DHA_STAEQ
ID DHA_STAEQ Reviewed; 371 AA.
AC Q5HNJ6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Alanine dehydrogenase;
DE EC=1.4.1.1;
GN Name=ald; OrderedLocusNames=SERP1272;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
CC -!- FUNCTION: Catalyzes the reversible reductive amination of pyruvate to
CC L-alanine. May play a role in cell wall synthesis as L-alanine is an
CC important constituent of the peptidoglycan layer (By similarity).
CC {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. Trimer of dimer (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}.
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DR EMBL; CP000029; AAW54667.1; -; Genomic_DNA.
DR RefSeq; WP_001830775.1; NC_002976.3.
DR AlphaFoldDB; Q5HNJ6; -.
DR SMR; Q5HNJ6; -.
DR STRING; 176279.SERP1272; -.
DR EnsemblBacteria; AAW54667; AAW54667; SERP1272.
DR GeneID; 50018502; -.
DR KEGG; ser:SERP1272; -.
DR eggNOG; COG0686; Bacteria.
DR HOGENOM; CLU_003376_3_0_9; -.
DR OMA; HPYYHLY; -.
DR OrthoDB; 673280at2; -.
DR UniPathway; UPA00527; UER00585.
DR Proteomes; UP000000531; Chromosome.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0000286; F:alanine dehydrogenase activity; ISS: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 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 NAD; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..371
FT /note="Alanine dehydrogenase"
FT /id="PRO_0000199008"
FT ACT_SITE 95
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 74
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 371 AA; 40195 MW; 78541923F8E7CD6F CRC64;
MKIGIPKEIK NNENRVGLSP SGVHALVDQG HEVLVETNAG LGSYFEDGDY QEAGAKIVDE
QSKAWDVDMV IKVKEPLESE YKFFKEELIL FTYLHLANEQ KLTQALVDNK VISIAYETVQ
LPDGSLPLLT PMSEVAGRMS TQVGAEFLQR FNGGMGILLG GIPGVPKGKV TIIGGGQAGT
NAAKIALGLG AEVTILDVNP KRLEELEDLF DGRVRTIMSN PLNIEMYVKE SDLVIGAVLI
PGAKAPNLVT EDMIKEMKDG SVIVDIAIDQ GGIFETTDKI TTHDNPTYTK HGVVHYAVAN
MPGAVPRTST IGLNNATLPY AQLLANKGYR EAFKVNHPLS LGLNTFNGHV TNKNVADTFN
FEYTSIEDAL K
