ID Q5KPL5_CRYNJ Unreviewed; 934 AA.
AC Q5KPL5;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 24-JAN-2024, entry version 95.
DE SubName: Full=Saccharopine dehydrogenase (NADP+, L-glutamate-forming), putative {ECO:0000313|EMBL:AAW40810.1};
GN OrderedLocusNames=CNA02370 {ECO:0000313|EMBL:AAW40810.1};
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684 {ECO:0000313|EMBL:AAW40810.1, ECO:0000313|Proteomes:UP000002149};
RN [1] {ECO:0000313|EMBL:AAW40810.1, ECO:0000313|Proteomes:UP000002149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565 {ECO:0000313|Proteomes:UP000002149};
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J., Koo H.L., Krzywinski M.I., Kwon-Chung J.K.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; AE017341; AAW40810.1; -; Genomic_DNA.
DR RefSeq; XP_566629.1; XM_566629.1.
DR AlphaFoldDB; Q5KPL5; -.
DR STRING; 214684.Q5KPL5; -.
DR PaxDb; 214684-Q5KPL5; -.
DR EnsemblFungi; AAW40810; AAW40810; CNA02370.
DR GeneID; 3253690; -.
DR KEGG; cne:CNA02370; -.
DR VEuPathDB; FungiDB:CNA02370; -.
DR eggNOG; KOG0172; Eukaryota.
DR HOGENOM; CLU_005231_0_0_1; -.
DR InParanoid; Q5KPL5; -.
DR OMA; TPHVHDI; -.
DR OrthoDB; 2184985at2759; -.
DR UniPathway; UPA00868; UER00835.
DR Proteomes; UP000002149; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0004753; F:saccharopine dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IBA:GO_Central.
DR CDD; cd12189; LKR_SDH_like; 1.
DR Gene3D; 1.10.1870.10; Domain 3, Saccharopine reductase; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032095; Sacchrp_dh-like_C.
DR InterPro; IPR005097; Sacchrp_dh_NADP.
DR PANTHER; PTHR11133:SF25; ALPHA-AMINOADIPIC SEMIALDEHYDE SYNTHASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11133; SACCHAROPINE DEHYDROGENASE; 1.
DR Pfam; PF05222; AlaDh_PNT_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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002149}.
FT DOMAIN 21..150
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 214..392
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 934 AA; 101537 MW; 893379EFF599E5E6 CRC64;
MRTLPLTRSP FITRRCLTTL GLRREDPSRI WERRTPLTPH AVQSLLADAK DQLKVEVESC
KRRCFPDSLY SDAGAKIVPS LSKDVDVILG IKEPRLSDIR NLVEASKNEG KKRTWMMFSH
THKGQEYNIP LLSAFLHPTQ TLIDHELLTA PAPGKDGKPQ LKRVAAFGWF AGAVGAGEAL
SLTGLALLRR GLATPLLSLS RPYSLGSLAA FKEALKKAGE EVKTSADLKG QEPIVIGVTG
AGNVSSGATE MLNELGVVWV GPEDLADLRQ SGSPNKIYAC AITPASYLQR IEGGIFDKQE
YYKSPDKYMS IFAAKIAPHL TTLINGVGWS KGFPRAITRP SLNKLIEKEN GKQKLVAVQD
ITCDKEGGLE FVDQFTTVDN PYFEGPGDIL ISAIDILPTE LAADASSYFS SALYPYIQGL
LFPSGQGDKN DITETLSRAA IVKDGVLQSQ HEWLGEKIEQ WKTGGAVAPD SLKQEKLRKG
GKKKVLLLGS GLVAGPAVDV FAARPDVHLI IASNNLAEGQ SHIRGRPNVE AMALDVADDA
SMSEIVEEAD IVVSLLPAPM HLRVAKHCLD HSRHLVTASY VSPELQALHS QAIEKDVIFL
GECGLDPGID SMAAMRILER AKREGKQVKS FVSWCGGLPE LSASKVPLRY KFSWSPKAVL
TAAQNDASYK LEGKHVKIPG NELLARRFPE VKLWDGLPLE GLANRDSMPY AKKYGLGPAE
GLTDLFRGTL RYQGFSSLLE SFRLLGLLRS DPLPGSPKSW TEFLSMTVER ELGLSKGLKG
EDVSSAVQDL VGEGSKDVIR ALKLFSLFPG SDTSLLPLPN LPTPSPIDFF AHLLSRKLAY
LPDERDTCLL HHSFTISTPS GDTQKVTASL RHMATPTQSS MSITVGKTLA FAALRIADGE
VKVRGVTGPY EPEVWAGVLS SLEGAGVVIE EKWH
//
