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Database: UniProt
Entry: A0A0A2M8J5_9FLAO
LinkDB: A0A0A2M8J5_9FLAO
Original site: A0A0A2M8J5_9FLAO 
ID   A0A0A2M8J5_9FLAO        Unreviewed;       400 AA.
AC   A0A0A2M8J5;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Saccharopine dehydrogenase [NAD(+), L-lysine-forming] {ECO:0000256|ARBA:ARBA00021221};
DE            EC=1.5.1.7 {ECO:0000256|ARBA:ARBA00012847};
DE   AltName: Full=Lysine--2-oxoglutarate reductase {ECO:0000256|ARBA:ARBA00033228};
GN   ORFNames=Q764_10385 {ECO:0000313|EMBL:KGO89002.1};
OS   Flavobacterium suncheonense GH29-5 = DSM 17707.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1121899 {ECO:0000313|EMBL:KGO89002.1, ECO:0000313|Proteomes:UP000030121};
RN   [1] {ECO:0000313|EMBL:KGO89002.1, ECO:0000313|Proteomes:UP000030121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GH29-5 {ECO:0000313|EMBL:KGO89002.1,
RC   ECO:0000313|Proteomes:UP000030121};
RA   Zeng Z., Chen C.;
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-saccharopine + NAD(+) = 2-oxoglutarate + H(+) + L-
CC         lysine + NADH; Xref=Rhea:RHEA:12440, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:32551,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57951; EC=1.5.1.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00001177};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC       pathway; L-lysine from L-alpha-aminoadipate (fungal route): step 3/3.
CC       {ECO:0000256|ARBA:ARBA00004884}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGO89002.1}.
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DR   EMBL; JRLW01000013; KGO89002.1; -; Genomic_DNA.
DR   RefSeq; WP_026980709.1; NZ_JRLW01000013.1.
DR   AlphaFoldDB; A0A0A2M8J5; -.
DR   STRING; 1121899.GCA_000430025_02292; -.
DR   eggNOG; COG0686; Bacteria.
DR   OrthoDB; 1141481at2; -.
DR   UniPathway; UPA00033; UER00034.
DR   Proteomes; UP000030121; Unassembled WGS sequence.
DR   GO; GO:0004754; F:saccharopine dehydrogenase (NAD+, L-lysine-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR   CDD; cd05199; SDH_like; 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; IPR027281; Lys1.
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   PIRSF; PIRSF018250; Saccharopine_DH_Lys; 2.
DR   SMART; SM01002; AlaDh_PNT_C; 1.
DR   SMART; SM01003; AlaDh_PNT_N; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   NAD {ECO:0000256|PIRSR:PIRSR018250-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          4..136
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          167..338
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
FT   ACT_SITE        72
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018250-1"
FT   ACT_SITE        90
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018250-1"
FT   BINDING         226
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
SQ   SEQUENCE   400 AA;  45183 MW;  4E90EE0DEC114F99 CRC64;
     MKFGIIKERK NPPDRRVVFT PSELVKLKEL YPQAGIEVES SDIRVFKDEE YTNLGFEVTE
     DVSDCDVLIG VKEVPVEALI PNKKYFFFSH TIKKQAYNRK LLVACLEKNI ELYDHETIVD
     HTNHRLIGFG RYAGIVGAYN GFRAFGIKYE LFNLPKAETL HDKAALVERL RRPMLPPIKI
     VLTGHGKVGM GAKEILDAMK IKQVSAEDFL NKTFDKPVYT QIDVLDYNRR KDGEAASKLD
     FYENPGDYES DFERFTKVAD IFMAGHFYGN GAPVILTREM LNAPDNKIKV IADISCDVNG
     PIESTLRAST IAEPLYGYYP SQGTEVDINH PGAIVVMAVD NLPCELPKDA SEGFGEMFLT
     HVIPAFFNDD KDGILARAKI TENGKLTERF QYLQDYVDGK
//
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