DHA1_STAAW
ID DHA1_STAAW Reviewed; 372 AA.
AC Q8NWQ3;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Alanine dehydrogenase 1;
DE EC=1.4.1.1;
GN Name=ald1; OrderedLocusNames=MW1328;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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; BA000033; BAB95193.1; -; Genomic_DNA.
DR RefSeq; WP_000959432.1; NC_003923.1.
DR AlphaFoldDB; Q8NWQ3; -.
DR SMR; Q8NWQ3; -.
DR EnsemblBacteria; BAB95193; BAB95193; BAB95193.
DR KEGG; sam:MW1328; -.
DR HOGENOM; CLU_003376_3_0_9; -.
DR OMA; GHQVILQ; -.
DR UniPathway; UPA00527; UER00585.
DR Proteomes; UP000000418; Chromosome.
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 1"
FT /id="PRO_0000199000"
FT ACT_SITE 94
FT /evidence="ECO:0000255"
FT BINDING 170..200
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 372 AA; 40234 MW; 7FF131E5E18D4035 CRC64;
MLVAVVKELK QGEGRVACTP ENVRKLTDAG HKVIVEKNAG IGSGFSNDMY EKEGAKIVTH
EQAWEADLVI KVKEPHESEY QYFKKNQIIW GFLHLASSKE IVEKMQEVGV TAISGETIIK
NGKAELLAPM SAIAGQRSAI MGAYYSEAQH GGQGTLVTGV HENVDIPGST YVIFGGGVAA
TNAANVALGL NAKVIIIELN DDRIKYLQDM YAEKDVTVVK STPENLAEQI KKADVFISTI
LIPGAKPPKL VTREMVKSMK KGSVLIDIAI DQGGTIETIR PTTISDPVYE EEGVIHYGVP
NQPGAVPRTS TMALAQGNID YILEICDKGL EQAIKDNEAL STGVNIYQGQ VTNQGLASSH
DLDYKEILNV IE