ID A0A1C0AN91_9ACTN Unreviewed; 512 AA.
AC A0A1C0AN91;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=Enoylpyruvate transferase {ECO:0000256|ARBA:ARBA00042443};
DE AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000256|ARBA:ARBA00042842};
GN ORFNames=BCR15_03435 {ECO:0000313|EMBL:OCL34746.1};
OS Tessaracoccus lapidicaptus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=1427523 {ECO:0000313|EMBL:OCL34746.1, ECO:0000313|Proteomes:UP000093501};
RN [1] {ECO:0000313|Proteomes:UP000093501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IPBSL-7 {ECO:0000313|Proteomes:UP000093501};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
CC acetylglucosamine. {ECO:0000256|ARBA:ARBA00037534}.
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:OCL34746.1}.
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DR EMBL; MBQD01000020; OCL34746.1; -; Genomic_DNA.
DR RefSeq; WP_068751428.1; NZ_MBQD01000020.1.
DR AlphaFoldDB; A0A1C0AN91; -.
DR Proteomes; UP000093501; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 3.65.10.10; Enolpyruvate transferase domain; 2.
DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
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 Pfam; PF01381; HTH_3; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF55205; EPT/RTPC-like; 1.
DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR PROSITE; PS50943; HTH_CROC1; 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000093501};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OCL34746.1}.
FT DOMAIN 12..66
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000259|PROSITE:PS50943"
SQ SEQUENCE 512 AA; 56146 MW; 68664DBF78995BB1 CRC64;
MSATSESIGR MIREARLARG WSQQRLADEL GTVQSAVHRI ENGQQNLSLS MINRLAEALD
MPLIQTATQG NVNFEIQGPT RLSGGIDVRT SKNAAMAILC ASLLNQGRTV LRGIARIEEV
DRISEVLTSI GVRLTWIGDN DLEIVRPGTL TPETIDARAA KRTRSILMLL GPLMHEFEQF
LLPYAGGCDL GARTVHPHMS ALSKMGLTVE ATEGNYHATV QPIEGVERSI TLIERGDTVT
ENAVMAAARA PGVTVLRNAS GNYMVQDLCF FLQELGVDID GIGTTTLTVR GRDHLEADVE
YHISEDPIEA MSLVTAGIVT RSGITVRRCP IEFLEVEFAV LDEMGQRLEL SPEYRSRNGR
TRLVDVTVVP SDLVAPLDKI HPMPFPGLNI DNLPFFAVIC ATATGQSVIY DWVYDNRAIH
LKKLADLGAN IQLMDAHRLL ILGPTKWRAR EIESPPALRP AVCLLLAAMA ARGTTNLMDV
YVINRGYEDL PQRLNKLGAS INVFWGTPQN DA
//
