ID Q5D1Z4_PHRAU Unreviewed; 379 AA.
AC Q5D1Z4;
DT 29-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2005, sequence version 2.
DT 24-JAN-2024, entry version 90.
DE RecName: Full=Alcohol dehydrogenase 1 {ECO:0000256|ARBA:ARBA00041139};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN Name=ADH1 {ECO:0000313|EMBL:AAX10138.2};
OS Phragmites australis (Common reed) (Arundo australis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Arundinoideae; Molinieae; Molininae; Phragmites.
OX NCBI_TaxID=29695 {ECO:0000313|EMBL:AAX10138.2};
RN [1] {ECO:0000313|EMBL:AAX10138.2}
RP NUCLEOTIDE SEQUENCE.
RA Lee S.-C., Choi H.-K.;
RT "Alcohol dehydrogenase of Phragmites australis.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001146};
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:0000256|ARBA:ARBA00000781};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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DR EMBL; AY917130; AAX10138.2; -; mRNA.
DR AlphaFoldDB; Q5D1Z4; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08301; alcohol_DH_plants; 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; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43880:SF40; ALCOHOL DEHYDROGENASE 1; 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.
PE 2: Evidence at transcript level;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 36..128
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 205..337
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 379 AA; 41058 MW; DA6CB7EFDE30BB7F CRC64;
MATAGQVIKC KAAVAWEAGK PLSMEEVDVA PPQAMEVRIK ILFTSLCHTD VYFWEAKDQT
PVFPRIFGHE AGGIVESVGE GVTDVAPGDH VLPVFTGECK ECAHCKSAES NMCDLLRINT
DRGVMIGDGK SRLSINGKPI YHFVGTSTFS EYTVMHVGCV AKINPEAPLD KVCVLSCGIS
TGLGASINVA KPPKGSTVAI FGLGAVGLAA AEGARIAGAS RIIGIDLNAN RFEEARKFGC
TEFVNPKDHN KPVQEVLAEM TNGGVDRSVE CTGNINAMIQ AFERVHDGWG VAVLVGVPHK
DAEFKTHPMN FLNERTLKGT FFGNFKPRTD LPNVVELYMK KELELEKFIT HTISFAEINK
AFDLMVKGEG IRCIIRMDN
//