MURI2_CALS4
ID MURI2_CALS4 Reviewed; 264 AA.
AC Q8RC52;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Glutamate racemase 2 {ECO:0000255|HAMAP-Rule:MF_00258};
DE EC=5.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00258};
GN Name=murI2 {ECO:0000255|HAMAP-Rule:MF_00258}; OrderedLocusNames=TTE0595;
OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobacter.
OX NCBI_TaxID=273068;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX PubMed=11997336; DOI=10.1101/gr.219302;
RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA Wang J., Yu J., Yang H.;
RT "A complete sequence of the T. tengcongensis genome.";
RL Genome Res. 12:689-700(2002).
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; AE008691; AAM23865.1; -; Genomic_DNA.
DR RefSeq; WP_011025010.1; NC_003869.1.
DR AlphaFoldDB; Q8RC52; -.
DR SMR; Q8RC52; -.
DR STRING; 273068.TTE0595; -.
DR EnsemblBacteria; AAM23865; AAM23865; TTE0595.
DR KEGG; tte:TTE0595; -.
DR eggNOG; COG0796; Bacteria.
DR HOGENOM; CLU_052344_0_2_9; -.
DR OMA; TCATIDK; -.
DR OrthoDB; 1718671at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000555; 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; 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; PS00924; ASP_GLU_RACEMASE_2; 1.
PE 3: Inferred from homology;
KW Cell shape; Cell wall biogenesis/degradation; Isomerase;
KW Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..264
FT /note="Glutamate racemase 2"
FT /id="PRO_0000095527"
FT ACT_SITE 73
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT ACT_SITE 181
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 10..11
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 42..43
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 74..75
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 182..183
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
SQ SEQUENCE 264 AA; 29724 MW; 7BD07F6218EB63B4 CRC64;
MDSRPIGVFD SGVGGLTVLK RLIQVLPEED YIYFGDTKRV PYGDRSKEEI ELFAGQIINF
MKEKNVKAVV IACNTTCATI DKGKYDIELF DVLKAGAESG VYCTKNKKVG VIATKRTVES
RSYEINIKSI NPQIEVYQKA CPEFVPLIEK GLYNSHLAYK AAKDCLEEFK GKEIDTLILG
CTHYPLMEPI IKAIMGDGVK VVDPAVRLSH EVKEYLERSR ILNFGKKGKI EFFVSGDAEN
FKRAAEMVLG KKIDEVFIVD IERY
