(data stored in SCRATCH zone)

SWISSPROT: D3VH82_XENNA

ID   D3VH82_XENNA            Unreviewed;       287 AA.
AC   D3VH82;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 59.
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:CBJ88367.1};
GN   OrderedLocusNames=XNC1_0279 {ECO:0000313|EMBL:CBJ88367.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88367.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88367.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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; FN667742; CBJ88367.1; -; Genomic_DNA.
DR   RefSeq; WP_013183212.1; NC_014228.1.
DR   STRING; 406817.XNC1_0279; -.
DR   EnsemblBacteria; CBJ88367; CBJ88367; XNC1_0279.
DR   KEGG; xne:XNC1_0279; -.
DR   eggNOG; ENOG4105F03; Bacteria.
DR   eggNOG; COG0796; LUCA.
DR   HOGENOM; HOG000262397; -.
DR   KO; K01776; -.
DR   OMA; VYGCTHY; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000008075; Chromosome.
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; D3VH82.
DR   SWISS-2DPAGE; D3VH82.
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:UP000008075};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00258,
KW   ECO:0000256|SAAS:SAAS00090451, ECO:0000313|EMBL:CBJ88367.1};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00258,
KW   ECO:0000256|SAAS:SAAS00436203};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075}.
FT   REGION       32     33       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00258}.
FT   REGION       64     65       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00258}.
FT   REGION       97     98       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00258}.
FT   REGION      209    210       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00258}.
FT   ACT_SITE     96     96       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00258}.
FT   ACT_SITE    208    208       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00258}.
SQ   SEQUENCE   287 AA;  31570 MW;  695EEC147AC13F59 CRC64;
     MAIARQEENT PSLAVTTSDL NKTARPTILV FDSGVGGLSV YKEIRKLLPD LHYIYAFDNE
     AFPYGEKTAD VIIDRVVKVV DAIQKKHPLA VVVIACNTAS TVSLPVLRER FSFPVVGVVP
     AIKPAAKLSC NRIVGLLATR ATVNRGYTKE LITRFATDCQ VHSIGSAELV ELAERKLHGK
     DVPLDELEKV LKPWLRMKEP PDTVILGCTH FPLIAEELSQ VLPDGTRLID SGAAIARRTA
     WLIKNRADLF LTTVDNLAYC TKLDADSEAL SPVLYEYGFL TLEKLAT
//

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