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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)]

 B5F382_SALA4            Unreviewed;       514 AA.
B5F382;
14-OCT-2008, integrated into UniProtKB/TrEMBL.
14-OCT-2008, sequence version 1.
18-JUL-2018, entry version 62.
RecName: Full=Bifunctional NAD(P)H-hydrate repair enzyme {ECO:0000256|PIRNR:PIRNR017184};
AltName: Full=Nicotinamide nucleotide repair protein {ECO:0000256|PIRNR:PIRNR017184};
Includes:
RecName: Full=ADP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000256|PIRNR:PIRNR017184};
EC=4.2.1.136 {ECO:0000256|PIRNR:PIRNR017184};
AltName: Full=ADP-dependent NAD(P)HX dehydratase {ECO:0000256|PIRNR:PIRNR017184};
Includes:
RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000256|PIRNR:PIRNR017184};
EC=5.1.99.6 {ECO:0000256|PIRNR:PIRNR017184};
Name=nnrD {ECO:0000256|HAMAP-Rule:MF_01965};
Synonyms=nnrE {ECO:0000256|HAMAP-Rule:MF_01966};
OrderedLocusNames=SeAg_B4633 {ECO:0000313|EMBL:ACH49905.1};
Salmonella agona (strain SL483).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Salmonella.
NCBI_TaxID=454166 {ECO:0000313|EMBL:ACH49905.1, ECO:0000313|Proteomes:UP000008819};
[1] {ECO:0000313|EMBL:ACH49905.1, ECO:0000313|Proteomes:UP000008819}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SL483 {ECO:0000313|EMBL:ACH49905.1,
ECO:0000313|Proteomes:UP000008819};
PubMed=21602358; DOI=10.1128/JB.00297-11;
Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
Leclerc J.E., Ravel J., Cebula T.A.;
"Comparative genomics of 28 Salmonella enterica isolates: evidence for
CRISPR-mediated adaptive sublineage evolution.";
J. Bacteriol. 193:3556-3568(2011).
-!- 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: (6R)-6-beta-hydroxy-1,4,5,6-
tetrahydronicotinamide-adenine dinucleotide = (6S)-6-beta-hydroxy-
1,4,5,6-tetrahydronicotinamide-adenine dinucleotide.
{ECO:0000256|PIRNR:PIRNR017184}.
-!- CATALYTIC ACTIVITY: (6R)-6-beta-hydroxy-1,4,5,6-
tetrahydronicotinamide-adenine dinucleotide phosphate = (6S)-6-
beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
phosphate. {ECO:0000256|PIRNR:PIRNR017184}.
-!- CATALYTIC ACTIVITY: ADP + (6S)-6-beta-hydroxy-1,4,5,6-
tetrahydronicotinamide adenine-dinucleotide = AMP + phosphate +
NADH. {ECO:0000256|PIRNR:PIRNR017184}.
-!- CATALYTIC ACTIVITY: ADP + (6S)-6-beta-hydroxy-1,4,5,6-
tetrahydronicotinamide adenine-dinucleotide phosphate = AMP +
phosphate + NADPH. {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; CP001138; ACH49905.1; -; Genomic_DNA.
ProteinModelPortal; B5F382; -.
EnsemblBacteria; ACH49905; ACH49905; SeAg_B4633.
KEGG; sea:SeAg_B4633; -.
HOGENOM; HOG000228406; -.
KO; K17758; -.
KO; K17759; -.
OMA; LVGPGHN; -.
BioCyc; SENT454166:GHBA-4484-MONOMER; -.
Proteomes; UP000008819; 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; PS01049; YJEF_C_1; 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:UP000008819};
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}.
DOMAIN 22 224 YjeF N-terminal.
{ECO:0000259|PROSITE:PS51385}.
NP_BIND 411 415 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
NP_BIND 431 440 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
REGION 70 74 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
REGION 138 144 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
REGION 374 380 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01965}.
METAL 71 71 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
METAL 134 134 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
METAL 170 170 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
BINDING 167 167 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
BINDING 328 328 NAD(P)HX; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01965}.
BINDING 441 441 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01965}.
SEQUENCE 514 AA; 54148 MW; B588B7A6BB367139 CRC64;
MDHNMKKNPV SIPHSIWPAD DIKRLERDAA DAFGLTLYEL MLRAGDAAFR VARDSYPDTR
HWLVLCGHGN NGGDGYVVAR LAQAAGISVT LLAQESDKPL PEEAAQARDA WLNAGGIIHA
ADIIWPEATD LIIDALLGTG IAQAPRDPVA GLIEQANAHP APVVAVDIPS GLLAQTGATP
GAVISAAHTV TFIALKPGLL TGKARDVTGI LHYDALGLEG WLASQTPPLR RFDATQLGQW
LTPRRPTSHK GDHGRLAIIG GDQGTAGAIR MAGEAALRTG AGLVRVLTRG ENIAPLLTAR
PELMVHELTP QSLEESLTWA DVVVIGPGLG QQEWGKKALQ KVENVRKPML WDADALNLLA
INPDKRHNRV ITPHPGEAAR LLGCSVAEIE SDRLLSAQRL VKRYGGVVVL KGAGTIIAAE
HHPLAIIDAG NAGMASGGMG DVLSGIIGAL LGQKFTPYDA ACVGCVAHGA AADLLAARYG
ARGMLATDLF TTLRRIVNPD VIDVNHDESS NSAT


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