ID R0GXU4_9BRAS Unreviewed; 1062 AA.
AC R0GXU4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EOA15943.1};
GN ORFNames=CARUB_v10004036mg {ECO:0000313|EMBL:EOA15943.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA15943.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
RN [2] {ECO:0000313|EMBL:EOA15943.1}
RP NUCLEOTIDE SEQUENCE.
RA Schmutz J., Prochnik S., Nordborg M., Weigel D., Rokhsar D., Wright S.;
RT "Genome sequencing of Capsella rubella.";
RL Nat. Genet. 0:0-0(2013).
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; KB870811; EOA15943.1; -; Genomic_DNA.
DR EMBL; KB870811; EOA15944.1; -; Genomic_DNA.
DR RefSeq; XP_006283045.1; XM_006282983.1.
DR RefSeq; XP_006283046.1; XM_006282984.1.
DR AlphaFoldDB; R0GXU4; -.
DR STRING; 81985.R0GXU4; -.
DR GeneID; 17877973; -.
DR KEGG; crb:17877973; -.
DR eggNOG; KOG0172; Eukaryota.
DR OrthoDB; 2184985at2759; -.
DR UniPathway; UPA00868; UER00835.
DR Proteomes; UP000029121; Unassembled WGS sequence.
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:UP000029121}.
FT DOMAIN 17..153
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 193..393
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 1062 AA; 117020 MW; 0092F10C858FAED2 CRC64;
MNSSGDEKSR LGNGVVGILA ETVNKWERRT PLTPSHCARL LHGGKDRTGV SRIVVQPSAK
RIHHDALYED VGCEVSDDLS DCGLILGIKQ PELEMILPDR AYAFFSHTHK AQKENMPLLD
KILSEGVTLC DYELIVGDHG RRLLAFGKYA GRAGLVDFLH GLGQRYLSLG YSTPFLSLGS
SYMYSSLAAA KAAVISVGEE IASQGLPLGI CPLVFVFTGT GNVSLGAQEI FKLLPHTFVE
PSKLPELFIK EKGISQNGKS TKRIYQVYGC IITSQDMVEH KDPSKSFDKA DYYAHPEHYN
PVFHEKISPY TSVLVNCMYW EKRFPRLLST KQLQDLTTKG CPLVGICDIT CDIGGSIEFV
NQATLIDSPF FRFNPSDNSY DDDMDGNGIL CMAVDILPTE FAKEASQHFG DILSEFVGSL
ASMTEIADLP AHLKRACISY KGELTSLYEY IPRMRKSNPE EAHENIANGV SSQRTYNILV
SLSGHLFDKF LINEALDMIE AAGGTFHLAK CELGQSADAE SYSELEVGAD DKKVLDQIID
SLTRLANPDE DYISPRRESN KISLKIEKVQ QENEVKEKPE MTKKSGVLII GAGRVCRPAA
ELLASVKTIS SQQWYKTYFG AESEEQTDVR VIVASLYLKD AKKTIEGIPD VEAVQLDVSD
SESLLKYVSE VDVVLSLLPA SCHTVVAKTC IELKKHLVTA SYVDDETSML HEKAKSSGIT
ILGEMGLDPG IDHMMAMKMI NEAHIKKGKV KSFTSYCGGL PSPAAANNPL AYKFSWSPAG
AIRAGSNPAK YKTNGDIVHV DGENLYDSAT RFRVPNLPAF ALECLPNRNS LVYGELYGIE
SEATTIFRGT LRYEGFSMIM ATLSKLGFFD YEANQVLTTG KKIMFGTLLS NILKKDADNE
SEPLAGEEEI CKRIIKLGHS KETAAKAAKT IVFLGFNEER EIPSLCKSAF DATCYLMEEK
LAYSGDEQDM VLLHHEVEVE FPESKRIEKH SATLLEFGEI KNGQTTTAMA KTVGIPAAIG
ALLLIEDKIK TRGVLRPLEP EVYLPALDIL QAYGIKLIEK TE
//
