ADHX_PEA
ID ADHX_PEA Reviewed; 378 AA.
AC P80572;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Alcohol dehydrogenase class-3;
DE EC=1.1.1.1 {ECO:0000269|PubMed:8643621};
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:8643621};
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP PROTEIN SEQUENCE, ACETYLATION AT ALA-1, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8643621; DOI=10.1073/pnas.93.11.5595;
RA Shafqat J., El-Ahmad M., Danielsson O., Martinez M.C., Persson B.,
RA Pares X., Joernvall H.;
RT "Pea formaldehyde-active class III alcohol dehydrogenase: common derivation
RT of the plant and animal forms but not of the corresponding ethanol-active
RT forms (classes I and P).";
RL Proc. Natl. Acad. Sci. U.S.A. 93:5595-5599(1996).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT ALA-1.
RX PubMed=7607314; DOI=10.1016/0014-5793(95)00572-q;
RA Hjelmqvist L., Hackett M., Shafqat J., Danielsson O., Iida J.,
RA Hendrickson R.C., Michel H., Shabanowitz J., Hunt D.F., Joernvall H.;
RT "Multiplicity of N-terminal structures of medium-chain alcohol
RT dehydrogenases. Mass-spectrometric analysis of plant, lower vertebrate and
RT higher vertebrate class I, II, and III forms of the enzyme.";
RL FEBS Lett. 367:237-240(1995).
CC -!- FUNCTION: Class-III ADH is remarkably ineffective in oxidizing ethanol,
CC but it readily catalyzes the oxidation of long-chain primary alcohols
CC and the oxidation of S-(hydroxymethyl) glutathione.
CC {ECO:0000269|PubMed:8643621}.
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:8643621};
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:8643621};
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:8643621};
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:8643621};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q96533};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q96533};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=840 uM for octanol (at pH 10) {ECO:0000269|PubMed:8643621};
CC KM=180 uM for 12-OH-dodecanoic acid (at pH 10)
CC {ECO:0000269|PubMed:8643621};
CC KM=6.5 uM for NAD(+) (at pH 10) {ECO:0000269|PubMed:8643621};
CC KM=2 uM for S-(hydroxymethyl)glutathione (at pH 8)
CC {ECO:0000269|PubMed:8643621};
CC Note=kcat is 190 min(-1) with octanol as substrate (at pH 10). kcat
CC is 110 min(-1) with 12-OH-dodecanoic acid as substrate (at pH 10).
CC kcat is 380 min(-1) with S-hydroxymethylglutathione as substrate (at
CC pH 8). {ECO:0000269|PubMed:8643621};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q96533}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06525}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-III subfamily. {ECO:0000305}.
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DR PIR; S66198; S66198.
DR AlphaFoldDB; P80572; -.
DR SMR; P80572; -.
DR iPTMnet; P80572; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
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; IEA:InterPro.
DR GO; GO:0006069; P:ethanol oxidation; IEA:InterPro.
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 Acetylation; Cytoplasm; Direct protein sequencing; Metal-binding; NAD;
KW Oxidoreductase; Zinc.
FT CHAIN 1..378
FT /note="Alcohol dehydrogenase class-3"
FT /id="PRO_0000160774"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q96533"
FT BINDING 47
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q96533"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00327"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q96533"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q96533"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96533"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96533"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96533"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96533"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q96533"
FT BINDING 201..206
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q96533"
FT BINDING 225
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q96533"
FT BINDING 230
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q96533"
FT BINDING 294..296
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q96533"
FT BINDING 319..321
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q96533"
FT BINDING 371
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q96533"
FT MOD_RES 1
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:7607314,
FT ECO:0000269|PubMed:8643621"
SQ SEQUENCE 378 AA; 40489 MW; 9ED1C511219FF45B CRC64;
ATQGQVITCK AAVAWEPNKP LTIEDVEVAP PQANEVRIQI LFTALCHTDA YTLGGKDPEG
LFPCILGHEA AGIVESVGEG VTDVKPGDHV IPSYQAECGE CKFCKSPKTN LCGKVRAATG
VGVMMADRKS RFSVKGKPIY HFMGTSTFSQ YTVVHDVSVA KIHPDAPLDK VCLLGCGVPT
GLGAVWNTAK VEPGSIVAIF GLGTVGLAVA EGAKSAGASR IIGIDIDSNK YDTAKNFGVT
EFINPKDHEK PIQQVIIDLT DGGVDYSFEC LGNVSVMRSA LECCHKGWGT SVIVGVAASG
QEISTRPFQL VTGRVWKGTA FGGFKSRSQV PWLVEKYLKK EIKVDEYITH NLTLLEINKA
FDLLHEGQCL RCVLAVHD
