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Database: UniProt
Entry: A0A286DGD4_9GAMM
LinkDB: A0A286DGD4_9GAMM
Original site: A0A286DGD4_9GAMM 
ID   A0A286DGD4_9GAMM        Unreviewed;       371 AA.
AC   A0A286DGD4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897, ECO:0000256|PIRNR:PIRNR000183};
DE            EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897, ECO:0000256|PIRNR:PIRNR000183};
GN   ORFNames=SAMN06296416_11522 {ECO:0000313|EMBL:SOD57646.1};
OS   Pseudoxanthomonas wuyuanensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=1073196 {ECO:0000313|EMBL:SOD57646.1, ECO:0000313|Proteomes:UP000219374};
RN   [1] {ECO:0000313|EMBL:SOD57646.1, ECO:0000313|Proteomes:UP000219374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10978 {ECO:0000313|EMBL:SOD57646.1,
RC   ECO:0000313|Proteomes:UP000219374};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-alanine + NAD(+) = H(+) + NADH + NH4(+) + pyruvate;
CC         Xref=Rhea:RHEA:18405, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:57972; EC=1.4.1.1;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000183};
CC   -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC       {ECO:0000256|ARBA:ARBA00005689, ECO:0000256|PIRNR:PIRNR000183}.
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DR   EMBL; OCND01000015; SOD57646.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286DGD4; -.
DR   OrthoDB; 9804592at2; -.
DR   Proteomes; UP000219374; Unassembled WGS sequence.
DR   GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:InterPro.
DR   CDD; cd05305; L-AlaDH; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR008141; Ala_DH.
DR   InterPro; IPR008143; Ala_DH/PNT_CS2.
DR   InterPro; IPR007886; AlaDH/PNT_N.
DR   InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00518; alaDH; 1.
DR   PANTHER; PTHR42795; ALANINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42795:SF1; ALANINE DEHYDROGENASE; 1.
DR   Pfam; PF01262; AlaDh_PNT_C; 1.
DR   Pfam; PF05222; AlaDh_PNT_N; 1.
DR   PIRSF; PIRSF000183; Alanine_dh; 1.
DR   SMART; SM01002; AlaDh_PNT_C; 1.
DR   SMART; SM01003; AlaDh_PNT_N; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00837; ALADH_PNT_2; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000183};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000183-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000183};
KW   Reference proteome {ECO:0000313|Proteomes:UP000219374}.
FT   DOMAIN          4..137
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          149..297
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
FT   ACT_SITE        96
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-1"
FT   ACT_SITE        270
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-1"
FT   BINDING         15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-2"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-2"
FT   BINDING         134
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         198
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         203
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         220
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         239..240
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         267..270
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         279
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         298..301
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
SQ   SEQUENCE   371 AA;  39382 MW;  4BAAE6D1E1431BFC CRC64;
     MLIGVPKEIK NHEYRIGLTP AGARELGALG HQVIVQRDGG KSIGLTDDQY VKAGAEIVDT
     PDEIFARADM IIKVKEPQPV ECAMLRPGQV LYTYLHLAPD PEQTKALVAS GATCIAYETV
     TDRKGGLPLL APMSEVAGRM SIQAGAHALE KAQGGSGILL GGVPGVKPAE VMVIGGGVVG
     INAARMAMGM NAHVTILDRS LDRLKYLDEV YGDRLTTIYS TRDAIEERLP YTDLVIGAVL
     IPGAAAPKLI AREQLSLMRP GSVLVDVAID QGGCFETSRA TTHQNPTYEV DGIIHYCVAN
     MPGGVARTST FALTNATLPY ALQLANKGAR QALLDDEHLR NGLNVHAGKI TYQAVATDLG
     YAYVPAHEAL A
//
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