ID DHA1_STAA3 Reviewed; 372 AA. AC Q2FH00; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 16-JUN-2009, entry version 21. DE RecName: Full=Alanine dehydrogenase 1; DE EC=1.4.1.1; GN Name=ald1; OrderedLocusNames=SAUSA300_1331; OS Staphylococcus aureus (strain USA300). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=367830; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16517273; DOI=10.1016/S0140-6736(06)68231-7; RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G., RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F., RA Perdreau-Remington F.; RT "Complete genome sequence of USA300, an epidemic clone of community- RT acquired meticillin-resistant Staphylococcus aureus."; RL Lancet 367:731-739(2006). CC -!- FUNCTION: May play a role in cell wall synthesis as L-alanine is CC an important constituent of the peptidoglycan layer (By CC similarity). CC -!- CATALYTIC ACTIVITY: L-alanine + H(2)O + NAD(+) = pyruvate + NH(3) CC + NADH. CC -!- PATHWAY: Amino-acid degradation; L-alanine degradation via CC dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step CC 1/1. CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000255; ABD21351.1; -; Genomic_DNA. DR RefSeq; YP_494028.1; -. DR GeneID; 3914134; -. DR GenomeReviews; CP000255_GR; SAUSA300_1331. DR KEGG; saa:SAUSA300_1331; -. DR HOGENOM; Q2FH00; -. DR OMA; Q2FH00; GNCEYIV. DR GO; GO:0000286; F:alanine dehydrogenase activity; IEA:EC. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR007698; Ala_DH/PNT_C. DR InterPro; IPR008142; Ala_DH/PNT_CS1. DR InterPro; IPR008143; Ala_DH/PNT_CS2. DR InterPro; IPR007886; Ala_DH/PNT_N. DR InterPro; IPR008141; Ala_DH_PNT. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Pfam; PF01262; AlaDh_PNT_C; 1. DR Pfam; PF05222; AlaDh_PNT_N; 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 Complete proteome; NAD; Oxidoreductase. FT CHAIN 1 372 Alanine dehydrogenase 1. FT /FTId=PRO_0000287322. FT NP_BIND 170 200 NAD (By similarity). FT ACT_SITE 94 94 Potential. 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 //