ID   Q1KL68_9ORYZ            Unreviewed;       974 AA.
AC   Q1KL68;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Lysine ketoglutarate reductase/saccharopine dehydrogenase biofunctional enzyme {ECO:0000313|EMBL:ABF18958.1};
GN   Name=LKR/SDH {ECO:0000313|EMBL:ABF18958.1};
OS   Zizania latifolia.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Zizaniinae; Zizania.
OX   NCBI_TaxID=58934 {ECO:0000313|EMBL:ABF18958.1};
RN   [1] {ECO:0000313|EMBL:ABF18958.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kong F.N., Jiang S.M., Meng X.B., Song C.L., Jin D.M., Wang B.;
RT   "Isolation, characterization and expression analysis of a LKR-SDH gene in
RT   Zizania latifolia (Greb).";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; DQ478935; ABF18958.1; -; mRNA.
DR   AlphaFoldDB; Q1KL68; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006553; P:lysine metabolic process; IEA:UniProt.
DR   CDD; cd12189; LKR_SDH_like; 1.
DR   CDD; cd12144; SDH_N_domain; 1.
DR   Gene3D; 1.10.1870.10; Domain 3, Saccharopine reductase; 1.
DR   Gene3D; 3.30.70.2690; LOR/SDH bifunctional enzyme, conserved domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR   InterPro; IPR007545; LOR/SDH_bifunc_enz_cons_dom.
DR   InterPro; IPR043009; LOR/SDH_bifunc_enz_cons_dom_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032095; Sacchrp_dh-like_C.
DR   InterPro; IPR005097; Sacchrp_dh_NADP.
DR   PANTHER; PTHR11133; SACCHAROPINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11133:SF22; SACCHAROPINE DEHYDROGENASE [NADP(+), L-GLUTAMATE-FORMING]-RELATED; 1.
DR   Pfam; PF04455; Saccharop_dh_N; 1.
DR   Pfam; PF16653; Sacchrp_dh_C; 1.
DR   Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR   SMART; SM01002; AlaDh_PNT_C; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   2: Evidence at transcript level;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        918..936
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          116..308
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
SQ   SEQUENCE   974 AA;  106916 MW;  ADBE65071A9C391C CRC64;
     MAAAGIRFIG IKQPKLEMIL PDRAYGFFSH THKAQKENMP LLDKILEERV SLFDYELIVG
     DDGKRLLAFG KFAGTAGLID FLHGLGQRYL GLGYSTPFLS LGQSHMYPSL AAAKSAVIAI
     GEEIATFGLP SGICPIVFVF TGTGSVSQGA QEIFKLLPHT FIDAEKLPEL SAVQSTKRVF
     QLYGCVVSSR DMVTPNDPNT RFNKADYYAH PEHYRPVFHE RIAPYASVIV NCMYWERRFP
     RLLSIDQFQQ LMKNGCPLVG ISDITCDIGG SIEFVNKSTS IESPFFRYDP STNSCHDNME
     GSGVICLAVD ILPTEFSKEA SQHFGDILSK FVASLASAKG LLELPLHLRK ACIAHAGGLT
     SLYEYIPRMR KTLIELPPAP TNPLLDKKYS TLVSLSGHLF DKFLINEALD IIETAGGSFH
     LVRCDVGQSI DDTSYSELEV GADDTATLDK IIDSLTSLAA LHGDTNARRD IELSLKIGKV
     NECGTDDSMV EGGSMVLILG AGRVCRPAAE FLTSYSNFIS SSDNNRDTDQ IHVIVASLYK
     KDAEETIDGI KNATATQVDV ADTKNLSNLV SQAEVVVSLL PASFHAAIAR VCIELKKHLV
     TASYVDEPMS KLDQAAEGAG VTILCEMGLD PGIDHMMSMK MIDEAHARKG KIKSFTSFCG
     GLPSPASANN PLAYKFSWSP AGAIRAGRNP AVYKFLGEII HVDGDKLYES AKRLRLPELP
     AFALEHLPNR NSLMYGDLYG ISEEASTVYR ATLRYEGFSE IMATFAKIGF FDVVNHPLLQ
     QTTRPTYRDF LIELFNAQNI STTAIKGSSE VSGGQEGELI SRLLSFGHCK EKEIAVKTVK
     TIKFLGLYEE TEIPKNCSSA FDVICQRMEQ RLAYGHNEQD MVLLHHEVEV EYPDGRPTEK
     HQATLLEFGK VENGRSTTAM ALTVGIPAAI GALLLLQNKI QRKGVIRPLE PEIYIPALEI
     LESSGIKLAE RVET
//