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Database: UniProt
Entry: AKR1_SOYBN
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Original site: AKR1_SOYBN 
ID   AKR1_SOYBN              Reviewed;         346 AA.
AC   C6TBN2; C0JRE4;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Probable aldo-keto reductase 1;
DE            Short=GmAKR1;
DE            EC=1.1.1.-;
GN   Name=AKR1;
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Cheung F., Xiao Y., Chan A., Moskal W., Town C.D.;
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 26-346, INDUCTION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND FUNCTION.
RC   STRAIN=cv. Shinpaldal;
RX   PubMed=19277505; DOI=10.1007/s10059-009-0027-x;
RA   Hur Y.S., Shin K.H., Kim S., Nam K.H., Lee M.S., Chun J.Y., Cheon C.I.;
RT   "Overexpression of GmAKR1, a stress-induced aldo/keto reductase from
RT   soybean, retards nodule development.";
RL   Mol. Cells 27:217-223(2009).
CC   -!- FUNCTION: May interfere with the nodulation process and inhibits nodule
CC       development. {ECO:0000269|PubMed:19277505}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots. Detected in leaves, stems and
CC       mature nodules. {ECO:0000269|PubMed:19277505}.
CC   -!- DEVELOPMENTAL STAGE: Down-regulated as the nodules mature.
CC       {ECO:0000269|PubMed:19277505}.
CC   -!- INDUCTION: Not induced by auxin. Up-regulated in leaves by ethylene and
CC       salt stress. Down-regulated by abscisic acid.
CC       {ECO:0000269|PubMed:19277505}.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase 13 family.
CC       {ECO:0000305}.
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DR   EMBL; BT094946; ACU19234.1; -; mRNA.
DR   EMBL; FJ430074; ACN56468.1; -; mRNA.
DR   RefSeq; NP_001236007.1; NM_001249078.1.
DR   AlphaFoldDB; C6TBN2; -.
DR   SMR; C6TBN2; -.
DR   STRING; 3847.C6TBN2; -.
DR   PaxDb; 3847-GLYMA03G40860-1; -.
DR   GeneID; 100301897; -.
DR   KEGG; gmx:100301897; -.
DR   eggNOG; KOG1575; Eukaryota.
DR   InParanoid; C6TBN2; -.
DR   OrthoDB; 3642308at2759; -.
DR   Proteomes; UP000008827; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004033; F:aldo-keto reductase (NADP) activity; IBA:GO_Central.
DR   CDD; cd19145; AKR_AKR13D1; 1.
DR   Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   PANTHER; PTHR43625; AFLATOXIN B1 ALDEHYDE REDUCTASE; 1.
DR   PANTHER; PTHR43625:SF100; ALDO-KETO REDUCTASE 1-RELATED; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
PE   2: Evidence at transcript level;
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..346
FT                   /note="Probable aldo-keto reductase 1"
FT                   /id="PRO_0000415752"
FT   ACT_SITE        62
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         209..218
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        102
FT                   /note="E -> K (in Ref. 2; ACN56468)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        114..115
FT                   /note="TG -> AS (in Ref. 2; ACN56468)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        130
FT                   /note="H -> R (in Ref. 2; ACN56468)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        310
FT                   /note="F -> S (in Ref. 2; ACN56468)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   346 AA;  38253 MW;  8A17BCEF80DCB5C1 CRC64;
     MTQAQIQPVK LGTQGFEVSK LGFGCMGLTG AYNDPLQEQD GISVIKYAFS KGITFFDTAD
     VYGANANELL VGKALKQLPR EKIQIATKFG IASRGFPDMK IEGSPEYVRS CCETGLKRLD
     VEYIDLYYQH RVDTSVPIEE TVGELKKLVE EGKVKYIGLS EASPDTIRRA HAIHPITAVQ
     IEWSLWTRDI EEEIVPLCRE LGIGIVPYSP LGRGFFGGKG VVENVPTNSS LKAHPRFQAE
     NLDKNKNIYE RIEGLAKKHQ ATPAQLALAW VLQQGEDVVP IPGTTKIKNL DQNIGALAVK
     LSEKDLREIF EAVPIGDVAG GRYYNGLDHF SWKYANTPPK DSKIST
//
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