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Database: UniProt
Entry: C9MM94_9BACT
LinkDB: C9MM94_9BACT
Original site: C9MM94_9BACT 
ID   C9MM94_9BACT            Unreviewed;       412 AA.
AC   C9MM94;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Saccharopine dehydrogenase {ECO:0000313|EMBL:EEX19279.1};
DE            EC=1.5.1.7 {ECO:0000313|EMBL:EEX19279.1};
GN   Name=LYS1 {ECO:0000313|EMBL:EEX19279.1};
GN   ORFNames=HMPREF0973_00724 {ECO:0000313|EMBL:EEX19279.1};
OS   Prevotella veroralis F0319.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=649761 {ECO:0000313|EMBL:EEX19279.1, ECO:0000313|Proteomes:UP000003327};
RN   [1] {ECO:0000313|EMBL:EEX19279.1, ECO:0000313|Proteomes:UP000003327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0319 {ECO:0000313|EMBL:EEX19279.1,
RC   ECO:0000313|Proteomes:UP000003327};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
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:EEX19279.1}.
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DR   EMBL; ACVA01000016; EEX19279.1; -; Genomic_DNA.
DR   RefSeq; WP_004382355.1; NZ_GG698712.1.
DR   AlphaFoldDB; C9MM94; -.
DR   STRING; 649761.HMPREF0973_00724; -.
DR   eggNOG; COG1748; Bacteria.
DR   HOGENOM; CLU_032114_0_0_10; -.
DR   OrthoDB; 9769367at2; -.
DR   Proteomes; UP000003327; Unassembled WGS sequence.
DR   GO; GO:0004754; F:saccharopine dehydrogenase (NAD+, L-lysine-forming) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032095; Sacchrp_dh-like_C.
DR   InterPro; IPR005097; Sacchrp_dh_NADP.
DR   PANTHER; PTHR43796; CARBOXYNORSPERMIDINE SYNTHASE; 1.
DR   PANTHER; PTHR43796:SF2; CARBOXYNORSPERMIDINE SYNTHASE; 1.
DR   Pfam; PF16653; Sacchrp_dh_C; 1.
DR   Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:EEX19279.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003327}.
FT   DOMAIN          4..138
FT                   /note="Saccharopine dehydrogenase NADP binding"
FT                   /evidence="ECO:0000259|Pfam:PF03435"
FT   DOMAIN          142..400
FT                   /note="Saccharopine dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16653"
SQ   SEQUENCE   412 AA;  46665 MW;  8DE806A9E2449B51 CRC64;
     MGKVLMIGAG GVATVAAFKI VQNQDVFTEF MIASRRKEKC DALVKAIHDK GYKADIKTAQ
     VDADDVEQLK ALFNDFKPEL VINLALPYQD LTIMDACLAC GCNYLDTANY EPKDEAHFEY
     SWQWAYKDKF EKAGLTAILG CGFDPGVSQA YTAYAAKHHF DEIHYLDIVD CNAGNHHKAF
     ATNFNPEINI REITQKGLYY ENGKWIETEP LAVHQDLTYP NIGPRDSYLM HHEELESLVK
     NYPTIKRARF WMTFGKQYLT YLDCIQNLGM SRIDEIEYEA PLADGSGKTA KVKIVPLQFL
     KAVLPNPQDL GENYDGETSI GCRIRGIKDG KEQTYYIYNN CKHQDAYNET GMQGVSYTTG
     VPAMAGAMMF FKGLWRKPGV WNVEDFDPDP FLEVLNKQGL PWHEEFGGDL EL
//
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