ID F4B158_DOKS4 Unreviewed; 365 AA. AC F4B158; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAR-2024, entry version 67. DE RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201}; DE EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201}; GN OrderedLocusNames=Krodi_1313 {ECO:0000313|EMBL:AEE19296.1}; OS Dokdonia sp. (strain 4H-3-7-5) (Krokinobacter sp. (strain 4H-3-7-5)). OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Dokdonia. OX NCBI_TaxID=983548 {ECO:0000313|EMBL:AEE19296.1, ECO:0000313|Proteomes:UP000008290}; RN [1] {ECO:0000313|EMBL:AEE19296.1, ECO:0000313|Proteomes:UP000008290} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4H-3-7-5 {ECO:0000313|EMBL:AEE19296.1, RC ECO:0000313|Proteomes:UP000008290}; RX PubMed=21725025; DOI=10.1128/JB.05518-11; RA Klippel B., Lochner A., Bruce D.C., Walston Davenport K., Detter C., RA Goodwin L.A., Han J., Han S., Hauser L., Land M.L., Nolan M., RA Ovchinnikova G., Pennacchio L., Pitluck S., Tapia R., Woyke T., RA Wiebusch S., Basner A., Abe F., Horikoshi K., Keller M., Antranikian G.; RT "Complete genome sequences of Krokinobacter sp. strain 4H-3-7-5 and RT Lacinutrix sp. strain 5H-3-7-4, polysaccharide-degrading members of the RT family Flavobacteriaceae."; RL J. Bacteriol. 193:4545-4546(2011). RN [2] {ECO:0000313|Proteomes:UP000008290} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4H-3-7-5 {ECO:0000313|Proteomes:UP000008290}; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Piela B., Lochner A., RA Antranikian F.I., Woyke T.; RT "Complete sequence of Krokinobacter diaphorus 4H-3-7-5."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4H-3-7-5; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Piela B., Lochner A., RA Antranikian F.I., Woyke T.; RT "Complete sequence of Krokinobacter sp. 4H-3-7-5."; RL Submitted (FEB-2011) 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; CP002528; AEE19296.1; -; Genomic_DNA. DR RefSeq; WP_013750804.1; NC_015496.1. DR AlphaFoldDB; F4B158; -. DR STRING; 983548.Krodi_1313; -. DR KEGG; kdi:Krodi_1313; -. DR eggNOG; COG0787; Bacteria. DR HOGENOM; CLU_028393_2_2_10; -. DR OrthoDB; 9801978at2; -. DR UniPathway; UPA00042; UER00497. DR Proteomes; UP000008290; 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; 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. 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}. FT DOMAIN 240..364 FT /note="Alanine racemase C-terminal" FT /evidence="ECO:0000259|SMART:SM01005" FT ACT_SITE 35 FT /note="Proton acceptor; specific for D-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT ACT_SITE 261 FT /note="Proton acceptor; specific for L-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT BINDING 133 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT BINDING 310 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT MOD_RES 35 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-50" SQ SEQUENCE 365 AA; 40302 MW; 69D66941D2EA12D8 CRC64; MAITRLEIDL AALRHNYSYL RKKVAPSVKM MAVVKAFGYG SDAGAVAQEL EMLGVDYFAV AYVSEGIALR DAGITTPILV LHPQPDTFDE LIERCLEPSI YSIRMMELFT AFAKGKGQEN YPIHLKFNTG LNRLGFLNTD VSWILDRLRE NVSVKVASLF SHLVASEDPA EEEFTLNQIL QFTNISKELL QALDYVPFMH MTNTSGVINY HRAHFDCVRI GIGLYGYGNS KEDTKKLKPV ARLKSVISQI HHIKPGQSIG YNRAYKATEE IVTATLPIGH ADGISRSLGN GVGYVMIAGQ KAPIVGNVCM DMLMVDITGI SCKEGDDVEV FGETTSAETL AGEMQSISYE LLTAIGQRVK RVILR //