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Database: UniProt
Entry: A0A0Q4UR01_9MICO
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Original site: A0A0Q4UR01_9MICO 
ID   A0A0Q4UR01_9MICO        Unreviewed;       366 AA.
AC   A0A0Q4UR01;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=ASF23_14325 {ECO:0000313|EMBL:KQO60387.1};
OS   Curtobacterium sp. Leaf261.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Curtobacterium.
OX   NCBI_TaxID=1736311 {ECO:0000313|EMBL:KQO60387.1, ECO:0000313|Proteomes:UP000050821};
RN   [1] {ECO:0000313|EMBL:KQO60387.1, ECO:0000313|Proteomes:UP000050821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf261 {ECO:0000313|EMBL:KQO60387.1,
RC   ECO:0000313|Proteomes:UP000050821};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQO60387.1, ECO:0000313|Proteomes:UP000050821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf261 {ECO:0000313|EMBL:KQO60387.1,
RC   ECO:0000313|Proteomes:UP000050821};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible reductive amination of pyruvate to
CC       L-alanine. {ECO:0000256|PIRNR:PIRNR000183}.
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   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via
CC       dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step 1/1.
CC       {ECO:0000256|PIRNR:PIRNR000183}.
CC   -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC       {ECO:0000256|ARBA:ARBA00005689, ECO:0000256|PIRNR:PIRNR000183}.
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:KQO60387.1}.
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DR   EMBL; LMMJ01000011; KQO60387.1; -; Genomic_DNA.
DR   RefSeq; WP_055955881.1; NZ_LMMJ01000011.1.
DR   AlphaFoldDB; A0A0Q4UR01; -.
DR   STRING; 1736311.ASF23_14325; -.
DR   OrthoDB; 9804592at2; -.
DR   UniPathway; UPA00527; UER00585.
DR   Proteomes; UP000050821; 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:UniProtKB-UniPathway.
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:UP000050821}.
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   366 AA;  37729 MW;  C6DD2F97D448415D CRC64;
     MLIGVPTEVK NNEFRVAATP AGVAEFVLHG HTVLVQTGAG LGSAFHDDEY TAAGATIVPT
     ADEVWARADM IVKVKEPVSS EYPLIRPGQV LFTYLHLAAD RPLTTALMES GATAIAYETV
     QLPDRSLPLL SPMSEIAGRL SAQVGANQLM KTNGGRGLLL GGVPGTPKGR VVVIGGGVAG
     EHAAEMALGL GAEVTVIDIS LPRLRALDAR FDGRVTTLRS SSYTIAEALR TADLVIGSVL
     IPGAAAPKLV TDAMVADMRP GSVLVDIAID QGGCFEGSRP TTHDDPTYAV HDTVYYSVAN
     MPGAVPRTST ISLTNATLPY ALAIAGKGWA QALSDDAALA AGLNVHEGRV VNAAVAAAHG
     LESATV
//
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