ID D6ZIQ8_MOBCV Unreviewed; 442 AA. AC D6ZIQ8; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAR-2024, entry version 79. DE RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201}; DE EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201}; GN Name=alr {ECO:0000313|EMBL:ADI66607.1}; GN OrderedLocusNames=HMPREF0573_10288 {ECO:0000313|EMBL:ADI66607.1}; OS Mobiluncus curtisii (strain ATCC 43063 / DSM 2711 / V125) (Falcivibrio OS vaginalis). OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae; OC Mobiluncus. OX NCBI_TaxID=548479 {ECO:0000313|EMBL:ADI66607.1, ECO:0000313|Proteomes:UP000006742}; RN [1] {ECO:0000313|Proteomes:UP000006742} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43063 / DSM 2711 / V125 RC {ECO:0000313|Proteomes:UP000006742}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V., RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G., RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A., RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R., Gibbs R.; RT "Complete sequence of Mobiluncus curtisii ATCC 43063."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. 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|HAMAP-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; CP001992; ADI66607.1; -; Genomic_DNA. DR RefSeq; WP_013188702.1; NC_014246.1. DR AlphaFoldDB; D6ZIQ8; -. DR STRING; 548479.HMPREF0573_10288; -. DR GeneID; 55564448; -. DR KEGG; mcu:HMPREF0573_10288; -. DR eggNOG; COG0787; Bacteria. DR HOGENOM; CLU_028393_2_2_11; -. DR UniPathway; UPA00042; UER00497. DR Proteomes; UP000006742; Chromosome. 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-UniPathway. DR CDD; cd00430; PLPDE_III_AR; 1. DR Gene3D; 3.20.20.10; Alanine racemase; 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:UP000006742}. FT DOMAIN 289..436 FT /note="Alanine racemase C-terminal" FT /evidence="ECO:0000259|SMART:SM01005" FT ACT_SITE 41 FT /note="Proton acceptor; specific for D-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT ACT_SITE 310 FT /note="Proton acceptor; specific for L-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT BINDING 173 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT BINDING 358 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT MOD_RES 41 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-50" SQ SEQUENCE 442 AA; 48376 MW; BFE7807CEF3DC5AC CRC64; MTNVDVSQWP VRAVVNLSAY QENLAQMRRF APHSQQMAIV KANAYGHGIE RMALAALGAG TEWLGVAKAS EAFRLRKYLD KHGVPRDHLV DTPTSAMMRS RLYQTAAMGL PSATRPRILT WLYVPHTDLL PVVKSEIDIS VSTLDQLDQV SRACDAAGKR ARLHLKVDTG LCRAGATDED FPVLCKLARA RERAGLVEVS AVWSHLARAD EDTAAAEAFT KSQLKAFDEA WEVAQEAGLR PQLRHIAATA GIIWYPESHY DLVRVGISGY GLSPNPEIAS SWQLGVRPVM RLETNVVQVK RVEKGAAVSY GGEWVAPGPR WLGLLPVGYA DGLHRLAKNR GETWIKGRRA PIVGRIPMDQ IVVDLGPAVD DTGTSVPCPV EPGELAIIFG DPKDRLLGGI PGVPALPTAD DWAEWTDTIN YEVITSISPN VPRVYVKDEP ER //