GENTAUR Molecular Products.

 A0A222AXZ3_ECOLX        Unreviewed;       515 AA.
 A0A222AXZ3;
 25-OCT-2017, integrated into UniProtKB/TrEMBL.
 25-OCT-2017, sequence version 1.
 28-MAR-2018, entry version 6.
 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=AKN40_4496 {ECO:0000313|EMBL:ASO81258.1};
 Escherichia coli.
 Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
 Enterobacteriaceae; Escherichia.
 NCBI_TaxID=562 {ECO:0000313|EMBL:ASO81258.1, ECO:0000313|Proteomes:UP000203621};
 [1] {ECO:0000313|EMBL:ASO81258.1, ECO:0000313|Proteomes:UP000203621}
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=MEM {ECO:0000313|EMBL:ASO81258.1,
 ECO:0000313|Proteomes:UP000203621};
 Liu B.;
 "Domestication mutations in four distinct E. coli isolates are strain-
 specific and environment dependent.";
 Submitted (AUG-2015) 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: (6R)-6-beta-hydroxy-1,4,5,6-
     tetrahydronicotinamide-adenine dinucleotide = (6S)-6-beta-hydroxy-
     1,4,5,6-tetrahydronicotinamide-adenine dinucleotide.
     {ECO:0000256|HAMAP-Rule:MF_01966, 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|HAMAP-Rule:MF_01966,
     ECO:0000256|PIRNR:PIRNR017184}.
 -!- CATALYTIC ACTIVITY: ADP + (6S)-6-beta-hydroxy-1,4,5,6-
     tetrahydronicotinamide adenine-dinucleotide = AMP + phosphate +
     NADH. {ECO:0000256|HAMAP-Rule:MF_01965,
     ECO:0000256|PIRNR:PIRNR017184}.
 -!- CATALYTIC ACTIVITY: ADP + (6S)-6-beta-hydroxy-1,4,5,6-
     tetrahydronicotinamide adenine-dinucleotide phosphate = AMP +
     phosphate + NADPH. {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; CP012378; ASO81258.1; -; Genomic_DNA.
 Proteomes; UP000203621; 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:UP000203621};
 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       23    225       YjeF N-terminal.
                              {ECO:0000259|PROSITE:PS51385}.
 NP_BIND     412    416       ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
 NP_BIND     432    441       ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
 REGION       71     75       NAD(P)HX. {ECO:0000256|HAMAP-
                              Rule:MF_01966}.
 REGION      139    145       NAD(P)HX. {ECO:0000256|HAMAP-
                              Rule:MF_01966}.
 REGION      375    381       NAD(P)HX. {ECO:0000256|HAMAP-
                              Rule:MF_01965}.
 METAL        72     72       Potassium. {ECO:0000256|HAMAP-
                              Rule:MF_01966}.
 METAL       135    135       Potassium. {ECO:0000256|HAMAP-
                              Rule:MF_01966}.
 METAL       171    171       Potassium. {ECO:0000256|HAMAP-
                              Rule:MF_01966}.
 BINDING     168    168       NAD(P)HX. {ECO:0000256|HAMAP-
                              Rule:MF_01966}.
 BINDING     329    329       NAD(P)HX; via amide nitrogen.
                              {ECO:0000256|HAMAP-Rule:MF_01965}.
 BINDING     442    442       NAD(P)HX. {ECO:0000256|HAMAP-
                              Rule:MF_01965}.
 SEQUENCE   515 AA;  54680 MW;  CE9FEB53F35B70F0 CRC64;
 MTDHTMKKNP VSIPHTVWYA DDIRRGEREA ADVLGLTLYE LMLRAGEAAF QVCRSAYPDA
 RHWLVLCGHG NNGGDGYVVA RLAKAVGIEV TLLAQESDKP LPEEAALARE AWLNAGGEIH
 ASNIVWPESV DLIVDALLGT GLRQAPRESI SQLIDHANSH PAPIVAVDIP SGLLAETGAT
 PGAVINADHT ITFIALKPGL LTGKARDVTG QLHFDSLGLD SWLAGQETKI QRFSAEQLSH
 WLKPRRPTSH KGDHGRLVII GGDHGTAGAI RMTGEAALRA GAGLVRVLTR SENIAPLLTA
 RPELMVHELM MDSLTESLEW ADVVVIGPGL GQQEWGKKAL QKVENFRKPM LWDADALNLL
 AINPDKRHNR VITPHPGEAA RLLGCSVAEI ESDRLHCAKR LVQRYGGVAV LKGAGTVVAA
 HPDALGIIDA GNAGMASGGM GDVLSGIIGA LLGQKLSPYD AACAGCVAHG AAADVLAARF
 GTRGMLATDL FSTLQRIVNP EVTDKNHDES SNSAP

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