ID B9RHR7_RICCO Unreviewed; 285 AA.
AC B9RHR7;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=2-alkenal reductase, putative {ECO:0000313|EMBL:EEF48689.1};
DE EC=1.3.1.74 {ECO:0000313|EMBL:EEF48689.1};
GN ORFNames=RCOM_1573010 {ECO:0000313|EMBL:EEF48689.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; EQ973781; EEF48689.1; -; Genomic_DNA.
DR AlphaFoldDB; B9RHR7; -.
DR STRING; 3988.B9RHR7; -.
DR eggNOG; ENOG502QPVS; Eukaryota.
DR InParanoid; B9RHR7; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032440; F:2-alkenal reductase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:InterPro.
DR GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR InterPro; IPR021135; PEP_COase.
DR InterPro; IPR018129; PEP_COase_Lys_AS.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR30523:SF47; PHOSPHOENOLPYRUVATE CARBOXYLASE 2; 1.
DR Pfam; PF00311; PEPcase; 1.
DR PRINTS; PR00150; PEPCARBXLASE.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR PROSITE; PS00781; PEPCASE_1; 1.
PE 4: Predicted;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Oxidoreductase {ECO:0000313|EMBL:EEF48689.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311}.
FT ACT_SITE 162
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
SQ SEQUENCE 285 AA; 32588 MW; B1950FC37D1D9BF8 CRC64;
MGTEGAEQNG VFRVTIKKKE VVAAVLPLQE HWLSLSDLDL LHQLVEVQDC YELSAEYEGK
HNPQKLAELG KVLTSLDLGD SIVVTKSFSH MLNLANLAEE VQIAYRRRIK LKKGDFADEN
SATTESDIEE TLKRLVVQLK KSPEEVFDAL KNQTVDLVLT AHPTQSVRRS LLQKHVRIRD
CLTQLYAKGI TPDDKQELDE ALQREIQAAF RTDEIRRTPP TPQDEMRAGM SYFHETIWKG
VPKFLRRVDT ALKNIGINER VPYNAPLIQF SSWWVEIVMV CFFVT
//