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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//