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Multifunctional fusion 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) (NAD(P)HX epimerase)]

 A0A1V3DBN5_STEMA        Unreviewed;       494 AA.
A0A1V3DBN5;
07-JUN-2017, integrated into UniProtKB/TrEMBL.
07-JUN-2017, sequence version 1.
16-JAN-2019, entry version 15.
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=nnrE {ECO:0000256|HAMAP-Rule:MF_01966};
Synonyms=nnrD {ECO:0000256|HAMAP-Rule:MF_01965};
ORFNames=BWP19_01730 {ECO:0000313|EMBL:OOD19744.1};
Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas
maltophilia).
Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
Xanthomonadaceae; Stenotrophomonas;
Stenotrophomonas maltophilia group.
NCBI_TaxID=40324 {ECO:0000313|EMBL:OOD19744.1, ECO:0000313|Proteomes:UP000189183};
[1] {ECO:0000313|EMBL:OOD19744.1, ECO:0000313|Proteomes:UP000189183}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13637 {ECO:0000313|EMBL:OOD19744.1,
ECO:0000313|Proteomes:UP000189183};
Kozyreva V.K., Truong C.-L., Greninger A.L., Mukhopadhyay R.,
Crandall J., Chaturvedi V.;
"Validation and Implementation of CLIA-Compliant Whole Genome
Sequencing (WGS) in Public Health Laboratory.";
Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
-!- 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}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:OOD19744.1}.
-----------------------------------------------------------------------
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EMBL; MTGD01000005; OOD19744.1; -; Genomic_DNA.
RefSeq; WP_024958294.1; NZ_MTGD01000005.1.
Proteomes; UP000189183; Unassembled WGS sequence.
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; 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:UP000189183};
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 13 214 YjeF N-terminal.
{ECO:0000259|PROSITE:PS51385}.
NP_BIND 403 407 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
NP_BIND 423 432 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
REGION 61 65 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
REGION 128 134 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
REGION 366 372 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01965}.
METAL 62 62 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
METAL 124 124 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
METAL 160 160 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
BINDING 157 157 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
BINDING 320 320 NAD(P)HX; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01965}.
BINDING 433 433 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01965}.
SEQUENCE 494 AA; 50342 MW; E711BEAF2E47AA3A CRC64;
MANLADLFDS AAARALDAQA SALAAESGWG LMAQAGQAAW QCLLQHWPQA QRIGVVVGAG
NNGGDGLVLA RHARKAGRAV TVIALPGKPP ATSLAQRAAS EFTSDGGTIT DFDGALPEVD
IWVDALFGLG FDRAPEGVAQ ALITALNAQT APVLALDVPS GVDADRGAVP GEAVKAALTL
QFIVPHRGLY TGDALDHCGR KALAPLQLPT AAWQGVSPAA EHWTQARLPA LLPPRRANTH
KGESGHVLCV GGNHGSGGAI AMAAEAALRA GAGLLSLATR RDHVGPLLAR LPEAMTHALE
DGDVLPALLD KARVVAIGPG LGQDEWARAM FAQLLDSDKA LVVDADALNL LAQDPRALPE
AILTPHPGEA ARLLDCSTAD IQADRYRCAQ ALAERFHAVV VLKGAGSIVT APGQVPRLIA
AGNPGMAVGG MGDLLTGIIA SLRAQGLAAF DAAATGALLH ALAGDAAAAD GARGMLPTDL
LVPLRQLANP ERSS


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