ID D2V9N7_NAEGR Unreviewed; 643 AA.
AC D2V9N7;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC46616.1};
GN ORFNames=NAEGRDRAFT_65503 {ECO:0000313|EMBL:EFC46616.1};
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:EFC46616.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC46616.1,
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 ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; GG738858; EFC46616.1; -; Genomic_DNA.
DR RefSeq; XP_002679360.1; XM_002679314.1.
DR AlphaFoldDB; D2V9N7; -.
DR STRING; 5762.D2V9N7; -.
DR EnsemblProtists; EFC46616; EFC46616; NAEGRDRAFT_65503.
DR GeneID; 8859854; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_65503; -.
DR eggNOG; KOG1238; Eukaryota.
DR InParanoid; D2V9N7; -.
DR OMA; ECARGKV; -.
DR OrthoDB; 3382025at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
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 InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 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|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT DOMAIN 124..147
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 340..354
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 126
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 298
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 643 AA; 72975 MW; E0A2B1DF4A6808C4 CRC64;
MLKLLITSSL IVIISFLYLF YQQYIKVENR FEKYHSDPTL SNITDFDYVI IGAGTAGSVL
SSRLSENPKI KVLVLESGVS NNDLIGIHFP LGFPKFTMNT SIDYDYKTIS QPQLRNREIY
MPRGKVIGGS SSVNANLYIR GHPLDYNEWN YLLFNNTSKN GNLSWSYKDM LKYFKKSEKH
LSKNINRKYH GTDGKWKIKH TKDIIEEIGP LVNFNLTSVI INSLSNGLNI PIRDDPNELL
PNEEELLEKG EGHSILESVS YHHHSIDENG RRHSLAEAFL DLETLKRPNL QIRTECIVKR
ILFTKNGKNE NVASGVEYLN KRTNQLIKIN VRKEVISSAG SIASPQILMV SGIGDKEELK
KFNIPIISNL KGVGKNLHDH LLGAVIGKLK EGYTSLHSYE SLWNLLQWIM QSSFNFLEFS
MVRKLFPAAI PNSWKLFNVG APHIQGFFKS KYAKENNQPY DLQIVSVPGF FVHHASIEYP
GENGISIGVV NLQPKARGYI SLRSNDTNDS PIIHGNYFGN EQDIKVLVDG ISQIQKTFLQ
EPFKSMVKEF IFCSPHDYKT HDEIRECLTQ MFTTLYHPTS TCKMGSENDE MSVVDEYCKV
RGVKNLRVVD ASIMPNVPRG NTNAPTAAIA EKAAEMILNE WNL
//
