ID F8A1C2_CELGA Unreviewed; 438 AA.
AC F8A1C2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE EC=2.5.1.7 {ECO:0000256|HAMAP-Rule:MF_00111};
DE AltName: Full=Enoylpyruvate transferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE Short=EPT {ECO:0000256|HAMAP-Rule:MF_00111};
GN Name=murA {ECO:0000256|HAMAP-Rule:MF_00111};
GN OrderedLocusNames=Celgi_1150 {ECO:0000313|EMBL:AEI11669.1};
OS Cellulomonas gilvus (strain ATCC 13127 / NRRL B-14078) (Cellvibrio gilvus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=593907 {ECO:0000313|EMBL:AEI11669.1, ECO:0000313|Proteomes:UP000000485};
RN [1] {ECO:0000313|Proteomes:UP000000485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13127 / NRRL B-14078 {ECO:0000313|Proteomes:UP000000485};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Munk A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA Woyke T.;
RT "Complete sequence of Cellvibrio gilvus ATCC 13127.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
CC acetylglucosamine. {ECO:0000256|ARBA:ARBA00037534, ECO:0000256|HAMAP-
CC Rule:MF_00111}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00111};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00111}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00111}.
CC -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
CC {ECO:0000256|ARBA:ARBA00038367, ECO:0000256|HAMAP-Rule:MF_00111}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00111}.
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DR EMBL; CP002665; AEI11669.1; -; Genomic_DNA.
DR RefSeq; WP_013883188.1; NC_015671.1.
DR AlphaFoldDB; F8A1C2; -.
DR STRING; 593907.Celgi_1150; -.
DR KEGG; cga:Celgi_1150; -.
DR eggNOG; COG0766; Bacteria.
DR HOGENOM; CLU_027387_0_0_11; -.
DR OrthoDB; 9803760at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000485; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IEA:UniProtKB-UniRule.
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-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0019277; P:UDP-N-acetylgalactosamine biosynthetic process; IEA:InterPro.
DR CDD; cd01555; UdpNAET; 1.
DR Gene3D; 3.65.10.10; Enolpyruvate transferase domain; 2.
DR HAMAP; MF_00111; MurA; 1.
DR InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR InterPro; IPR005750; UDP_GlcNAc_COvinyl_MurA.
DR NCBIfam; TIGR01072; murA; 1.
DR PANTHER; PTHR43783; UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE; 1.
DR PANTHER; PTHR43783:SF1; UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE; 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, ECO:0000256|HAMAP-
KW Rule:MF_00111};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_00111};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_00111};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_00111};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00111};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_00111}; Pyruvate {ECO:0000256|HAMAP-Rule:MF_00111};
KW Reference proteome {ECO:0000313|Proteomes:UP000000485};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00111}.
FT DOMAIN 7..428
FT /note="Enolpyruvate transferase"
FT /evidence="ECO:0000259|Pfam:PF00275"
FT ACT_SITE 121
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT BINDING 23..24
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT BINDING 97
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT BINDING 311
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT BINDING 333
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT MOD_RES 121
FT /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
SQ SEQUENCE 438 AA; 47223 MW; 2BDDA3F8A71DFD45 CRC64;
MNDLLYVNGG TPLRGEITVR GAKNFVSKAM VAALLGETPS VLRNVPQIRD VAVVTGLLEL
HGVRVDADPV AGTLHLDPTD VETAHVADID AHAGSSRIPI LFCGPLLHRL GEAFIPDLGG
CRIGDRPINY HLDILRQFGA VVDKRPQGIY LSAPRRLQGT KIALPYPSVG ATEQLLLTAV
RAEGITELAG AAIEPEIMDL INVLQKMGAI ISVDTDRVIR IEGVERLEGY QHTALSDRIE
GASWASAALA TGGDIYVRGA TQPEMTTFLN TFRKVGGEFT VDDEGIRFFH PGGDLRSIQL
ETDVHPGFMT DWQQPLVVAL TQAKGLSIVH ETVYENRFGF ADALVGMGAT IQVYKECLGG
RPCRFGQRNF YHSAVISGPT PLSAADIEVP DLRGGFSHLI AALTAKGTSA VRGISLIDRG
YEHFMDKLEA LGAEFSRD
//
