AL3F1_ARATH
ID AL3F1_ARATH Reviewed; 484 AA.
AC Q70E96; O65516;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Aldehyde dehydrogenase family 3 member F1;
DE EC=1.2.1.3;
GN Name=ALDH3F1; OrderedLocusNames=At4g36250; ORFNames=F23E13.140;
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 [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15830124; DOI=10.1007/s11103-004-7796-6;
RA Kirch H.-H., Schlingensiepen S., Kotchoni S., Sunkar R., Bartels D.;
RT "Detailed expression analysis of selected genes of the aldehyde
RT dehydrogenase(ALDH) gene superfamily in Arabidopsis thaliana.";
RL Plant Mol. Biol. 57:315-332(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
RP NOMENCLATURE.
RX PubMed=15358267; DOI=10.1016/j.tplants.2004.06.004;
RA Kirch H.-H., Bartels D., Wei Y., Schnable P.S., Wood A.J.;
RT "The ALDH gene superfamily of Arabidopsis.";
RL Trends Plant Sci. 9:371-377(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Constituively expressed at low levels.
CC {ECO:0000269|PubMed:15830124}.
CC -!- INDUCTION: Not induced by abscisic acid (ABA), dehydration and salt
CC stress. {ECO:0000269|PubMed:15830124}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18131.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80296.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ584644; CAE48163.1; -; mRNA.
DR EMBL; AL022141; CAA18131.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161589; CAB80296.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86639.1; -; Genomic_DNA.
DR PIR; T04594; T04594.
DR RefSeq; NP_195348.2; NM_119793.5.
DR AlphaFoldDB; Q70E96; -.
DR SMR; Q70E96; -.
DR BioGRID; 15064; 9.
DR IntAct; Q70E96; 8.
DR STRING; 3702.AT4G36250.1; -.
DR iPTMnet; Q70E96; -.
DR PaxDb; Q70E96; -.
DR PRIDE; Q70E96; -.
DR ProteomicsDB; 245039; -.
DR EnsemblPlants; AT4G36250.1; AT4G36250.1; AT4G36250.
DR GeneID; 829782; -.
DR Gramene; AT4G36250.1; AT4G36250.1; AT4G36250.
DR KEGG; ath:AT4G36250; -.
DR Araport; AT4G36250; -.
DR TAIR; locus:2122224; AT4G36250.
DR eggNOG; KOG2456; Eukaryota.
DR HOGENOM; CLU_005391_3_0_1; -.
DR InParanoid; Q70E96; -.
DR OMA; RHGKRWM; -.
DR OrthoDB; 646662at2759; -.
DR PhylomeDB; Q70E96; -.
DR BioCyc; ARA:AT4G36250-MON; -.
DR PRO; PR:Q70E96; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q70E96; baseline and differential.
DR Genevisible; Q70E96; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISS:TAIR.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR PANTHER; PTHR43570; PTHR43570; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
PE 2: Evidence at transcript level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..484
FT /note="Aldehyde dehydrogenase family 3 member F1"
FT /id="PRO_0000256059"
FT ACT_SITE 214
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 252
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 192..197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 119
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 59
FT /note="H -> L (in Ref. 1; CAE48163)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="Missing (in Ref. 1; CAE48163)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 53615 MW; A243419F0C926265 CRC64;
MEAMKETVEE SLREMRETFA SGRTRSLKWR KAQIGAIYEM VKDNEDKICN ALFQDLGKHS
TEAFRDELGV VLRTATVAIN CLDKWAVPKH SKLPLLFYPA KGKVISEPYG TVLVLSSWNF
PISLSLDPLI GAIAAGNTVL LKSSELSPNA SAFLAKTIPA YLDTKAIKVI EGGPDVATIL
LQHQWDKIFF TGSPKIGRII MAAAAQHLTP VTLELGGKCP TIVDHHTISK NIKSVVKRIA
GGKWGSCNGQ ACISVDYVLI EKSFAPTLID MLKPTIKSFF GENPKESGCL SRIANKHHVQ
RLSRLLSDPR VQASIVYGGS IDEDKLYVEP TILLDPPLDS EIMNEEIFGP ILPIITVRDI
QESIGIINTK PKPLAIYAFT NDENLKTRIL SETSSGSVTF NDVMIQYMCD ALPFGGVGES
GIGRYHGKYS FDCFSHEKAI MEGSLGMDLE ARYPPWNNFK LTFIRLAFRE AYFKLILLML
GLKR
