(data stored in ACNUC7421 zone)

SWISSPROT: MURI_RHILO

ID   MURI_RHILO              Reviewed;         262 AA.
AC   Q98NP9;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2002, sequence version 2.
DT   11-DEC-2019, entry version 99.
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=mlr0039;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB47712.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; BA000012; BAB47712.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_044547414.1; NC_002678.2.
DR   SMR; Q98NP9; -.
DR   STRING; 266835.14021099; -.
DR   EnsemblBacteria; BAB47712; BAB47712; BAB47712.
DR   KEGG; mlo:mlr0039; -.
DR   PATRIC; fig|266835.9.peg.32; -.
DR   eggNOG; ENOG4105F03; Bacteria.
DR   eggNOG; COG0796; LUCA.
DR   HOGENOM; HOG000262397; -.
DR   KO; K01776; -.
DR   OrthoDB; 1718671at2; -.
DR   BioCyc; MLOT266835:G1G20-31-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000552; 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;
DR   PRODOM; Q98NP9.
DR   SWISS-2DPAGE; Q98NP9.
KW   Cell shape; Cell wall biogenesis/degradation; Isomerase;
KW   Peptidoglycan synthesis.
FT   CHAIN           1..262
FT                   /note="Glutamate racemase"
FT                   /id="PRO_0000095501"
FT   REGION          10..11
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   REGION          42..43
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   REGION          75..76
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   REGION          190..191
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   ACT_SITE        74
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"
SQ   SEQUENCE   262 AA;  28885 MW;  F18C51BD53BCF8DD CRC64;
     MTDQPILMFD SGVGGLTVLR EARVLMPDRR FVYVADDAAF PFGAWEEPAL RTHILDLFVK
     LLDRFAPAIS VIACNTASTL VIDALRERFP GHPFVGTVPA VKPAAERTRS GLVSVLATPG
     TVKRQYTRDL ISKWAQKCHV RLVGSDRLAG LAEVYMREGF VDEEAVRAEI APCFMEHEGL
     RTDIVVLACT HYPFLVNRMR KTAPWPVDWI DPAEAIARRA LSLLPPVDGA LPQGEPDIAV
     FTSGKTDFAI GRLMQGFGLS VR
//

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