ID A0A2V4UWN7_9GAMM Unreviewed; 599 AA. AC A0A2V4UWN7; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 05-JUN-2019, 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=DFP82_109122 {ECO:0000313|EMBL:PYE38172.1}; OS Psychrobacter fozii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=198480 {ECO:0000313|EMBL:PYE38172.1, ECO:0000313|Proteomes:UP000247746}; RN [1] {ECO:0000313|EMBL:PYE38172.1, ECO:0000313|Proteomes:UP000247746} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 5889 {ECO:0000313|EMBL:PYE38172.1, RC ECO:0000313|Proteomes:UP000247746}; RA Whitman W.; RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the RT genomes of soil and plant-associated and newly described type RT strains."; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. 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-and CC R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, CC a damaged form of NAD(P)H that is a result of enzymatic or heat- CC 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 -!- 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 -!- 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:57945, ChEBI:CHEBI:64074, ChEBI:CHEBI:456215, CC ChEBI:CHEBI:456216; EC=4.2.1.136; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01965}; 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:57783, ChEBI:CHEBI:64076, ChEBI:CHEBI:456215, CC ChEBI:CHEBI:456216; EC=4.2.1.136; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01965}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01966}; CC Note=Binds 1 potassium ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01966}; 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 -!- 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:PYE38172.1}. 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; QJSU01000009; PYE38172.1; -; Genomic_DNA. DR Proteomes; UP000247746; 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-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; IPR017953; Carbohydrate_kinase_pred_CS. DR InterPro; IPR000631; CARKD. 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 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000247746}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01966}; KW Kinase {ECO:0000313|EMBL:PYE38172.1}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01965}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01966}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01965}; KW NADP {ECO:0000256|HAMAP-Rule:MF_01965}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01965}; KW Potassium {ECO:0000256|HAMAP-Rule:MF_01966}; KW Transferase {ECO:0000313|EMBL:PYE38172.1}. FT DOMAIN 23 279 YjeF N-terminal. {ECO:0000259|PROSITE: FT PS51385}. FT NP_BIND 487 491 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}. FT NP_BIND 510 519 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}. FT REGION 89 93 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT REGION 120 140 Disordered. {ECO:0000256|MobiDB-lite: FT A0A2V4UWN7}. FT REGION 188 194 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT REGION 450 456 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01965}. FT COILED 422 442 {ECO:0000256|SAM:Coils}. FT METAL 90 90 Potassium. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT METAL 184 184 Potassium. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT METAL 224 224 Potassium. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT BINDING 199 199 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT BINDING 221 221 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT BINDING 387 387 NAD(P)HX; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01965}. FT BINDING 520 520 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01965}. SQ SEQUENCE 599 AA; 64777 MW; 41FDCC0F9D5E0E18 CRC64; MQIHGHSSID KKHPISLYSS KQLYAMEQAW FSEGHDSFGL MQQAAWQMAK HIEQLYEKKY LNHHSSASVN FSHRHNHQYR VSIWVGKGNN GGDGWLIAYY LKQAGWQVQI VTVGFEDSDF SNSDSDQVNS DKSDTTAISN SKSSITDAQK ALQVARSANC KYERFEDSQN DLRSTALQAD VYIDALFGIG LDRTPEGIYK QAIRAFNELT EQNNGLAIAV DIPSGVVAST GEVFDRIAIK ADATLCLIAR KFGLHTKDGV DYSGQVTDIP LIPYQVDNVA FEPVAKLITT GQAFSPRRQN SYKGSYGHVL VIGGNRIDGS QGMGGAAILS ASSSMAAGAG KITVACHEAF HGALLTSLPD AMTINLHDAQ GVQHLIKAAS VVAIGMGLGR DDKAQALFVN YIQAAMTAKK PIVIDADGLY HLASLQLKND KLISQLREYS TDNEVCLTPH SGEAAKLLNK KIHEIESDRL SAIKLCAQTY GGNWVLKGAG SLVLERGLDQ EQVYVCGVGN AGMATAGMGD VLSGVIAGLL AQQDLEPEMR SLHQAVIIHG LAGDILVSQT NQYNSGKSDR GHLLIGQRGL QAQDMPVAIR HVMQLLVDS //