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Database: UniProt
Entry: A0A494ZU94_9BACI
LinkDB: A0A494ZU94_9BACI
Original site: A0A494ZU94_9BACI 
ID   A0A494ZU94_9BACI        Unreviewed;       370 AA.
AC   A0A494ZU94;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   13-SEP-2023, entry version 16.
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:RKQ29876.1};
GN   ORFNames=D8M06_16795 {ECO:0000313|EMBL:RKQ29876.1};
OS   Oceanobacillus halophilus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=930130 {ECO:0000313|EMBL:RKQ29876.1, ECO:0000313|Proteomes:UP000269301};
RN   [1] {ECO:0000313|EMBL:RKQ29876.1, ECO:0000313|Proteomes:UP000269301}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23996 {ECO:0000313|EMBL:RKQ29876.1,
RC   ECO:0000313|Proteomes:UP000269301};
RX   PubMed=26869142; DOI=.1099/ijsem.0.000952;
RA   Amoozegar M.A., Bagheri M., Makhdoumi A., Nikou M.M., Fazeli S.A.S.,
RA   Schumann P., Sproer C., Sanchez-Porro C., Ventosa A.;
RT   "Oceanobacillus halophilus sp. nov., a novel moderately halophilic
RT   bacterium from a hypersaline lake.";
RL   Int. J. Syst. Evol. Microbiol. 66:1317-1322(2016).
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|ARBA:ARBA00005206}.
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:RKQ29876.1}.
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DR   EMBL; RBZP01000021; RKQ29876.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A494ZU94; -.
DR   OrthoDB; 9804592at2; -.
DR   UniPathway; UPA00527; UER00585.
DR   Proteomes; UP000269301; 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:UP000269301}.
FT   DOMAIN          4..136
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          148..297
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
FT   ACT_SITE        95
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-1"
FT   ACT_SITE        269
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         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-2"
FT   BINDING         133
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         197
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         202
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         219
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         238..239
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         266..269
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   370 AA;  39152 MW;  58099EB43C807525 CRC64;
     MKIGVPKEIM NSENRVAIAP SGVLTLISAG HEVFVETGAG LGSSFTDDQY AEAGAMIVSS
     ADEAWGQEMV MKVKEPLPEE YKYFYEGLIL FTYLHLANEP GLTKALIEHK VIGIAYETVQ
     LPNGSLPLLT PMSEVAGRMA TQVGAQYLEK PKGGKGVLLS GIPGVKRGKV TIIGGGGVGT
     NAAKIAIGLG ADVTIIDLNP ERLRQLDDLF GASVNTLISN SLNISESVVE SDLVIGSVLI
     PGAKAPQLVT EEMVKKMKDG SVIVDVAIDQ GGNFETSDRI TTHDNPTYVK HGVVHYTVAN
     MPGAVPRTST IGLTNVTVPY ALQLANKGYK KACIDNQALL KGINTLDGYV TFKAVAEAHG
     VKYSEAQSLL
//
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