GenomeNet

Database: UniProt
Entry: F8KUZ6_PARAV
LinkDB: F8KUZ6_PARAV
Original site: F8KUZ6_PARAV 
ID   F8KUZ6_PARAV            Unreviewed;       255 AA.
AC   F8KUZ6;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 71.
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:CCB85062.1};
GN   OrderedLocusNames=PUV_01120 {ECO:0000313|EMBL:CCB85062.1};
OS   Parachlamydia acanthamoebae (strain UV7).
OC   Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC   Parachlamydia.
OX   NCBI_TaxID=765952 {ECO:0000313|EMBL:CCB85062.1, ECO:0000313|Proteomes:UP000000495};
RN   [1] {ECO:0000313|EMBL:CCB85062.1, ECO:0000313|Proteomes:UP000000495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UV7 {ECO:0000313|Proteomes:UP000000495};
RX   PubMed=21690563; DOI=10.1093/molbev/msr161;
RA   Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., Brunham R.C.,
RA   Read T.D., Bavoil P.M., Sachse K., Kahane S., Friedman M.G., Rattei T.,
RA   Myers G.S., Horn M.;
RT   "Unity in variety--the pan-genome of the Chlamydiae.";
RL   Mol. Biol. Evol. 28:3253-3270(2011).
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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {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; FR872580; CCB85062.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8KUZ6; -.
DR   STRING; 765952.PUV_01120; -.
DR   KEGG; puv:PUV_01120; -.
DR   eggNOG; COG0796; Bacteria.
DR   HOGENOM; CLU_052344_0_2_0; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000495; 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:UP000000495}.
FT   ACT_SITE        55
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   ACT_SITE        166
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         24..25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         56..57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         167..168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
SQ   SEQUENCE   255 AA;  28436 MW;  5F57529E93B06339 CRC64;
     MRAVMQLLPY ESVLYFGDTA HFPYGNNAAE TIIQYSLANA HFLMEQDIKL LVIACNTASA
     FAFSTLQDQF LIPIIDVISP SIEAAIAQTQ SGSIAVLGTK GTIRSGVYKQ KILDLMPQAR
     VVSLACPLLA PLVEEQWLEH PATRLIVQEY LQPLKKSDVD TLILGCTHYP LLKSLIEEEM
     EGQVKIIDSA SACALKVEEI LGNQQLQSLK EKTPHFRYYV SDDPERFQQA GEQFLRSPIT
     HVQSHQDTQI SVFSV
//
DBGET integrated database retrieval system