GenomeNet

Database: UniProt
Entry: R6M1R4_9FIRM
LinkDB: R6M1R4_9FIRM
Original site: R6M1R4_9FIRM 
ID   R6M1R4_9FIRM            Unreviewed;       285 AA.
AC   R6M1R4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase {ECO:0000256|ARBA:ARBA00039754};
DE            EC=2.5.1.7 {ECO:0000256|ARBA:ARBA00039108};
DE   AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000256|ARBA:ARBA00042842};
GN   ORFNames=BN515_00453 {ECO:0000313|EMBL:CDB88361.1};
OS   Firmicutes bacterium CAG:170.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263006 {ECO:0000313|EMBL:CDB88361.1, ECO:0000313|Proteomes:UP000018279};
RN   [1] {ECO:0000313|EMBL:CDB88361.1, ECO:0000313|Proteomes:UP000018279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:170 {ECO:0000313|Proteomes:UP000018279};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine =
CC         phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine;
CC         Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00036669};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
CC       {ECO:0000256|ARBA:ARBA00038367}.
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:CDB88361.1}.
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; CBEH010000330; CDB88361.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6M1R4; -.
DR   Proteomes; UP000018279; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.65.10.10; Enolpyruvate transferase domain; 2.
DR   InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR   InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
DR   InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR   PANTHER; PTHR43783; UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE; 1.
DR   PANTHER; PTHR43783:SF2; UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE 2; 1.
DR   Pfam; PF00275; EPSP_synthase; 1.
DR   SUPFAM; SSF55205; EPT/RTPC-like; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CDB88361.1}.
FT   DOMAIN          6..250
FT                   /note="Enolpyruvate transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00275"
SQ   SEQUENCE   285 AA;  29885 MW;  BC4B0A2D2CA396E7 CRC64;
     MIQYHVQGGT RLSGTVSISG AKNAAVAILP AALLVNGTCR IENVPDISDV RLLLEILSDM
     GANIRRLSRN AVEIDCRHAR NATAPIELVR RIRASYYLIG VQLGRFGHAH VAMPGGCNFG
     VRPIDQHIKG FEAMGATVEQ NGGYVCADAP EGGLQGGHVY LDIVSVGATM NILLAAVLSN
     GMTIIENCAK EPHIVDLANF LNAMGARISG AGTDVIKVRG VKVLRGGSYS IIPDQIEAGT
     YMAAAAACGG NPPVAPPLPP PSLWPTSFPS ISTASPRSCV KWARV
//
DBGET integrated database retrieval system