NNRE_GIAIC
ID NNRE_GIAIC Reviewed; 273 AA.
AC A8BQZ5;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=NAD(P)H-hydrate epimerase;
DE EC=5.1.99.6;
DE AltName: Full=NAD(P)HX epimerase;
GN ORFNames=GL50803_17366;
OS Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=184922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50803 / WB clone C6;
RX PubMed=17901334; DOI=10.1126/science.1143837;
RA Morrison H.G., McArthur A.G., Gillin F.D., Aley S.B., Adam R.D.,
RA Olsen G.J., Best A.A., Cande W.Z., Chen F., Cipriano M.J., Davids B.J.,
RA Dawson S.C., Elmendorf H.G., Hehl A.B., Holder M.E., Huse S.M., Kim U.U.,
RA Lasek-Nesselquist E., Manning G., Nigam A., Nixon J.E.J., Palm D.,
RA Passamaneck N.E., Prabhu A., Reich C.I., Reiner D.S., Samuelson J.,
RA Svard S.G., Sogin M.L.;
RT "Genomic minimalism in the early diverging intestinal parasite Giardia
RT lamblia.";
RL Science 317:1921-1926(2007).
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 (By similarity). {ECO:0000250}.
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 -!- 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 -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250};
CC Note=Binds 1 potassium ion per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the NnrE/AIBP family. {ECO:0000305}.
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DR EMBL; AACB02000035; EDO77716.1; -; Genomic_DNA.
DR RefSeq; XP_001705390.1; XM_001705338.1.
DR AlphaFoldDB; A8BQZ5; -.
DR SMR; A8BQZ5; -.
DR STRING; 5741.EDO77716; -.
DR EnsemblProtists; EDO77716; EDO77716; GL50803_17366.
DR GeneID; 5698292; -.
DR KEGG; gla:GL50803_0017366; -.
DR VEuPathDB; GiardiaDB:GL50803_17366; -.
DR HOGENOM; CLU_024853_3_0_1; -.
DR InParanoid; A8BQZ5; -.
DR OMA; TIYYPKP; -.
DR OrthoDB; 1030667at2759; -.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052856; F:NADHX epimerase activity; IBA:GO_Central.
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; -; 1.
DR InterPro; IPR004443; YjeF_N_dom.
DR InterPro; IPR036652; YjeF_N_dom_sf.
DR InterPro; IPR032976; YJEFN_prot_NAXE-like.
DR PANTHER; PTHR13232; PTHR13232; 2.
DR Pfam; PF03853; YjeF_N; 1.
DR SUPFAM; SSF64153; SSF64153; 1.
DR TIGRFAMs; TIGR00197; yjeF_nterm; 1.
DR PROSITE; PS51385; YJEF_N; 1.
PE 3: Inferred from homology;
KW Isomerase; Metal-binding; NAD; NADP; Nucleotide-binding; Potassium.
FT CHAIN 1..273
FT /note="NAD(P)H-hydrate epimerase"
FT /id="PRO_0000416329"
FT DOMAIN 18..257
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00719"
FT BINDING 71..75
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 150..157
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
SQ SEQUENCE 273 AA; 29580 MW; 4DE26FD44260BB8C CRC64;
MQQAQQKPFI PTIPAYQALK LDEDLINKCN YSIEQLMEIA GTAVAQATTH YIESTSSVSK
AGVLVVCGPG NNGGDGLVAA RHLSSGSMSS ATVRVWLPKE PSSSVNKRML SIAKHAGVVF
IKDTNEEALH AILEFINSCE SFYLVDAIFG FSFHGGPIKP PYDTVINTLL QMQTSMAIGP
KTRIVSVDVP SGWSVDAQEW GLNTDKELIP DGLLRPDALI SLTVPKNCSL WLPPGTAHYL
GGNFLTPLLA MEYDVQEIQH YWSGVSSLFV VLS