ID A0A0M4MCZ2_9ACTN Unreviewed; 367 AA.
AC A0A0M4MCZ2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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 Name=ald {ECO:0000313|EMBL:VHO01557.1};
GN ORFNames=AL705_07505 {ECO:0000313|EMBL:ALE19399.1}, LC603019_01492
GN {ECO:0000313|EMBL:VHO01557.1};
OS Lawsonella clevelandensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Lawsonellaceae;
OC Lawsonella.
OX NCBI_TaxID=1528099 {ECO:0000313|EMBL:ALE19399.1, ECO:0000313|Proteomes:UP000068137};
RN [1] {ECO:0000313|EMBL:ALE19399.1, ECO:0000313|Proteomes:UP000068137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X1698 {ECO:0000313|EMBL:ALE19399.1,
RC ECO:0000313|Proteomes:UP000068137};
RX PubMed=26659691;
RA Nicholson A.C., Bell M., Humrighouse B.W., McQuiston J.R.;
RT "Complete Genome Sequences for Two Strains of a Novel Fastidious, Partially
RT Acid-Fast, Gram-Positive Corynebacterineae Bacterium, Derived from Human
RT Clinical Samples.";
RL Genome Announc. 3:e01462-15(2015).
RN [2] {ECO:0000313|EMBL:ALE19399.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=X1698 {ECO:0000313|EMBL:ALE19399.1};
RX PubMed=27130323; DOI=10.1099/ijsem.0.001122;
RA Bell M.E., Bernard K.A., Harrington S.M., Patel N.B., Tucker T.A.,
RA Metcalfe M.G., McQuiston J.R.;
RT "Lawsonella clevelandensis gen. nov., sp. nov., a new member of the
RT suborder Corynebacterineae isolated from human abscesses.";
RL Int. J. Syst. Evol. Microbiol. 66:2929-2935(2016).
RN [3] {ECO:0000313|EMBL:VHO01557.1, ECO:0000313|Proteomes:UP000324288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USB-603019 {ECO:0000313|EMBL:VHO01557.1};
RA Seth-Smith MB H., Seth-Smith H.;
RL Submitted (APR-2019) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP012390; ALE19399.1; -; Genomic_DNA.
DR EMBL; LR584267; VHO01557.1; -; Genomic_DNA.
DR RefSeq; WP_053962469.1; NZ_LR584267.1.
DR AlphaFoldDB; A0A0M4MCZ2; -.
DR STRING; 1528099.AL705_07505; -.
DR GeneID; 84895387; -.
DR KEGG; cbq:AL705_07505; -.
DR PATRIC; fig|1528099.3.peg.1475; -.
DR OrthoDB; 9804592at2; -.
DR UniPathway; UPA00527; UER00585.
DR Proteomes; UP000068137; Chromosome.
DR Proteomes; UP000324288; Chromosome 1.
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; 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; 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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRNR:PIRNR000183, ECO:0000256|PIRSR:PIRSR000183-3};
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:UP000068137}.
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 178..179
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 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 298..301
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
SQ SEQUENCE 367 AA; 38906 MW; 11ABF645E44A3AE5 CRC64;
MRIGIPKEVK NNEFRVSVTP SGVAELVHRG HEVFVEKSAG VGSNFPDEEY IEAGATMIET
ADEVWEKGDL IIKVKEPIAE EFPRMRENQV LFTYLHLAAC TDCCDALLKA GTTSIAYEVV
QTPDRKLPLL APMSEVAGRL SVQVGAQHLM KQYGGGGRLL GGVSGVRPAN VVVLGAGTAG
SNAIAMAVGM RADVTVFDIN IAALKALDDI YQGRVHTVVS NKAEITKALK TADLVVGSVL
IPGASAPKLV TNDMVAQMKK GSVLVDIAID QGGCFEDSHA TTHEDPTFPV HDTVFYCVAN
MPGAVPNTST WALSNATLPY VLQIAEQGWE MAVKKNSALK AGLSTHKGKL YSAPVAEALG
LPLATLD
//
