ID ADHL6_ARATH Reviewed; 381 AA.
AC Q8LEB2; Q3E967; Q8RV10; Q9FT42;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 27-MAR-2024, entry version 142.
DE RecName: Full=Alcohol dehydrogenase-like 6;
DE EC=1.1.1.1 {ECO:0000250|UniProtKB:P06525};
GN OrderedLocusNames=At5g24760; ORFNames=T4C12_30;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
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 [3]
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 [4]
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.
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:0000250|UniProtKB:P06525};
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:0000250|UniProtKB:P06525};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P06525};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P06525};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06525}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06525}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8LEB2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8LEB2-2; Sequence=VSP_027586;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-III subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC08250.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL392145; CAC08250.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93355.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93356.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93357.1; -; Genomic_DNA.
DR EMBL; AY079163; AAL85002.1; -; mRNA.
DR EMBL; AY094000; AAM16261.1; -; mRNA.
DR EMBL; AY085523; AAM62747.1; -; mRNA.
DR RefSeq; NP_001078619.1; NM_001085150.1. [Q8LEB2-2]
DR RefSeq; NP_568453.1; NM_122385.5. [Q8LEB2-1]
DR RefSeq; NP_974831.1; NM_203102.2. [Q8LEB2-2]
DR AlphaFoldDB; Q8LEB2; -.
DR SMR; Q8LEB2; -.
DR STRING; 3702.Q8LEB2; -.
DR iPTMnet; Q8LEB2; -.
DR PaxDb; 3702-AT5G24760-1; -.
DR ProteomicsDB; 244647; -. [Q8LEB2-1]
DR EnsemblPlants; AT5G24760.1; AT5G24760.1; AT5G24760. [Q8LEB2-1]
DR EnsemblPlants; AT5G24760.2; AT5G24760.2; AT5G24760. [Q8LEB2-2]
DR EnsemblPlants; AT5G24760.3; AT5G24760.3; AT5G24760. [Q8LEB2-2]
DR GeneID; 832545; -.
DR Gramene; AT5G24760.1; AT5G24760.1; AT5G24760. [Q8LEB2-1]
DR Gramene; AT5G24760.2; AT5G24760.2; AT5G24760. [Q8LEB2-2]
DR Gramene; AT5G24760.3; AT5G24760.3; AT5G24760. [Q8LEB2-2]
DR KEGG; ath:AT5G24760; -.
DR Araport; AT5G24760; -.
DR TAIR; AT5G24760; -.
DR eggNOG; KOG0022; Eukaryota.
DR HOGENOM; CLU_026673_14_0_1; -.
DR InParanoid; Q8LEB2; -.
DR OMA; QVNEGYQ; -.
DR OrthoDB; 451143at2759; -.
DR PhylomeDB; Q8LEB2; -.
DR BioCyc; ARA:AT5G24760-MONOMER; -.
DR PRO; PR:Q8LEB2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LEB2; baseline and differential.
DR Genevisible; Q8LEB2; AT.
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 GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
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 InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43880:SF5; ALCOHOL DEHYDROGENASE-LIKE 6; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 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 Alternative splicing; Cytoplasm; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome; Zinc.
FT CHAIN 1..381
FT /note="Alcohol dehydrogenase-like 6"
FT /id="PRO_0000299188"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 55
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00327"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 204..209
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 233
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 297..299
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00327"
FT BINDING 324
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 374
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT VAR_SEQ 1..29
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_027586"
FT CONFLICT 125
FT /note="G -> C (in Ref. 4; AAM62747)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="R -> S (in Ref. 4; AAM62747)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 40724 MW; 535CDF294FF6FE1B CRC64;
MSASSSSFEQ PQVITCNAAV AWRAGEPLVM EEVEVSPPQP LEIRIKVVCT SLCRSDLSAW
ESQSLLPRIF GHEAAGIVES IGEGVTEFEK GDHVLAVFTG ECGSCRHCIS GKSNMCQVLG
MERKGLMHSD QKTRFSIKGK PVYHYCAVSS FSEYTVVHSG CAVKVDPLAP LHKICLLSCG
VAAGLGAAWN VADVQKGSSV VIFGLGTVGL SVAQGAKLRG AAQILGVDIN PAKAEQAKTF
GVTDFINSND LSEPIPQVIK RMTGGGADFS FECVGDTGIA TTALQSCSDG WGMTVTLGVP
KAKPEVSAHY GLFLSGKSLK GTLFGGWKPK SDLPSLIDKY MNKEIMIDEF ITHNLSFDEI
NKAFVLMREG KCLRCVLHMP K
//
