ID   A0A2V5BL89_9GAMM        Unreviewed;       483 AA.
AC   A0A2V5BL89;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   28-JUN-2023, entry version 20.
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=nnrD {ECO:0000256|HAMAP-Rule:MF_01965};
GN   Synonyms=nnrE {ECO:0000256|HAMAP-Rule:MF_01966};
GN   ORFNames=DEU53_105268 {ECO:0000313|EMBL:PYG48848.1};
OS   Pantoea sp. AG1095.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=2184004 {ECO:0000313|EMBL:PYG48848.1, ECO:0000313|Proteomes:UP000247871};
RN   [1] {ECO:0000313|EMBL:PYG48848.1, ECO:0000313|Proteomes:UP000247871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG1095 {ECO:0000313|EMBL:PYG48848.1,
RC   ECO:0000313|Proteomes:UP000247871};
RA   Venturi V.;
RT   "Genome sequencing of rice bacterial endophytes.";
RL   Submitted (JUN-2018) 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: 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:PYG48848.1}.
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DR   EMBL; QKMJ01000005; PYG48848.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5BL89; -.
DR   EnsemblBacteria; PYG48848; PYG48848; DEU53_105268.
DR   Proteomes; UP000247871; 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; IPR017953; Carbohydrate_kinase_pred_CS.
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   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   TIGRFAMs; TIGR00196; yjeF_cterm; 1.
DR   TIGRFAMs; TIGR00197; yjeF_nterm; 1.
DR   PROSITE; PS01050; YJEF_C_2; 1.
DR   PROSITE; PS51383; YJEF_C_3; 1.
DR   PROSITE; PS51385; YJEF_N; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01965,
KW   ECO:0000256|PIRNR:PIRNR017184};
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|HAMAP-Rule:MF_01966,
KW   ECO:0000256|PIRNR:PIRNR017184};
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|HAMAP-Rule:MF_01965,
KW   ECO:0000256|PIRNR:PIRNR017184};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_01966, ECO:0000256|PIRNR:PIRNR017184}.
FT   DOMAIN          1..203
FT                   /note="YjeF N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51385"
FT   BINDING         49..53
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   BINDING         50
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   BINDING         113
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   BINDING         117..123
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   BINDING         128
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   BINDING         146
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   BINDING         149
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   BINDING         247
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT   BINDING         307
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT   BINDING         353
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT   BINDING         390..394
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT   BINDING         419
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT   BINDING         420
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
SQ   SEQUENCE   483 AA;  50469 MW;  0788CE753E99D228 CRC64;
     MAQLERDAAD SLGLTLFELM QRAGQASYEL GCQLWPQAQH WLILCGHGNN GGDGYVVARL
     AQAAGLNVTL LACAGSKALP EEAQQAQDAW LAAGGVIHAA DAPWPEQVEV IVDALLGTGL
     NRAPADPYDR LITLINAHAA PVLAIDIPSG LLAANGTAPG KTVIADHTLS MITLKPGQLT
     GKARDYVGVL HNHELGLSAY LAAEQAPISR YDAGDLTCWL KPRRATSHKG DQGRLLVVGG
     DSGTAGAIRM TGEAALRTGA GLVRVLTHED NIGPILTARP ELMVDALSDE RLDQALEWAD
     VIAVGPGLGQ RDWAQKALKK IAASEKPMLW DADALNLLAI KQDNRQNRII TPHPGEAARL
     LGVKTSEIES DRLHAARALA KRYGGVVVLK GAGTVIASAA GDIAIADVGN AGMASGGMGD
     VLSGIIAALL GQKLTLLDAA CAGCVAHGAT ADAVARQRGT RGMLATDLFE LLWQFVNPEM
     IQQ
//