ID   MURI_MYCPA              Reviewed;         275 AA.
AC   Q73X85;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Glutamate racemase {ECO:0000255|HAMAP-Rule:MF_00258};
DE            EC=5.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00258};
GN   Name=murI {ECO:0000255|HAMAP-Rule:MF_00258}; OrderedLocusNames=MAP_2424c;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
CC   -!- FUNCTION: Provides the (R)-glutamate required for cell wall
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00258}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate = D-glutamate; Xref=Rhea:RHEA:12813,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:29986; EC=5.1.1.3;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00258};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00258}.
CC   -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC       {ECO:0000255|HAMAP-Rule:MF_00258}.
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DR   EMBL; AE016958; AAS04741.1; -; Genomic_DNA.
DR   RefSeq; WP_003873195.1; NC_002944.2.
DR   AlphaFoldDB; Q73X85; -.
DR   SMR; Q73X85; -.
DR   STRING; 262316.MAP_2424c; -.
DR   EnsemblBacteria; AAS04741; AAS04741; MAP_2424c.
DR   KEGG; mpa:MAP_2424c; -.
DR   PATRIC; fig|262316.17.peg.2575; -.
DR   eggNOG; COG0796; Bacteria.
DR   HOGENOM; CLU_052344_0_1_11; -.
DR   OMA; MPWGPRT; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000580; Chromosome.
DR   GO; GO:0008881; F:glutamate racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_00258; Glu_racemase; 1.
DR   InterPro; IPR015942; Asp/Glu/hydantoin_racemase.
DR   InterPro; IPR001920; Asp/Glu_race.
DR   InterPro; IPR018187; Asp/Glu_racemase_AS_1.
DR   InterPro; IPR033134; Asp/Glu_racemase_AS_2.
DR   InterPro; IPR004391; Glu_race.
DR   PANTHER; PTHR21198:SF2; PTHR21198:SF2; 1.
DR   Pfam; PF01177; Asp_Glu_race; 1.
DR   SUPFAM; SSF53681; SSF53681; 2.
DR   TIGRFAMs; TIGR00067; glut_race; 1.
DR   PROSITE; PS00923; ASP_GLU_RACEMASE_1; 1.
DR   PROSITE; PS00924; ASP_GLU_RACEMASE_2; 1.
PE   3: Inferred from homology;
KW   Cell shape; Cell wall biogenesis/degradation; Isomerase;
KW   Peptidoglycan synthesis; Reference proteome.
FT   CHAIN           1..275
FT                   /note="Glutamate racemase"
FT                   /id="PRO_1000047585"
FT   ACT_SITE        75
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   ACT_SITE        185
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         12..13
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         44..45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         76..77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         186..187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
SQ   SEQUENCE   275 AA;  29114 MW;  00D3F79DFA0340AA CRC64;
     MSSALAPVGI FDSGVGGLTV ARAIIDQLPD EHIIYVGDTG HGPYGPLSIP EVRAHALAIG
     DDLVGRGVKA LVIACNTASA ACLRDARERY EVPVVEVILP AVRRAVATTR NGRIGVIGTQ
     ATINSHAYQD AFAAARDTEI TAVACPRFVD FVERGVTSGR QVLGLAEGYL EPLQRAQVDT
     LVLGCTHYPL LSGLIQLAMG DNVTLVSSAE ETAKEVLRVL AERDLLHPHP DDPRAAGPSR
     VFEATGDPEA FTRLAARFLG PAVSGVRPVH HVRID