MURI_MICAN
ID MURI_MICAN Reviewed; 283 AA.
AC B0JGW5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=MAE_55590;
OS Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Microcystaceae; Microcystis.
OX NCBI_TaxID=449447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-843 / IAM M-247;
RX PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT Microcystis aeruginosa NIES-843.";
RL DNA Res. 14:247-256(2007).
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; AP009552; BAG05381.1; -; Genomic_DNA.
DR RefSeq; WP_012267850.1; NC_010296.1.
DR AlphaFoldDB; B0JGW5; -.
DR SMR; B0JGW5; -.
DR STRING; 449447.MAE_55590; -.
DR PaxDb; B0JGW5; -.
DR EnsemblBacteria; BAG05381; BAG05381; MAE_55590.
DR KEGG; mar:MAE_55590; -.
DR PATRIC; fig|449447.4.peg.5072; -.
DR eggNOG; COG0796; Bacteria.
DR HOGENOM; CLU_052344_0_2_3; -.
DR OMA; MPWGPRT; -.
DR OrthoDB; 1718671at2; -.
DR BioCyc; MAER449447:MAE_RS24165-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001510; 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..283
FT /note="Glutamate racemase"
FT /id="PRO_1000119189"
FT ACT_SITE 76
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT ACT_SITE 186
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 13..14
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 45..46
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 77..78
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 187..188
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
SQ SEQUENCE 283 AA; 31602 MW; 3706F15772F43769 CRC64;
MRESQLSPIG VFDSGVGGLT VLRELYRQLP QESILYFADT ARLPYGTRSK GEIIEFVLEI
LTWMSERRVK MVIMACNTSS ALALEEVQAE FKDLPILGVI LPGAKTAVQK GKRIGVISTP
ATAKSNAYKQ AIQEIDPTAQ VWQIPCPEFV PLIEANRIFD PYTTQVAREY LQPLLAENID
TLVYGCTHYR HLSPVLRRLL PSSVRLVDPA ASVVRAAEKE LELLGLKNPE TPLPTNFAVS
GDPDTFARLS RQWLGFSPRV EKVYLQCRVK TLGFTDGMKQ RPV