ID ALR1_AGRFC Reviewed; 391 AA. AC P58736; DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 05-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 127. DE RecName: Full=Alanine racemase, biosynthetic; DE EC=5.1.1.1; GN Name=alr; OrderedLocusNames=Atu1080; ORFNames=AGR_C_1996; OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens OS (strain C58)). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=176299; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C58 / ATCC 33970; RX PubMed=11743193; DOI=10.1126/science.1066804; RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K., RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y., RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P., RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R., RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G., RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y., RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S., RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F., RA Gordon M.P., Olson M.V., Nester E.W.; RT "The genome of the natural genetic engineer Agrobacterium tumefaciens RT C58."; RL Science 294:2317-2323(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C58 / ATCC 33970; RX PubMed=11743194; DOI=10.1126/science.1066803; RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B., RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K., RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M., RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C., RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.; RT "Genome sequence of the plant pathogen and biotechnology agent RT Agrobacterium tumefaciens C58."; RL Science 294:2323-2328(2001). CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. CC Provides the D-alanine required for cell wall biosynthesis (By CC similarity). {ECO:0000250}. 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 -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine CC from L-alanine: step 1/1. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000305}. 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; AE007869; AAK86889.1; -; Genomic_DNA. DR PIR; AG2709; AG2709. DR PIR; H97491; H97491. DR RefSeq; NP_354104.1; NC_003062.2. DR RefSeq; WP_010971382.1; NC_003062.2. DR AlphaFoldDB; P58736; -. DR SMR; P58736; -. DR STRING; 176299.Atu1080; -. DR EnsemblBacteria; AAK86889; AAK86889; Atu1080. DR KEGG; atu:Atu1080; -. DR PATRIC; fig|176299.10.peg.1095; -. DR eggNOG; COG0787; Bacteria. DR HOGENOM; CLU_028393_1_1_5; -. DR OrthoDB; 9813814at2; -. DR PhylomeDB; P58736; -. DR BioCyc; AGRO:ATU1080-MONOMER; -. DR UniPathway; UPA00042; UER00497. DR UniPathway; UPA00219; -. DR Proteomes; UP000000813; Chromosome circular. 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:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. 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 Cell shape; Cell wall biogenesis/degradation; Isomerase; KW Peptidoglycan synthesis; Pyridoxal phosphate; Reference proteome. FT CHAIN 1..391 FT /note="Alanine racemase, biosynthetic" FT /id="PRO_0000114492" FT ACT_SITE 52 FT /note="Proton acceptor; specific for D-alanine" FT /evidence="ECO:0000250" FT ACT_SITE 271 FT /note="Proton acceptor; specific for L-alanine" FT /evidence="ECO:0000250" FT BINDING 149 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 330 FT /ligand="substrate" FT /evidence="ECO:0000250" FT MOD_RES 52 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000250" SQ SEQUENCE 391 AA; 42091 MW; 82F6B0320F92B770 CRC64; MTDDFEDSFP DNETDAFEQA PLRLTVDLGA LADNWRDMKK RSGRARTAAV VKADAYGLGI EDCGATLYHA GARDFFVATV AEGATLRSYA PEARIFVLSG IWQGQERQVF DNDLVPVLAS EEQLSFWMAT VAERGDHPCA LHVDTGFNRL GLPLDDALFL ADDVTRPASF DPVLVLSHLA CADTPSSPMN RAQLESFRRV SAAFEGIESS LSASAGIFLG PDYHFDLTRP GIALYGGEAV NDVANPMRPV AKAEARIIQI REAGEGQTVS YGSSFLLKRA SRLAIASVGY ADGYQRSLSG SGIPLREMGH GGAYGVVNGH KVPVAGRVTM DLTIFDVTDV PANAIRAGDY IELFGPNVPV DETARAAGTI GYEMLTGLGL RYERQYLVAD D //