MURI_AQUPY
ID MURI_AQUPY Reviewed; 254 AA.
AC P56868;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Glutamate racemase {ECO:0000255|HAMAP-Rule:MF_00258, ECO:0000303|PubMed:10484173};
DE EC=5.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00258, ECO:0000269|PubMed:10331867, ECO:0000269|PubMed:10484173};
GN Name=murI {ECO:0000255|HAMAP-Rule:MF_00258};
OS Aquifex pyrophilus.
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=2714;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, SUBUNIT, AND CATALYTIC
RP ACTIVITY.
RX PubMed=10484173; DOI=10.1007/s007920050114;
RA Kim S.S., Choi I.G., Kim S.H., Yu Y.G.;
RT "Molecular cloning, expression, and characterization of a thermostable
RT glutamate racemase from a hyperthermophilic bacterium, Aquifex
RT pyrophilus.";
RL Extremophiles 3:175-183(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GLUTAMATE, CATALYTIC
RP ACTIVITY, SUBUNIT, AND MUTAGENESIS OF ASP-7 AND GLU-147.
RX PubMed=10331867; DOI=10.1038/8223;
RA Hwang K.Y., Cho C.-S., Kim S.S., Sung H.-C., Yu Y.G., Cho Y.;
RT "Structure and mechanism of glutamate racemase from Aquifex pyrophilus.";
RL Nat. Struct. Biol. 6:422-426(1999).
CC -!- FUNCTION: Provides the (R)-glutamate required for cell wall
CC biosynthesis. Converts L- or D-glutamate to D- or L-glutamate,
CC respectively, but not other amino acids such as alanine, aspartate, and
CC glutamine.
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 ECO:0000269|PubMed:10331867, ECO:0000269|PubMed:10484173};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermostable.;
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00258}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10331867,
CC ECO:0000269|PubMed:10484173}.
CC -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC {ECO:0000255|HAMAP-Rule:MF_00258}.
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DR EMBL; AF212972; AAF25672.1; -; Genomic_DNA.
DR PDB; 1B73; X-ray; 2.30 A; A=1-254.
DR PDB; 1B74; X-ray; 2.30 A; A=1-254.
DR PDBsum; 1B73; -.
DR PDBsum; 1B74; -.
DR AlphaFoldDB; P56868; -.
DR SMR; P56868; -.
DR DrugBank; DB02174; D-Glutamine.
DR BRENDA; 5.1.1.3; 397.
DR SABIO-RK; P56868; -.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; P56868; -.
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.
FT CHAIN 1..254
FT /note="Glutamate racemase"
FT /id="PRO_0000095449"
FT ACT_SITE 70
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT ACT_SITE 178
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT BINDING 7..8
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22634, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT BINDING 39..40
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22634, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT BINDING 71..72
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000269|PubMed:10331867, ECO:0007744|PDB:1B74"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10331867,
FT ECO:0007744|PDB:1B74"
FT BINDING 179..180
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22634, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT MUTAGEN 7
FT /note="D->S: Strongly reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:10331867"
FT MUTAGEN 147
FT /note="E->N: Strongly reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:10331867"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:1B73"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:1B73"
FT HELIX 15..22
FT /evidence="ECO:0007829|PDB:1B73"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1B74"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:1B73"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:1B73"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:1B74"
FT HELIX 44..59
FT /evidence="ECO:0007829|PDB:1B73"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1B73"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:1B73"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:1B73"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:1B73"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1B73"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1B73"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:1B73"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:1B73"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:1B73"
FT HELIX 122..128
FT /evidence="ECO:0007829|PDB:1B73"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:1B73"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1B73"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:1B73"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1B73"
FT HELIX 156..163
FT /evidence="ECO:0007829|PDB:1B73"
FT TURN 165..170
FT /evidence="ECO:0007829|PDB:1B73"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:1B73"
FT HELIX 185..191
FT /evidence="ECO:0007829|PDB:1B73"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:1B73"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:1B73"
FT TURN 207..211
FT /evidence="ECO:0007829|PDB:1B73"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:1B73"
FT HELIX 231..239
FT /evidence="ECO:0007829|PDB:1B73"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:1B73"
SQ SEQUENCE 254 AA; 27993 MW; D9E7B16F33A90711 CRC64;
MKIGIFDSGV GGLTVLKAIR NRYRKVDIVY LGDTARVPYG IRSKDTIIRY SLECAGFLKD
KGVDIIVVAC NTASAYALER LKKEINVPVF GVIEPGVKEA LKKSRNKKIG VIGTPATVKS
GAYQRKLEEG GADVFAKACP LFVPLAEEGL LEGEITRKVV EHYLKEFKGK IDTLILGCTH
YPLLKKEIKK FLGDVEVVDS SEALSLSLHN FIKDDGSSSL ELFFTDLSPN LQFLIKLILG
RDYPVKLAEG VFTH
