MURI_HELPY
ID MURI_HELPY Reviewed; 255 AA.
AC P56068; P94841;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Glutamate racemase {ECO:0000255|HAMAP-Rule:MF_00258};
DE EC=5.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00258};
GN Name=murI {ECO:0000255|HAMAP-Rule:MF_00258}; Synonyms=glr;
GN OrderedLocusNames=HP_0549;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 4867 / CCUG 17874 / NCTC 11638;
RX PubMed=8962108; DOI=10.1073/pnas.93.25.14648;
RA Censini S., Lange C., Xiang Z., Crabtree J., Ghiara P., Borodovsky M.,
RA Rappuoli R., Covacci A.;
RT "cag, a pathogenicity island of Helicobacter pylori, encodes type I-
RT specific and disease-associated virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:14648-14653(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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 ---------------------------------------------------------------------------
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; AF282853; AAC44708.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD07615.1; -; Genomic_DNA.
DR PIR; E64588; E64588.
DR RefSeq; NP_207344.1; NC_000915.1.
DR RefSeq; WP_000690349.1; NC_018939.1.
DR AlphaFoldDB; P56068; -.
DR SMR; P56068; -.
DR IntAct; P56068; 1.
DR STRING; 85962.C694_02840; -.
DR BindingDB; P56068; -.
DR ChEMBL; CHEMBL6078; -.
DR DrugCentral; P56068; -.
DR PaxDb; P56068; -.
DR EnsemblBacteria; AAD07615; AAD07615; HP_0549.
DR KEGG; hpy:HP_0549; -.
DR PATRIC; fig|85962.47.peg.594; -.
DR eggNOG; COG0796; Bacteria.
DR OMA; LDFFKPH; -.
DR PhylomeDB; P56068; -.
DR SABIO-RK; P56068; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000429; 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 3: Inferred from homology;
KW Cell shape; Cell wall biogenesis/degradation; Isomerase;
KW Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..255
FT /note="Glutamate racemase"
FT /id="PRO_0000095476"
FT ACT_SITE 70
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT ACT_SITE 181
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 7..8
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 39..40
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 71..72
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 182..183
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT CONFLICT 64
FT /note="K -> E (in Ref. 1; AAC44708)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="V -> I (in Ref. 1; AAC44708)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="E -> K (in Ref. 1; AAC44708)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="V -> I (in Ref. 1; AAC44708)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="E -> G (in Ref. 1; AAC44708)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="N -> K (in Ref. 1; AAC44708)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="C -> H (in Ref. 1; AAC44708)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="V -> I (in Ref. 1; AAC44708)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 255 AA; 28413 MW; 7DC46DE96D9709E8 CRC64;
MKIGVFDSGV GGFSVLKSLL KAQLFDEIIY YGDSARVPYG TKDPTTIKQF GLEALDFFKP
HQIKLLIVAC NTASALALEE MQKHSKIPVV GVIEPSILAI KRQVKDKNAP ILVLGTKATI
QSNAYDNALK QQGYLNVSHL ATSLFVPLIE ESILEGELLE TCMRYYFTPL EILPEVVILG
CTHFPLIAQK IEGYFMEHFA LSTPPLLIHS GDAIVEYLQQ NYALKKNACA FPKVEFHASG
DVVWLEKQAK EWLKL
