ID A0A2N8NSB6_STREU Unreviewed; 482 AA. AC A0A2N8NSB6; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 05-DEC-2018, entry version 6. DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01965, ECO:0000256|HAMAP-Rule:MF_01966}; DE Includes: DE RecName: Full=ADP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000256|HAMAP-Rule:MF_01965}; DE EC=4.2.1.136 {ECO:0000256|HAMAP-Rule:MF_01965}; DE AltName: Full=ADP-dependent NAD(P)HX dehydratase {ECO:0000256|HAMAP-Rule:MF_01965}; DE Includes: DE RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000256|HAMAP-Rule:MF_01966}; DE EC=5.1.99.6 {ECO:0000256|HAMAP-Rule:MF_01966}; DE AltName: Full=NAD(P)HX epimerase {ECO:0000256|HAMAP-Rule:MF_01966}; GN Name=nnrD {ECO:0000256|HAMAP-Rule:MF_01965}; GN Synonyms=nnrE {ECO:0000256|HAMAP-Rule:MF_01966}; GN ORFNames=AF335_22665 {ECO:0000313|EMBL:PNE31668.1}; OS Streptomyces eurocidicus (Streptoverticillium eurocidicus). OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=66423 {ECO:0000313|EMBL:PNE31668.1, ECO:0000313|Proteomes:UP000235945}; RN [1] {ECO:0000313|EMBL:PNE31668.1, ECO:0000313|Proteomes:UP000235945} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27428 {ECO:0000313|EMBL:PNE31668.1, RC ECO:0000313|Proteomes:UP000235945}; RA Noorani M.; RL Submitted (JUL-2015) 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: CC Reaction=(6R)-NADHX = (6S)-NADHX; Xref=Rhea:RHEA:32215, CC ChEBI:CHEBI:64074, ChEBI:CHEBI:64075; EC=5.1.99.6; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01966, CC ECO:0000256|PIRNR:PIRNR017184}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(6R)-NADPHX = (6S)-NADPHX; Xref=Rhea:RHEA:32227, CC ChEBI:CHEBI:64076, ChEBI:CHEBI:64077; EC=5.1.99.6; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01966, CC ECO:0000256|PIRNR:PIRNR017184}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate; CC Xref=Rhea:RHEA:32223, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:64074; EC=4.2.1.136; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(6S)-NADPHX + ADP = AMP + H(+) + NADPH + phosphate; CC Xref=Rhea:RHEA:32235, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:64076; EC=4.2.1.136; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01965, 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:PNE31668.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LGUI01000008; PNE31668.1; -; Genomic_DNA. DR Proteomes; UP000235945; 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:0016301; F:kinase activity; IEA:UniProtKB-KW. 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 TIGRFAMs; TIGR00197; yjeF_nterm; 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:UP000235945}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01966, KW ECO:0000256|PIRNR:PIRNR017184}; Kinase {ECO:0000313|EMBL:PNE31668.1}; 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_01965, ECO:0000256|PIRNR:PIRNR017184}; KW NADP {ECO:0000256|HAMAP-Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01965, KW ECO:0000256|PIRNR:PIRNR017184}; KW Potassium {ECO:0000256|HAMAP-Rule:MF_01966, KW ECO:0000256|PIRNR:PIRNR017184}; KW Transferase {ECO:0000313|EMBL:PNE31668.1}. FT DOMAIN 10 208 YjeF N-terminal. {ECO:0000259|PROSITE: FT PS51385}. FT NP_BIND 390 394 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}. FT NP_BIND 411 420 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}. FT REGION 58 62 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT REGION 124 130 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT REGION 353 359 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01965}. FT METAL 59 59 Potassium. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT METAL 120 120 Potassium. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT METAL 154 154 Potassium. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT BINDING 151 151 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT BINDING 305 305 NAD(P)HX; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01965}. FT BINDING 421 421 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01965}. SQ SEQUENCE 482 AA; 47900 MW; DC07F2EF1CEF701F CRC64; MRTAYSVETV RAAERALMAQ LPQGALMQRA AAGLAAACAD LLGRTYGARV ALLVGSGDNG GDALYAGARL ARRGAGVTAV LLAPERTHQG GLAALRAAGG RVASAEEGDR AVRRADLVVD GIVGIGGRGG LRPEAEALVA AAEGALVLAV DLPSGVDADS GEVRGATVRA DATVTFGAYK PGLLIDPARE RAGALRLIDI GLGPHLPRRP EAEALQHADV AALLPRPAAE SDKYRRGVVG VVAGSARYPG AAVLAVAGAL HGGAGAVRYA GPAAEAVVSR FPETLVSEGP PSKAGRVQAW VVGPGVGDDA AARRALDDVL ASDVPVLVDA DGLRLLPEAA VRARGAETVL TPHAGEAAAL LGVSRSRVES ARLSAARELA ARFGATALLK GSTTVVAAPG RTAVRVNPTG TPWLATAGSG DVLSGVTGSL LAAGLRGLDA ASVGAYLHGL AARSLGGAPL TASGVAEALA GAWGEVTGHS YE //