MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Glutamate racemase {ECO:0000255|HAMAP-Rule:MF_00258}; EC=5.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00258}; |
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| MyHits synonyms | MURI_HELP2 , B6JLD2 , 741338442767E987 |
 Legends: 1, ACT_SITE Proton donor/acceptor. {ECO:0000255|HAMAP-Rule:MF_00258}; 2, REGION Substrate binding. {ECO:0000255|HAMAP- Rule:MF_00258}; 3, ipat:ASP_GLU_RACEMASE_2 [T]; 4, ipat:ASP_GLU_RACEMASE_1 [T].
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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 177 187 ipat:ASP_GLU_RACEMASE_2 [T]
FT MYHIT 67 75 ipat:ASP_GLU_RACEMASE_1 [T]
FT MYHIT 1 255 ihamap:Glu_racemase [T]
FT MYHIT 3 215 ipfam:Asp_Glu_race [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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