ID   A0A2N8NSB6_STREU        Unreviewed;       482 AA.
AC   A0A2N8NSB6;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   22-APR-2020, entry version 10.
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=AF335_22665 {ECO:0000313|EMBL:PNE31668.1};
OS   Streptomyces eurocidicus (Streptoverticillium eurocidicus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=66423 {ECO:0000313|EMBL:PNE31668.1, ECO:0000313|Proteomes:UP000235945};
RN   [1] {ECO:0000313|EMBL:PNE31668.1, ECO:0000313|Proteomes:UP000235945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27428 {ECO:0000313|EMBL:PNE31668.1,
RC   ECO:0000313|Proteomes:UP000235945};
RA   Noorani M.;
RL   Submitted (JUL-2015) 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|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|HAMAP-Rule:MF_01966,
CC         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|HAMAP-Rule:MF_01966,
CC         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; Evidence={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; Evidence={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|PIRNR:PIRNR017184}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the NnrE/AIBP family.
CC       {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:PNE31668.1}.
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DR   EMBL; LGUI01000008; PNE31668.1; -; Genomic_DNA.
DR   Proteomes; UP000235945; 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:0016301; F:kinase activity; IEA:UniProtKB-KW.
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; -; 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   Pfam; PF01256; Carb_kinase; 1.
DR   Pfam; PF03853; YjeF_N; 1.
DR   PIRSF; PIRSF017184; Nnr; 1.
DR   SUPFAM; SSF53613; SSF53613; 1.
DR   SUPFAM; SSF64153; SSF64153; 1.
DR   TIGRFAMs; TIGR00196; yjeF_cterm; 1.
DR   TIGRFAMs; TIGR00197; yjeF_nterm; 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|HAMAP-Rule:MF_01966, ECO:0000256|PIRNR:PIRNR017184};
KW   Kinase {ECO:0000313|EMBL:PNE31668.1};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01966,
KW   ECO:0000256|PIRNR:PIRNR017184};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184};
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};
KW   Transferase {ECO:0000313|EMBL:PNE31668.1}.
FT   DOMAIN          10..208
FT                   /note="YjeF N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51385"
FT   NP_BIND         390..394
FT                   /note="ADP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT   NP_BIND         411..420
FT                   /note="ADP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT   REGION          58..62
FT                   /note="NAD(P)HX"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   REGION          124..130
FT                   /note="NAD(P)HX"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   REGION          353..359
FT                   /note="NAD(P)HX"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT   METAL           59
FT                   /note="Potassium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   METAL           120
FT                   /note="Potassium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   METAL           154
FT                   /note="Potassium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   BINDING         151
FT                   /note="NAD(P)HX"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   BINDING         305
FT                   /note="NAD(P)HX; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT   BINDING         421
FT                   /note="NAD(P)HX"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
SQ   SEQUENCE   482 AA;  47900 MW;  DC07F2EF1CEF701F CRC64;
     MRTAYSVETV RAAERALMAQ LPQGALMQRA AAGLAAACAD LLGRTYGARV ALLVGSGDNG
     GDALYAGARL ARRGAGVTAV LLAPERTHQG GLAALRAAGG RVASAEEGDR AVRRADLVVD
     GIVGIGGRGG LRPEAEALVA AAEGALVLAV DLPSGVDADS GEVRGATVRA DATVTFGAYK
     PGLLIDPARE RAGALRLIDI GLGPHLPRRP EAEALQHADV AALLPRPAAE SDKYRRGVVG
     VVAGSARYPG AAVLAVAGAL HGGAGAVRYA GPAAEAVVSR FPETLVSEGP PSKAGRVQAW
     VVGPGVGDDA AARRALDDVL ASDVPVLVDA DGLRLLPEAA VRARGAETVL TPHAGEAAAL
     LGVSRSRVES ARLSAARELA ARFGATALLK GSTTVVAAPG RTAVRVNPTG TPWLATAGSG
     DVLSGVTGSL LAAGLRGLDA ASVGAYLHGL AARSLGGAPL TASGVAEALA GAWGEVTGHS
     YE
//