ID MURI_HELP2 Reviewed; 255 AA.
AC B6JLD2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 02-NOV-2016, entry version 53.
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};
GN OrderedLocusNames=HPP12_0556;
OS Helicobacter pylori (strain P12).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=570508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P12;
RA Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.;
RT "The complete genome sequence of Helicobacter pylori strain P12.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Provides the (R)-glutamate required for cell wall
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00258}.
CC -!- CATALYTIC ACTIVITY: L-glutamate = D-glutamate. {ECO:0000255|HAMAP-
CC 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}.
DR EMBL; CP001217; ACJ07710.1; -; Genomic_DNA.
DR RefSeq; WP_000690335.1; NC_011498.1.
DR EnsemblBacteria; ACJ07710; ACJ07710; HPP12_0556.
DR KEGG; hpp:HPP12_0556; -.
DR PATRIC; 20609084; VBIHelPyl2824_0582.
DR HOGENOM; HOG000262396; -.
DR KO; K01776; -.
DR OMA; ELLETCM; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008198; 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 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 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; Complete proteome;
KW Isomerase; Peptidoglycan synthesis.
FT CHAIN 1 255 Glutamate racemase.
FT /FTId=PRO_1000114046.
FT REGION 7 8 Substrate binding. {ECO:0000255|HAMAP-
FT Rule:MF_00258}.
FT REGION 39 40 Substrate binding. {ECO:0000255|HAMAP-
FT Rule:MF_00258}.
FT REGION 71 72 Substrate binding. {ECO:0000255|HAMAP-
FT Rule:MF_00258}.
FT REGION 182 183 Substrate binding. {ECO:0000255|HAMAP-
FT Rule:MF_00258}.
FT ACT_SITE 70 70 Proton donor/acceptor.
FT {ECO:0000255|HAMAP-Rule:MF_00258}.
FT ACT_SITE 181 181 Proton donor/acceptor.
FT {ECO:0000255|HAMAP-Rule:MF_00258}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 3 215 ipfam:Asp_Glu_race [T]
FT MYHIT 1 255 ihamap:Glu_racemase [T]
FT MYHIT 177 187 ipat:ASP_GLU_RACEMASE_2 [T]
FT MYHIT 67 75 ipat:ASP_GLU_RACEMASE_1 [T]
SQ SEQUENCE 255 AA; 28353 MW; 741338442767E987 CRC64;
MKIGVFDSGV GGFSVLKSLL KAQLFDEIIY YGDSARVPYG TKDPTTIKQF GLEALDFFKP
HQIKLLIVAC NTASALALEE MQKHSKIPIV GVIEPSILAI KQQVKDKNAP ILVLGTKATI
QSNAYDNALK QQGYLNVSHL ATSLFVPLIE ENILEGELLE TCMRYYFTPL KILPEVIILG
CTHFPLIAQK IEGYFMGHFA LPTPPLLIHS GDAIVGYLQQ KYALKKNAHA FPKVEFHASG
DVVWLEKQAK EWLKL
//
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