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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
 
 
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