ID D5UIS2_CELFN Unreviewed; 410 AA. AC D5UIS2; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 18-JUN-2025, entry version 82. DE RecName: Full=Alanine racemase {ECO:0000256|ARBA:ARBA00072221, ECO:0000256|HAMAP-Rule:MF_01201}; DE EC=5.1.1.1 {ECO:0000256|ARBA:ARBA00013089, ECO:0000256|HAMAP-Rule:MF_01201}; GN OrderedLocusNames=Cfla_2600 {ECO:0000313|EMBL:ADG75488.1}; OS Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / BCRC 11376 / JCM OS 18109 / NBRC 3775 / NCIMB 8073 / NRS 134). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales; OC Cellulomonadaceae; Cellulomonas. OX NCBI_TaxID=446466 {ECO:0000313|EMBL:ADG75488.1, ECO:0000313|Proteomes:UP000000849}; RN [1] {ECO:0000313|EMBL:ADG75488.1, ECO:0000313|Proteomes:UP000000849} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 482 / DSM 20109 / BCRC 11376 / JCM 18109 / NBRC 3775 / RC NCIMB 8073 / NRS 134 {ECO:0000313|Proteomes:UP000000849}; RX PubMed=21304688; DOI=10.4056/sigs.1012662; RA Abt B., Foster B., Lapidus A., Clum A., Sun H., Pukall R., Lucas S., RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Pitluck S., Liolios K., RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Goodwin L., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Cellulomonas flavigena type strain (134)."; RL Stand. Genomic Sci. 3:15-25(2010). CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May CC also act on other amino acids. {ECO:0000256|HAMAP-Rule:MF_01201}. 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:0000256|ARBA:ARBA00000316, ECO:0000256|HAMAP- CC Rule:MF_01201}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933, ECO:0000256|HAMAP- CC Rule:MF_01201, ECO:0000256|PIRSR:PIRSR600821-50}; CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine CC from L-alanine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01201}. CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000256|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; CP001964; ADG75488.1; -; Genomic_DNA. DR AlphaFoldDB; D5UIS2; -. DR STRING; 446466.Cfla_2600; -. DR KEGG; cfl:Cfla_2600; -. DR eggNOG; COG0787; Bacteria. DR HOGENOM; CLU_028393_0_0_11; -. DR UniPathway; UPA00042; UER00497. DR Proteomes; UP000000849; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule. DR GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:TreeGrafter. DR CDD; cd00430; PLPDE_III_AR; 1. DR FunFam; 2.40.37.10:FF:000015; 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. PE 3: Inferred from homology; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP- KW Rule:MF_01201}; Reference proteome {ECO:0000313|Proteomes:UP000000849}. FT DOMAIN 261..394 FT /note="Alanine racemase C-terminal" FT /evidence="ECO:0000259|SMART:SM01005" FT ACT_SITE 49 FT /note="Proton acceptor; specific for D-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT ACT_SITE 282 FT /note="Proton acceptor; specific for L-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT BINDING 148 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT BINDING 335 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT MOD_RES 49 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-50" SQ SEQUENCE 410 AA; 41951 MW; ACD23BCB97DA0DDA CRC64; MPTHDPRGER LAGVNDFPAR AVVDLGAVRG NVRALAAHAP TAQVMAVVKA DAYGHGLVPS ALAALEGGAT WLGTAQVPEA LHLRRAGVTG ARILTWLYAP GAPLREAVEA DVDLSVASRW ALDDVVAAAR EAGRTARVHL KVDTGLGRNG LVPAQLPEVL TAALAAEAEG VVRVVGVWSH LAFADAPDHA VVAQQAGVFA EAVAAVEAAG ARLEVRHLAN SAATLTSPAL HWDLVRPGIA VYGLSPVPQL GGPERFGLVP AMTFEAQLAT VKPVPAGSGV SYGHEYVVPH DTVLGVVPVG YADGVPRHAS GSAERWGGPV QVGGRRLGVA GRVCMDQVVL DLGPGATESA GDRVVLWGDG RDGGPTAQDW ADVAGTISYE LVTRLGARVP RTYVDSARVA APAPSEGGGA //