ID   A0A0N5CDR4_STREA        Unreviewed;       945 AA.
AC   A0A0N5CDR4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Saccharopine dehydrogenase {ECO:0000313|WBParaSite:SPAL_0001600700.1};
OS   Strongyloides papillosus (Intestinal threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0001600700.1};
RN   [1] {ECO:0000313|WBParaSite:SPAL_0001600700.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) 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}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT family.
CC       {ECO:0000256|ARBA:ARBA00005624}.
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DR   AlphaFoldDB; A0A0N5CDR4; -.
DR   STRING; 174720.A0A0N5CDR4; -.
DR   WBParaSite; SPAL_0001600700.1; SPAL_0001600700.1; SPAL_0001600700.
DR   UniPathway; UPA00868; UER00835.
DR   Proteomes; UP000046392; Unplaced.
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   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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          36..166
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          206..408
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
SQ   SEQUENCE   945 AA;  105711 MW;  C62E4CD5820C1ADB CRC64;
     MITKLFTLRG QSSLHQLRYL TSEKSTFYGK GQPCLGIRRE TINAWERRAP LAPQHVNKLT
     KAGIKVLIQP SNRRAFPIQD YQSAGAIVKE DLAEAHLIVS VKQVPIDQLI PNKTYAFFSH
     TIKAQDDNMQ MLDTILQRKI RLIDYEKLVD NTGKRVVMFG KWAGYAGFID ILHGLGLRLL
     ALGHHTPFLH IGLAHNYNSS HMAINAVRDC GYEIALNRLP HSLGPLTFVF TGSGNVSQGA
     QELFKHLPHE FVDVKTLPEV AKKGHRNKVY GCVIGRAEHM MRKDGRPFDE GDYLKNPRQY
     ISKFSTEIAP YANVIINGVY WDVDTPRLIT IPDAKNLLSP KKTNVDVPGC PTLPHKLTAI
     CDISADPGGS IEFMQECTTI DKPFVMYDAD FNKTANTFDA PSGCLVCSID NMPAQMPIEA
     TSMFGDLLTP YIMEMINCTT DIPFEQLTVS ETIKNAIITD NGYYTPDFEY IKYLREDKIK
     LARRRPITTM NQKKILLLGA GMVSDPFAAY FSKYDDDISV TVGTQSQSDG DRLRKYGANI
     DSIVVDVTKE EDTLCKLVGE HDLVVSLLPY TFHAQIAKHC IKNKTNLVTS SYISPEIQAL
     ENDAINSGIT IMMESGLDPG IDHMLAMECI DQVHEHGGKI KSFVSFCGGL PAPQFSDNAL
     RYKFSWSPKG VLMALMNPAR YLYNGDIIEL EADGGVLNQL YPIDFMPGFN LIGYANRDST
     KYNSIYGIQN ECHTMLRGTL RYNGFDKTIK ALKTLGLLDT SDKDFLNPNN GPDLTWKQVM
     AILLNQQQDI FPDSIKNMAK DILSADDYDI TPLEQLGLFS DNIIAEKMSN PLDTLVGHLS
     KVLSFKKNEQ DLVILNHDIG AEMPNGKFIK HRISLTAYGD PNGHSAMAKT VGYTTAIVSH
     MVANGEIQKR GLVRPVTKDI YRPALKRLED LNVKATSQII YQRRL
//