GenomeNet

Database: UniProt
Entry: A0A2U2ADW4_9GAMM
LinkDB: A0A2U2ADW4_9GAMM
Original site: A0A2U2ADW4_9GAMM 
ID   A0A2U2ADW4_9GAMM        Unreviewed;       284 AA.
AC   A0A2U2ADW4;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
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:PWD80841.1};
GN   ORFNames=DC083_06965 {ECO:0000313|EMBL:PWD80841.1};
OS   Ignatzschineria ureiclastica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC   Ignatzschineriaceae; Ignatzschineria.
OX   NCBI_TaxID=472582 {ECO:0000313|EMBL:PWD80841.1, ECO:0000313|Proteomes:UP000245020};
RN   [1] {ECO:0000313|Proteomes:UP000245020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 22644 {ECO:0000313|Proteomes:UP000245020};
RA   Tsang C.C., Tang J.Y.M., Fong J.Y.H., Kinne J., Lee H.H., Joseph M.,
RA   Jose S., Schuster R.K., Tang Y., Sivakumar S., Chen J.H.K., Teng J.L.L.,
RA   Lau S.K.P., Wernery U., Woo P.C.Y.;
RT   "Ignatzschineria dubaiensis sp. nov., isolated from necrotic foot tissues
RT   of dromedaries (Camelus dromedarius) and associated maggots in Dubai,
RT   United Arab Emirates.";
RL   Submitted (MAY-2018) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWD80841.1}.
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; QEWQ01000004; PWD80841.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U2ADW4; -.
DR   OrthoDB; 9801055at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000245020; Unassembled WGS sequence.
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:SF3; 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:UP000245020}.
FT   ACT_SITE        80
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   ACT_SITE        192
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         15..16
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         49..50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         81..82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         193..194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
SQ   SEQUENCE   284 AA;  31713 MW;  132DB11B6ED31A5F CRC64;
     MQQNLPCNLK IGLIDSGVGG FSILNSFLHR SLPGNSHYYY IADSGHLPYG LKSDRYIYQR
     MLALTQYLLT LKIDVLVIAC NTATAVSVDL LRTRYPELPI IGVEPAIKPA AEMTKTMHIA
     VAATESTLKS QRLSNLVNRY ASHCTLHPIT GTKWVDLVES GEYLDSSVVD KILAKSLEVV
     WDYPVDQLIL GCTHFPFLTE AIIRHIPERV SLINPARSIV AQCDQRLSEI GKLASLDSNN
     QTEGIEPQVH LTLMTTGNMD NFKQQVSTLV SPHYHQLRLQ RIDC
//
DBGET integrated database retrieval system