AKRC8_ARATH
ID AKRC8_ARATH Reviewed; 311 AA.
AC O80944; B3H474; Q3E6N6; Q3EBK9; Q93YR4;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Aldo-keto reductase family 4 member C8;
DE EC=1.1.1.-;
GN Name=AKR4C8; OrderedLocusNames=At2g37760; ORFNames=F13M22, T8P21.6;
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] (ISOFORM 1), X-RAY CRYSTALLOGRAPHY (1.4
RP ANGSTROMS) IN COMPLEX WITH NADP, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND INDUCTION.
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
CC -!- FUNCTION: Oxidoreductase acting on a broad range of substrates: reduces
CC ketosteroids, aromatic aldehydes, ketones, sugars and other aliphatic
CC aldehydes, and oxidizes hydroxysteroids. May function as detoxifiying
CC enzyme by reducing a range of toxic aldehydes and ketones produced
CC during stress. {ECO:0000269|PubMed:19616008}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.4 uM for 9,10-phenanthrenequinone {ECO:0000269|PubMed:19616008};
CC KM=35 uM for isatin {ECO:0000269|PubMed:19616008};
CC KM=1.6 mM for glyoxal {ECO:0000269|PubMed:19616008};
CC KM=3.3 mM for methylglyoxal {ECO:0000269|PubMed:19616008};
CC KM=22.4 mM for glyceraldehyde {ECO:0000269|PubMed:19616008};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O80944-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O80944-2; Sequence=VSP_040012, VSP_040015;
CC Name=3;
CC IsoId=O80944-3; Sequence=VSP_040013, VSP_040014;
CC -!- INDUCTION: By drought, salt and cold stresses.
CC {ECO:0000269|PubMed:19616008}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; AC004684; AAC23646.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09443.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09444.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09445.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09446.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09447.1; -; Genomic_DNA.
DR EMBL; AY059798; AAL24146.1; -; mRNA.
DR EMBL; AY117171; AAM51246.1; -; mRNA.
DR EMBL; DQ837653; ABH07514.1; -; mRNA.
DR PIR; T02542; T02542.
DR RefSeq; NP_001078019.1; NM_001084550.1. [O80944-3]
DR RefSeq; NP_001118465.1; NM_001124993.1. [O80944-2]
DR RefSeq; NP_565871.1; NM_129332.5. [O80944-1]
DR RefSeq; NP_973626.2; NM_201897.4. [O80944-1]
DR RefSeq; NP_973627.1; NM_201898.2. [O80944-3]
DR PDB; 3H7R; X-ray; 1.40 A; A=1-311.
DR PDBsum; 3H7R; -.
DR AlphaFoldDB; O80944; -.
DR SMR; O80944; -.
DR IntAct; O80944; 1.
DR STRING; 3702.AT2G37760.1; -.
DR PaxDb; O80944; -.
DR PRIDE; O80944; -.
DR ProteomicsDB; 244666; -. [O80944-1]
DR EnsemblPlants; AT2G37760.1; AT2G37760.1; AT2G37760. [O80944-1]
DR EnsemblPlants; AT2G37760.2; AT2G37760.2; AT2G37760. [O80944-1]
DR EnsemblPlants; AT2G37760.3; AT2G37760.3; AT2G37760. [O80944-3]
DR EnsemblPlants; AT2G37760.4; AT2G37760.4; AT2G37760. [O80944-3]
DR EnsemblPlants; AT2G37760.5; AT2G37760.5; AT2G37760. [O80944-2]
DR GeneID; 818353; -.
DR Gramene; AT2G37760.1; AT2G37760.1; AT2G37760. [O80944-1]
DR Gramene; AT2G37760.2; AT2G37760.2; AT2G37760. [O80944-1]
DR Gramene; AT2G37760.3; AT2G37760.3; AT2G37760. [O80944-3]
DR Gramene; AT2G37760.4; AT2G37760.4; AT2G37760. [O80944-3]
DR Gramene; AT2G37760.5; AT2G37760.5; AT2G37760. [O80944-2]
DR KEGG; ath:AT2G37760; -.
DR Araport; AT2G37760; -.
DR TAIR; locus:2040751; AT2G37760.
DR eggNOG; KOG1577; Eukaryota.
DR OMA; HKSKGIH; -.
DR PhylomeDB; O80944; -.
DR BioCyc; ARA:AT2G37760-MON; -.
DR BioCyc; MetaCyc:AT2G37760-MON; -.
DR SABIO-RK; O80944; -.
DR EvolutionaryTrace; O80944; -.
DR PRO; PR:O80944; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80944; baseline and differential.
DR Genevisible; O80944; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; IDA:UniProtKB.
DR GO; GO:0070401; F:NADP+ binding; IDA:UniProtKB.
DR GO; GO:0016229; F:steroid dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
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; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Detoxification; NADP;
KW Oxidoreductase; Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q0PGJ6"
FT CHAIN 2..311
FT /note="Aldo-keto reductase family 4 member C8"
FT /id="PRO_0000400312"
FT ACT_SITE 48
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 23..24
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19616008"
FT BINDING 43
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19616008"
FT BINDING 110
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19616008"
FT BINDING 154..155
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19616008"
FT BINDING 176
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19616008"
FT BINDING 203..208
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19616008"
FT BINDING 252..254
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19616008"
FT BINDING 258..262
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19616008"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q0PGJ6"
FT VAR_SEQ 284..291
FT /note="EKFCRATE -> AREVLPSY (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040012"
FT VAR_SEQ 284..290
FT /note="EKFCRAT -> AKVLPSY (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_040013"
FT VAR_SEQ 291..311
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_040014"
FT VAR_SEQ 292..311
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040015"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:3H7R"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:3H7R"
FT HELIX 28..37
FT /evidence="ECO:0007829|PDB:3H7R"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:3H7R"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:3H7R"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:3H7R"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:3H7R"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:3H7R"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:3H7R"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:3H7R"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:3H7R"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:3H7R"
FT HELIX 132..144
FT /evidence="ECO:0007829|PDB:3H7R"
FT STRAND 147..155
FT /evidence="ECO:0007829|PDB:3H7R"
FT HELIX 158..167
FT /evidence="ECO:0007829|PDB:3H7R"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:3H7R"
FT HELIX 186..195
FT /evidence="ECO:0007829|PDB:3H7R"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:3H7R"
FT TURN 210..214
FT /evidence="ECO:0007829|PDB:3H7R"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:3H7R"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:3H7R"
FT HELIX 234..244
FT /evidence="ECO:0007829|PDB:3H7R"
FT HELIX 256..262
FT /evidence="ECO:0007829|PDB:3H7R"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:3H7R"
FT HELIX 276..280
FT /evidence="ECO:0007829|PDB:3H7R"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:3H7R"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:3H7R"
FT HELIX 303..306
FT /evidence="ECO:0007829|PDB:3H7R"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:3H7R"
SQ SEQUENCE 311 AA; 34685 MW; 07958944BA05F2D9 CRC64;
MAAPIRFFEL NTGAKLPCVG LGTYAMVATA IEQAIKIGYR HIDCASIYGN EKEIGGVLKK
LIGDGFVKRE ELFITSKLWS NDHLPEDVPK ALEKTLQDLQ IDYVDLYLIH WPASLKKESL
MPTPEMLTKP DITSTWKAME ALYDSGKARA IGVSNFSSKK LTDLLNVARV TPAVNQVECH
PVWQQQGLHE LCKSKGVHLS GYSPLGSQSK GEVRLKVLQN PIVTEVAEKL GKTTAQVALR
WGLQTGHSVL PKSSSGARLK ENLDVFDWSI PEDLFTKFSN IPQEKFCRAT EFAHETHGFY
KTIEELWDGE I
