ID X1AJ61_9ZZZZ Unreviewed; 268 AA.
AC X1AJ61;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=ADP-dependent NAD(P)H-hydrate dehydratase {ECO:0000256|ARBA:ARBA00013129};
DE EC=4.2.1.136 {ECO:0000256|ARBA:ARBA00013129};
DE AltName: Full=Nicotinamide nucleotide repair protein {ECO:0000256|ARBA:ARBA00032624};
DE Flags: Fragment;
GN ORFNames=S01H4_35889 {ECO:0000313|EMBL:GAG82249.1};
OS marine sediment metagenome.
OC unclassified sequences; metagenomes; ecological metagenomes.
OX NCBI_TaxID=412755 {ECO:0000313|EMBL:GAG82249.1};
RN [1] {ECO:0000313|EMBL:GAG82249.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Expedition CK06-06 {ECO:0000313|EMBL:GAG82249.1};
RX PubMed=24624126; DOI=10.3389/fmicb.2014.00080;
RA Kawai M., Futagami T., Toyoda A., Takaki Y., Nishi S., Hori S., Arai W.,
RA Tsubouchi T., Morono Y., Uchiyama I., Ito T., Fujiyama A., Inagaki F.,
RA Takami H.;
RT "High frequency of phylogenetically diverse reductive dehalogenase-
RT homologous genes in deep subseafloor sedimentary metagenomes.";
RL Front. Microbiol. 5:80-80(2014).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the epimerization of the
CC S- and R-forms of NAD(P)HX and the dehydration of the S-form of
CC NAD(P)HX at the expense of ADP, which is converted to AMP. This allows
CC the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that
CC is a result of enzymatic or heat-dependent hydration.
CC {ECO:0000256|ARBA:ARBA00025153}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate;
CC Xref=Rhea:RHEA:32223, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:64074, ChEBI:CHEBI:456215,
CC ChEBI:CHEBI:456216; EC=4.2.1.136;
CC Evidence={ECO:0000256|ARBA:ARBA00001026};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-NADPHX + ADP = AMP + H(+) + NADPH + phosphate;
CC Xref=Rhea:RHEA:32235, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:64076, ChEBI:CHEBI:456215,
CC ChEBI:CHEBI:456216; EC=4.2.1.136;
CC Evidence={ECO:0000256|ARBA:ARBA00001241};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
CC -!- SIMILARITY: In the C-terminal section; belongs to the NnrD/CARKD
CC family. {ECO:0000256|ARBA:ARBA00009524}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the NnrE/AIBP family.
CC {ECO:0000256|ARBA:ARBA00006001}.
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:GAG82249.1}.
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DR EMBL; BART01019127; GAG82249.1; -; Genomic_DNA.
DR AlphaFoldDB; X1AJ61; -.
DR GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0052856; F:NADHX epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0052857; F:NADPHX epimerase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.1190.20; -; 1.
DR Gene3D; 3.40.50.10260; YjeF N-terminal domain; 1.
DR HAMAP; MF_01966; NADHX_epimerase; 1.
DR InterPro; IPR000631; CARKD.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR004443; YjeF_N_dom.
DR InterPro; IPR036652; YjeF_N_dom_sf.
DR NCBIfam; TIGR00197; yjeF_nterm; 1.
DR PANTHER; PTHR13612:SF0; ENHANCER OF MRNA-DECAPPING PROTEIN 3; 1.
DR PANTHER; PTHR13612; UNCHARACTERIZED; 1.
DR Pfam; PF03853; YjeF_N; 1.
DR SUPFAM; SSF64153; YjeF N-terminal domain-like; 1.
DR PROSITE; PS51383; YJEF_C_3; 1.
DR PROSITE; PS51385; YJEF_N; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 9..221
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51385"
FT DOMAIN 230..268
FT /note="YjeF C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51383"
FT NON_TER 268
FT /evidence="ECO:0000313|EMBL:GAG82249.1"
SQ SEQUENCE 268 AA; 29014 MW; F6E3C0C7EA9D8167 CRC64;
MKVVTSQEMK RLDELTIKTI GIPSIVLMEN AGIKVVEVIE KEYSPLPEKS VYILCGPGSN
GGDGMVIARH LFNRRVRVKV FLLAKKNRVK GDAATNLSIA EKLGIEVKEI NSAQDLKLLR
QELPHADIIV DALLGTGSTL PLRGLMREAV GLINQCSSYT MAVDLPTGLH ADTGEVPGEA
IKANVTVTFA YPKRGLYLYP GINYTGKIEV ADIGIPSFLG EERIKCNLLT SSDIQKDLFY
RKPSSHKGNF GHLLIIAGSP GMTGAATL
//