ID ADHX_ARATH Reviewed; 379 AA. AC Q96533; Q0WWE1; Q43384; Q9FND2; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 27-MAR-2002, sequence version 2. DT 27-MAR-2024, entry version 184. DE RecName: Full=Alcohol dehydrogenase class-3; DE EC=1.1.1.1 {ECO:0000269|PubMed:12913179, ECO:0000269|PubMed:8944774}; DE AltName: Full=Alcohol dehydrogenase class-III; DE AltName: Full=Glutathione-dependent formaldehyde dehydrogenase; DE Short=FALDH; DE Short=FDH; DE Short=GSH-FDH; DE EC=1.1.1.-; DE AltName: Full=S-(hydroxymethyl)glutathione dehydrogenase; DE EC=1.1.1.284 {ECO:0000269|PubMed:12913179, ECO:0000269|PubMed:8944774}; GN Name=ADH2; Synonyms=ADHIII, FDH1; OrderedLocusNames=At5g43940; GN ORFNames=MRH10.4; 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 [GENOMIC DNA]. RC STRAIN=cv. C24; RX PubMed=9215914; DOI=10.1093/genetics/146.3.1131; RA Dolferus R., Osterman J.C., Peacock W.J., Dennis E.S.; RT "Cloning of the Arabidopsis and rice formaldehyde dehydrogenase genes: RT implications for the origin of plant ADH enzymes."; RL Genetics 146:1131-1141(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CATALYTIC ACTIVITY, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=cv. Landsberg erecta; TISSUE=Flower; RX PubMed=8944774; DOI=10.1111/j.1432-1033.1996.00849.x; RA Martinez M.C., Achkor H., Persson B., Fernandez M.R., Shafqat J., RA Farres J., Joernvall H., Pares X.; RT "Arabidopsis formaldehyde dehydrogenase. Molecular properties of plant RT class III alcohol dehydrogenase provide further insights into the origins, RT structure and function of plant class P and liver class I alcohol RT dehydrogenases."; RL Eur. J. Biochem. 241:849-857(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=9405937; DOI=10.1093/dnares/4.4.291; RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence RT features of the regions of 1,044,062 bp covered by thirteen physically RT assigned P1 clones."; RL DNA Res. 4:291-300(1997). RN [4] 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 [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., RA Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [8] RP INDUCTION. RX PubMed=12753920; DOI=10.1016/s0014-5793(03)00426-5; RA Diaz M., Achkor H., Titarenko E., Martinez M.C.; RT "The gene encoding glutathione-dependent formaldehyde dehydrogenase/GSNO RT reductase is responsive to wounding, jasmonic acid and salicylic acid."; RL FEBS Lett. 543:136-139(2003). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND HOMODIMER. RX PubMed=12913179; DOI=10.1104/pp.103.022277; RA Achkor H., Diaz M., Fernandez M.R., Biosca J.A., Pares X., Martinez M.C.; RT "Enhanced formaldehyde detoxification by overexpression of glutathione- RT dependent formaldehyde dehydrogenase from Arabidopsis."; RL Plant Physiol. 132:2248-2255(2003). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=17951448; DOI=10.1105/tpc.107.050989; RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E., RA Rasche N., Lueder F., Weckwerth W., Jahn O.; RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting RT peptides, metabolic pathways, and defense mechanisms."; RL Plant Cell 19:3170-3193(2007). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=cv. Columbia; RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004; RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., RA Rathjen J.P., Peck S.C.; RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis RT thaliana."; RL J. Proteomics 72:439-451(2009). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 2-379 IN COMPLEX WITH NAD AND RP ZINC, AND HOMODIMER. RA Crotty J., Greving M., Brettschneider S., Weichsel A., Wildner G.F., RA Vierling E., Montfort W.R.; RT "Crystal structure and kinetic behavior of alcohol dehydrogenase III /S- RT nitrosoglutathione reductase from arabidopsis thaliana."; RL Submitted (NOV-2011) to the PDB data bank. CC -!- FUNCTION: Plays a central role in formaldehyde detoxification. CC {ECO:0000269|PubMed:12913179}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; CC Evidence={ECO:0000269|PubMed:12913179, ECO:0000269|PubMed:8944774}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH; CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087, CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; CC Evidence={ECO:0000269|PubMed:12913179, ECO:0000269|PubMed:8944774}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NADP(+) + S-(hydroxymethyl)glutathione = H(+) + NADPH + S- CC formylglutathione; Xref=Rhea:RHEA:19981, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57688, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:58758; EC=1.1.1.284; CC Evidence={ECO:0000269|PubMed:12913179, ECO:0000269|PubMed:8944774}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + S-(hydroxymethyl)glutathione = H(+) + NADH + S- CC formylglutathione; Xref=Rhea:RHEA:19985, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57688, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:58758; EC=1.1.1.284; CC Evidence={ECO:0000269|PubMed:12913179, ECO:0000269|PubMed:8944774}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|Ref.13}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|Ref.13}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.4 uM for S-(hydroxymethyl)glutathione CC {ECO:0000269|PubMed:8944774}; CC KM=7 uM for S-hydroxymethylglutathione (at pH 8 and 25 degrees CC Celsius) {ECO:0000269|PubMed:12913179}; CC KM=7.7 uM for farnesol (at pH 7.5 and 25 degrees Celsius) CC {ECO:0000269|PubMed:12913179}; CC KM=22000 uM for cinnamylalcohol (at pH 7.5 and 25 degrees Celsius) CC {ECO:0000269|PubMed:12913179}; CC KM=3 uM for farnesol (at pH 10 and 25 degrees Celsius) CC {ECO:0000269|PubMed:12913179}; CC KM=800 uM for geraniol (at pH 10 and 25 degrees Celsius) CC {ECO:0000269|PubMed:12913179}; CC KM=3500 uM for cinnamylalcohol (at pH 10 and 25 degrees Celsius) CC {ECO:0000269|PubMed:12913179}; CC KM=4700 uM for 12-Hydroxydodecanoic acid (at pH 10 and 25 degrees CC Celsius) {ECO:0000269|PubMed:12913179}; CC Vmax=1.22 umol/min/mg enzyme {ECO:0000269|PubMed:8944774}; CC Note=kcat is 1351 min(-1) with S-hydroxymethylglutathione as CC substrate (at pH 8 and 25 degrees Celsius). kcat is 6 min(-1) with CC farnesol as substrate (at pH 7.5 and 25 degrees Celsius). kcat is 324 CC min(-1) with cinnamylalcohol as substrate (at pH 7.5 and 25 degrees CC Celsius). kcat is 126 min(-1) with farnesol as substrate (at pH 10 CC and 25 degrees Celsius). kcat is 1200 min(-1) with geraniol as CC substrate (at pH 10 and 25 degrees Celsius). kcat is 1220 min(-1) CC with cinnamylalcohol as substrate (at pH 10 and 25 degrees Celsius). CC kcat is 335 min(-1) with 12-Hydroxydodecanoic acid as substrate (at CC pH 10 and 25 degrees Celsius). {ECO:0000269|PubMed:12913179}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12913179, ECO:0000269|Ref.13}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06525}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced. According to EST CC sequences.; CC Name=1; CC IsoId=Q96533-1; Sequence=Displayed; CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8944774}. CC -!- INDUCTION: Down-regulated by wounding and activated by salicylic acid CC (SA). {ECO:0000269|PubMed:12753920}. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. Class-III subfamily. {ECO:0000305}. 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; U63931; AAB06322.1; -; Genomic_DNA. DR EMBL; X82647; CAA57973.1; -; mRNA. DR EMBL; AB006703; BAB09054.1; -; Genomic_DNA. DR EMBL; CP002688; AED95034.1; -; Genomic_DNA. DR EMBL; AY039601; AAK62656.1; -; mRNA. DR EMBL; BT010169; AAQ22638.1; -; mRNA. DR EMBL; AK226412; BAE98557.1; -; mRNA. DR EMBL; AY087250; AAM64806.1; -; mRNA. DR PIR; S71244; S71244. DR RefSeq; NP_199207.1; NM_123761.4. [Q96533-1] DR PDB; 3UKO; X-ray; 1.40 A; A/B=2-379. DR PDB; 4GL4; X-ray; 1.80 A; A/B=2-379. DR PDB; 4JJI; X-ray; 1.80 A; A/B=2-379. DR PDB; 4L0Q; X-ray; 1.95 A; A/B=2-379. DR PDBsum; 3UKO; -. DR PDBsum; 4GL4; -. DR PDBsum; 4JJI; -. DR PDBsum; 4L0Q; -. DR AlphaFoldDB; Q96533; -. DR SMR; Q96533; -. DR BioGRID; 19667; 4. DR STRING; 3702.Q96533; -. DR iPTMnet; Q96533; -. DR PaxDb; 3702-AT5G43940-2; -. DR ProteomicsDB; 244654; -. [Q96533-1] DR EnsemblPlants; AT5G43940.1; AT5G43940.1; AT5G43940. [Q96533-1] DR GeneID; 834417; -. DR Gramene; AT5G43940.1; AT5G43940.1; AT5G43940. [Q96533-1] DR KEGG; ath:AT5G43940; -. DR Araport; AT5G43940; -. DR TAIR; AT5G43940; HOT5. DR eggNOG; KOG0022; Eukaryota. DR HOGENOM; CLU_026673_14_0_1; -. DR InParanoid; Q96533; -. DR OMA; IKGRSEM; -. DR PhylomeDB; Q96533; -. DR BioCyc; ARA:AT5G43940-MONOMER; -. DR SABIO-RK; Q96533; -. DR PRO; PR:Q96533; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; Q96533; baseline and differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IBA:GO_Central. DR GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase activity; IBA:GO_Central. DR GO; GO:0106322; F:S-(hydroxymethyl)glutathione dehydrogenase NAD activity; IEA:UniProtKB-EC. DR GO; GO:0106321; F:S-(hydroxymethyl)glutathione dehydrogenase NADP activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central. DR GO; GO:0006069; P:ethanol oxidation; IEA:InterPro. DR GO; GO:0046294; P:formaldehyde catabolic process; IBA:GO_Central. DR CDD; cd08300; alcohol_DH_class_III; 1. DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR013149; ADH-like_C. DR InterPro; IPR013154; ADH-like_N. DR InterPro; IPR014183; ADH_3. DR InterPro; IPR002328; ADH_Zn_CS. DR InterPro; IPR011032; GroES-like_sf. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR02818; adh_III_F_hyde; 1. DR PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1. DR PANTHER; PTHR43880:SF58; ALCOHOL DEHYDROGENASE CLASS-3; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SUPFAM; SSF50129; GroES-like; 2. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00059; ADH_ZINC; 1. DR Genevisible; Q96533; AT. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Metal-binding; KW NAD; Oxidoreductase; Reference proteome; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22223895" FT CHAIN 2..379 FT /note="Alcohol dehydrogenase class-3" FT /id="PRO_0000160771" FT BINDING 47 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:3UKO, FT ECO:0007744|PDB:4GL4, ECO:0007744|PDB:4JJI, FT ECO:0007744|PDB:4L0Q" FT BINDING 48 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:3UKO, FT ECO:0007744|PDB:4GL4, ECO:0007744|PDB:4JJI, FT ECO:0007744|PDB:4L0Q" FT BINDING 49 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P06525" FT BINDING 69 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00327" FT BINDING 69 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:3UKO, FT ECO:0007744|PDB:4GL4, ECO:0007744|PDB:4JJI, FT ECO:0007744|PDB:4L0Q" FT BINDING 70 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:3UKO, FT ECO:0007744|PDB:4GL4, ECO:0007744|PDB:4JJI, FT ECO:0007744|PDB:4L0Q" FT BINDING 99 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:3UKO, FT ECO:0007744|PDB:4GL4, ECO:0007744|PDB:4JJI, FT ECO:0007744|PDB:4L0Q" FT BINDING 102 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:3UKO, FT ECO:0007744|PDB:4GL4, ECO:0007744|PDB:4JJI, FT ECO:0007744|PDB:4L0Q" FT BINDING 105 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:3UKO, FT ECO:0007744|PDB:4GL4, ECO:0007744|PDB:4JJI, FT ECO:0007744|PDB:4L0Q" FT BINDING 113 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:3UKO, FT ECO:0007744|PDB:4GL4, ECO:0007744|PDB:4JJI, FT ECO:0007744|PDB:4L0Q" FT BINDING 177 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:3UKO, FT ECO:0007744|PDB:4GL4, ECO:0007744|PDB:4JJI, FT ECO:0007744|PDB:4L0Q" FT BINDING 202..207 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:3UKO, FT ECO:0007744|PDB:4GL4, ECO:0007744|PDB:4JJI, FT ECO:0007744|PDB:4L0Q" FT BINDING 226 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:3UKO, FT ECO:0007744|PDB:4GL4, ECO:0007744|PDB:4JJI, FT ECO:0007744|PDB:4L0Q" FT BINDING 231 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:3UKO, FT ECO:0007744|PDB:4JJI, ECO:0007744|PDB:4L0Q" FT BINDING 272 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:3UKO, FT ECO:0007744|PDB:4GL4, ECO:0007744|PDB:4JJI, FT ECO:0007744|PDB:4L0Q" FT BINDING 295..297 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:3UKO, FT ECO:0007744|PDB:4GL4, ECO:0007744|PDB:4JJI, FT ECO:0007744|PDB:4L0Q" FT BINDING 320..322 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:3UKO, FT ECO:0007744|PDB:4GL4, ECO:0007744|PDB:4JJI, FT ECO:0007744|PDB:4L0Q" FT BINDING 372 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:3UKO, FT ECO:0007744|PDB:4JJI, ECO:0007744|PDB:4L0Q" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22223895" FT CONFLICT 84 FT /note="E -> G (in Ref. 1; AAB06322)" FT /evidence="ECO:0000305" FT CONFLICT 354 FT /note="T -> S (in Ref. 2; CAA57973)" FT /evidence="ECO:0000305" FT STRAND 8..15 FT /evidence="ECO:0007829|PDB:3UKO" FT STRAND 23..29 FT /evidence="ECO:0007829|PDB:3UKO" FT STRAND 36..46 FT /evidence="ECO:0007829|PDB:3UKO" FT HELIX 48..54 FT /evidence="ECO:0007829|PDB:3UKO" FT STRAND 63..65 FT /evidence="ECO:0007829|PDB:3UKO" FT STRAND 70..78 FT /evidence="ECO:0007829|PDB:3UKO" FT STRAND 90..93 FT /evidence="ECO:0007829|PDB:3UKO" FT STRAND 100..102 FT /evidence="ECO:0007829|PDB:3UKO" FT HELIX 103..107 FT /evidence="ECO:0007829|PDB:3UKO" FT HELIX 117..120 FT /evidence="ECO:0007829|PDB:3UKO" FT TURN 121..123 FT /evidence="ECO:0007829|PDB:3UKO" FT TURN 126..128 FT /evidence="ECO:0007829|PDB:3UKO" FT STRAND 132..135 FT /evidence="ECO:0007829|PDB:3UKO" FT STRAND 138..141 FT /evidence="ECO:0007829|PDB:3UKO" FT TURN 144..146 FT /evidence="ECO:0007829|PDB:3UKO" FT STRAND 149..156 FT /evidence="ECO:0007829|PDB:3UKO" FT HELIX 157..159 FT /evidence="ECO:0007829|PDB:3UKO" FT STRAND 160..162 FT /evidence="ECO:0007829|PDB:3UKO" FT HELIX 169..172 FT /evidence="ECO:0007829|PDB:3UKO" FT HELIX 173..176 FT /evidence="ECO:0007829|PDB:3UKO" FT HELIX 178..187 FT /evidence="ECO:0007829|PDB:3UKO" FT TURN 188..190 FT /evidence="ECO:0007829|PDB:3UKO" FT STRAND 198..201 FT /evidence="ECO:0007829|PDB:3UKO" FT HELIX 205..217 FT /evidence="ECO:0007829|PDB:3UKO" FT STRAND 222..225 FT /evidence="ECO:0007829|PDB:3UKO" FT HELIX 231..236 FT /evidence="ECO:0007829|PDB:3UKO" FT TURN 237..239 FT /evidence="ECO:0007829|PDB:3UKO" FT STRAND 242..244 FT /evidence="ECO:0007829|PDB:3UKO" FT HELIX 246..248 FT /evidence="ECO:0007829|PDB:3UKO" FT HELIX 253..260 FT /evidence="ECO:0007829|PDB:3UKO" FT STRAND 265..270 FT /evidence="ECO:0007829|PDB:3UKO" FT HELIX 275..283 FT /evidence="ECO:0007829|PDB:3UKO" FT TURN 287..289 FT /evidence="ECO:0007829|PDB:3UKO" FT STRAND 291..294 FT /evidence="ECO:0007829|PDB:3UKO" FT STRAND 304..306 FT /evidence="ECO:0007829|PDB:3UKO" FT HELIX 309..312 FT /evidence="ECO:0007829|PDB:3UKO" FT STRAND 316..319 FT /evidence="ECO:0007829|PDB:3UKO" FT HELIX 322..324 FT /evidence="ECO:0007829|PDB:3UKO" FT HELIX 327..339 FT /evidence="ECO:0007829|PDB:3UKO" FT HELIX 346..348 FT /evidence="ECO:0007829|PDB:3UKO" FT STRAND 349..354 FT /evidence="ECO:0007829|PDB:3UKO" FT HELIX 355..357 FT /evidence="ECO:0007829|PDB:3UKO" FT HELIX 358..364 FT /evidence="ECO:0007829|PDB:3UKO" FT STRAND 371..376 FT /evidence="ECO:0007829|PDB:3UKO" SQ SEQUENCE 379 AA; 40699 MW; 045054298F16B258 CRC64; MATQGQVITC KAAVAYEPNK PLVIEDVQVA PPQAGEVRIK ILYTALCHTD AYTWSGKDPE GLFPCILGHE AAGIVESVGE GVTEVQAGDH VIPCYQAECR ECKFCKSGKT NLCGKVRSAT GVGIMMNDRK SRFSVNGKPI YHFMGTSTFS QYTVVHDVSV AKIDPTAPLD KVCLLGCGVP TGLGAVWNTA KVEPGSNVAI FGLGTVGLAV AEGAKTAGAS RIIGIDIDSK KYETAKKFGV NEFVNPKDHD KPIQEVIVDL TDGGVDYSFE CIGNVSVMRA ALECCHKGWG TSVIVGVAAS GQEISTRPFQ LVTGRVWKGT AFGGFKSRTQ VPWLVEKYMN KEIKVDEYIT HNLTLGEINK AFDLLHEGTC LRCVLDTSK //