GenomeNet

Database: UniProt
Entry: A0A0Q9YNN6_9COXI
LinkDB: A0A0Q9YNN6_9COXI
Original site: A0A0Q9YNN6_9COXI 
ID   A0A0Q9YNN6_9COXI        Unreviewed;       285 AA.
AC   A0A0Q9YNN6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=racE {ECO:0000313|EMBL:KRG18398.1};
GN   Synonyms=murI {ECO:0000256|HAMAP-Rule:MF_00258};
GN   ORFNames=CC99x_01610 {ECO:0000313|EMBL:KRG18398.1};
OS   Candidatus Berkiella cookevillensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Berkiella.
OX   NCBI_TaxID=437022 {ECO:0000313|EMBL:KRG18398.1, ECO:0000313|Proteomes:UP000051494};
RN   [1] {ECO:0000313|EMBL:KRG18398.1, ECO:0000313|Proteomes:UP000051494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC99 {ECO:0000313|EMBL:KRG18398.1,
RC   ECO:0000313|Proteomes:UP000051494};
RA   Mehari Y.T., Arivett B.A., Farone A.L., Gunderson J.H., Farone M.B.;
RT   "Draft Genome Sequences of Two Novel Amoeba-resistant Intranuclear
RT   Bacteria, Candidatus Berkiella cookevillensis and Candidatus Berkiella
RT   aquae.";
RL   Submitted (SEP-2015) 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:KRG18398.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LKHV01000007; KRG18398.1; -; Genomic_DNA.
DR   RefSeq; WP_057624693.1; NZ_LKHV02000001.1.
DR   AlphaFoldDB; A0A0Q9YNN6; -.
DR   STRING; 437022.CC99x_01610; -.
DR   PATRIC; fig|1590042.3.peg.1635; -.
DR   OrthoDB; 9801055at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000051494; 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; IPR018187; Asp/Glu_racemase_AS_1.
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:SF2; GLUTAMATE RACEMASE; 1.
DR   Pfam; PF01177; Asp_Glu_race; 1.
DR   SUPFAM; SSF53681; Aspartate/glutamate racemase; 2.
DR   PROSITE; PS00923; ASP_GLU_RACEMASE_1; 1.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051494}.
FT   ACT_SITE        78
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   ACT_SITE        194
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         15..16
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         47..48
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         79..80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         195..196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
SQ   SEQUENCE   285 AA;  31322 MW;  C2FA7D7C1CAB0C15 CRC64;
     MNFKTDTTLP IGVFDSGMGG LTVLNALMQL LPNENFIYLG DTARLPYGTK SKDTVIHYSY
     NASKHLIDRG IKLLVVACNT ASSVALETLE RDFYPVPVIG VIQPSAEMTL TQLPEGPIAV
     IATEGTVKSR AYTQTILKQS PNREVIEWPC SLLVALAEEG WHSGPLVEDI IEHMLTPLWQ
     QLDNPAQKAL LLGCTHFPVL KSAIQKVIDQ NTIIIDSAFS VADAVLARLT ANNLVNQQST
     CGKIQYLVTD GIERFQRVGK FFLDSRNQVL SPELVSINII KSTQT
//
DBGET integrated database retrieval system