ID A0A0E0FLX8_ORYNI Unreviewed; 1237 AA.
AC A0A0E0FLX8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:ONIVA01G18810.1};
OS Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA01G18810.1};
RN [1] {ECO:0000313|EnsemblPlants:ONIVA01G18810.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA01G18810.1};
RA Wing R.A., Hsing Y.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ONIVA01G18810.1}
RP IDENTIFICATION.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA01G18810.1};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 1/6.
CC {ECO:0000256|ARBA:ARBA00004682}.
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 2/6.
CC {ECO:0000256|ARBA:ARBA00004720}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the saccharopine
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00025744}.
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DR AlphaFoldDB; A0A0E0FLX8; -.
DR STRING; 4536.A0A0E0FLX8; -.
DR EnsemblPlants; ONIVA01G18810.1; ONIVA01G18810.1; ONIVA01G18810.
DR Gramene; ONIVA01G18810.1; ONIVA01G18810.1; ONIVA01G18810.
DR eggNOG; KOG0172; Eukaryota.
DR HOGENOM; CLU_005231_1_0_1; -.
DR OMA; TPHVHDI; -.
DR UniPathway; UPA00868; UER00835.
DR Proteomes; UP000006591; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0047131; F:saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0047130; F:saccharopine dehydrogenase (NADP+, L-lysine-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
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; IPR007886; AlaDH/PNT_N.
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; PF05222; AlaDh_PNT_N; 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 SMART; SM01003; AlaDh_PNT_N; 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 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006591};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1181..1199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 198..335
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 375..574
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 1237 AA; 136246 MW; 6B1FA8C032A887F6 CRC64;
MLGKGGEDKF ANCCHAPIHG HAAASYCRPR PPRRRRLHSA QNQLLSRSRS SDAAFLSRGV
VGPASPSHGQ WRRRSRRVQI ARFFFFRLPI LLVPPWKLEA GAHPFLESLR LRLHSAACYD
SVVVSVPRRS EETIGTTFAR IPGSAAGLRP LGEAVARIHD HEPLVLRGGG VHAHLPAACD
TCQRLRNSDT LLGNGVVGIL AETANMWERR APLTPSHCAR LLLGGGKRGT GVNRIIVQPS
TKRIHHDAQY EDVGCEISKD LSECGLIIGI KQPKLEMILP HRAYGFFSHT HKAQKENMPL
LDEILEKRVS LFDYELIAGD DGKRLLAFGK FAGRAGLIDF LHGLGQRYLS LGYSTPFLSL
GQSHMYPSLA AAKAAVIAIG EEIATFGLPS GICPIVFVFT GTGNVSQGAQ EIFKLLPHSF
VDAGKLPELS AARSLSQHPQ SSKRVFQLYG CVVSSRDMVT PKDPTRCFNK ADYYAHPEHY
KPVFHERIAP YASAIVNCMY WERRFPRLLS IDQLQQLMKN GCPLVGISDI TCDIGGSIEF
VNKSTSIERP FFRYDPCTNS CHDDMEGNGV ICLAVDILPT EFSKEASQHF GDILSKFVAR
LASAKELLEL PSHLRKACIA HAGRLTSLYE YIPRMRKTII ELPPAPTNLL PDKKYNSLVS
LSGHLFDKFL INEALDIIET AGGSFHLIRC DVGQSIDDMS YSELEVGADD TATLDKIIDS
LTSLANAHGD PNARREIELS LKIGKVNECG TDDSMAKEGS KVLILGAGRV CRPAAEFLAS
YSNIFSSSAY DHDIDQIHVI VASLYQKDAE ETIDGIRNAT AAQLDVADIK NLSNLVSQVE
VVVSLLPASF HAAIARVCIE MKKHLVTASY VDESMSKLEQ SAEGAGVTIL CEMGLDPGID
HMMSMKMIDE AHSRKGKIKS FTSFCGGLPS PASANNPLAY KFSWSPAGAI RAGRNPAIYK
FHGEIIHVDG DKLYESAKRL RLPELPAFAL EHLPNRNSLM YGDLYGISKE ASTVYRATLR
FSEIMATFAK IGFFDAASHP LLQQTTRPTY RDFLVELFNA CNISTTARKE YSEVSGGQDG
ELISRLLSFG HCKDKEIAAK TVKTIKFLGL YEETQIPENC SSAFDVICQR MEQRMAYIHN
EQDMVLLHHE VEVEYPDGRP TEKHQATLLE FGKVENGRPT TAMALTVGIP AAIGALLLLQ
NKIQKKGVIR PLEPEIYIPA LEILESSGIK LAERVET
//
