(data stored in SCRATCH zone)

SWISSPROT: B8IB07_METNO

ID   B8IB07_METNO            Unreviewed;       312 AA.
AC   B8IB07;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 63.
DE   RecName: Full=Glutamate racemase {ECO:0000256|HAMAP-Rule:MF_00258, ECO:0000256|SAAS:SAAS00629040};
DE            EC=5.1.1.3 {ECO:0000256|HAMAP-Rule:MF_00258, ECO:0000256|SAAS:SAAS00639986};
GN   Name=murI {ECO:0000256|HAMAP-Rule:MF_00258};
GN   OrderedLocusNames=Mnod_0357 {ECO:0000313|EMBL:ACL55400.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL55400.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55400.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Provides the (R)-glutamate required for cell wall
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00258,
CC       ECO:0000256|SAAS:SAAS00639995}.
CC   -!- CATALYTIC ACTIVITY: L-glutamate = D-glutamate. {ECO:0000256|HAMAP-
CC       Rule:MF_00258, ECO:0000256|SAAS:SAAS00639998}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00258, ECO:0000256|SAAS:SAAS00639993}.
CC   -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC       {ECO:0000256|HAMAP-Rule:MF_00258, ECO:0000256|SAAS:SAAS00651964}.
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DR   EMBL; CP001349; ACL55400.1; -; Genomic_DNA.
DR   ProteinModelPortal; B8IB07; -.
DR   STRING; 460265.Mnod_0357; -.
DR   EnsemblBacteria; ACL55400; ACL55400; Mnod_0357.
DR   KEGG; mno:Mnod_0357; -.
DR   eggNOG; ENOG4105F03; Bacteria.
DR   eggNOG; COG0796; LUCA.
DR   HOGENOM; HOG000262397; -.
DR   KO; K01776; -.
DR   OMA; LDFFKPH; -.
DR   OrthoDB; POG091H00P1; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000008207; Chromosome.
DR   GO; GO:0008881; F:glutamate racemase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP.
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:SF9; PTHR21198:SF9; 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; B8IB07.
DR   SWISS-2DPAGE; B8IB07.
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00258,
KW   ECO:0000256|SAAS:SAAS00639990};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00258,
KW   ECO:0000256|SAAS:SAAS00639985};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008207};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00258,
KW   ECO:0000256|SAAS:SAAS00651926, ECO:0000313|EMBL:ACL55400.1};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00258,
KW   ECO:0000256|SAAS:SAAS00639999};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008207}.
FT   REGION       48     49       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00258}.
FT   REGION       80     81       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00258}.
FT   REGION      113    114       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00258}.
FT   REGION      227    228       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00258}.
FT   ACT_SITE    112    112       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00258}.
FT   ACT_SITE    226    226       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00258}.
SQ   SEQUENCE   312 AA;  32871 MW;  2685BA5B5BA67539 CRC64;
     MRFEGMPVQQ HGRARPNELM RMRFDLLAGA GAAPLAPAMR APAVLVFDSG LGGLTVLAEV
     RRARPDARVV YAADDAAFPY GDLSEPALVA RVVAVMERLI ALHAPDLVVV ACNTATTLVL
     PALRARFAIP FVGTVPAIKP AAAATRSGLI SVLATPGTVR RDYTRELIDA YAGAYAVTLV
     GATRLAAFAE AELAGTPVGD DLLREEIAPC FVGAGESRTD VVVLGCTHYP LLLRRFERLV
     PWPVTWIDPA PAIARRMAQL LGPAPHPAPP EDAAPVAAVF TGGERITPSL RDALAARGMG
     SIAVEAMPLA RQ
//

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