(data stored in ACNUC7421 zone)

SWISSPROT: A4ATU2_MARSH

ID   A4ATU2_MARSH            Unreviewed;       262 AA.
AC   A4ATU2;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 87.
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   OrderedLocusNames=FB2170_17296 {ECO:0000313|EMBL:EAR00862.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00862.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00862.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(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; CP002157; EAR00862.1; -; Genomic_DNA.
DR   RefSeq; WP_013304665.1; NC_014472.1.
DR   STRING; 313603.FB2170_17296; -.
DR   EnsemblBacteria; EAR00862; EAR00862; FB2170_17296.
DR   KEGG; fbc:FB2170_17296; -.
DR   eggNOG; ENOG4105F03; Bacteria.
DR   eggNOG; COG0796; LUCA.
DR   HOGENOM; HOG000262395; -.
DR   KO; K01776; -.
DR   OMA; VYGCTHY; -.
DR   OrthoDB; 1718671at2; -.
DR   BioCyc; MSP313603:G1GNS-235-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001602; 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; A4ATU2.
DR   SWISS-2DPAGE; A4ATU2.
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:UP000001602};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00258,
KW   ECO:0000256|SAAS:SAAS00090451};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00258,
KW   ECO:0000256|SAAS:SAAS00436203};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602}.
FT   REGION       10     11       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00258}.
FT   REGION       42     43       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00258}.
FT   REGION       74     75       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00258}.
FT   REGION      184    185       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00258}.
FT   ACT_SITE     73     73       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00258}.
FT   ACT_SITE    183    183       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00258}.
SQ   SEQUENCE   262 AA;  28546 MW;  9DBC2CFA640FB4F6 CRC64;
     MSVDPIGIFD SGVGGTSIWK EINVQLPNEN TVYFADSENA PYGEKSSEEI IQLSVKNTEL
     LLGKGCKLIV VACNTATTNA IDHLRKNYDV PFIGIEPAIK PAALQSKSKT VGVLATKGTL
     TSSLFHSTSE NHTNGITVIE QVGKGLVPLI EEGKINSKET RELLFSYIGP MLEKGIDYLV
     LGCTHYPYLI PVLNDLIPDH VKIIDSGEAV ARQARAVLEQ KKITNSSHNT AYHKFYTNAG
     VSVLKSFLED VEGSLEISHL DF
//

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