(data stored in ACNUC7421 zone)

SWISSPROT: Q3IDS7_PSEHT

ID   Q3IDS7_PSEHT            Unreviewed;       265 AA.
AC   Q3IDS7;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 106.
DE   RecName: Full=Glutamate racemase {ECO:0000256|HAMAP-Rule:MF_00258, ECO:0000256|SAAS:SAAS00524481};
DE            EC=5.1.1.3 {ECO:0000256|HAMAP-Rule:MF_00258, ECO:0000256|SAAS:SAAS00358505};
GN   Name=murI {ECO:0000256|HAMAP-Rule:MF_00258,
GN   ECO:0000313|EMBL:CAI85355.1};
GN   OrderedLocusNames=PSHAa0252 {ECO:0000313|EMBL:CAI85355.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85355.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85355.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Provides the (R)-glutamate required for cell wall
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00258,
CC       ECO:0000256|SAAS:SAAS00551341}.
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|HAMAP-Rule:MF_00258,
CC         ECO:0000256|SAAS:SAAS01120479};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00258, ECO:0000256|SAAS:SAAS00041181}.
CC   -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC       {ECO:0000256|HAMAP-Rule:MF_00258, ECO:0000256|SAAS:SAAS00571648}.
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DR   EMBL; CR954246; CAI85355.1; -; Genomic_DNA.
DR   RefSeq; WP_011326969.1; NC_007481.1.
DR   STRING; 326442.PSHAa0252; -.
DR   EnsemblBacteria; CAI85355; CAI85355; PSHAa0252.
DR   KEGG; pha:PSHAa0252; -.
DR   PATRIC; fig|326442.8.peg.243; -.
DR   eggNOG; ENOG4105F03; Bacteria.
DR   eggNOG; COG0796; LUCA.
DR   HOGENOM; HOG000262397; -.
DR   KO; K01776; -.
DR   OMA; VYGCTHY; -.
DR   OrthoDB; 1718671at2; -.
DR   BioCyc; PHAL326442:PSHA_RS01245-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000006843; Chromosome I.
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   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;
DR   PRODOM; Q3IDS7.
DR   SWISS-2DPAGE; Q3IDS7.
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00258,
KW   ECO:0000256|SAAS:SAAS00436155};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00258,
KW   ECO:0000256|SAAS:SAAS00041303};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00258,
KW   ECO:0000256|SAAS:SAAS00090451, ECO:0000313|EMBL:CAI85355.1};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00258,
KW   ECO:0000256|SAAS:SAAS00436203};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843}.
FT   REGION        9     10       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00258}.
FT   REGION       41     42       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00258}.
FT   REGION       75     76       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00258}.
FT   REGION      186    187       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00258}.
FT   ACT_SITE     74     74       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00258}.
FT   ACT_SITE    185    185       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00258}.
SQ   SEQUENCE   265 AA;  29037 MW;  BECA7E82EAFF874C CRC64;
     MSAHIMVFDS GIGGTTVLEH IQQSIPDAQY SYFMDNALLP YGAQSQQTII NRLCALIHFI
     NQQALNVDLI VIACNTASTS ALGAVRQITT IPIVGVVPAI KPAAQLTQSK HIGLLATPAT
     ISSPYTRTLI QEHTNNIAVS LYSSVELVTL AERLFFEQSL DTTKLHQELD RLNIDQSIDV
     LVLGCTHFPI LAEPISQYFN RKVQLLDSGA AIAKRVHYLI SQLNLTNNNI ADTKKPLQYY
     ATASVSSKLA VKLVTLIDPA QNEER
//

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