ID   DHA_OCEIH               Reviewed;         376 AA.
AC   Q8CX61;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Alanine dehydrogenase;
DE            EC=1.4.1.1;
GN   Name=ald; OrderedLocusNames=OB3225;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
CC   -!- FUNCTION: Catalyzes the reversible reductive amination of pyruvate to
CC       L-alanine. This enzyme is a key factor in the assimilation of L-alanine
CC       as an energy source through the tricarboxylic acid cycle during
CC       sporulation (By similarity). {ECO:0000250}.
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   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via
CC       dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step 1/1.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}.
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DR   EMBL; BA000028; BAC15181.1; -; Genomic_DNA.
DR   RefSeq; WP_011067621.1; NC_004193.1.
DR   AlphaFoldDB; Q8CX61; -.
DR   SMR; Q8CX61; -.
DR   STRING; 221109.22778914; -.
DR   EnsemblBacteria; BAC15181; BAC15181; BAC15181.
DR   KEGG; oih:OB3225; -.
DR   eggNOG; COG0686; Bacteria.
DR   HOGENOM; CLU_003376_3_0_9; -.
DR   OMA; RDIDEMF; -.
DR   OrthoDB; 673280at2; -.
DR   PhylomeDB; Q8CX61; -.
DR   UniPathway; UPA00527; UER00585.
DR   Proteomes; UP000000822; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   CDD; cd05305; L-AlaDH; 1.
DR   InterPro; IPR008141; Ala_DH.
DR   InterPro; IPR008143; Ala_DH/PNT_CS2.
DR   InterPro; IPR008142; AlaDH/PNT_CS1.
DR   InterPro; IPR007886; AlaDH/PNT_N.
DR   InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42795; PTHR42795; 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; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00518; alaDH; 1.
DR   PROSITE; PS00836; ALADH_PNT_1; 1.
DR   PROSITE; PS00837; ALADH_PNT_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NAD; Nucleotide-binding; Oxidoreductase; Reference proteome;
KW   Sporulation.
FT   CHAIN           1..376
FT                   /note="Alanine dehydrogenase"
FT                   /id="PRO_0000198993"
FT   ACT_SITE        96
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        269
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         177..178
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         219
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         238..239
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         266..269
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         298..301
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   376 AA;  39619 MW;  EAC9F969A2041BC0 CRC64;
     MIIGVPKEIK NNENRVAMTP AGVVHLINAG HTVQIEKGAG LGSNFADAEY KEAGAELIDS
     AASVWENADM IMKVKEPLSS EYKYFRKGLI LFTYLHLAAA PELTKALVDS EVTAIAYETI
     TVNGTLPLLT PMSEVAGRMA TQIGAQYLEK SEGGKGILLG GIPGVSRGKV TVIGGGVVGT
     HAAKIALGLG AEVTIIDLNP VRLRQLDDIF GSSIQTLMSN PYNIAEAVKD SDLVIGSVLI
     PGRKAPKLVT DEMIQSMQPG SVLVDVAIDQ GGNFETVDHP TTHDEPIYVK HDVLHYAVAN
     IPGAVPRTAT VGLTNVTVPY AVQIASKGAV KAIQDNPAIL TGVNVMNGKV TYEAVAADLG
     YDFVSPEDAI KDAELV