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   16-JUN-2009, entry version 37.
DE   RecName: Full=Alanine dehydrogenase;
DE            EC=1.4.1.1;
GN   Name=ald; OrderedLocusNames=OB3225;
OS   Oceanobacillus iheyensis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=182710;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / JCM 11309 / KCTC 3954 / HTE831;
RX   MEDLINE=22220767; PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya
RT   Ridge and its unexpected adaptive capabilities to extreme
RT   environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
CC   -!- FUNCTION: This enzyme is a key factor in the assimilation of L-
CC       alanine as an energy source through the tricarboxylic acid cycle
CC       during sporulation (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-alanine + H(2)O + NAD(+) = pyruvate + NH(3)
CC       + NADH.
CC   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via
CC       dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step
CC       1/1.
CC   -!- SUBUNIT: Homohexamer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the AlaDH/PNT family.
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DR   EMBL; BA000028; BAC15181.1; -; Genomic_DNA.
DR   RefSeq; NP_694147.1; -.
DR   HSSP; O52942; 1SAY.
DR   GeneID; 1016523; -.
DR   GenomeReviews; BA000028_GR; OB3225.
DR   KEGG; oih:OB3225; -.
DR   NMPDR; fig|221109.1.peg.3227; -.
DR   HOGENOM; Q8CX61; -.
DR   OMA; Q8CX61; MIATMRT.
DR   BioCyc; OIHE221109:OB3225-MON; -.
DR   BRENDA; 1.4.1.1; 278212.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000286; F:alanine dehydrogenase activity; IEA:EC.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cel...; IEA:UniProtKB-KW.
DR   InterPro; IPR007698; Ala_DH/PNT_C.
DR   InterPro; IPR008142; Ala_DH/PNT_CS1.
DR   InterPro; IPR008143; Ala_DH/PNT_CS2.
DR   InterPro; IPR007886; Ala_DH/PNT_N.
DR   InterPro; IPR008141; Ala_DH_PNT.
DR   Pfam; PF01262; AlaDh_PNT_C; 1.
DR   Pfam; PF05222; AlaDh_PNT_N; 1.
DR   ProDom; PD000139; FAD_pyr_redox; 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   Complete proteome; Cytoplasm; NAD; Oxidoreductase; Sporulation.
FT   CHAIN         1    376       Alanine dehydrogenase.
FT                                /FTId=PRO_0000198993.
FT   NP_BIND     169    199       NAD (By similarity).
FT   ACT_SITE     96     96       Potential.
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
//