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DHA_LYSSH
ID   DHA_LYSSH               Reviewed;         372 AA.
AC   P17556;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Alanine dehydrogenase {ECO:0000303|PubMed:488097};
DE            EC=1.4.1.1 {ECO:0000269|PubMed:488097};
GN   Name=ald;
OS   Lysinibacillus sphaericus (Bacillus sphaericus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=1421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-23; 64-73;
RP   112-151; 157-167; 204-205; 214-230; 281-321; 329-331 AND 343-372, FUNCTION
RP   AS AN ALANINE DEHYDROGENASE, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=ATCC 10208 / DSM 5019 / NBRC 3525 / NCIMB 11935 / NRS 966 / 1911;
RX   PubMed=2340274; DOI=10.1021/bi00456a025;
RA   Kuroda S., Tanizawa K., Sakamoto Y., Tanaka H., Soda K.;
RT   "Alanine dehydrogenases from two Bacillus species with distinct
RT   thermostabilities: molecular cloning, DNA and protein sequence
RT   determination, and structural comparison with other NAD(P)(+)-dependent
RT   dehydrogenases.";
RL   Biochemistry 29:1009-1015(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 1 AND 372, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP   SPECIFICITY, REACTION MECHANISM, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RC   STRAIN=ATCC 10208 / DSM 5019 / NBRC 3525 / NCIMB 11935 / NRS 966 / 1911;
RX   PubMed=488097; DOI=10.1111/j.1432-1033.1979.tb02030.x;
RA   Ohashima T., Soda K.;
RT   "Purification and properties of alanine dehydrogenase from Bacillus
RT   sphaericus.";
RL   Eur. J. Biochem. 100:29-30(1979).
CC   -!- FUNCTION: Catalyzes the reversible reductive amination of pyruvate to
CC       L-alanine. Prefers L-alanine for oxidative deamination, other
CC       substrates are poorly reactive. In the other direction 2-oxobutyrate is
CC       almost as reactive as pyruvate. Ammonia is the sole amino donor for the
CC       reductive amination of pyruvate, NADPH is inert. Reductive amination
CC       proceeds through a sequential, ordered ternary-binary mechanism, where
CC       NADH binds first followed by ammonia and pyruvate; the products are
CC       released in the order L-alanine and NAD(+) (PubMed:488097,
CC       PubMed:2340274). A key factor in the assimilation of L-alanine as an
CC       energy source via the tricarboxylic acid cycle during sporulation (By
CC       similarity). {ECO:0000250|UniProtKB:Q08352, ECO:0000269|PubMed:2340274,
CC       ECO:0000269|PubMed:488097}.
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:0000269|PubMed:488097};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18406;
CC         Evidence={ECO:0000269|PubMed:488097};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18407;
CC         Evidence={ECO:0000269|PubMed:488097};
CC   -!- ACTIVITY REGULATION: Inhibited by p-chloromercuribenzoate and HgCl(2)
CC       and by Cu(2+) and Pb(2+) salts, unaffected by amino acids such as D-
CC       alanine and beta-alanine or by nucleotides or nucleosides.
CC       {ECO:0000269|PubMed:488097}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=18.9 uM for oxidative deamination of L-alanine
CC         {ECO:0000269|PubMed:488097};
CC         KM=330 uM for oxidative deamination of L-2-aminobutyrate
CC         {ECO:0000269|PubMed:488097};
CC         KM=39 uM for oxidative deamination of L-serine
CC         {ECO:0000269|PubMed:488097};
CC         KM=20 uM for oxidative deamination of L-valine
CC         {ECO:0000269|PubMed:488097};
CC         KM=14 uM for oxidative deamination of L-norvaline
CC         {ECO:0000269|PubMed:488097};
CC         KM=1.7 mM for reductive amination of pyruvate
CC         {ECO:0000269|PubMed:488097};
CC         KM=80 mM for reductive amination of 3-hydroxypyruvate
CC         {ECO:0000269|PubMed:488097};
CC         KM=23 mM for reductive amination of 2-oxovalerate
CC         {ECO:0000269|PubMed:488097};
CC         KM=12 mM for reductive amination of glyoxylate
CC         {ECO:0000269|PubMed:488097};
CC         KM=11 mM for reductive amination of 2-oxobutyrate
CC         {ECO:0000269|PubMed:488097};
CC         KM=11 mM for reductive amination of 2-oxo-3-methylbutanoate
CC         {ECO:0000269|PubMed:488097};
CC       pH dependence:
CC         Optimum pH is 10.0-10.5 for the oxidative deamination of L-alanine
CC         and about 9.0 for reductive amination of pyruvate.
CC         {ECO:0000269|PubMed:488097};
CC       Temperature dependence:
CC         Loses about 50% of its initial activity when heated at 65 degrees
CC         Celsius for 5 min. {ECO:0000269|PubMed:2340274,
CC         ECO:0000269|PubMed:488097};
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:0000269|PubMed:2340274,
CC       ECO:0000269|PubMed:488097}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0QVQ8}.
CC   -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}.
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DR   EMBL; M33298; AAA22210.1; -; Genomic_DNA.
DR   PIR; A34261; A34261.
DR   AlphaFoldDB; P17556; -.
DR   SMR; P17556; -.
DR   UniPathway; UPA00527; UER00585.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0000286; F:alanine dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006524; P:alanine catabolic process; ISS:UniProtKB.
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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; NAD; Nucleotide-binding;
KW   Oxidoreductase; Sporulation.
FT   CHAIN           1..372
FT                   /note="Alanine dehydrogenase"
FT                   /id="PRO_0000198990"
FT   ACT_SITE        96
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        270
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         134
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         178..179
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         198
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         239..240
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         267..270
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         280
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         299..302
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   372 AA;  39460 MW;  5E6FD5E4D93AA98B CRC64;
     MKIGIPKEIK NNENRVAMTP AGVVSLTHAG HERLAIETGG GIGSSFTDAE YVAAGAAYRC
     IGKEAWAQEM ILKVKEPVAS EYDYFYEGQI LFTYLHLAPR AELTQALIDK KVVGIAYETV
     QLANGSLPLL TPMSEVAGKM ATQIGAQYLE KNHGGKGILL GGVSGVHARK VTVIGGGIAG
     TNAAKIAVGM GADVTVIDLS PERLRQLEDM FGRDVQTLMS NPYNIAESVK HSDLVVGAVL
     IPGAKAPKLV SEEMIQSMQP GSVVVDIAID QGGIFATSDR VTTHDDPTYV KHGVVHYAVA
     NMPGAVPRTS TIALTNNTIP YALQIANKGY KQACIDNPAL KKGVNALEGH ITYKAVAEAQ
     GLPYVNVDEL IQ
 
 
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