ID   G2T5Z4_ROSHA            Unreviewed;       389 AA.
AC   G2T5Z4;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 70.
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=RHOM_15980 {ECO:0000313|EMBL:AEN98302.1};
OS   Roseburia hominis (strain DSM 16839 / JCM 17582 / NCIMB 14029 / A2-183).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX   NCBI_TaxID=585394 {ECO:0000313|EMBL:AEN98302.1, ECO:0000313|Proteomes:UP000008178};
RN   [1] {ECO:0000313|EMBL:AEN98302.1, ECO:0000313|Proteomes:UP000008178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16839 / JCM 17582 / NCIMB 14029 / A2-183
RC   {ECO:0000313|Proteomes:UP000008178};
RX   PubMed=26543119; DOI=10.1128/genomeA.01286-15;
RA   Travis A.J., Kelly D., Flint H.J., Aminov R.I.;
RT   "Complete genome sequence of the human gut symbiont Roseburia hominis.";
RL   Genome Announc. 3:E0128615-E0128615(2015).
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}.
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DR   EMBL; CP003040; AEN98302.1; -; Genomic_DNA.
DR   RefSeq; WP_014081223.1; NC_015977.1.
DR   AlphaFoldDB; G2T5Z4; -.
DR   STRING; 585394.RHOM_15980; -.
DR   GeneID; 77460727; -.
DR   KEGG; rho:RHOM_15980; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_2_2_9; -.
DR   OrthoDB; 9813814at2; -.
DR   BioCyc; RHOM585394:G1H02-3172-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000008178; 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:UP000008178}.
FT   DOMAIN          251..375
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        39
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        272
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         320
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         39
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   389 AA;  42862 MW;  98F8125DF2D51C07 CRC64;
     MESTLRRTWA EIDLDALAHN YHKLRERIGA DVKFLGVVKA DAYGHGSVQV SHLLQELGAD
     YLAVSSIDEA VELRLNDVTM PILILGHTPK EQVSRLIKYH ITQAVSCEAK ALEYSEEAVK
     CGGILKIHIK VDTGMSRLGY LCDGDHFETG VAGICHGCSL PGLDAEGIFT HFAVSDEPGE
     DCKKYTEHQF DLFMRVIEEV EKRLGRKFAL RHCANTGAVA RYPETFLDMV RPGLLLYGYG
     EFADELGLLP VMTLKTTVST IKIYPAGTAI SYGGIFKTEH TTRIGVVPYG YADGFFRCLS
     NRCALMTKEG PAPQRGKICM DMCMIDLTGK MGVDVGSEVE VFGKQNSIND LAALAGTIPY
     ELTCAVSKRV PRIYIRNGKV VEKELLLRG
//