ID   A0A2N7WEL6_9BURK        Unreviewed;       534 AA.
AC   A0A2N7WEL6;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   20-JUN-2018, entry version 3.
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=C0Z19_03500 {ECO:0000313|EMBL:PMS27880.1};
OS   Paraburkholderia soli.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=380675 {ECO:0000313|EMBL:PMS27880.1, ECO:0000313|Proteomes:UP000235347};
RN   [1] {ECO:0000313|EMBL:PMS27880.1, ECO:0000313|Proteomes:UP000235347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GP25-8 {ECO:0000313|EMBL:PMS27880.1,
RC   ECO:0000313|Proteomes:UP000235347};
RA   Estrada-de los Santos P., Palmer M., Chavez-Ramirez B., Beukes C.,
RA   Steenkamp E.T., Hirsch A.M., Manyaka P., Maluk M., Lafos M., Crook M.,
RA   Gross E., Simon M.F., Bueno dos Reis Junior F., Poole P.S.,
RA   Venter S.N., James E.K.;
RT   "Whole genome analyses suggest that Burkholderia sensu lato contains
RT   two further novel genera in the rhizoxinica-symbiotica group
RT   Mycetohabitans gen. nov., and Trinickia gen. nov.: implications for
RT   the evolution of diazotrophy and nodulation in the Burkholderiaceae.";
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes the epimerization of
CC       the S- and R-forms of NAD(P)HX and the dehydration of the S-form
CC       of NAD(P)HX at the expense of ADP, which is converted to AMP. This
CC       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|PIRNR:PIRNR017184}.
CC   -!- FUNCTION: Catalyzes the dehydration of the S-form of NAD(P)HX at
CC       the expense of ADP, which is converted to AMP. Together with
CC       NAD(P)HX epimerase, which catalyzes the epimerization of the
CC       S- and R-forms, the enzyme allows the repair of both epimers of
CC       NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic
CC       or heat-dependent hydration. {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
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_01966}.
CC   -!- CATALYTIC ACTIVITY: (6R)-6-beta-hydroxy-1,4,5,6-
CC       tetrahydronicotinamide-adenine dinucleotide = (6S)-6-beta-hydroxy-
CC       1,4,5,6-tetrahydronicotinamide-adenine dinucleotide.
CC       {ECO:0000256|PIRNR:PIRNR017184}.
CC   -!- CATALYTIC ACTIVITY: (6R)-6-beta-hydroxy-1,4,5,6-
CC       tetrahydronicotinamide-adenine dinucleotide phosphate = (6S)-6-
CC       beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
CC       phosphate. {ECO:0000256|PIRNR:PIRNR017184}.
CC   -!- CATALYTIC ACTIVITY: ADP + (6S)-6-beta-hydroxy-1,4,5,6-
CC       tetrahydronicotinamide adenine-dinucleotide = AMP + phosphate +
CC       NADH. {ECO:0000256|PIRNR:PIRNR017184}.
CC   -!- CATALYTIC ACTIVITY: ADP + (6S)-6-beta-hydroxy-1,4,5,6-
CC       tetrahydronicotinamide adenine-dinucleotide phosphate = AMP +
CC       phosphate + NADPH. {ECO:0000256|PIRNR:PIRNR017184}.
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01966, 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; Evidence={ECO:0000256|HAMAP-
CC         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
CC       family. {ECO:0000256|PIRNR:PIRNR017184}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01966}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PMS27880.1}.
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DR   EMBL; PNYB01000002; PMS27880.1; -; Genomic_DNA.
DR   Proteomes; UP000235347; 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: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   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   Complete proteome {ECO:0000313|Proteomes:UP000235347};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01966,
KW   ECO:0000256|PIRNR:PIRNR017184};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01965,
KW   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_01966, ECO:0000256|PIRNR:PIRNR017184};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_01966, ECO:0000256|PIRNR:PIRNR017184};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01966,
KW   ECO:0000256|PIRNR:PIRNR017184};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_01966,
KW   ECO:0000256|PIRNR:PIRNR017184};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235347}.
FT   DOMAIN       30    239       YjeF N-terminal. {ECO:0000259|PROSITE:
FT                                PS51385}.
FT   NP_BIND     438    442       ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
FT   NP_BIND     458    467       ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
FT   REGION       82     86       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   REGION      148    154       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   REGION      401    407       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01965}.
FT   METAL        83     83       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   METAL       144    144       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   METAL       183    183       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   BINDING     180    180       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   BINDING     337    337       NAD(P)HX; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01965}.
FT   BINDING     468    468       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01965}.
SQ   SEQUENCE   534 AA;  53705 MW;  0294C1152F2C73E6 CRC64;
     MTNPRPLPDH PPQLLSPNDR PLPLFTVAQL RELEARGAAG LPAHTLMVRA GAASAHYLIE
     RAAHEGSLAT EHPVWIAAGP GNNGGDALVL ATRLRQAGIA AEVCMPVEVK AEDARWALGE
     ARAAGVPISH VPPASLDAFG WVVDGLFGIG LARPLEGIFA ELAVRIGRRA TTHGRVLALD
     VPSGLDSDTG NVVDGGLAVR ATETVTFLGA KPGLYMTYGR DLAGSVTLAP LGVDLPPAAD
     VARLNAPALF APHFPARSFA SHKGTFGSLA VVGGDTGMCG APILAARAAL HTGAGKVHVA
     FVGEGAPAYD APYPELMLHP PGTLAFDAMD ALAVGCGMGR GANAIASLQK ALGCNAPLLL
     DADALNLIAS DTSLAGVLTA GAVKGASGAD GTARPCVLTP HPLEAARLLG TDSTSIQRDR
     LGSARALAAR FAAVVVLKGA GTVIASPDGR AAVNPTGNAA LATGGTGDVL GGIIGALLAE
     RLPGYEAALA GVYLHGLAAE TLTAGGSGPA GLTAGELAPT VRTLLNRLIY PVRD
//