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ALKR2_ARATH
ID   ALKR2_ARATH             Reviewed;         346 AA.
AC   Q84M96; O22706;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Probable aldo-keto reductase 2;
DE            EC=1.1.1.-;
DE   AltName: Full=ARF-GAP domain-containing protein 2;
GN   Name=AGD2; OrderedLocusNames=At1g60680; ORFNames=F8A5.20;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto
CC       reductase 13 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB71980.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAB71980.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC002292; AAB71980.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE33719.1; -; Genomic_DNA.
DR   EMBL; BT006462; AAP21270.1; -; mRNA.
DR   EMBL; AK227526; BAE99526.1; -; mRNA.
DR   PIR; B96632; B96632.
DR   RefSeq; NP_176267.3; NM_104751.5.
DR   AlphaFoldDB; Q84M96; -.
DR   SMR; Q84M96; -.
DR   STRING; 3702.AT1G60680.1; -.
DR   iPTMnet; Q84M96; -.
DR   PaxDb; Q84M96; -.
DR   PRIDE; Q84M96; -.
DR   ProteomicsDB; 244999; -.
DR   EnsemblPlants; AT1G60680.1; AT1G60680.1; AT1G60680.
DR   GeneID; 842362; -.
DR   Gramene; AT1G60680.1; AT1G60680.1; AT1G60680.
DR   KEGG; ath:AT1G60680; -.
DR   Araport; AT1G60680; -.
DR   TAIR; locus:2036591; AT1G60680.
DR   eggNOG; KOG1575; Eukaryota.
DR   HOGENOM; CLU_023205_2_1_1; -.
DR   OMA; DHIDVYR; -.
DR   OrthoDB; 1136766at2759; -.
DR   PhylomeDB; Q84M96; -.
DR   BioCyc; ARA:AT1G60680-MON; -.
DR   PRO; PR:Q84M96; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q84M96; baseline and differential.
DR   Genevisible; Q84M96; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004033; F:aldo-keto reductase (NADP) activity; IBA:GO_Central.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; SSF51430; 1.
PE   2: Evidence at transcript level;
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..346
FT                   /note="Probable aldo-keto reductase 2"
FT                   /id="PRO_0000415741"
FT   ACT_SITE        63
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         210..220
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   346 AA;  38269 MW;  8E1493F5468B56E1 CRC64;
     MAEACRVRRM KLGSQGLEVS AQGLGCMALS ARYGAPKPET DAIALLHHAI NSGVTFFDTS
     DMYGPETNEL LLGKALKDGV KEKVELATKF GFFIVEGEIS EVRGDPEYVR AACEASLKRL
     DIACIDLYYQ HRIDTRVPIE ITMRELKKLV EEGKIKYIGL SEASASTIRR AHAVHPITAV
     QIEWSLWSRD AEEDIIPICR ELGIGIVAYS PLGRGFLAAG PKLAENLEND DFRKTLPRFQ
     QENVDHNKIL FEKVSAMAEK KGCTPAQLAL AWVHHQGDDV CPIPGTTKIE NLNQNIRALS
     VKLTPEEISE LDSLAKPESV KGERYMASMS TFKNSNTPPL SSWKAT
 
 
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