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MURI_LISMO
ID   MURI_LISMO              Reviewed;         266 AA.
AC   Q8Y7N7;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 119.
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}; Synonyms=racE;
GN   OrderedLocusNames=lmo1237;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH SUCCINATE.
RA   Majorek K.A., Chruszcz M., Skarina T., Onopriyenko O., Stam J.,
RA   Anderson W.F., Savchenko A., Bujnicki J.M., Minor W.;
RT   "Crystal structure of glutamate racemase from Listeria monocytogenes in
RT   complex with succinic acid.";
RL   Submitted (AUG-2009) to the PDB data bank.
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; AL591978; CAC99315.1; -; Genomic_DNA.
DR   PIR; AE1229; AE1229.
DR   RefSeq; NP_464762.1; NC_003210.1.
DR   RefSeq; WP_003723856.1; NZ_CP023861.1.
DR   PDB; 3HFR; X-ray; 2.30 A; A/B=1-266.
DR   PDB; 3IST; X-ray; 1.65 A; A/B=1-266.
DR   PDB; 3ISV; X-ray; 1.85 A; A/B=1-266.
DR   PDBsum; 3HFR; -.
DR   PDBsum; 3IST; -.
DR   PDBsum; 3ISV; -.
DR   AlphaFoldDB; Q8Y7N7; -.
DR   SMR; Q8Y7N7; -.
DR   STRING; 169963.lmo1237; -.
DR   DrugBank; DB02343; 3,6,9,12,15-Pentaoxaheptadecane.
DR   PaxDb; Q8Y7N7; -.
DR   EnsemblBacteria; CAC99315; CAC99315; CAC99315.
DR   GeneID; 986027; -.
DR   KEGG; lmo:lmo1237; -.
DR   PATRIC; fig|169963.11.peg.1269; -.
DR   eggNOG; COG0796; Bacteria.
DR   HOGENOM; CLU_052344_0_2_9; -.
DR   OMA; MPWGPRT; -.
DR   PhylomeDB; Q8Y7N7; -.
DR   BioCyc; LMON169963:LMO1237-MON; -.
DR   UniPathway; UPA00219; -.
DR   EvolutionaryTrace; Q8Y7N7; -.
DR   Proteomes; UP000000817; 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   1: Evidence at protein level;
KW   3D-structure; Cell shape; Cell wall biogenesis/degradation; Isomerase;
KW   Peptidoglycan synthesis; Reference proteome.
FT   CHAIN           1..266
FT                   /note="Glutamate racemase"
FT                   /id="PRO_0000095487"
FT   ACT_SITE        72
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-
FT                   Rule:MF_00258"
FT   ACT_SITE        183
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-
FT                   Rule:MF_00258"
FT   BINDING         9..10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P22634, ECO:0000255|HAMAP-
FT                   Rule:MF_00258"
FT   BINDING         41..42
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P22634, ECO:0000255|HAMAP-
FT                   Rule:MF_00258, ECO:0007744|PDB:3IST"
FT   BINDING         73..74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P22634, ECO:0000255|HAMAP-
FT                   Rule:MF_00258"
FT   BINDING         184..185
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P22634, ECO:0000255|HAMAP-
FT                   Rule:MF_00258"
FT   STRAND          5..12
FT                   /evidence="ECO:0007829|PDB:3IST"
FT   HELIX           15..24
FT                   /evidence="ECO:0007829|PDB:3IST"
FT   STRAND          30..34
FT                   /evidence="ECO:0007829|PDB:3IST"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:3IST"
FT   HELIX           46..62
FT                   /evidence="ECO:0007829|PDB:3IST"
FT   STRAND          66..70
FT                   /evidence="ECO:0007829|PDB:3IST"
FT   HELIX           73..86
FT                   /evidence="ECO:0007829|PDB:3IST"
FT   STRAND          91..94
FT                   /evidence="ECO:0007829|PDB:3IST"
FT   HELIX           95..105
FT                   /evidence="ECO:0007829|PDB:3IST"
FT   STRAND          107..115
FT                   /evidence="ECO:0007829|PDB:3IST"
FT   HELIX           117..122
FT                   /evidence="ECO:0007829|PDB:3IST"
FT   HELIX           124..132
FT                   /evidence="ECO:0007829|PDB:3IST"
FT   STRAND          137..142
FT                   /evidence="ECO:0007829|PDB:3IST"
FT   HELIX           145..151
FT                   /evidence="ECO:0007829|PDB:3IST"
FT   HELIX           158..168
FT                   /evidence="ECO:0007829|PDB:3IST"
FT   HELIX           169..173
FT                   /evidence="ECO:0007829|PDB:3IST"
FT   STRAND          178..181
FT                   /evidence="ECO:0007829|PDB:3IST"
FT   HELIX           186..189
FT                   /evidence="ECO:0007829|PDB:3IST"
FT   HELIX           190..197
FT                   /evidence="ECO:0007829|PDB:3IST"
FT   STRAND          201..204
FT                   /evidence="ECO:0007829|PDB:3IST"
FT   HELIX           207..220
FT                   /evidence="ECO:0007829|PDB:3IST"
FT   STRAND          234..239
FT                   /evidence="ECO:0007829|PDB:3IST"
FT   HELIX           241..252
FT                   /evidence="ECO:0007829|PDB:3IST"
FT   STRAND          259..261
FT                   /evidence="ECO:0007829|PDB:3IST"
SQ   SEQUENCE   266 AA;  29160 MW;  912A19482409991B CRC64;
     MKQAIGFIDS GVGGLTVVRE VLKQLPHEQV YYLGDTARCP YGPRDKEEVA KFTWEMTNFL
     VDRGIKMLVI ACNTATAAAL YDIREKLDIP VIGVIQPGSR AALKATRNNK IGVLGTLGTV
     ESMAYPTALK GLNRRVEVDS LACPKFVSVV ESGEYKSAIA KKVVAESLLP LKSTKIDTVI
     LGCTHYPLLK PIIENFMGDG VAVINSGEET ASEVSALLDY HNLLDATDEE IEHRFFTTGS
     TQIFKDIAKD WLNMPDMTVE HIKLGK
 
 
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