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Database: UniProt
Entry: B6WBT1_9FIRM
LinkDB: B6WBT1_9FIRM
Original site: B6WBT1_9FIRM 
ID   B6WBT1_9FIRM            Unreviewed;       249 AA.
AC   B6WBT1;
DT   20-JAN-2009, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Glutamate racemase {ECO:0000256|ARBA:ARBA00013090, ECO:0000256|HAMAP-Rule:MF_00258};
DE            EC=5.1.1.3 {ECO:0000256|ARBA:ARBA00013090, ECO:0000256|HAMAP-Rule:MF_00258};
GN   Name=murI {ECO:0000256|HAMAP-Rule:MF_00258,
GN   ECO:0000313|EMBL:EEB35100.1};
GN   ORFNames=ANHYDRO_02064 {ECO:0000313|EMBL:EEB35100.1};
OS   Anaerococcus hydrogenalis DSM 7454.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Anaerococcus.
OX   NCBI_TaxID=561177 {ECO:0000313|EMBL:EEB35100.1, ECO:0000313|Proteomes:UP000005451};
RN   [1] {ECO:0000313|EMBL:EEB35100.1, ECO:0000313|Proteomes:UP000005451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7454 {ECO:0000313|EMBL:EEB35100.1,
RC   ECO:0000313|Proteomes:UP000005451};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEB35100.1, ECO:0000313|Proteomes:UP000005451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7454 {ECO:0000313|EMBL:EEB35100.1,
RC   ECO:0000313|Proteomes:UP000005451};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Anaerococcus hydrogenalis (DSM 7454).";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Provides the (R)-glutamate required for cell wall
CC       biosynthesis. {ECO:0000256|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:0000256|ARBA:ARBA00001602, ECO:0000256|HAMAP-
CC         Rule:MF_00258};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00258}.
CC   -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC       {ECO:0000256|HAMAP-Rule:MF_00258}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEB35100.1}.
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DR   EMBL; ABXA01000049; EEB35100.1; -; Genomic_DNA.
DR   RefSeq; WP_004815914.1; NZ_ABXA01000049.1.
DR   AlphaFoldDB; B6WBT1; -.
DR   STRING; 561177.ANHYDRO_02064; -.
DR   eggNOG; COG0796; Bacteria.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000005451; Unassembled WGS sequence.
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   Gene3D; 3.40.50.1860; -; 2.
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   NCBIfam; TIGR00067; glut_race; 1.
DR   PANTHER; PTHR21198; GLUTAMATE RACEMASE; 1.
DR   PANTHER; PTHR21198:SF3; GLUTAMATE RACEMASE; 1.
DR   Pfam; PF01177; Asp_Glu_race; 1.
DR   SUPFAM; SSF53681; Aspartate/glutamate racemase; 2.
DR   PROSITE; PS00924; ASP_GLU_RACEMASE_2; 1.
PE   3: Inferred from homology;
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00258};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00258};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00258};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00258}.
FT   ACT_SITE        70
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   ACT_SITE        178
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         8..9
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         39..40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         71..72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         179..180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
SQ   SEQUENCE   249 AA;  28480 MW;  7ABE8D51402F73A6 CRC64;
     MTNIGVFDSG LGGLTVLREL SKKHKANYFY LGDNKNVPYG NRSNEEIIKL SKDIVRFLIK
     KDIDFFVIAC NTISVVAIKE LRKEFDKKFI SITDEGIKEA LNRNGDVFVM ATKATCKNHA
     YKKIIEGRSS KKVYEKSCPK LVDYIEEGIL SGEKIDSQLK DYLTLANEKK IENIILGCTH
     YPIIKKTIEK NLTYKANIID PAKVLARDIV FDEDYNLNIE IYMTDVNKIS QDMTNKIMGK
     NIKIKSLYK
//
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