ID   A0A1I7MYG7_9BACT        Unreviewed;       400 AA.
AC   A0A1I7MYG7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Alanine dehydrogenase {ECO:0000313|EMBL:SFV27461.1};
GN   ORFNames=SAMN05660895_0117 {ECO:0000313|EMBL:SFV27461.1};
OS   Thermoflavifilum thermophilum.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Thermoflavifilum.
OX   NCBI_TaxID=1393122 {ECO:0000313|EMBL:SFV27461.1, ECO:0000313|Proteomes:UP000199537};
RN   [1] {ECO:0000313|Proteomes:UP000199537}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14807 {ECO:0000313|Proteomes:UP000199537};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FPCJ01000001; SFV27461.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I7MYG7; -.
DR   STRING; 1393122.SAMN05660895_0117; -.
DR   OrthoDB; 1141481at2; -.
DR   Proteomes; UP000199537; Unassembled WGS sequence.
DR   GO; GO:0004754; F:saccharopine dehydrogenase (NAD+, L-lysine-forming) activity; IEA:InterPro.
DR   GO; GO:0009085; P:lysine biosynthetic process; IEA:InterPro.
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; 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; SM01003; AlaDh_PNT_N; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
PE   4: Predicted;
KW   NAD {ECO:0000256|PIRSR:PIRSR018250-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199537}.
FT   DOMAIN          5..137
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   ACT_SITE        73
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018250-1"
FT   ACT_SITE        91
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018250-1"
FT   BINDING         268
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
SQ   SEQUENCE   400 AA;  45723 MW;  9A0A53259F04FA1C CRC64;
     MLKIGLIREG KQPADHRVAL TPSQCRWIMQ HHPQIQIVVQ PSAIRCYSDE EYQQAGIPLQ
     EDLSNCQILM GIKEVPPQQL LPEKTYFFFS HTKKKQPHNK PLMQACVKKH ITLIDYECLV
     HNDGQRMLGF GFFAGVVGAH NGLMAYGKKT GLFDFRRAYS CHDLQELTES YYGVKLPPLK
     IAITGSGRVA AGILEVMGLL GIKDITPEEF LINEYQYPVY TQLKAGDLYL HKTERSYSRE
     HFHAHPKEYE CKFLPFTTAA DILMNGIYWE QGMAPLFTWD DLCNPHFRIR VIADITNDRE
     GSIPCNLGDS TIEDPVYGVD RCTRQKLPPY LPHTVDMMCV GNLPDELPRD ASRYFGEQLI
     KYVIPELLQE KSVILEKATI LLNGKLTPRF SYLEDYAYGS
//