKT
     KVCKNELVNS YPPSLWDVKN QQCYNKHHCD SHDIQVHNTP TVMENSETLH LHQHGFTFIP
     LLLQPKSRGG LKLKSNNPFV APIIDSNFVG HKHDKETMAE AIRSASLDGY YQELANRN
//