ID Q9HQ90_HALSA Unreviewed; 472 AA. AC Q9HQ90; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 07-SEP-2016, entry version 76. DE RecName: Full=Bifunctional NAD(P)H-hydrate repair enzyme {ECO:0000256|PIRNR:PIRNR017184}; DE AltName: Full=Nicotinamide nucleotide repair protein {ECO:0000256|PIRNR:PIRNR017184}; GN OrderedLocusNames=VNG_1272C {ECO:0000313|EMBL:AAG19626.1}; OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) OS (Halobacterium halobium). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Halobacterium. OX NCBI_TaxID=64091 {ECO:0000313|EMBL:AAG19626.1, ECO:0000313|Proteomes:UP000000554}; RN [1] {ECO:0000313|EMBL:AAG19626.1, ECO:0000313|Proteomes:UP000000554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1 RC {ECO:0000313|Proteomes:UP000000554}; RX PubMed=11016950; DOI=10.1073/pnas.190337797; RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., RA Shukla H.D., Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., RA Swartzell S., Weir D., Hall J., Dahl T.A., Welti R., Goo Y.A., RA Leithauser B., Keller K., Cruz R., Danson M.J., Hough D.W., RA Maddocks D.G., Jablonski P.E., Krebs M.P., Angevine C.M., Dale H., RA Isenbarger T.A., Peck R.F., Pohlschroder M., Spudich J.L., Jung K.W., RA Alam M., Freitas T., Hou S., Daniels C.J., Dennis P.P., Omer A.D., RA Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L., DasSarma S.; RT "Genome sequence of Halobacterium species NRC-1."; RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000). 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 -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000256|PIRNR:PIRNR017184}; CC Note=Binds 1 potassium ion per subunit. CC {ECO:0000256|PIRNR:PIRNR017184}; 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 --------------------------------------------------------------------------- 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; AE004437; AAG19626.1; -; Genomic_DNA. DR PIR; F84282; F84282. DR ProteinModelPortal; Q9HQ90; -. DR STRING; 64091.VNG1272C; -. DR PaxDb; Q9HQ90; -. DR PRIDE; Q9HQ90; -. DR EnsemblBacteria; AAG19626; AAG19626; VNG_1272C. DR KEGG; hal:VNG1272C; -. DR eggNOG; arCOG00018; Archaea. DR eggNOG; ENOG4102TCZ; Archaea. DR eggNOG; COG0062; LUCA. DR eggNOG; COG0063; LUCA. DR InParanoid; Q9HQ90; -. DR KO; K17758; -. DR KO; K17759; -. DR OMA; NSWAATA; -. DR Proteomes; UP000000554; Chromosome. DR GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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 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|PIRNR:PIRNR017184}; KW Complete proteome {ECO:0000313|Proteomes:UP000000554}; KW Isomerase {ECO:0000256|PIRNR:PIRNR017184}; KW Lyase {ECO:0000256|PIRNR:PIRNR017184}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR017184}; KW NAD {ECO:0000256|PIRNR:PIRNR017184}; KW NADP {ECO:0000256|PIRNR:PIRNR017184}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR017184}; KW Potassium {ECO:0000256|PIRNR:PIRNR017184}; KW Reference proteome {ECO:0000313|Proteomes:UP000000554}. FT DOMAIN 1 198 YjeF N-terminal. {ECO:0000259|PROSITE: FT PS51385}. SQ SEQUENCE 472 AA; 47080 MW; DBFDC5231D4FFEA4 CRC64; MAAVDRNAAA LGVPRAQLME SSGHAVGRAV KRVADPGASV AIVAGRGNNG GDAFAAARFL DDYAVSVSLL GRPESINDRI SRANWDALQA GGYDTTTVRD AHALALDDPD VVVDALLGTG ISGPPREPEA TAIERINATD APTVAVDVPS GLDADTGATP GSAVDADRVV TFHDTTPGLA DHDHVTVADI GIPEAAETVV GPGDLLGVDR DPHGHKGDAG SVLVIGGGPY TGAPALCAQA ALRAGADLVR LAVPDAVAAE VQGFDETFIV DSVVGTRLVE EHVPDLLARA EDADAVVIGP GLGDADTTQA AVAAFLAAFE GRAVVDADAL TAVPDVETDA TLVCTPHRGE LQAMGGPTVD GSQPSRDAVE GFAAELGQTL LVTGARDVLS DGDTTRVNRS GTPGMTVGGT GDVLAGTAAA MLATQPPIQA ASAAAYATGG AGERAAEARG HGLLATDICD ALPAAIWGGQ DA //