ID A0A0M3RIU9_9FLAO Unreviewed; 487 AA. AC A0A0M3RIU9; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 30-AUG-2017, entry version 15. 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=nnrE {ECO:0000256|HAMAP-Rule:MF_01966}; GN Synonyms=nnrD {ECO:0000256|HAMAP-Rule:MF_01965}; GN ORFNames=AM608_08180 {ECO:0000313|EMBL:ALC97622.1}; OS Capnocytophaga sp. oral taxon 323. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Capnocytophaga. OX NCBI_TaxID=1705617 {ECO:0000313|EMBL:ALC97622.1}; RN [1] {ECO:0000313|EMBL:ALC97622.1, ECO:0000313|Proteomes:UP000068952} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0383 {ECO:0000313|EMBL:ALC97622.1, RC ECO:0000313|Proteomes:UP000068952}; RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V., RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., RA Henderson B.A., Jones I.B., McGettigan J.A., Micheletti S.J., RA Nasrallah M.E., Ortiz D., Piller C.R., Privatt S.R., Schneider S.L., RA Sharp S., Smith T.C., Stanton J.D., Ullery H.E., Wilson R.J., RA Serrano M.G., Buck G., Lee V., Wang Y., Carvalho R., Voegtly L., RA Shi R., Duckworth R., Johnson A., Loviza R., Walstead R., Shah Z., RA Kiflezghi M., Wade K., Ball S.L., Bradley K.W., Asai D.J., RA Bowman C.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W., RA Hatfull G.F.; RL Submitted (AUG-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 S- CC 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: (6R)-6-beta-hydroxy-1,4,5,6- CC tetrahydronicotinamide-adenine dinucleotide = (6S)-6-beta-hydroxy- CC 1,4,5,6-tetrahydronicotinamide-adenine dinucleotide. CC {ECO:0000256|HAMAP-Rule:MF_01966}. CC -!- CATALYTIC ACTIVITY: (6R)-6-beta-hydroxy-1,4,5,6- CC tetrahydronicotinamide-adenine dinucleotide phosphate = (6S)-6- CC beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide CC phosphate. {ECO:0000256|HAMAP-Rule:MF_01966}. CC -!- CATALYTIC ACTIVITY: ADP + (6S)-6-beta-hydroxy-1,4,5,6- CC tetrahydronicotinamide adenine-dinucleotide = AMP + phosphate + CC NADH. {ECO:0000256|HAMAP-Rule:MF_01965}. CC -!- CATALYTIC ACTIVITY: ADP + (6S)-6-beta-hydroxy-1,4,5,6- CC tetrahydronicotinamide adenine-dinucleotide phosphate = AMP + CC phosphate + NADPH. {ECO:0000256|HAMAP-Rule:MF_01965}. 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 --------------------------------------------------------------------------- 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; CP012589; ALC97622.1; -; Genomic_DNA. DR RefSeq; WP_053581390.1; NZ_CP012589.1. DR EnsemblBacteria; ALC97622; ALC97622; AM608_08180. DR KEGG; col:AM608_08180; -. DR PATRIC; fig|1705617.3.peg.1726; -. DR Proteomes; UP000068952; Chromosome. DR GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:UniProtKB-HAMAP. 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-HAMAP. DR GO; GO:0046496; P:nicotinamide nucleotide metabolic process; IEA:UniProtKB-HAMAP. 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; IPR017953; Carbohydrate_kinase_pred_CS. DR InterPro; IPR000631; CARKD. DR InterPro; IPR030677; Nnr. DR InterPro; IPR029056; Ribokinase-like. DR InterPro; IPR004443; YjeF_N_dom. 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; PS01050; YJEF_C_2; 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:UP000068952}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01966, KW ECO:0000256|PIRNR:PIRNR017184}; Kinase {ECO:0000313|EMBL:ALC97622.1}; 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:ALC97622.1}. FT DOMAIN 9 215 YjeF N-terminal. {ECO:0000259|PROSITE: FT PS51385}. FT NP_BIND 409 413 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}. FT NP_BIND 428 437 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}. FT REGION 57 61 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT REGION 128 134 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT REGION 374 380 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01965}. FT METAL 58 58 Potassium. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT METAL 124 124 Potassium. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT METAL 160 160 Potassium. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT BINDING 157 157 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT BINDING 322 322 NAD(P)HX; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01965}. FT BINDING 438 438 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01965}. SQ SEQUENCE 487 AA; 53566 MW; FF1828F166302050 CRC64; MKILNTQQMR EADAHTISAE GITSWQLMER AATKLFEWIK EHLPKERTVT VLAGTGNNGG DGLALARMLI ADGWQVNTYL LCFSEHLSPD CQQNKELLEA QGIAIAEIRA EQVNNITFGK IVIDAAFGIG LNRPAPKWIQ QIFGNLNNSN SYILSVDMPS GLPTERIPSP EEIWVHPHQV LTFQTPKLPF FLPSTGCYIR KWEVLNIGLD EHFLKTLHPD FYYLESDIQQ LQRRRAKFSH KGTYGHALLV GGSYGKIGAV VLSGTAVLRA GAGLLTVAIP QCGYNILQTA LPEAMVLTCE EEKHYKTVEI SFTPSAIGVG IGWGTHPETA SALFGLFQQY PDTPFVIDAD ALNILAQHPE QLKTLPKNAI LTPHPKELER LIGKWDDDLH KLTKAKAFAK EHKVILLIKG AYTMMTDGEK YWINSSGNAG MATAGSGDVL TGMLTGLRAQ GYSAVEAACL GVFLHGLQGD RAAKKMGMER LIARDLL //