DHA1_STAA8
ID DHA1_STAA8 Reviewed; 372 AA.
AC Q2FYJ2;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Alanine dehydrogenase 1;
DE EC=1.4.1.1;
GN Name=ald1; OrderedLocusNames=SAOUHSC_01452;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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; CP000253; ABD30540.1; -; Genomic_DNA.
DR RefSeq; WP_000959429.1; NZ_LS483365.1.
DR RefSeq; YP_499973.1; NC_007795.1.
DR AlphaFoldDB; Q2FYJ2; -.
DR SMR; Q2FYJ2; -.
DR STRING; 1280.SAXN108_1460; -.
DR EnsemblBacteria; ABD30540; ABD30540; SAOUHSC_01452.
DR GeneID; 3919897; -.
DR KEGG; sao:SAOUHSC_01452; -.
DR PATRIC; fig|93061.5.peg.1324; -.
DR eggNOG; COG0686; Bacteria.
DR HOGENOM; CLU_003376_3_0_9; -.
DR OMA; GHQVILQ; -.
DR UniPathway; UPA00527; UER00585.
DR PRO; PR:Q2FYJ2; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0000286; F:alanine dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0006524; P:alanine catabolic process; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..372
FT /note="Alanine dehydrogenase 1"
FT /id="PRO_0000287320"
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; 40225 MW; 65F43EB678C5D8EE 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
LISGAKPPKL VTREMVKSMK KGSVLIDIAI DQGGTIETIR PTTISDPVYE EEGVIHYGVP
NQPGAVPRTS TMALAQGNID YILEICDKGL EQAIKDNEAL STGVNIYQGQ VTNQGLASSH
DLDYKEILNV IE