(data stored in SCRATCH zone)

SWISSPROT: C5DD19_LACTC

ID   C5DD19_LACTC            Unreviewed;       241 AA.
AC   C5DD19;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000256|HAMAP-Rule:MF_03159};
DE            EC=5.1.99.6 {ECO:0000256|HAMAP-Rule:MF_03159};
DE   AltName: Full=NAD(P)HX epimerase {ECO:0000256|HAMAP-Rule:MF_03159};
GN   OrderedLocusNames=KLTH0B07612g {ECO:0000313|EMBL:CAR21680.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21680.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21680.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P.,
RA   Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F.,
RA   Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R.,
RA   Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T.,
RA   Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G.,
RA   Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C.,
RA   Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E.,
RA   Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C.,
RA   Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C.,
RA   Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
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
CC       or heat-dependent hydration. This is a prerequisite for the S-
CC       specific NAD(P)H-hydrate dehydratase to allow the repair of both
CC       epimers of 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|HAMAP-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|HAMAP-Rule:MF_03159};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|HAMAP-
CC         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
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03159}.
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DR   EMBL; CU928166; CAR21680.1; -; Genomic_DNA.
DR   RefSeq; XP_002552118.1; XM_002552072.1.
DR   STRING; 381046.XP_002552118.1; -.
DR   EnsemblFungi; CAR21680; CAR21680; KLTH0B07612g.
DR   GeneID; 8290958; -.
DR   KEGG; lth:KLTH0B07612g; -.
DR   HOGENOM; HOG000174236; -.
DR   InParanoid; C5DD19; -.
DR   KO; K17759; -.
DR   OMA; FKGRHFI; -.
DR   OrthoDB; 1030667at2759; -.
DR   Proteomes; UP000002036; Chromosome B.
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:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10260; -; 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_eukaryotes.
DR   PANTHER; PTHR13232; PTHR13232; 1.
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;
DR   PRODOM; C5DD19.
DR   SWISS-2DPAGE; C5DD19.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002036};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03159};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_03159};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03159};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03159};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_03159};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03159};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_03159};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036}.
FT   DOMAIN       11    228       YjeF N-terminal. {ECO:0000259|PROSITE:
FT                                PS51385}.
FT   REGION       64     68       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_03159}.
FT   REGION      136    142       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_03159}.
FT   METAL        65     65       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_03159}.
FT   METAL       132    132       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_03159}.
FT   METAL       170    170       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_03159}.
FT   BINDING     167    167       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_03159}.
SQ   SEQUENCE   241 AA;  26591 MW;  6DBB369A6FE2296A CRC64;
     MALRTISSQL AAQLDKELMG PEVGFTLEQL MELAGLSVAQ AVVKEFPYSE TRKSQVLVIA
     GPGNNGGDGL VCARHLALSG FQPVVYYPKR TTKTPFYAQL VNQLKFFKVP VLGAGDNWAQ
     YLDHTKTLCV VDAIFGFSFK PPVREPFGSI LQQLRHAQQN LPIVSVDIPT GWDVDEGPAD
     SDCIIPSVLV SLTVPKPCAA KIDTCETHHY VGGRFIPRDF ALKYGFEPFP YENLDQVLRL
     H
//

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