ADH1_GADMC
ID ADH1_GADMC Reviewed; 375 AA.
AC P26325;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Alcohol dehydrogenase 1;
DE EC=1.1.1.1;
OS Gadus morhua subsp. callarias (Baltic cod) (Gadus callarias).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX NCBI_TaxID=8053;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT ALA-1.
RC TISSUE=Liver;
RX PubMed=1567829; DOI=10.1021/bi00130a004;
RA Danielsson O., Eklund H., Joernvall H.;
RT "The major piscine liver alcohol dehydrogenase has class-mixed properties
RT in relation to mammalian alcohol dehydrogenases of classes I and III.";
RL Biochemistry 31:3751-3759(1992).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
RC TISSUE=Liver;
RX PubMed=8845755; DOI=10.1002/pro.5560050410;
RA Ramaswamy S., el Ahmad M., Danielsson O., Joernvall H., Eklund H.;
RT "Crystal structure of cod liver class I alcohol dehydrogenase: substrate
RT pocket and structurally variable segments.";
RL Protein Sci. 5:663-671(1996).
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 -!- 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 2 Zn(2+) ions per subunit.;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Functionally related to class-I mammalian enzymes, but
CC structurally related to class-III.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR PIR; A42343; A42343.
DR PDB; 1CDO; X-ray; 2.05 A; A/B=1-374.
DR PDBsum; 1CDO; -.
DR AlphaFoldDB; P26325; -.
DR SMR; P26325; -.
DR iPTMnet; P26325; -.
DR EvolutionaryTrace; P26325; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; Zinc.
FT CHAIN 1..375
FT /note="Alcohol dehydrogenase 1"
FT /id="PRO_0000160679"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 200..205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 224
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 293..295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 369
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT MOD_RES 1
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:1567829"
FT STRAND 7..14
FT /evidence="ECO:0007829|PDB:1CDO"
FT STRAND 22..28
FT /evidence="ECO:0007829|PDB:1CDO"
FT STRAND 35..44
FT /evidence="ECO:0007829|PDB:1CDO"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:1CDO"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1CDO"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:1CDO"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1CDO"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1CDO"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:1CDO"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1CDO"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:1CDO"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1CDO"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1CDO"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:1CDO"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:1CDO"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:1CDO"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1CDO"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:1CDO"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:1CDO"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:1CDO"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:1CDO"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:1CDO"
FT HELIX 203..214
FT /evidence="ECO:0007829|PDB:1CDO"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:1CDO"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:1CDO"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:1CDO"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1CDO"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:1CDO"
FT HELIX 251..259
FT /evidence="ECO:0007829|PDB:1CDO"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:1CDO"
FT HELIX 273..281
FT /evidence="ECO:0007829|PDB:1CDO"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:1CDO"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:1CDO"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:1CDO"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:1CDO"
FT HELIX 305..309
FT /evidence="ECO:0007829|PDB:1CDO"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:1CDO"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:1CDO"
FT HELIX 324..336
FT /evidence="ECO:0007829|PDB:1CDO"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:1CDO"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:1CDO"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:1CDO"
FT HELIX 355..363
FT /evidence="ECO:0007829|PDB:1CDO"
FT STRAND 368..373
FT /evidence="ECO:0007829|PDB:1CDO"
SQ SEQUENCE 375 AA; 40128 MW; 0A8BDEAA0C9BCEAD CRC64;
ATVGKVIKCK AAVAWEANKP LVIEEIEVDV PHANEIRIKI IATGVCHTDL YHLFEGKHKD
GFPVVLGHEG AGIVESVGPG VTEFQPGEKV IPLFISQCGE CRFCQSPKTN QCVKGWANES
PDVMSPKETR FTCKGRKVLQ FLGTSTFSQY TVVNQIAVAK IDPSAPLDTV CLLGCGVSTG
FGAAVNTAKV EPGSTCAVFG LGAVGLAAVM GCHSAGAKRI IAVDLNPDKF EKAKVFGATD
FVNPNDHSEP ISQVLSKMTN GGVDFSLECV GNVGVMRNAL ESCLKGWGVS VLVGWTDLHD
VATRPIQLIA GRTWKGSMFG GFKGKDGVPK MVKAYLDKKV KLDEFITHRM PLESVNDAID
LMKHGKCIRT VLSLE
