ID   A0A3A9UX21_9FLAO        Unreviewed;       401 AA.
AC   A0A3A9UX21;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Alanine dehydrogenase {ECO:0000313|EMBL:AXT21289.1};
GN   ORFNames=D1817_13305 {ECO:0000313|EMBL:AXT21289.1};
OS   Flavobacteriaceae bacterium.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1871037 {ECO:0000313|EMBL:AXT21289.1, ECO:0000313|Proteomes:UP000260281};
RN   [1] {ECO:0000313|EMBL:AXT21289.1, ECO:0000313|Proteomes:UP000260281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU392 {ECO:0000313|EMBL:AXT21289.1,
RC   ECO:0000313|Proteomes:UP000260281};
RA   Song W., Thomas T., Edwards R.;
RT   "Complete genome sequences of pooled genomic DNA from 10 marine bacteria
RT   using PacBio sequencing.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP031964; AXT21289.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A9UX21; -.
DR   OrthoDB; 1141481at2; -.
DR   Proteomes; UP000260281; Chromosome.
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000260281}.
FT   DOMAIN          4..136
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
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"
SQ   SEQUENCE   401 AA;  45252 MW;  52F19108C1886020 CRC64;
     MKFAIIKERK NPPDRRVVFS PEKLKEAASQ FPNAIFKVEP SDIRVFSNNA YKAQGFEVTS
     DINDCDVMIG VKEVPIEALI SNKKYFFFSH TIKKQPYNRK LLQAVLDKNI EMYDHETIVR
     ENGLRLIGFG RYAGLVGAYN GFRALGLRDG LFNLPKVENL PDLDAVKAEL DKITLPHIKI
     LLSGTGKVAR GAKEILDHLK IKQVSDALYL TSRFTEPIYC LIDVMEYSKR VDGKVGNTSE
     FYKDPSGYES NFMPYAKETN FFIAGHFYGD GAPYLFTKDD AKHPDFKINL IADISCDIDG
     PIASTIRPST IAEPFYGYNS QTETEVAYDT KDAITVMAVD NLPCELPKDA SEGFGDMFLE
     HVIPAFFNND KDGILQRAKI TENGKLTKRF SYLQDYVDGK E
//