ID B0WA74_CULQU Unreviewed; 242 AA.
AC B0WA74;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000256|ARBA:ARBA00012228, ECO:0000256|HAMAP-Rule:MF_03159};
DE EC=5.1.99.6 {ECO:0000256|ARBA:ARBA00012228, ECO:0000256|HAMAP-Rule:MF_03159};
DE AltName: Full=NAD(P)HX epimerase {ECO:0000256|HAMAP-Rule:MF_03159};
GN Name=6035415 {ECO:0000313|EnsemblMetazoa:CPIJ004022-PA};
GN ORFNames=CpipJ_CPIJ004022 {ECO:0000313|EMBL:EDS40903.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS40903.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS40903.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ004022-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ004022-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- FUNCTION: Catalyzes the epimerization of the S- and R-forms of
CC NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or
CC heat-dependent hydration. This is a prerequisite for the S-specific
CC NAD(P)H-hydrate dehydratase to allow the repair of both epimers of
CC NAD(P)HX. {ECO:0000256|HAMAP-Rule:MF_03159}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-NADHX = (6S)-NADHX; Xref=Rhea:RHEA:32215,
CC ChEBI:CHEBI:64074, ChEBI:CHEBI:64075; EC=5.1.99.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000013, ECO:0000256|HAMAP-
CC Rule:MF_03159};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-NADPHX = (6S)-NADPHX; Xref=Rhea:RHEA:32227,
CC ChEBI:CHEBI:64076, ChEBI:CHEBI:64077; EC=5.1.99.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000909, ECO:0000256|HAMAP-
CC Rule:MF_03159};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03159};
CC Note=Binds 1 potassium ion per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_03159};
CC -!- SIMILARITY: Belongs to the NnrE/AIBP family. {ECO:0000256|HAMAP-
CC Rule:MF_03159}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03159}.
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DR EMBL; DS231869; EDS40903.1; -; Genomic_DNA.
DR RefSeq; XP_001845608.1; XM_001845556.1.
DR AlphaFoldDB; B0WA74; -.
DR STRING; 7176.B0WA74; -.
DR EnsemblMetazoa; CPIJ004022-RA; CPIJ004022-PA; CPIJ004022.
DR KEGG; cqu:CpipJ_CPIJ004022; -.
DR VEuPathDB; VectorBase:CPIJ004022; -.
DR VEuPathDB; VectorBase:CQUJHB006948; -.
DR eggNOG; KOG2585; Eukaryota.
DR HOGENOM; CLU_024853_3_0_1; -.
DR InParanoid; B0WA74; -.
DR OMA; CHHMEIP; -.
DR OrthoDB; 1493at2759; -.
DR Proteomes; UP000002320; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052856; F:NADHX epimerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0052857; F:NADPHX epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.10260; YjeF N-terminal domain; 1.
DR HAMAP; MF_01966; NADHX_epimerase; 1.
DR InterPro; IPR004443; YjeF_N_dom.
DR InterPro; IPR036652; YjeF_N_dom_sf.
DR InterPro; IPR032976; YJEFN_prot_NAXE-like.
DR NCBIfam; TIGR00197; yjeF_nterm; 1.
DR PANTHER; PTHR13232; NAD(P)H-HYDRATE EPIMERASE; 1.
DR PANTHER; PTHR13232:SF10; NAD(P)H-HYDRATE EPIMERASE; 1.
DR Pfam; PF03853; YjeF_N; 1.
DR SUPFAM; SSF64153; YjeF N-terminal domain-like; 1.
DR PROSITE; PS51385; YJEF_N; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_03159};
KW Lipoprotein {ECO:0000313|EMBL:EDS40903.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03159};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_03159};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03159}; Potassium {ECO:0000256|HAMAP-Rule:MF_03159};
KW Reference proteome {ECO:0000313|Proteomes:UP000002320}.
FT DOMAIN 9..217
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51385"
FT BINDING 60..64
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT BINDING 61
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT BINDING 125
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT BINDING 129..135
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT BINDING 158
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT BINDING 161
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
SQ SEQUENCE 242 AA; 26794 MW; 756A995793BB0537 CRC64;
MKYLNQQEAI NVDEELFNEY KFSVDQLMEL AGLSCAHAIN DCYGATVEKR KVLVCCGPGN
NGGDGLVAAR HLVLMNYEPH VYYPKRTQKV LFVNLQHQCE SMGIAVSEDC PTLDVVNREF
GLVVDALFGF SFKPPVREAF APIMGVLEKT TVPIVSIDIP SGWHVEEGPQ NETSIKPSCL
ISLTAPKMCA KHLANAKHYL GGRFVPPKLQ EKYSMDLPTY AGNPVSVAFI IENSEDRIEN
NS
//
