GenomeNet

Database: UniProt
Entry: F5XQ65_MICPN
LinkDB: F5XQ65_MICPN
Original site: F5XQ65_MICPN 
ID   F5XQ65_MICPN            Unreviewed;       279 AA.
AC   F5XQ65;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Glutamate racemase {ECO:0000256|ARBA:ARBA00013090, ECO:0000256|HAMAP-Rule:MF_00258};
DE            EC=5.1.1.3 {ECO:0000256|ARBA:ARBA00013090, ECO:0000256|HAMAP-Rule:MF_00258};
GN   Name=murI {ECO:0000256|HAMAP-Rule:MF_00258,
GN   ECO:0000313|EMBL:BAK36896.1};
GN   OrderedLocusNames=MLP_38820 {ECO:0000313|EMBL:BAK36896.1};
OS   Microlunatus phosphovorus (strain ATCC 700054 / DSM 10555 / JCM 9379 / NBRC
OS   101784 / NCIMB 13414 / VKM Ac-1990 / NM-1).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Microlunatus.
OX   NCBI_TaxID=1032480 {ECO:0000313|EMBL:BAK36896.1, ECO:0000313|Proteomes:UP000007947};
RN   [1] {ECO:0000313|EMBL:BAK36896.1, ECO:0000313|Proteomes:UP000007947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700054 / DSM 10555 / JCM 9379 / NBRC 101784 / NCIMB 13414
RC   / VKM Ac-1990 / NM-1 {ECO:0000313|Proteomes:UP000007947};
RA   Hosoyama A., Sasaki K., Harada T., Igarashi R., Kawakoshi A., Sasagawa M.,
RA   Fukada J., Nakamura S., Katano Y., Hanada S., Kamagata Y., Nakamura N.,
RA   Yamazaki S., Fujita N.;
RT   "Whole genome sequence of Microlunatus phosphovorus NM-1.";
RL   Submitted (MAY-2011) 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   -!- 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:0000256|ARBA:ARBA00001602, ECO:0000256|HAMAP-
CC         Rule:MF_00258};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00258}.
CC   -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC       {ECO:0000256|HAMAP-Rule:MF_00258}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP012204; BAK36896.1; -; Genomic_DNA.
DR   AlphaFoldDB; F5XQ65; -.
DR   STRING; 1032480.MLP_38820; -.
DR   KEGG; mph:MLP_38820; -.
DR   eggNOG; COG0796; Bacteria.
DR   HOGENOM; CLU_052344_0_1_11; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000007947; 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   Gene3D; 3.40.50.1860; -; 2.
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   NCBIfam; TIGR00067; glut_race; 1.
DR   PANTHER; PTHR21198; GLUTAMATE RACEMASE; 1.
DR   PANTHER; PTHR21198:SF2; GLUTAMATE RACEMASE; 1.
DR   Pfam; PF01177; Asp_Glu_race; 1.
DR   SUPFAM; SSF53681; Aspartate/glutamate racemase; 2.
DR   PROSITE; PS00923; ASP_GLU_RACEMASE_1; 1.
DR   PROSITE; PS00924; ASP_GLU_RACEMASE_2; 1.
PE   3: Inferred from homology;
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00258};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00258};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00258};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00258};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007947}.
FT   ACT_SITE        83
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   ACT_SITE        193
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         20..21
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         52..53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         84..85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         194..195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
SQ   SEQUENCE   279 AA;  29949 MW;  4626722FDF9CF7F0 CRC64;
     MSRFSDQRSP LAEAPIGIFD SGFGGLTVAR AVIDQLPYED VVYLGDTART PYGDQPIADV
     REFALECLDH LVDQGVKMLV IACNSASAAV LRDARERYAV PVVEVIMPAV RRAVAATRSG
     NVGVICTTAT ATSQAYDDAF TAAPQVELRT VACPRFVGFV EAGITSGDEL RACAEDYLAS
     LRAERIDTLI LGCTHYPLLT GVISYVLGDG VTLVSSADEC AKDVYATLTR LGLIHDRPRT
     ARHRFWTTGH PGDFAGIGRR LMGGGMIDEV EQLAAVPRI
//
DBGET integrated database retrieval system