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Bifunctional NAD(P)H-hydrate repair enzyme (Nicotinamide nucleotide repair protein) [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6)]

 M5DU56_9GAMM            Unreviewed;       506 AA.
M5DU56;
29-MAY-2013, integrated into UniProtKB/TrEMBL.
29-MAY-2013, sequence version 1.
10-APR-2019, entry version 43.
RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01965, ECO:0000256|HAMAP-Rule:MF_01966};
Includes:
RecName: Full=ADP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000256|HAMAP-Rule:MF_01965};
EC=4.2.1.136 {ECO:0000256|HAMAP-Rule:MF_01965};
AltName: Full=ADP-dependent NAD(P)HX dehydratase {ECO:0000256|HAMAP-Rule:MF_01965};
Includes:
RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000256|HAMAP-Rule:MF_01966};
EC=5.1.99.6 {ECO:0000256|HAMAP-Rule:MF_01966};
AltName: Full=NAD(P)HX epimerase {ECO:0000256|HAMAP-Rule:MF_01966};
Name=nnrD {ECO:0000256|HAMAP-Rule:MF_01965};
Synonyms=nnrE {ECO:0000256|HAMAP-Rule:MF_01966};
ORFNames=TOL_3030 {ECO:0000313|EMBL:CCU73426.1};
Thalassolituus oleivorans MIL-1.
Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
Oceanospirillaceae; Thalassolituus.
NCBI_TaxID=1298593 {ECO:0000313|EMBL:CCU73426.1, ECO:0000313|Proteomes:UP000011866};
[1] {ECO:0000313|EMBL:CCU73426.1, ECO:0000313|Proteomes:UP000011866}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MIL-1 {ECO:0000313|EMBL:CCU73426.1};
PubMed=23599290; DOI=10.1128/genomeA.00141-13;
Golyshin P.N., Werner J., Chernikova T.N., Tran H., Ferrer M.,
Yakimov M.M., Teeling H., Golyshina O.V.;
"Genome Sequence of Thalassolituus oleivorans MIL-1 (DSM 14913T).";
Genome Announc. 1:1-3(2013).
-!- FUNCTION: Bifunctional enzyme that catalyzes the epimerization of
the S- and R-forms of NAD(P)HX and the dehydration of the S-form
of NAD(P)HX at the expense of ADP, which is converted to AMP. This
allows the repair of both epimers of NAD(P)HX, a damaged form of
NAD(P)H that is a result of enzymatic or heat-dependent hydration.
{ECO:0000256|PIRNR:PIRNR017184}.
-!- FUNCTION: Catalyzes the dehydration of the S-form of NAD(P)HX at
the expense of ADP, which is converted to AMP. Together with
NAD(P)HX epimerase, which catalyzes the epimerization of the S-and
R-forms, the enzyme allows the repair of both epimers of NAD(P)HX,
a damaged form of NAD(P)H that is a result of enzymatic or heat-
dependent hydration. {ECO:0000256|HAMAP-Rule:MF_01965}.
-!- FUNCTION: Catalyzes the epimerization of the S- and R-forms of
NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic
or heat-dependent hydration. This is a prerequisite for the S-
specific NAD(P)H-hydrate dehydratase to allow the repair of both
epimers of NAD(P)HX. {ECO:0000256|HAMAP-Rule:MF_01966}.
-!- CATALYTIC ACTIVITY:
Reaction=(6R)-NADHX = (6S)-NADHX; Xref=Rhea:RHEA:32215,
ChEBI:CHEBI:64074, ChEBI:CHEBI:64075; EC=5.1.99.6;
Evidence={ECO:0000256|HAMAP-Rule:MF_01966,
ECO:0000256|PIRNR:PIRNR017184};
-!- CATALYTIC ACTIVITY:
Reaction=(6R)-NADPHX = (6S)-NADPHX; Xref=Rhea:RHEA:32227,
ChEBI:CHEBI:64076, ChEBI:CHEBI:64077; EC=5.1.99.6;
Evidence={ECO:0000256|HAMAP-Rule:MF_01966,
ECO:0000256|PIRNR:PIRNR017184};
-!- CATALYTIC ACTIVITY:
Reaction=(6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate;
Xref=Rhea:RHEA:32223, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
ChEBI:CHEBI:57945, ChEBI:CHEBI:64074, ChEBI:CHEBI:456215,
ChEBI:CHEBI:456216; EC=4.2.1.136; Evidence={ECO:0000256|HAMAP-
Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184};
-!- CATALYTIC ACTIVITY:
Reaction=(6S)-NADPHX + ADP = AMP + H(+) + NADPH + phosphate;
Xref=Rhea:RHEA:32235, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
ChEBI:CHEBI:57783, ChEBI:CHEBI:64076, ChEBI:CHEBI:456215,
ChEBI:CHEBI:456216; EC=4.2.1.136; Evidence={ECO:0000256|HAMAP-
Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184};
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000256|HAMAP-Rule:MF_01966,
ECO:0000256|PIRNR:PIRNR017184};
Note=Binds 1 potassium ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_01966, ECO:0000256|PIRNR:PIRNR017184};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_01965};
-!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01965}.
-!- SIMILARITY: Belongs to the NnrD/CARKD family. {ECO:0000256|HAMAP-
Rule:MF_01965}.
-!- SIMILARITY: Belongs to the NnrE/AIBP family. {ECO:0000256|HAMAP-
Rule:MF_01966}.
-!- SIMILARITY: In the C-terminal section; belongs to the NnrD/CARKD
family. {ECO:0000256|PIRNR:PIRNR017184}.
-!- SIMILARITY: In the N-terminal section; belongs to the NnrE/AIBP
family. {ECO:0000256|PIRNR:PIRNR017184}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01966}.
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EMBL; HF680312; CCU73426.1; -; Genomic_DNA.
RefSeq; WP_015488136.1; NC_020888.1.
STRING; 1298593.TOL_3030; -.
EnsemblBacteria; CCU73426; CCU73426; TOL_3030.
KEGG; tol:TOL_3030; -.
PATRIC; fig|1298593.3.peg.2929; -.
KO; K17758; -.
KO; K17759; -.
BioCyc; TOLE1298593:G1HGH-2937-MONOMER; -.
Proteomes; UP000011866; Chromosome.
GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
GO; GO:0052856; F:NADHX epimerase activity; IEA:UniProtKB-UniRule.
GO; GO:0046496; P:nicotinamide nucleotide metabolic process; IEA:UniProtKB-UniRule.
CDD; cd01171; YXKO-related; 1.
Gene3D; 3.40.1190.20; -; 1.
Gene3D; 3.40.50.10260; -; 1.
HAMAP; MF_01965; NADHX_dehydratase; 1.
HAMAP; MF_01966; NADHX_epimerase; 1.
InterPro; IPR017953; Carbohydrate_kinase_pred_CS.
InterPro; IPR000631; CARKD.
InterPro; IPR030677; Nnr.
InterPro; IPR029056; Ribokinase-like.
InterPro; IPR004443; YjeF_N_dom.
InterPro; IPR036652; YjeF_N_dom_sf.
Pfam; PF01256; Carb_kinase; 1.
Pfam; PF03853; YjeF_N; 1.
PIRSF; PIRSF017184; Nnr; 1.
SUPFAM; SSF53613; SSF53613; 1.
SUPFAM; SSF64153; SSF64153; 1.
TIGRFAMs; TIGR00196; yjeF_cterm; 1.
TIGRFAMs; TIGR00197; yjeF_nterm; 1.
PROSITE; PS01050; YJEF_C_2; 1.
PROSITE; PS51383; YJEF_C_3; 1.
PROSITE; PS51385; YJEF_N; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01965,
ECO:0000256|PIRNR:PIRNR017184};
Complete proteome {ECO:0000313|Proteomes:UP000011866};
Isomerase {ECO:0000256|HAMAP-Rule:MF_01966,
ECO:0000256|PIRNR:PIRNR017184};
Lyase {ECO:0000256|HAMAP-Rule:MF_01965,
ECO:0000256|PIRNR:PIRNR017184};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01966,
ECO:0000256|PIRNR:PIRNR017184};
NAD {ECO:0000256|HAMAP-Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184};
NADP {ECO:0000256|HAMAP-Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01965,
ECO:0000256|PIRNR:PIRNR017184};
Potassium {ECO:0000256|HAMAP-Rule:MF_01966,
ECO:0000256|PIRNR:PIRNR017184};
Reference proteome {ECO:0000313|Proteomes:UP000011866}.
DOMAIN 21 223 YjeF N-terminal.
{ECO:0000259|PROSITE:PS51385}.
NP_BIND 419 423 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
NP_BIND 439 448 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
REGION 69 73 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
REGION 137 143 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
REGION 382 388 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01965}.
METAL 70 70 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
METAL 133 133 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
METAL 169 169 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
BINDING 166 166 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
BINDING 332 332 NAD(P)HX; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01965}.
BINDING 449 449 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01965}.
SEQUENCE 506 AA; 52303 MW; 8B627EFFA3708614 CRC64;
MNRPFSAKDH LPAQLFSVAQ IRELDRQTIA AQGDDGFTLM HEAATSALSV LQHHWVDARK
ITVIAGPGNN GGDAFILAAL AFECGIRVRV FTLGDLTKQT SAAQKALNMA VQTGISIERL
STASDLSGDV LVDGLLGTGL SSEPRDEFAQ AIAAINAADI PVLALDVPSG LNADSGVVYG
PVVKADVTIT FIGVKRGLLT ASGPDVCGAL ELAELSVIDS AHANIVADAE RISWARLHDE
MRGLAPRRGN AHKGHFGHVL VIGGESGFGG AAMMAVEAAG RIGAGLVSCA TRPEHVPALL
TRRPEVMALG VNSGLELAPA IQRATILAIG PGLGQTSWSE LLLQQVLGAQ QPVVLDADAL
NLLASPGWHC EFSERVAVLT PHPGEAARML GMTVTEVQTD RFASARLLAQ RYQAVVVLKG
QGSLIADPSG RVALCTDGNP GMSCGGMGDV LTGVIAALLA QGLNAWDAAC LGVCCHSAAA
DVAVADAGVR GLLATDLMPI LRELIN


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