ADH1A_HUMAN
ID ADH1A_HUMAN Reviewed; 375 AA.
AC P07327; A8K3E3; Q17R68;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Alcohol dehydrogenase 1A;
DE EC=1.1.1.1 {ECO:0000269|PubMed:2738060};
DE AltName: Full=Alcohol dehydrogenase subunit alpha;
GN Name=ADH1A; Synonyms=ADH1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-375, CLEAVAGE OF
RP INITIATOR METHIONINE, AND ACETYLATION AT SER-2.
RC TISSUE=Liver;
RX PubMed=3013304; DOI=10.1021/bi00357a026;
RA von Bahr-Lindstroem H., Hoeoeg J.-O., Heden L.-O., Kaiser R., Fleetwood L.,
RA Larsson K., Lake M., Holmquist B., Holmgren A., Hempel J., Vallee B.L.,
RA Joernvall H.;
RT "cDNA and protein structure for the alpha subunit of human liver alcohol
RT dehydrogenase.";
RL Biochemistry 25:2465-2470(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2935875; DOI=10.1073/pnas.83.3.634;
RA Ikuta T., Szeto S., Yoshida A.;
RT "Three human alcohol dehydrogenase subunits: cDNA structure and molecular
RT and evolutionary divergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:634-638(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2920825; DOI=10.1016/0014-5793(89)81217-7;
RA Matsuo Y., Yokoyama S.;
RT "Molecular structure of the human alcohol dehydrogenase 1 gene.";
RL FEBS Lett. 243:57-60(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RX PubMed=2347582; DOI=10.1016/0888-7543(90)90535-3;
RA Yasunami M., Kikuchi I., Sarapata D., Yoshida A.;
RT "The human class I alcohol dehydrogenase gene cluster: three genes are
RT tandemly organized in an 80-kb-long segment of the genome.";
RL Genomics 7:152-158(1990).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=2738060; DOI=10.1016/s0021-9258(18)60436-3;
RA Stone C.L., Li T.K., Bosron W.F.;
RT "Stereospecific oxidation of secondary alcohols by human alcohol
RT dehydrogenases.";
RL J. Biol. Chem. 264:11112-11116(1989).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 2-375 IN COMPLEX WITH NAD AND
RP ZINC IONS.
RX PubMed=15449945; DOI=10.1021/bi0489107;
RA Gibbons B.J., Hurley T.D.;
RT "Structure of three class I human alcohol dehydrogenases complexed with
RT isoenzyme specific formamide inhibitors.";
RL Biochemistry 43:12555-12562(2004).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-375 IN COMPLEX WITH NAD AND ZINC
RP IONS.
RX PubMed=11274460; DOI=10.1110/ps.45001;
RA Niederhut M.S., Gibbons B.J., Perez-Miller S., Hurley T.D.;
RT "Three-dimensional structures of the three human class I alcohol
RT dehydrogenases.";
RL Protein Sci. 10:697-706(2001).
CC -!- FUNCTION: Alcohol dehydrogenase (PubMed:2738060). Oxidizes primary as
CC well as secondary alcohols. Ethanol is a very poor substrate
CC (PubMed:2738060). {ECO:0000269|PubMed:2738060}.
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:2738060};
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:2738060};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butan-1-ol + NAD(+) = butanal + H(+) + NADH;
CC Xref=Rhea:RHEA:33199, ChEBI:CHEBI:15378, ChEBI:CHEBI:15743,
CC ChEBI:CHEBI:28885, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:2738060};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-propanol + NAD(+) = H(+) + NADH + propanal;
CC Xref=Rhea:RHEA:50704, ChEBI:CHEBI:15378, ChEBI:CHEBI:17153,
CC ChEBI:CHEBI:28831, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:2738060};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:11274460, ECO:0000269|PubMed:15449945};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:11274460,
CC ECO:0000269|PubMed:15449945};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=32 uM for butan-1-ol {ECO:0000269|PubMed:2738060};
CC KM=14 uM for 1-propanol {ECO:0000269|PubMed:2738060};
CC KM=6100 uM for ethanol {ECO:0000269|PubMed:2738060};
CC -!- SUBUNIT: Dimer of identical or heterodimer of closely related subunits
CC alpha, beta, or gamma that are encoded by genes ADH1A, ADH1B, and
CC ADH1C, respectively. {ECO:0000269|PubMed:11274460,
CC ECO:0000269|PubMed:15449945}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: There are 7 different ADH's isozymes in human: three
CC belongs to class-I: ADH1A, ADH1B, and ADH1C, one to class-II: ADH4, one
CC to class-III: ADH5, one to class-IV: ADH7 and one to class-V: ADH6.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/adh1a/";
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DR EMBL; M12963; AAA51590.1; -; mRNA.
DR EMBL; M12271; AAA68131.1; -; mRNA.
DR EMBL; BT019812; AAV38615.1; -; mRNA.
DR EMBL; AY948115; AAX20115.1; -; Genomic_DNA.
DR EMBL; AK290558; BAF83247.1; -; mRNA.
DR EMBL; CH471057; EAX06094.1; -; Genomic_DNA.
DR EMBL; BC074738; AAH74738.1; -; mRNA.
DR EMBL; BC117442; AAI17443.1; -; mRNA.
DR EMBL; BC126306; AAI26307.1; -; mRNA.
DR EMBL; M37066; AAA51591.1; -; Genomic_DNA.
DR CCDS; CCDS3648.1; -.
DR PIR; S02265; DEHUAA.
DR RefSeq; NP_000658.1; NM_000667.3.
DR PDB; 1HSO; X-ray; 2.50 A; A/B=2-375.
DR PDB; 1U3T; X-ray; 2.49 A; A/B=2-375.
DR PDBsum; 1HSO; -.
DR PDBsum; 1U3T; -.
DR AlphaFoldDB; P07327; -.
DR SMR; P07327; -.
DR BioGRID; 106636; 4.
DR IntAct; P07327; 2.
DR STRING; 9606.ENSP00000209668; -.
DR BindingDB; P07327; -.
DR ChEMBL; CHEMBL1970; -.
DR DrugBank; DB02721; 4-Iodopyrazole.
DR DrugBank; DB00898; Ethanol.
DR DrugBank; DB01213; Fomepizole.
DR DrugBank; DB04065; N-Cyclopentyl-N-Cyclobutylformamide.
DR DrugBank; DB00157; NADH.
DR DrugCentral; P07327; -.
DR iPTMnet; P07327; -.
DR PhosphoSitePlus; P07327; -.
DR BioMuta; ADH1A; -.
DR DMDM; 113390; -.
DR jPOST; P07327; -.
DR MassIVE; P07327; -.
DR MaxQB; P07327; -.
DR PaxDb; P07327; -.
DR PeptideAtlas; P07327; -.
DR PRIDE; P07327; -.
DR ProteomicsDB; 51988; -.
DR Antibodypedia; 4031; 262 antibodies from 32 providers.
DR DNASU; 124; -.
DR Ensembl; ENST00000209668.3; ENSP00000209668.2; ENSG00000187758.8.
DR GeneID; 124; -.
DR KEGG; hsa:124; -.
DR MANE-Select; ENST00000209668.3; ENSP00000209668.2; NM_000667.4; NP_000658.1.
DR UCSC; uc003hur.3; human.
DR CTD; 124; -.
DR DisGeNET; 124; -.
DR GeneCards; ADH1A; -.
DR HGNC; HGNC:249; ADH1A.
DR HPA; ENSG00000187758; Tissue enriched (liver).
DR MIM; 103700; gene.
DR neXtProt; NX_P07327; -.
DR OpenTargets; ENSG00000187758; -.
DR PharmGKB; PA24570; -.
DR VEuPathDB; HostDB:ENSG00000187758; -.
DR eggNOG; KOG0022; Eukaryota.
DR GeneTree; ENSGT00940000155234; -.
DR HOGENOM; CLU_026673_14_0_1; -.
DR InParanoid; P07327; -.
DR OMA; ITPGHEF; -.
DR OrthoDB; 664798at2759; -.
DR PhylomeDB; P07327; -.
DR TreeFam; TF300429; -.
DR PathwayCommons; P07327; -.
DR Reactome; R-HSA-2161541; Abacavir metabolism.
DR Reactome; R-HSA-5365859; RA biosynthesis pathway.
DR Reactome; R-HSA-71384; Ethanol oxidation.
DR SABIO-RK; P07327; -.
DR SignaLink; P07327; -.
DR BioGRID-ORCS; 124; 13 hits in 1061 CRISPR screens.
DR ChiTaRS; ADH1A; human.
DR EvolutionaryTrace; P07327; -.
DR GeneWiki; ADH1A; -.
DR GenomeRNAi; 124; -.
DR Pharos; P07327; Tclin.
DR PRO; PR:P07327; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P07327; protein.
DR Bgee; ENSG00000187758; Expressed in right lobe of liver and 110 other tissues.
DR Genevisible; P07327; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IDA:UniProtKB.
DR GO; GO:1990362; F:butanol dehydrogenase activity; IEA:RHEA.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0006066; P:alcohol metabolic process; IDA:UniProtKB.
DR GO; GO:0006069; P:ethanol oxidation; IBA:GO_Central.
DR GO; GO:0042573; P:retinoic acid metabolic process; IBA:GO_Central.
DR GO; GO:0042572; P:retinol metabolic process; IBA:GO_Central.
DR InterPro; IPR013149; ADH-like_C.
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 InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Metal-binding; NAD; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3013304"
FT CHAIN 2..375
FT /note="Alcohol dehydrogenase 1A"
FT /id="PRO_0000160658"
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|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HSO,
FT ECO:0007744|PDB:1U3T"
FT BINDING 48..52
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HSO,
FT ECO:0007744|PDB:1U3T"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HSO,
FT ECO:0007744|PDB:1U3T"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HSO,
FT ECO:0007744|PDB:1U3T"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HSO,
FT ECO:0007744|PDB:1U3T"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HSO,
FT ECO:0007744|PDB:1U3T"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HSO,
FT ECO:0007744|PDB:1U3T"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HSO,
FT ECO:0007744|PDB:1U3T"
FT BINDING 200..205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HSO,
FT ECO:0007744|PDB:1U3T"
FT BINDING 224
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HSO,
FT ECO:0007744|PDB:1U3T"
FT BINDING 229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HSO,
FT ECO:0007744|PDB:1U3T"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HSO,
FT ECO:0007744|PDB:1U3T"
FT BINDING 293..295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HSO,
FT ECO:0007744|PDB:1U3T"
FT BINDING 318..320
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HSO,
FT ECO:0007744|PDB:1U3T"
FT BINDING 370
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HSO,
FT ECO:0007744|PDB:1U3T"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:3013304"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00325"
FT STRAND 8..15
FT /evidence="ECO:0007829|PDB:1U3T"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:1U3T"
FT STRAND 36..45
FT /evidence="ECO:0007829|PDB:1U3T"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:1U3T"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:1U3T"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:1U3T"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1U3T"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1U3T"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:1U3T"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1U3T"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1U3T"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1U3T"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:1U3T"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:1U3T"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:1U3T"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1U3T"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:1U3T"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:1U3T"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:1U3T"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:1U3T"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:1U3T"
FT HELIX 203..214
FT /evidence="ECO:0007829|PDB:1U3T"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:1U3T"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:1U3T"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:1U3T"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:1U3T"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:1U3T"
FT HELIX 251..258
FT /evidence="ECO:0007829|PDB:1U3T"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:1U3T"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:1U3T"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:1U3T"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:1U3T"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:1U3T"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:1U3T"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:1U3T"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:1U3T"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:1U3T"
FT HELIX 325..337
FT /evidence="ECO:0007829|PDB:1U3T"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:1U3T"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:1U3T"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:1U3T"
FT HELIX 356..364
FT /evidence="ECO:0007829|PDB:1U3T"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:1U3T"
SQ SEQUENCE 375 AA; 39859 MW; B6DF4D57080D9BC1 CRC64;
MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAVGICGTD DHVVSGTMVT
PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLAIPQCGK CRICKNPESN YCLKNDVSNP
QGTLQDGTSR FTCRRKPIHH FLGISTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG
YGSAVNVAKV TPGSTCAVFG LGGVGLSAIM GCKAAGAARI IAVDINKDKF AKAKELGATE
CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ
NLSMNPMLLL TGRTWKGAIL GGFKSKECVP KLVADFMAKK FSLDALITHV LPFEKINEGF
DLLHSGKSIR TILMF
