AKRCB_ARATH
ID AKRCB_ARATH Reviewed; 315 AA.
AC Q9M338;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Aldo-keto reductase family 4 member C11;
DE EC=1.1.1.-;
GN Name=AKR4C11; OrderedLocusNames=At3g53880; ORFNames=F5K20.180;
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].
RC STRAIN=cv. Columbia; TISSUE=Flower bud;
RX PubMed=19616008; DOI=10.1016/j.jmb.2009.07.023;
RA Simpson P.J., Tantitadapitak C., Reed A.M., Mather O.C., Bunce C.M.,
RA White S.A., Ride J.P.;
RT "Characterization of two novel aldo-keto reductases from Arabidopsis:
RT expression patterns, broad substrate specificity, and an open active-site
RT structure suggest a role in toxicant metabolism following stress.";
RL J. Mol. Biol. 392:465-480(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 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.
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Oxidoreductase that may act on a broad range of substrates
CC such as ketosteroids, aldehydes, ketones and sugars. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; DQ837656; ABH07517.1; -; mRNA.
DR EMBL; AL132960; CAB88350.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79153.1; -; Genomic_DNA.
DR EMBL; AY084865; AAM61428.1; -; mRNA.
DR PIR; T45928; T45928.
DR RefSeq; NP_190956.1; NM_115248.2.
DR AlphaFoldDB; Q9M338; -.
DR SMR; Q9M338; -.
DR BioGRID; 9872; 1.
DR IntAct; Q9M338; 1.
DR STRING; 3702.AT3G53880.1; -.
DR iPTMnet; Q9M338; -.
DR PaxDb; Q9M338; -.
DR PRIDE; Q9M338; -.
DR ProteomicsDB; 245062; -.
DR EnsemblPlants; AT3G53880.1; AT3G53880.1; AT3G53880.
DR GeneID; 824555; -.
DR Gramene; AT3G53880.1; AT3G53880.1; AT3G53880.
DR KEGG; ath:AT3G53880; -.
DR Araport; AT3G53880; -.
DR TAIR; locus:2084505; AT3G53880.
DR eggNOG; KOG1577; Eukaryota.
DR HOGENOM; CLU_023205_0_0_1; -.
DR InParanoid; Q9M338; -.
DR OMA; TWQAKPE; -.
DR OrthoDB; 1016440at2759; -.
DR PhylomeDB; Q9M338; -.
DR BioCyc; ARA:AT3G53880-MON; -.
DR PRO; PR:Q9M338; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M338; baseline and differential.
DR Genevisible; Q9M338; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR CDD; cd19125; AKR_AKR4C1-15; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044498; AKR4C.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; NADP; Oxidoreductase; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..315
FT /note="Aldo-keto reductase family 4 member C11"
FT /id="PRO_0000400315"
FT ACT_SITE 52
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 23..24
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 158..159
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 207..213
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 256..258
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 262..266
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q84TF0"
SQ SEQUENCE 315 AA; 35036 MW; 2C9E151EAA8A424F CRC64;
MADEIGFFQL NTGAKIPSVG LGTWQAAPGV VGDAVAAAVK IGYQHIDCAS RYGNEIEIGK
VLKKLFDDGV VKREKLFITS KIWLTDLDPP DVQDALNRTL QDLQLDYVDL YLMHWPVRLK
KGTVDFKPEN IMPIDIPSTW KAMEALVDSG KARAIGVSNF STKKLSDLVE AARVPPAVNQ
VECHPSWQQH KLHEFCKSKG IHLSGYSPLG SPGTTWVKAD VLKSPVIEMI AKEIGKSPAQ
TALRWGLQMG HSILPKSTNE GRIRENFDVL GWSIPKEMFD KFSKIEQARL VQGTSFVHET
LSPYKTLEEL WDGEI
