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MURI_MYCS2
ID   MURI_MYCS2              Reviewed;         277 AA.
AC   A0R1X0; I7GEC4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=MSMEG_4903, MSMEI_4776;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
CC   -!- FUNCTION: Provides the (R)-glutamate required for cell wall
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00258}.
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:0000255|HAMAP-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}.
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DR   EMBL; CP000480; ABK72762.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP41224.1; -; Genomic_DNA.
DR   RefSeq; WP_011730179.1; NZ_SIJM01000024.1.
DR   RefSeq; YP_889158.1; NC_008596.1.
DR   PDB; 5IJW; X-ray; 1.76 A; A/B=1-277.
DR   PDBsum; 5IJW; -.
DR   AlphaFoldDB; A0R1X0; -.
DR   SMR; A0R1X0; -.
DR   STRING; 246196.MSMEI_4776; -.
DR   EnsemblBacteria; ABK72762; ABK72762; MSMEG_4903.
DR   EnsemblBacteria; AFP41224; AFP41224; MSMEI_4776.
DR   GeneID; 66736207; -.
DR   KEGG; msg:MSMEI_4776; -.
DR   KEGG; msm:MSMEG_4903; -.
DR   PATRIC; fig|246196.19.peg.4784; -.
DR   eggNOG; COG0796; Bacteria.
DR   OMA; MPWGPRT; -.
DR   OrthoDB; 1718671at2; -.
DR   BRENDA; 5.1.1.3; 3512.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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   1: Evidence at protein level;
KW   3D-structure; Cell shape; Cell wall biogenesis/degradation; Isomerase;
KW   Peptidoglycan synthesis; Reference proteome.
FT   CHAIN           1..277
FT                   /note="Glutamate racemase"
FT                   /id="PRO_1000047586"
FT   ACT_SITE        75
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   ACT_SITE        186
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         12..13
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         44..45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         76..77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         187..188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   STRAND          8..15
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   HELIX           18..27
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   STRAND          33..37
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   TURN            39..41
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   HELIX           49..65
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   STRAND          69..73
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   HELIX           76..82
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   TURN            83..85
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   HELIX           86..90
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   STRAND          95..99
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   HELIX           100..109
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   STRAND          111..119
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   HELIX           121..125
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   HELIX           128..132
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   HELIX           133..135
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   STRAND          140..145
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   HELIX           149..154
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   HELIX           161..176
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   STRAND          180..186
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   HELIX           189..192
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   HELIX           193..200
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   STRAND          205..208
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   HELIX           209..223
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   STRAND          240..246
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   HELIX           248..259
FT                   /evidence="ECO:0007829|PDB:5IJW"
FT   TURN            263..265
FT                   /evidence="ECO:0007829|PDB:5IJW"
SQ   SEQUENCE   277 AA;  29283 MW;  6E4BD345B82C8F62 CRC64;
     MSDRLAPIGI FDSGVGGLTV ARAIIDQLPD EDIVYVGDTG NGPYGPLTIP QIRAHSLAIG
     DDLVSRGVKA LVIACNTASS ACLRDARERY SPVPVVEVIL PAVRRAVAAT RNGRIGVIGT
     QATIASGAYQ DAFAAARDTE VFTVACPRFV DFVERGVTSG RQVLGLAEGY LEPLQLAEVD
     TLVLGCTHYP MLSGLIQLAM GDNVTLVSSA EETAKDLLRV LTELDLLRPH PDDPSVTAVR
     RFEATGDPEA FTALAARFLG PTLDGVRPVR RHAGAGR
 
 
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