MURI_MYCTU
ID MURI_MYCTU Reviewed; 271 AA.
AC P9WPW9; L0T6C6; P63635; Q10626;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 46.
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}; OrderedLocusNames=Rv1338;
GN ORFNames=MTCY02B10.02, MTCY130.23;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; AL123456; CCP44096.1; -; Genomic_DNA.
DR PIR; F70771; F70771.
DR RefSeq; NP_215854.1; NC_000962.3.
DR RefSeq; WP_003406919.1; NZ_NVQJ01000031.1.
DR PDB; 5HJ7; X-ray; 2.30 A; A/B=1-271.
DR PDBsum; 5HJ7; -.
DR AlphaFoldDB; P9WPW9; -.
DR SMR; P9WPW9; -.
DR STRING; 83332.Rv1338; -.
DR ChEMBL; CHEMBL4295588; -.
DR MoonProt; P9WPW9; -.
DR PaxDb; P9WPW9; -.
DR DNASU; 886866; -.
DR GeneID; 886866; -.
DR KEGG; mtu:Rv1338; -.
DR TubercuList; Rv1338; -.
DR eggNOG; COG0796; Bacteria.
DR OMA; MPWGPRT; -.
DR PhylomeDB; P9WPW9; -.
DR BioCyc; MetaCyc:G185E-5517-MON; -.
DR BRENDA; 5.1.1.1; 3445.
DR BRENDA; 5.1.1.3; 3445.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0047661; F:amino-acid racemase activity; IBA:GO_Central.
DR GO; GO:0008657; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) inhibitor activity; IDA:MTBBASE.
DR GO; GO:0008881; F:glutamate racemase activity; IDA:MTBBASE.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IDA:MTBBASE.
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..271
FT /note="Glutamate racemase"
FT /id="PRO_0000095489"
FT ACT_SITE 75
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT ACT_SITE 185
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 186..187
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT STRAND 8..15
FT /evidence="ECO:0007829|PDB:5HJ7"
FT HELIX 18..27
FT /evidence="ECO:0007829|PDB:5HJ7"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:5HJ7"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:5HJ7"
FT HELIX 49..65
FT /evidence="ECO:0007829|PDB:5HJ7"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:5HJ7"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:5HJ7"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:5HJ7"
FT HELIX 99..108
FT /evidence="ECO:0007829|PDB:5HJ7"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:5HJ7"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:5HJ7"
FT HELIX 127..131
FT /evidence="ECO:0007829|PDB:5HJ7"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:5HJ7"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:5HJ7"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:5HJ7"
FT HELIX 160..175
FT /evidence="ECO:0007829|PDB:5HJ7"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:5HJ7"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:5HJ7"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:5HJ7"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:5HJ7"
FT HELIX 208..222
FT /evidence="ECO:0007829|PDB:5HJ7"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:5HJ7"
FT HELIX 244..254
FT /evidence="ECO:0007829|PDB:5HJ7"
SQ SEQUENCE 271 AA; 28643 MW; 29DE3CE67A27EEBA CRC64;
MNSPLAPVGV FDSGVGGLTV ARAIIDQLPD EDIVYVGDTG NGPYGPLTIP EIRAHALAIG
DDLVGRGVKA LVIACNSASS ACLRDARERY QVPVVEVILP AVRRAVAATR NGRIGVIGTR
ATITSHAYQD AFAAARDTEI TAVACPRFVD FVERGVTSGR QVLGLAQGYL EPLQRAEVDT
LVLGCTHYPL LSGLIQLAMG ENVTLVSSAE ETAKEVVRVL TEIDLLRPHD APPATRIFEA
TGDPEAFTKL AARFLGPVLG GVQPVHPSRI H
