MURI1_BACSU
ID MURI1_BACSU Reviewed; 272 AA.
AC P94556; O82826;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Glutamate racemase 1 {ECO:0000255|HAMAP-Rule:MF_00258};
DE EC=5.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00258};
GN Name=racE; Synonyms=glr, murI; OrderedLocusNames=BSU28390;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9063446; DOI=10.1111/j.1432-1033.1997.00059.x;
RA Goethel S.F., Schmid R., Wipat A., Carter N.M., Emmerson P.T.,
RA Harwood C.R., Marahiel M.A.;
RT "An internal FK506-binding domain is the catalytic core of the prolyl
RT isomerase activity associated with the Bacillus subtilis trigger factor.";
RL Eur. J. Biochem. 244:59-65(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA Emmerson P.T., Harwood C.R.;
RT "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT chromosome containing genes responsible for stress responses, the
RT utilization of plant cell walls and primary metabolism.";
RL Microbiology 142:3067-3078(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP SEQUENCE REVISION TO 160.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-272.
RC STRAIN=NBRC 3336;
RX PubMed=9604005; DOI=10.1093/oxfordjournals.jbchem.a022055;
RA Ashiuchi M., Tani K., Soda K., Misono H.;
RT "Properties of glutamate racemase from Bacillus subtilis IFO 3336 producing
RT poly-gamma-glutamate.";
RL J. Biochem. 123:1156-1163(1998).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
RX PubMed=16271894; DOI=10.1016/j.str.2005.07.024;
RA Ruzheinikov S.N., Taal M.A., Sedelnikova S.E., Baker P.J., Rice D.W.;
RT "Substrate-induced conformational changes in Bacillus subtilis glutamate
RT racemase and their implications for drug discovery.";
RL Structure 13:1707-1713(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA28871.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z75208; CAA99552.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14799.2; -; Genomic_DNA.
DR EMBL; AB003685; BAA28871.1; ALT_INIT; Genomic_DNA.
DR PIR; B69688; B69688.
DR RefSeq; NP_390717.2; NC_000964.3.
DR RefSeq; WP_010886589.1; NZ_JNCM01000036.1.
DR PDB; 1ZUW; X-ray; 1.75 A; A/B/C=1-272.
DR PDBsum; 1ZUW; -.
DR AlphaFoldDB; P94556; -.
DR SMR; P94556; -.
DR STRING; 224308.BSU28390; -.
DR jPOST; P94556; -.
DR PaxDb; P94556; -.
DR PRIDE; P94556; -.
DR EnsemblBacteria; CAB14799; CAB14799; BSU_28390.
DR GeneID; 935934; -.
DR KEGG; bsu:BSU28390; -.
DR PATRIC; fig|224308.43.peg.2969; -.
DR eggNOG; COG0796; Bacteria.
DR InParanoid; P94556; -.
DR OMA; MPWGPRT; -.
DR PhylomeDB; P94556; -.
DR BioCyc; BSUB:BSU28390-MON; -.
DR BRENDA; 5.1.1.1; 658.
DR BRENDA; 5.1.1.3; 658.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; P94556; -.
DR Proteomes; UP000001570; 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..272
FT /note="Glutamate racemase 1"
FT /id="PRO_0000095453"
FT ACT_SITE 74
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT ACT_SITE 185
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT BINDING 10..11
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000269|PubMed:16271894, ECO:0007744|PDB:1ZUW"
FT BINDING 42..43
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000269|PubMed:16271894, ECO:0007744|PDB:1ZUW"
FT BINDING 75..76
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000269|PubMed:16271894, ECO:0007744|PDB:1ZUW"
FT BINDING 186..187
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000269|PubMed:16271894, ECO:0007744|PDB:1ZUW"
FT CONFLICT 160
FT /note="K -> Q (in Ref. 2; CAA99552)"
FT /evidence="ECO:0000305"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:1ZUW"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:1ZUW"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:1ZUW"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1ZUW"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1ZUW"
FT HELIX 47..64
FT /evidence="ECO:0007829|PDB:1ZUW"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:1ZUW"
FT HELIX 75..88
FT /evidence="ECO:0007829|PDB:1ZUW"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:1ZUW"
FT HELIX 97..107
FT /evidence="ECO:0007829|PDB:1ZUW"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:1ZUW"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:1ZUW"
FT HELIX 126..134
FT /evidence="ECO:0007829|PDB:1ZUW"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:1ZUW"
FT HELIX 148..152
FT /evidence="ECO:0007829|PDB:1ZUW"
FT HELIX 159..175
FT /evidence="ECO:0007829|PDB:1ZUW"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:1ZUW"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:1ZUW"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:1ZUW"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:1ZUW"
FT HELIX 208..223
FT /evidence="ECO:0007829|PDB:1ZUW"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:1ZUW"
FT HELIX 243..253
FT /evidence="ECO:0007829|PDB:1ZUW"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:1ZUW"
SQ SEQUENCE 272 AA; 29998 MW; 97489B93A48471FA CRC64;
MLEQPIGVID SGVGGLTVAK EIMRQLPKEN IIYVGDTKRC PYGPRPEEEV LQYTWELTNY
LLENHHIKML VIACNTATAI ALDDIQRSVG IPVVGVIQPG ARAAIKVTDN QHIGVIGTEN
TIKSNAYEEA LLALNPDLKV ENLACPLLVP FVESGKFLDK TADEIVKTSL YPLKDTSIDS
LILGCTHYPI LKEAIQRYMG EHVNIISSGD ETAREVSTIL SYKGLLNQSP IAPDHQFLTT
GARDQFAKIA DDWFGHEVGH VECISLQEPI KR
