NNRD_ARATH
ID NNRD_ARATH Reviewed; 365 AA.
AC Q94AF2;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=ATP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000255|HAMAP-Rule:MF_03157};
DE EC=4.2.1.93 {ECO:0000255|HAMAP-Rule:MF_03157};
DE AltName: Full=ATP-dependent NAD(P)HX dehydratase {ECO:0000255|HAMAP-Rule:MF_03157};
DE Flags: Precursor;
GN OrderedLocusNames=At5g19150; ORFNames=T24G5;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Catalyzes the dehydration of the S-form of NAD(P)HX at the
CC expense of ATP, which is converted to ADP. Together with NAD(P)HX
CC epimerase, which catalyzes the epimerization of the S- and R-forms, the
CC enzyme 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:0000255|HAMAP-Rule:MF_03157}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-NADHX + ATP = ADP + H(+) + NADH + phosphate;
CC Xref=Rhea:RHEA:19017, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57945, ChEBI:CHEBI:64074,
CC ChEBI:CHEBI:456216; EC=4.2.1.93; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03157};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-NADPHX + ATP = ADP + H(+) + NADPH + phosphate;
CC Xref=Rhea:RHEA:32231, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:64076,
CC ChEBI:CHEBI:456216; EC=4.2.1.93;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03157};
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Plastid, chloroplast {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q94AF2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94AF2-2; Sequence=VSP_059336;
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative initiation at Met-
CC 45 of isoform 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NnrD/CARKD family. {ECO:0000255|HAMAP-
CC Rule:MF_03157}.
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DR EMBL; AC069326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92660.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92661.1; -; Genomic_DNA.
DR EMBL; AY048225; AAK82488.1; -; mRNA.
DR EMBL; AY101541; AAM26662.1; -; mRNA.
DR RefSeq; NP_568369.1; NM_121920.4. [Q94AF2-1]
DR RefSeq; NP_974811.1; NM_203082.1. [Q94AF2-1]
DR AlphaFoldDB; Q94AF2; -.
DR SMR; Q94AF2; -.
DR BioGRID; 17311; 3.
DR IntAct; Q94AF2; 3.
DR STRING; 3702.AT5G19150.1; -.
DR iPTMnet; Q94AF2; -.
DR PaxDb; Q94AF2; -.
DR PRIDE; Q94AF2; -.
DR ProteomicsDB; 251067; -. [Q94AF2-1]
DR EnsemblPlants; AT5G19150.1; AT5G19150.1; AT5G19150. [Q94AF2-1]
DR EnsemblPlants; AT5G19150.2; AT5G19150.2; AT5G19150. [Q94AF2-1]
DR GeneID; 832035; -.
DR Gramene; AT5G19150.1; AT5G19150.1; AT5G19150. [Q94AF2-1]
DR Gramene; AT5G19150.2; AT5G19150.2; AT5G19150. [Q94AF2-1]
DR KEGG; ath:AT5G19150; -.
DR Araport; AT5G19150; -.
DR TAIR; locus:2182147; AT5G19150.
DR eggNOG; KOG3974; Eukaryota.
DR HOGENOM; CLU_030651_2_2_1; -.
DR InParanoid; Q94AF2; -.
DR OMA; HIPHTNE; -.
DR PhylomeDB; Q94AF2; -.
DR BRENDA; 4.2.1.136; 399.
DR BRENDA; 4.2.1.93; 399.
DR PRO; PR:Q94AF2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94AF2; baseline and differential.
DR Genevisible; Q94AF2; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
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:0047453; F:ATP-dependent NAD(P)H-hydrate dehydratase activity; IDA:TAIR.
DR GO; GO:0110051; P:metabolite repair; IBA:GO_Central.
DR GO; GO:0006734; P:NADH metabolic process; IMP:TAIR.
DR GO; GO:0006739; P:NADP metabolic process; IMP:TAIR.
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 HAMAP; MF_01965; NADHX_dehydratase; 1.
DR InterPro; IPR000631; CARKD.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF01256; Carb_kinase; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR00196; yjeF_cterm; 1.
DR PROSITE; PS51383; YJEF_C_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative initiation; ATP-binding; Chloroplast; Cytoplasm;
KW Lyase; NAD; NADP; Nucleotide-binding; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..43
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 44..365
FT /note="ATP-dependent (S)-NAD(P)H-hydrate dehydratase"
FT /id="PRO_0000416173"
FT DOMAIN 53..361
FT /note="YjeF C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 169
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 222..228
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 262..266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 281..290
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 291
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT VAR_SEQ 1..44
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_059336"
FT INIT_MET Q94AF2-2:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES Q94AF2-2:2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 365 AA; 39269 MW; F9A56BE398A439A0 CRC64;
MLVKPSIISG LVRLTSHSPS SSSSVLRRQE FLVRTLCGSP IIRAMSSTSE ADAESVLRTV
TPSLDLKRHK GQAGKIAVIG GCREYTGAPY FAAISALKIG ADLSHVFCTK DAAPVIKSYS
PELIVHPVLE ESYSISQLSE EDKREVQDKV LGEVGKWMER FDCLVIGPGL GRDPFLLECV
SIIMLLAKKS NVPFVIDGDG LFLVTNSIDL VHSYPLAVLT PNVNEYKRLV QKVLNCEVDE
QNAEDQLRSL AKQIGGVTIL RKGKSDLISN GETVKSVSIY GSPRRCGGQG DILSGGVAVF
LSWAQQLKSD PESPSENPAI LGCIAASGLL RKAASLAFTK HKRSTLTSDI IECLGESLED
ICPAS
