ID A0A172TA10_9DEIO Unreviewed; 368 AA.
AC A0A172TA10;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=SU48_08260 {ECO:0000313|EMBL:ANE43767.1};
OS Deinococcus puniceus.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=1182568 {ECO:0000313|EMBL:ANE43767.1, ECO:0000313|Proteomes:UP000077363};
RN [1] {ECO:0000313|EMBL:ANE43767.1, ECO:0000313|Proteomes:UP000077363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY1 {ECO:0000313|EMBL:ANE43767.1,
RC ECO:0000313|Proteomes:UP000077363};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Deinococcus puniceus/DY1/ whole genome sequencing.";
RL Submitted (JAN-2015) 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; CP011387; ANE43767.1; -; Genomic_DNA.
DR RefSeq; WP_064014836.1; NZ_CP011387.1.
DR AlphaFoldDB; A0A172TA10; -.
DR STRING; 1182568.SU48_08260; -.
DR KEGG; dpu:SU48_08260; -.
DR PATRIC; fig|1182568.3.peg.1718; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000077363; Chromosome.
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; 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:UP000077363}.
FT DOMAIN 4..135
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 147..295
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT ACT_SITE 94
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-1"
FT ACT_SITE 268
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 73
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-2"
FT BINDING 132
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT BINDING 196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT BINDING 201
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT BINDING 218
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT BINDING 237..238
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT BINDING 265..268
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT BINDING 296..299
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT BINDING 325
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-4"
SQ SEQUENCE 368 AA; 38300 MW; FA8EA7D012903EFD CRC64;
MKIGLPKEIK VKENRVALTP GGVGTLVRRG HTVTVEHGAG VGSGIADAEY VAAGAVMGTA
DEAWAAQMVV KVKEPIEREY GYLRDDLLLF TYLHLAADRA LTEALLKAGT TAIAYETVQV
EDGSLPLLMP MSEVAGRLSV QAGAYHLQKP VGGRGVLLGG VPGVQAGHVV IVGGGVVGTN
AAKMAMGLGA KVTVLDVSHR RLTYLDDVFF GKLTTMMSSE ANIRALLPET DLLVGAVLIP
GAKAPHLVTR DMLPLMQEGS VIVDVAVDQG GCVETIHATT HDDPTYLVDG VIHYGVANMP
GAVPRTSTFA LTNQTLPYAL LLADHGIGAL SRNKALSLGL NTHAGQLTYA GVADALGMEY
VETGAVLA
//
