DHA1_STAAC
ID DHA1_STAAC Reviewed; 372 AA.
AC Q5HFY4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Alanine dehydrogenase 1;
DE EC=1.4.1.1;
GN Name=ald1; OrderedLocusNames=SACOL1478;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
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: 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; CP000046; AAW36674.1; -; Genomic_DNA.
DR RefSeq; WP_000959424.1; NC_002951.2.
DR AlphaFoldDB; Q5HFY4; -.
DR SMR; Q5HFY4; -.
DR EnsemblBacteria; AAW36674; AAW36674; SACOL1478.
DR KEGG; sac:SACOL1478; -.
DR HOGENOM; CLU_003376_3_0_9; -.
DR OMA; GHQVILQ; -.
DR UniPathway; UPA00527; UER00585.
DR Proteomes; UP000000530; 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_0000198995"
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; 40235 MW; CAF521B4A8C5D8EC CRC64;
MLVAVVKELK QGEGRVACTP ENVRKLTDAG HKVIVEKNAG IGSGFSNDMY EKEGAKIVTH
EQAWEADLVI KVKEPHESEY QYFKKNQIIW GFLHLASSKE IVEKMQEVGV TAISGETIIK
NGKAELLAPM SAIAGQRSAI MGAYYSEAQH GGQGTLVTGV HENVDIPGST YVIFGGGVAA
TNAANVALGL NAKVIIIELN DDRIKYLEDM YAEKDVTVVK STPENLAEQI KKADVFISTI
LIPGAKPPKL VTREMVKSMK KGSVLIDIAI DQGGTIETIR PTTISDPVYE EEGVIHYGVP
NQPGAVPRTS TMALAQGNID YILEICDKGL EQAIKDNEAL STGVNIYQGQ VTNQGLASSH
DLDYKEILNV IE