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Database: UniProt
Entry: G5F1T7_9ACTN
LinkDB: G5F1T7_9ACTN
Original site: G5F1T7_9ACTN 
ID   G5F1T7_9ACTN            Unreviewed;       539 AA.
AC   G5F1T7;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=Bifunctional NAD(P)H-hydrate repair enzyme {ECO:0000256|PIRNR:PIRNR017184};
DE   AltName: Full=Nicotinamide nucleotide repair protein {ECO:0000256|PIRNR:PIRNR017184};
DE   Includes:
DE     RecName: Full=ADP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000256|PIRNR:PIRNR017184};
DE              EC=4.2.1.136 {ECO:0000256|PIRNR:PIRNR017184};
DE     AltName: Full=ADP-dependent NAD(P)HX dehydratase {ECO:0000256|PIRNR:PIRNR017184};
DE   Includes:
DE     RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000256|PIRNR:PIRNR017184};
DE              EC=5.1.99.6 {ECO:0000256|PIRNR:PIRNR017184};
GN   Name=nnrE {ECO:0000256|HAMAP-Rule:MF_01966};
GN   Synonyms=nnrD {ECO:0000256|HAMAP-Rule:MF_01965};
GN   ORFNames=HMPREF1008_00331 {ECO:0000313|EMBL:EHF02686.1};
OS   Olsenella sp. oral taxon 809 str. F0356.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC   Olsenella.
OX   NCBI_TaxID=661087 {ECO:0000313|EMBL:EHF02686.1, ECO:0000313|Proteomes:UP000003446};
RN   [1] {ECO:0000313|EMBL:EHF02686.1, ECO:0000313|Proteomes:UP000003446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0356 {ECO:0000313|EMBL:EHF02686.1,
RC   ECO:0000313|Proteomes:UP000003446};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M.,
RA   Baranova O.V., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA   Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Olsenella sp. oral taxon 809 strain F0356.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|PIRNR:PIRNR017184}.
CC   -!- FUNCTION: Catalyzes the dehydration of the S-form of NAD(P)HX at the
CC       expense of ADP, which is converted to AMP. Together with NAD(P)HX
CC       epimerase, which catalyzes the epimerization of the S- and R-forms, the
CC       enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of
CC       NAD(P)H that is a result of enzymatic or heat-dependent hydration.
CC       {ECO:0000256|HAMAP-Rule:MF_01965}.
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_01966}.
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_01966, ECO:0000256|PIRNR:PIRNR017184};
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_01966, ECO:0000256|PIRNR:PIRNR017184};
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, ECO:0000256|HAMAP-
CC         Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184};
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, ECO:0000256|HAMAP-
CC         Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01966,
CC         ECO:0000256|PIRNR:PIRNR017184};
CC       Note=Binds 1 potassium ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01966, ECO:0000256|PIRNR:PIRNR017184};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01965};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01965}.
CC   -!- SIMILARITY: Belongs to the NnrD/CARKD family. {ECO:0000256|HAMAP-
CC       Rule:MF_01965}.
CC   -!- SIMILARITY: Belongs to the NnrE/AIBP family. {ECO:0000256|HAMAP-
CC       Rule:MF_01966}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NnrD/CARKD
CC       family. {ECO:0000256|ARBA:ARBA00009524, ECO:0000256|PIRNR:PIRNR017184}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the NnrE/AIBP family.
CC       {ECO:0000256|ARBA:ARBA00006001, ECO:0000256|PIRNR:PIRNR017184}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01966}.
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:EHF02686.1}.
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DR   EMBL; ACVE01000002; EHF02686.1; -; Genomic_DNA.
DR   RefSeq; WP_009278121.1; NZ_JH376563.1.
DR   AlphaFoldDB; G5F1T7; -.
DR   STRING; 661087.HMPREF1008_00331; -.
DR   PATRIC; fig|661087.3.peg.332; -.
DR   eggNOG; COG0062; Bacteria.
DR   eggNOG; COG0063; Bacteria.
DR   HOGENOM; CLU_024853_4_1_11; -.
DR   OrthoDB; 9806925at2; -.
DR   Proteomes; UP000003446; Unassembled WGS sequence.
DR   GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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:0046496; P:nicotinamide nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01171; YXKO-related; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   Gene3D; 3.40.50.10260; YjeF N-terminal domain; 1.
DR   HAMAP; MF_01965; NADHX_dehydratase; 1.
DR   HAMAP; MF_01966; NADHX_epimerase; 1.
DR   InterPro; IPR000631; CARKD.
DR   InterPro; IPR030677; Nnr.
DR   InterPro; IPR029056; Ribokinase-like.
DR   InterPro; IPR004443; YjeF_N_dom.
DR   InterPro; IPR036652; YjeF_N_dom_sf.
DR   NCBIfam; TIGR00196; yjeF_cterm; 1.
DR   NCBIfam; TIGR00197; yjeF_nterm; 1.
DR   PANTHER; PTHR12592:SF0; ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE; 1.
DR   PANTHER; PTHR12592; ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE FAMILY MEMBER; 1.
DR   Pfam; PF01256; Carb_kinase; 1.
DR   Pfam; PF03853; YjeF_N; 1.
DR   PIRSF; PIRSF017184; Nnr; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 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, ECO:0000256|HAMAP-
KW   Rule:MF_01965};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01966};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01965};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01966}; Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01965};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01965};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01965};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_01966, ECO:0000256|PIRNR:PIRNR017184};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003446}.
FT   DOMAIN          10..216
FT                   /note="YjeF N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51385"
FT   DOMAIN          227..524
FT                   /note="YjeF C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51383"
FT   BINDING         56..60
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   BINDING         57
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   BINDING         126
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   BINDING         130..136
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   BINDING         159
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   BINDING         162
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   BINDING         262
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT   BINDING         333
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT   BINDING         390
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT   BINDING         432..436
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT   BINDING         460
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT   BINDING         461
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
SQ   SEQUENCE   539 AA;  54797 MW;  18F0D66B0C535897 CRC64;
     MQPVLNIEDI KRVEAGLTNV GVSISELMHR AGTAAANEAL RLAHPQGAVV LCGLGNNGGD
     GWVAAEELLS KGVEVYAVTP VEPDQIKGDL ARVVAKSAQV AGVSIVVAPP RELLEGLLSD
     ADVAIDAMLG TGFRGVPRAP FDIWIDCLNG SDVQVVSVDV PSGLSAQTGL AEDACVAADL
     TVTMLALKPG LLSDDGRDAC GAIVVAPLAE QTERLVLEAD PVAWRADLDD YDSVLRPSSS
     ADDKFRRGSV LVVGGSSRFP GAPMMAALAA ARAGAGYVTL AVPAAIAPIV QSQMLEIPVI
     ALPCEADGTF SAKAAEAVAE LAAKRTATVV GPGMRVSSGT VGVVSALLGT PVPLVVDADG
     LNCISRLTSN ALDDFPELLR RDSPLVLTPH RGELGRLVGL QDTPPASLTA AMEAARRIVW
     SDGGSELCVV SKGSATACVS VDAAFLPKPG PAALATAGSG DVLGGIIAAY LARSNVEADD
     LPVLAAYACE VHGYAGSIAA QRVGANAVMA HDLIDAIGLA EDALLEQVNA AVTGMGEKN
//
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