ID   MURI_HAEIN              Reviewed;         269 AA.
AC   P52973; O86245;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   03-AUG-2022, entry version 131.
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=HI_1739.2;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=8805245; DOI=10.1016/s0960-9822(02)00478-5;
RA   Tatusov R.L., Mushegian A.R., Bork P., Brown N.P., Hayes W.S.,
RA   Borodovsky M., Rudd K.E., Koonin E.V.;
RT   "Metabolism and evolution of Haemophilus influenzae deduced from a whole-
RT   genome comparison with Escherichia coli.";
RL   Curr. Biol. 6:279-291(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J.,
RA   Hickey E., Dodson R., Gwinn M.;
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
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; L42023; AAC23386.1; -; Genomic_DNA.
DR   PIR; T09430; T09430.
DR   RefSeq; NP_439883.1; NC_000907.1.
DR   RefSeq; WP_010869285.1; NC_000907.1.
DR   AlphaFoldDB; P52973; -.
DR   SMR; P52973; -.
DR   STRING; 71421.HI_1739.2; -.
DR   EnsemblBacteria; AAC23386; AAC23386; HI_1739.2.
DR   KEGG; hin:HI_1739.2; -.
DR   PATRIC; fig|71421.8.peg.1822; -.
DR   eggNOG; COG0796; Bacteria.
DR   HOGENOM; CLU_052344_2_0_6; -.
DR   OMA; MPWGPRT; -.
DR   PhylomeDB; P52973; -.
DR   BioCyc; HINF71421:G1GJ1-1762-MON; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0047661; F:amino-acid racemase activity; IBA:GO_Central.
DR   GO; GO:0008881; F:glutamate racemase activity; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
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..269
FT                   /note="Glutamate racemase"
FT                   /id="PRO_0000095475"
FT   ACT_SITE        78
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   ACT_SITE        189
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         14..15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         46..47
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         79..80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         190..191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
SQ   SEQUENCE   269 AA;  30535 MW;  F64A6E741154CC0D CRC64;
     MDKKEKRPTV LFFDSGVGGF SVYREAKKLL PNWHYLYCFD NAGFPYSERK EESIIHRTLA
     ACQLINQRYP LDAMVIACNT ASTVVLPPLR AAFDIPIIGT VPAIKPASEI TKTKHIGLLA
     TKGTVKRHYI DELIDKFAQD CIVERLGTTK LVEIAEQKIR GHSVDLISLK DELSSWAGMA
     DLDTLVLGCT HFPLIKDEIQ LCLPQVKYFM EPSAAIAKRI KYLLDDKNLQ AQNEKYNQMF
     CTAHFPEESQ FKKALHLWGF ESLEVIKID