DHA_GEOSE
ID DHA_GEOSE Reviewed; 372 AA.
AC P17557;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Alanine dehydrogenase {ECO:0000303|PubMed:2340274};
DE EC=1.4.1.1 {ECO:0000305|PubMed:2340274};
GN Name=ald;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 29-48; 231-245;
RP 256-327 AND 342-372, PROBABLE FUNCTION AS AN ALANINE DEHYDROGENASE,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 12980 / DSM 22 / CCM 2062 / JCM 2501 / NBRC 12550 / NCIMB 8923
RC / NCTC 10339 / R-35646 / VKM B-510;
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).
CC -!- FUNCTION: Catalyzes the reversible reductive amination of pyruvate to
CC L-alanine (Probable). A key factor in the assimilation of L-alanine as
CC an energy source via the tricarboxylic acid cycle during sporulation
CC (By similarity). {ECO:0000250|UniProtKB:Q08352,
CC ECO:0000305|PubMed:2340274}.
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:0000305|PubMed:2340274};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Retains about 50% of its initial activity when heated at 85 degrees
CC Celsius for 5 min at pH 7.2. {ECO:0000269|PubMed:2340274};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0QVQ8}.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}.
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DR EMBL; M33299; AAA22211.1; -; Genomic_DNA.
DR PIR; B34261; B34261.
DR AlphaFoldDB; P17557; -.
DR SMR; P17557; -.
DR UniPathway; UPA00527; UER00585.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0000286; F:alanine dehydrogenase activity; TAS: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_0000198991"
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 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 266..269
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 279
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 372 AA; 39695 MW; 99AE8E621ED1F23A CRC64;
MKIGIPKEIK NNENRVAITP AGVMTLVKAG HEVYVETEGG AGSGFSDSEY EKAGAADRCR
TWRDAWTAEM VLKVKEPLAR EFRYFRPGLI LFTYLHLAAA ERVTKAVVEQ KVVGIAYETV
QLANGSLPLL TPMSEVAGRM SVQVGAQFLE KPHGGKGILL GGVPGVRRGK VTIIGGGTAG
TNAAKIGVGL GADVTILDIN AERLRELDDL FGDHVTTLMS NSYHIAECVR ESDLVVGAVL
IPGAKAKLVT EEMVRSMTPG SVLVDIAIDQ GGIFETTDRV TTHDDPTYVK HGVVHYAVAN
MPGAVPRTST FALTNVTIPY ALQIANKGYR AGCLDNPALL KGINTLDGHI VYEAVAAAHN
MPYTDVHSLL HG
