ID Q6LM08_PHOPR Unreviewed; 404 AA. AC Q6LM08; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 133. DE RecName: Full=Broad specificity amino-acid racemase {ECO:0000256|HAMAP-Rule:MF_02212}; DE EC=5.1.1.10 {ECO:0000256|HAMAP-Rule:MF_02212}; DE Flags: Precursor; GN Name=ALR {ECO:0000313|EMBL:CAG21670.1}; GN OrderedLocusNames=PBPRA3385 {ECO:0000313|EMBL:CAG21670.1}; OS Photobacterium profundum (strain SS9). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Photobacterium. OX NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG21670.1, ECO:0000313|Proteomes:UP000000593}; RN [1] {ECO:0000313|Proteomes:UP000000593} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593}; RX PubMed=15746425; DOI=10.1126/science.1103341; RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M., RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C., RA Bartlett D.H., Valle G.; RT "Life at depth: Photobacterium profundum genome sequence and expression RT analysis."; RL Science 307:1459-1461(2005). CC -!- FUNCTION: Amino-acid racemase able to utilize a broad range of CC substrates. {ECO:0000256|HAMAP-Rule:MF_02212}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-arginine = D-arginine; Xref=Rhea:RHEA:18069, CC ChEBI:CHEBI:32682, ChEBI:CHEBI:32689; Evidence={ECO:0000256|HAMAP- CC Rule:MF_02212}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysine = D-lysine; Xref=Rhea:RHEA:22864, ChEBI:CHEBI:32551, CC ChEBI:CHEBI:32557; Evidence={ECO:0000256|HAMAP-Rule:MF_02212}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an L-alpha-amino acid = a D-alpha-amino acid; CC Xref=Rhea:RHEA:18317, ChEBI:CHEBI:59869, ChEBI:CHEBI:59871; CC EC=5.1.1.10; Evidence={ECO:0000256|HAMAP-Rule:MF_02212}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933, ECO:0000256|HAMAP- CC Rule:MF_02212, ECO:0000256|PIRSR:PIRSR600821-50}; CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418, CC ECO:0000256|HAMAP-Rule:MF_02212}. CC -!- SIMILARITY: Belongs to the alanine racemase family. Bsr subfamily. CC {ECO:0000256|ARBA:ARBA00023456, ECO:0000256|HAMAP-Rule:MF_02212}. 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; CR378673; CAG21670.1; -; Genomic_DNA. DR AlphaFoldDB; Q6LM08; -. DR STRING; 298386.PBPRA3385; -. DR KEGG; ppr:PBPRA3385; -. DR eggNOG; COG0787; Bacteria. DR HOGENOM; CLU_028393_2_2_6; -. DR Proteomes; UP000000593; Chromosome 1. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0008784; F:alanine racemase activity; IEA:InterPro. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule. DR GO; GO:0006522; P:alanine metabolic process; IEA:InterPro. DR CDD; cd06826; PLPDE_III_AR2; 1. DR Gene3D; 3.20.20.10; Alanine racemase; 1. DR HAMAP; MF_02212; Bsr_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 InterPro; IPR043698; Racemase_Bsr/Lyr. 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. PE 3: Inferred from homology; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP- KW Rule:MF_02212}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_02212}; KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|HAMAP-Rule:MF_02212}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP- KW Rule:MF_02212}; Reference proteome {ECO:0000313|Proteomes:UP000000593}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_02212}. FT SIGNAL 1..20 FT /evidence="ECO:0000256|HAMAP-Rule:MF_02212" FT CHAIN 21..404 FT /note="Broad specificity amino-acid racemase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02212" FT /id="PRO_5026407334" FT DOMAIN 276..404 FT /note="Alanine racemase C-terminal" FT /evidence="ECO:0000259|SMART:SM01005" FT ACT_SITE 72 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02212" FT ACT_SITE 297 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02212" FT BINDING 171 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02212, FT ECO:0000256|PIRSR:PIRSR600821-52" FT BINDING 345 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02212, FT ECO:0000256|PIRSR:PIRSR600821-52" FT MOD_RES 72 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02212, FT ECO:0000256|PIRSR:PIRSR600821-50" FT DISULFID 68..94 FT /evidence="ECO:0000256|HAMAP-Rule:MF_02212" SQ SEQUENCE 404 AA; 44408 MW; BC0E50D155592F87 CRC64; MKLKLSLVAL ALMGQTTANA APLLVDFDNN EREERVQSSN AWLEIDTQAF SGNIQLLQNQ LKADTKICAI MKADAYGNGI AGLMPSIIAN QVPCVGITSN EEARVVRKHG FIGKIMRVRA ASKNEIEGGL QYQMEELIGT KAQADQIIEI ARANGTTIPV HLALNTSGMG RNGLDLTTYE GQVEGVEIAG DPNLEIVGMM THFPNEGLDE IKRKVKRFKV ETKWLMDSTD LKRKDVTLHV ANSYITLNLP EAHLDMVRPG GMLYGDYPAT APYQRIVSFK THVASLHHFP AGSTIGYGST AVLERDSVLA NLPIGYSDGF ARSLGNKAEV LINGQRARVM GMVSMNTTMV DVTDIVDVQT NEEVVIFGRQ GFEEITGEET EEKSNRILPE HYTVWGATNP RIYR //