ADHX_ARATH
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 03-AUG-2022, entry version 177.
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}.
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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.AT5G43940.2; -.
DR iPTMnet; Q96533; -.
DR PaxDb; Q96533; -.
DR PRIDE; Q96533; -.
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 eggNOG; KOG0022; Eukaryota.
DR HOGENOM; CLU_026673_14_0_1; -.
DR InParanoid; Q96533; -.
DR OMA; IHHYMGT; -.
DR PhylomeDB; Q96533; -.
DR BioCyc; ARA:AT5G43940-MON; -.
DR SABIO-RK; Q96533; -.
DR PRO; PR:Q96533; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q96533; baseline and differential.
DR Genevisible; Q96533; AT.
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 InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR014183; ADH_3.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR02818; adh_III_F_hyde; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
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
