ID   A0A1M7KD38_9BACT        Unreviewed;       401 AA.
AC   A0A1M7KD38;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Alanine dehydrogenase {ECO:0000313|EMBL:SHM63180.1};
GN   ORFNames=SAMN05444266_109259 {ECO:0000313|EMBL:SHM63180.1};
OS   Chitinophaga jiangningensis.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=1419482 {ECO:0000313|EMBL:SHM63180.1, ECO:0000313|Proteomes:UP000184420};
RN   [1] {ECO:0000313|EMBL:SHM63180.1, ECO:0000313|Proteomes:UP000184420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27406 {ECO:0000313|EMBL:SHM63180.1,
RC   ECO:0000313|Proteomes:UP000184420};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FRBL01000009; SHM63180.1; -; Genomic_DNA.
DR   RefSeq; WP_073085780.1; NZ_FRBL01000009.1.
DR   AlphaFoldDB; A0A1M7KD38; -.
DR   STRING; 1419482.SAMN05444266_109259; -.
DR   OrthoDB; 1141481at2; -.
DR   Proteomes; UP000184420; 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:UP000184420}.
FT   DOMAIN          8..140
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   ACT_SITE        76
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018250-1"
FT   ACT_SITE        94
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018250-1"
FT   BINDING         244
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
FT   BINDING         271
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
SQ   SEQUENCE   401 AA;  45520 MW;  727E324DF8AAC3B7 CRC64;
     MQKSVHIGLI REEKHPHDNR VAFTPKQCQW IMHHFPHVAL YAQPSPHRCF KDEEYAKAGV
     TISQNLENCC ILLGIKEVPP TFLLPNKTYL FFSHTKKKQP HNRDMLKAIL EKNIRLVDYE
     CLVHPDGQRI LGFGFFAGVV GAHNGLLAYG QKTGLFKLKP VHQSHDFQEL ISHYFGVKLP
     PLKIVATGSG RVAAGVLEIM GLLGIKYIPP EEFLMNSYNY PVYTQLKAGE LYLRKDDKTY
     SRADFHAHPE QYDCKFLPFV AASDILMNGI YWDKNIPPLF SAKDLQKDNF RIQVIADITD
     DTNGSIPCNL GDSTIDDPVY GVDKQTMTRT APYLPDTVDM MCVSNLPNEL PRDASQYFGD
     QLMKYVFEDL LSGNSEMIKK ATIAENGALT SYFDYLQDYI A
//