ID ALR2_PSEAE Reviewed; 357 AA. AC Q9HTQ2; Q9S419; DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 10-JUN-2026, entry version 150. DE RecName: Full=Alanine racemase, catabolic {ECO:0000305|PubMed:10977898}; DE EC=5.1.1.1 {ECO:0000269|PubMed:10977898}; GN Name=dadX {ECO:0000303|PubMed:10977898, ECO:0000312|EMBL:AAG08687.1}; GN OrderedLocusNames=PA5302; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pseudomonadales; Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=10977898; DOI=10.1007/s002840010136; RA Strych U., Huang H.-C., Krause K.L., Benedik M.J.; RT "Characterization of the alanine racemases from Pseudomonas aeruginosa RT PAO1."; RL Curr. Microbiol. 41:290-294(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE RP AND LYSINE, COFACTOR, SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-33, AND RP CARBOXYLATION AT LYS-122. RX PubMed=14674749; DOI=10.1021/bi030165v; RA LeMagueres P., Im H., Dvorak A., Strych U., Benedik M.J., Krause K.L.; RT "Crystal structure at 1.45 A resolution of alanine racemase from a RT pathogenic bacterium, Pseudomonas aeruginosa, contains both internal and RT external aldimine forms."; RL Biochemistry 42:14752-14761(2003). CC -!- FUNCTION: Isomerizes L-alanine to D-alanine which is then oxidized to CC pyruvate by DadA. {ECO:0000269|PubMed:10977898}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249, CC ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1; CC Evidence={ECO:0000269|PubMed:10977898}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000269|PubMed:14674749}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.4 mM for D-alanine {ECO:0000269|PubMed:10977898}; CC KM=1.4 mM for L-alanine {ECO:0000269|PubMed:10977898}; CC Vmax=134 umol/min/mg enzyme toward D-alanine CC {ECO:0000269|PubMed:10977898}; CC Vmax=155 umol/min/mg enzyme toward L-alanine CC {ECO:0000269|PubMed:10977898}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14674749}. CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000255|HAMAP- CC Rule:MF_01201}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF165881; AAD47081.1; -; Genomic_DNA. DR EMBL; AE004091; AAG08687.1; -; Genomic_DNA. DR PIR; F82982; F82982. DR RefSeq; NP_253989.1; NC_002516.2. DR RefSeq; WP_003114351.1; NC_002516.2. DR PDB; 1RCQ; X-ray; 1.45 A; A=1-357. DR AlphaFoldDB; Q9HTQ2; -. DR SMR; Q9HTQ2; -. DR FunCoup; Q9HTQ2; 324. DR STRING; 208964.PA5302; -. DR DrugBank; DB03252; D-Lysine. DR DrugBank; DB03801; Lysine Nz-Carboxylic Acid. DR PaxDb; 208964-PA5302; -. DR GeneID; 878055; -. DR KEGG; pae:PA5302; -. DR PATRIC; fig|208964.12.peg.5556; -. DR PseudoCAP; PA5302; -. DR HOGENOM; CLU_028393_1_0_6; -. DR InParanoid; Q9HTQ2; -. DR OrthoDB; 9813814at2; -. DR PhylomeDB; Q9HTQ2; -. DR BioCyc; PAER208964:G1FZ6-5423-MONOMER; -. DR BRENDA; 5.1.1.1; 5087. DR SABIO-RK; Q9HTQ2; -. DR EvolutionaryTrace; Q9HTQ2; -. DR Proteomes; UP000002438; Chromosome. DR AbasyAtlas; Q9HTQ2; -. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008784; F:alanine racemase activity; IDA:PseudoCAP. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0030632; P:D-alanine biosynthetic process; IBA:GO_Central. DR CDD; cd06827; PLPDE_III_AR_proteobact; 1. DR FunFam; 2.40.37.10:FF:000002; Alanine racemase; 1. DR FunFam; 3.20.20.10:FF:000002; Alanine racemase; 1. DR Gene3D; 3.20.20.10; Alanine racemase; 1. DR Gene3D; 2.40.37.10; Lyase, Ornithine Decarboxylase, Chain A, domain 1; 1. DR HAMAP; MF_01201; Ala_racemase; 1. DR InterPro; IPR000821; Ala_racemase. DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C. DR InterPro; IPR011079; Ala_racemase_C. DR InterPro; IPR001608; Ala_racemase_N. DR InterPro; IPR020622; Ala_racemase_pyridoxalP-BS. DR InterPro; IPR029066; PLP-binding_barrel. DR NCBIfam; TIGR00492; alr; 1. DR PANTHER; PTHR30511; ALANINE RACEMASE; 1. DR PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1. DR Pfam; PF00842; Ala_racemase_C; 1. DR Pfam; PF01168; Ala_racemase_N; 1. DR PRINTS; PR00992; ALARACEMASE. DR SMART; SM01005; Ala_racemase_C; 1. DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1. DR SUPFAM; SSF51419; PLP-binding barrel; 1. DR PROSITE; PS00395; ALANINE_RACEMASE; 1. DR PDBsum; 1RCQ; -. PE 1: Evidence at protein level; KW 3D-structure; Isomerase; Pyridoxal phosphate; Reference proteome. FT CHAIN 1..357 FT /note="Alanine racemase, catabolic" FT /id="PRO_0000114547" FT ACT_SITE 33 FT /note="Proton acceptor; specific for D-alanine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201" FT ACT_SITE 253 FT /note="Proton acceptor; specific for L-alanine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201" FT BINDING 129 FT /ligand="substrate" FT /evidence="ECO:0000305|PubMed:14674749" FT BINDING 301 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201" FT MOD_RES 33 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000269|PubMed:14674749" FT MOD_RES 122 FT /note="N6-carboxylysine" FT /evidence="ECO:0000269|PubMed:14674749" FT CONFLICT 138 FT /note="S -> R (in Ref. 1; AAD47081)" FT /evidence="ECO:0000305" FT CONFLICT 178 FT /note="A -> S (in Ref. 1; AAD47081)" FT /evidence="ECO:0000305" FT CONFLICT 262 FT /note="S -> R (in Ref. 1; AAD47081)" FT /evidence="ECO:0000305" FT STRAND 5..9 FT /evidence="ECO:0007829|PDB:1RCQ" FT HELIX 10..24 FT /evidence="ECO:0007829|PDB:1RCQ" FT STRAND 26..31 FT /evidence="ECO:0007829|PDB:1RCQ" FT HELIX 33..37 FT /evidence="ECO:0007829|PDB:1RCQ" FT HELIX 41..48 FT /evidence="ECO:0007829|PDB:1RCQ" FT TURN 49..51 FT /evidence="ECO:0007829|PDB:1RCQ" FT STRAND 53..59 FT /evidence="ECO:0007829|PDB:1RCQ" FT HELIX 60..68 FT /evidence="ECO:0007829|PDB:1RCQ" FT STRAND 75..77 FT /evidence="ECO:0007829|PDB:1RCQ" FT HELIX 84..86 FT /evidence="ECO:0007829|PDB:1RCQ" FT HELIX 87..92 FT /evidence="ECO:0007829|PDB:1RCQ" FT STRAND 95..99 FT /evidence="ECO:0007829|PDB:1RCQ" FT HELIX 102..110 FT /evidence="ECO:0007829|PDB:1RCQ" FT STRAND 117..123 FT /evidence="ECO:0007829|PDB:1RCQ" FT STRAND 125..127 FT /evidence="ECO:0007829|PDB:1RCQ" FT STRAND 129..132 FT /evidence="ECO:0007829|PDB:1RCQ" FT HELIX 134..146 FT /evidence="ECO:0007829|PDB:1RCQ" FT STRAND 150..156 FT /evidence="ECO:0007829|PDB:1RCQ" FT HELIX 169..181 FT /evidence="ECO:0007829|PDB:1RCQ" FT HELIX 193..198 FT /evidence="ECO:0007829|PDB:1RCQ" FT STRAND 205..207 FT /evidence="ECO:0007829|PDB:1RCQ" FT HELIX 211..214 FT /evidence="ECO:0007829|PDB:1RCQ" FT STRAND 218..221 FT /evidence="ECO:0007829|PDB:1RCQ" FT HELIX 226..228 FT /evidence="ECO:0007829|PDB:1RCQ" FT STRAND 233..245 FT /evidence="ECO:0007829|PDB:1RCQ" FT STRAND 250..252 FT /evidence="ECO:0007829|PDB:1RCQ" FT HELIX 253..255 FT /evidence="ECO:0007829|PDB:1RCQ" FT STRAND 260..269 FT /evidence="ECO:0007829|PDB:1RCQ" FT HELIX 272..274 FT /evidence="ECO:0007829|PDB:1RCQ" FT STRAND 285..288 FT /evidence="ECO:0007829|PDB:1RCQ" FT STRAND 291..295 FT /evidence="ECO:0007829|PDB:1RCQ" FT STRAND 304..307 FT /evidence="ECO:0007829|PDB:1RCQ" FT STRAND 319..327 FT /evidence="ECO:0007829|PDB:1RCQ" FT HELIX 329..335 FT /evidence="ECO:0007829|PDB:1RCQ" FT HELIX 340..345 FT /evidence="ECO:0007829|PDB:1RCQ" FT STRAND 352..355 FT /evidence="ECO:0007829|PDB:1RCQ" SQ SEQUENCE 357 AA; 38915 MW; 199F4021D02FFF48 CRC64; MRPARALIDL QALRHNYRLA REATGARALA VIKADAYGHG AVRCAEALAA EADGFAVACI EEGLELREAG IRQPILLLEG FFEASELELI VAHDFWCVVH CAWQLEAIER ASLARPLNVW LKMDSGMHRV GFFPEDFSAA HERLRASGKV AKIVMMSHFS RADELDCPRT EEQLAAFAAA SQGLEGEISL RNSPAVLGWP KVPSDWVRPG ILLYGATPFE RAHPLADRLR PVMTLESKVI SVRDLPAGEP VGYGARYSTE RSQRIGVVAM GYADGYPRHA ADGTLVFIDG KPGRLVGRVS MDMLTVDLTD HPQAGLGSRV ELWGPNVPVG ALAAQFGSIP YQLLCNLKRV PRVYSGA //