DHA2_STAAS
ID DHA2_STAAS Reviewed; 372 AA.
AC Q6G8L8;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Alanine dehydrogenase 2;
DE EC=1.4.1.1;
GN Name=ald2; OrderedLocusNames=SAS1636;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC -!- FUNCTION: May play a role in cell wall synthesis as L-alanine is an
CC important constituent of the peptidoglycan layer. {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 -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}.
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DR EMBL; BX571857; CAG43438.1; -; Genomic_DNA.
DR RefSeq; WP_000689998.1; NC_002953.3.
DR AlphaFoldDB; Q6G8L8; -.
DR SMR; Q6G8L8; -.
DR KEGG; sas:SAS1636; -.
DR HOGENOM; CLU_003376_3_0_9; -.
DR OMA; HPYYHLY; -.
DR UniPathway; UPA00527; UER00585.
DR GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-EC.
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; Oxidoreductase.
FT CHAIN 1..372
FT /note="Alanine dehydrogenase 2"
FT /id="PRO_0000199005"
FT ACT_SITE 95
FT /evidence="ECO:0000255"
FT BINDING 169..199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 372 AA; 40105 MW; 32BA3DA4734EC9FB CRC64;
MKIGIPREIK NNENRVGLSP SGVHALVESG HTVLVETNAG SGSFFEDVDY KEAGAEIVAE
QAKVWDVDMV IKVKEPLESE YPYFKEGLVL FTYLHLANEE KLTQALIDRK VISIAYETVQ
LPDRSLPLLS PMSEVAGRMS AQVGAEFLQK LNGGMGILLG GVPGVPKGKV TIIGGGQAGT
NAAKIALGLG ADVTILDVNP KRLQQLDDLF GGRVHTIMSN PLNIELYVKQ SDLVIGAVLI
PGAKAPRLVT EDMIKQMKNG SVIIDIAIDQ GGIFETTDKI TTHDDPTYIK HGVVHYAVAN
MPGAVPRTST LALNNATLPY ALMLANKGYR EAFKSNQPLS LGLNTYKGHV TNKGVAEAFE
MEYKSVEEAL QL