ID A0A3B6PRW5_WHEAT Unreviewed; 1049 AA.
AC A0A3B6PRW5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KAF7086326.1, ECO:0000313|EnsemblPlants:TraesCS6B02G376200.1};
GN ORFNames=CFC21_089625 {ECO:0000313|EMBL:KAF7086326.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS6B02G376200.1};
RN [1] {ECO:0000313|EMBL:KAF7086326.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7086326.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS6B02G376200.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS6B02G376200.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS6B02G376200.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7086326.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7086326.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CM022227; KAF7086326.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6PRW5; -.
DR EnsemblPlants; TraesCS6B02G376200.1; TraesCS6B02G376200.1; TraesCS6B02G376200.
DR Gramene; TraesCS6B02G376200.1; TraesCS6B02G376200.1; TraesCS6B02G376200.
DR Gramene; TraesCS6B03G1065800.1; TraesCS6B03G1065800.1.CDS; TraesCS6B03G1065800.
DR OMA; CIAQKTH; -.
DR UniPathway; UPA00868; UER00835.
DR Proteomes; UP000019116; Chromosome 6B.
DR Proteomes; UP000815260; Chromosome 6B.
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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116}.
FT DOMAIN 19..156
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 196..395
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 1049 AA; 115564 MW; CC89C572FE94E2C3 CRC64;
MGSETTERND TLLGNGVIGI LAETVNMWER RAPLTPSHCA RLMLGGGKHE SGVNRIIVQP
STKRIHHDAQ YEDAGCEISE DLSECGLIVG IKQPKLEMIL PDRAYAFFSH THKAQKENMP
LLDKIMEERV SLFDYELIVD DDGKRMLAFG KFAGRAGLID FLHGLGQRYL SLGYSTPFLS
LGQSHMYPSL AAAKAAVIAI GEEIATYGLP SGICPIVFAF TGSGNVSQGA QEIFKLLPHT
FVDAEKLPEL SAGKSLPPHH QSTRRAFQLY GCVVTSKDMV APKDPNRCFD KADYYAHPEY
YRPVFHERIA PYASAIVNCM YWERRFPRLL SIDQLQQLMK NGCPLVGISD ITCDIGGSIE
FVNKSTSIER PFFRYDTSTN LYHDDMEGDG VICLAVDILP TEFSREASQH FGDILSRFVT
SLASAKGLLE LPSHLRRACI AYAGKLTPLY EYIPRMRKTM IELPPTPANL LPDKKYTTLV
SLCGHLFDKF LINEALDIIE TAGGSFHLVK CDVGQSIDDM SYSELEVGAD DTTTLDKIID
SLTSIANAHR GDPNATEISL KIGRVSECGI DGSMDKVGPK VLILGAGRVC RPAAEFLTSY
QNIDQVHVVV ASLYQKDAEE TVDGIKNATA AQLDVSDTES LSNLVSQVDV VVSLLPASFH
AAIARVCIEL KKHLVTASYV DDSMSKLEQA AQGAGVTILC EMGLDPGIDH MLSMKMIDEA
HARDGKIKAF TSFCGGLPSP AAANNPLAYK FSWSPAGAIR AGRNPAVYKF LGEIINVDGS
KLYESAKRLR LPELPAFALE HLPNRNSLMY GDLYGISKEA STVYRSTLRY EGFSEIMAIL
AKIGFFDAEN HPLLQETNRP TYRNFLNELL NVNNISTSNT KINGEESGGH DDELVSRLMM
LGHCKEKELA VKILKTIKFL GLHEETQIPK DCSSAFSVIC QRMEQRMAYG HNEQDMVLLH
HEVEVEYPDG RPTEKHQATL MEFGKTENGR STTAMALTVG VPAAIGALLL LQNKVQKKGV
IRPLQPEIYI PALEILEASG IKVIERVET
//
