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Database: UniProt
Entry: K1WGG7_TRIAC
LinkDB: K1WGG7_TRIAC
Original site: K1WGG7_TRIAC 
ID   K1WGG7_TRIAC            Unreviewed;       250 AA.
AC   K1WGG7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 44.
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   ORFNames=A1Q2_05072 {ECO:0000313|EMBL:EKD00584.1};
OS   Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Trichosporon.
OX   NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKD00584.1, ECO:0000313|Proteomes:UP000006757};
RN   [1] {ECO:0000313|EMBL:EKD00584.1, ECO:0000313|Proteomes:UP000006757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD00584.1,
RC   ECO:0000313|Proteomes:UP000006757};
RX   PubMed=23193141; DOI=10.1128/EC.00264-12;
RA   Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT   "Genome sequence of the Trichosporon asahii environmental strain CBS
RT   8904.";
RL   Eukaryot. Cell 11:1586-1587(2012).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03159}.
CC       Mitochondrion {ECO:0000256|HAMAP-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKD00584.1}.
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DR   EMBL; AMBO01000338; EKD00584.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1WGG7; -.
DR   STRING; 1220162.K1WGG7; -.
DR   eggNOG; KOG2585; Eukaryota.
DR   HOGENOM; CLU_024853_3_0_1; -.
DR   InParanoid; K1WGG7; -.
DR   OMA; TIYYPKP; -.
DR   OrthoDB; 1493at2759; -.
DR   Proteomes; UP000006757; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03159};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_03159};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_03159}; Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03159};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_03159};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_03159};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_03159};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006757}.
FT   DOMAIN          11..231
FT                   /note="YjeF N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51385"
FT   BINDING         62..66
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT   BINDING         63
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT   BINDING         127
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT   BINDING         131..137
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT   BINDING         160
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT   BINDING         163
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
SQ   SEQUENCE   250 AA;  27660 MW;  E5D7645D95D50B34 CRC64;
     MSIRYIGQKL AQQIDEELMS SAGAFSLDQL MELAGLSCAQ ALGKSYPPKT HKKVLVCCGP
     GNQGGDGLVA ARHLHHFHYT PTLYYPKPGK KEIYQRLLKQ CTNLDIPVLS TLDEFHSALK
     ANDVVMDAIF GFSFEPPVRA PFDRILDALA ESKTPIVSVD MPSGWNVEKG RQELFTQPDD
     QGKSRPVKTI DPEVLVSLTV PKEGAKEFKG KHWLGGRFVS DSLDKKYDLN IPDYPGFDEV
     VELSPGNSKL
//
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