ID D2V6C0_NAEGR Unreviewed; 530 AA.
AC D2V6C0;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC47543.1};
GN ORFNames=NAEGRDRAFT_31574 {ECO:0000313|EMBL:EFC47543.1};
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:EFC47543.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC47543.1,
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 class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|RuleBase:RU003691}.
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DR EMBL; GG738854; EFC47543.1; -; Genomic_DNA.
DR AlphaFoldDB; D2V6C0; -.
DR STRING; 5762.D2V6C0; -.
DR EnsemblProtists; EFC47543; EFC47543; NAEGRDRAFT_31574.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_31574; -.
DR eggNOG; KOG4716; Eukaryota.
DR InParanoid; D2V6C0; -.
DR OMA; KWVNTEA; -.
DR OrthoDB; 5473641at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR046952; GSHR/TRXR-like.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
DR NCBIfam; TIGR01438; TGR; 1.
DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR PANTHER; PTHR42737:SF3; THIOREDOXIN-DISULFIDE REDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT DOMAIN 16..382
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 402..513
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 530 AA; 58732 MW; B53D4D3A12719417 CRC64;
MNLGGATNKQ EIPAHFDYIV IGGGSGGLSL SKQLSSLSSK ETRICLLDYR DPSSQWLRER
NGKLNGWMWQ LGGTCVNVGC IPKKLMHNSA LIGEGINHDA EYFGWNDGKQ EGKLSGKHDW
KTLVANVQQY IKSLNFGYRT SVTQTYAFDN EDPSLKKLYY LNMKGRFVDD HTLELTDPRK
GITKTISGKV IILSVGGTPN IPQDVPGATE YAITSDDIFS LKEEPGKTLV IGASYIALET
ASFLKGLGYE SSVMMRSIPL RGFDQECAWK VVDGMKERGV KFLEQCIPVK IEKSSDHETT
GEYTVHYKDL STQQVYTENY KTIMFAVGRR AVTKELNIDL DMDESGKIIV SDNEQTSKKH
IYAIGDCINK KTELTPVAIR AGKLLASRLT NKGTELMDYD NVPTSIFTHP YEYGCCGLSE
EEAVQRYGED DIEVYISLYS PIEHQLSHRD TNKTFMKIIT LKSANEKVIG FHYVGANAGE
ITQGIAVAIK AGATKEHFDN TIGIHPTAAE EMTLLSITKR SGNSAEKDGC
//