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Database: UniProt
Entry: F5XGS3_MICPN
LinkDB: F5XGS3_MICPN
Original site: F5XGS3_MICPN 
ID   F5XGS3_MICPN            Unreviewed;       508 AA.
AC   F5XGS3;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
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   Name=murA {ECO:0000313|EMBL:BAK35555.1};
GN   OrderedLocusNames=MLP_25410 {ECO:0000313|EMBL:BAK35555.1};
OS   Microlunatus phosphovorus (strain ATCC 700054 / DSM 10555 / JCM 9379 / NBRC
OS   101784 / NCIMB 13414 / VKM Ac-1990 / NM-1).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Microlunatus.
OX   NCBI_TaxID=1032480 {ECO:0000313|EMBL:BAK35555.1, ECO:0000313|Proteomes:UP000007947};
RN   [1] {ECO:0000313|EMBL:BAK35555.1, ECO:0000313|Proteomes:UP000007947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700054 / DSM 10555 / JCM 9379 / NBRC 101784 / NCIMB 13414
RC   / VKM Ac-1990 / NM-1 {ECO:0000313|Proteomes:UP000007947};
RA   Hosoyama A., Sasaki K., Harada T., Igarashi R., Kawakoshi A., Sasagawa M.,
RA   Fukada J., Nakamura S., Katano Y., Hanada S., Kamagata Y., Nakamura N.,
RA   Yamazaki S., Fujita N.;
RT   "Whole genome sequence of Microlunatus phosphovorus NM-1.";
RL   Submitted (MAY-2011) 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}.
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DR   EMBL; AP012204; BAK35555.1; -; Genomic_DNA.
DR   RefSeq; WP_013863424.1; NC_015635.1.
DR   AlphaFoldDB; F5XGS3; -.
DR   STRING; 1032480.MLP_25410; -.
DR   KEGG; mph:MLP_25410; -.
DR   eggNOG; COG0766; Bacteria.
DR   HOGENOM; CLU_027387_0_1_11; -.
DR   OrthoDB; 9803760at2; -.
DR   Proteomes; UP000007947; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IEA:UniProtKB-EC.
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   GO; GO:0019277; P:UDP-N-acetylgalactosamine biosynthetic process; IEA:InterPro.
DR   CDD; cd00093; HTH_XRE; 1.
DR   CDD; cd01555; UdpNAET; 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   InterPro; IPR005750; UDP_GlcNAc_COvinyl_MurA.
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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007947};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAK35555.1}.
FT   DOMAIN          13..67
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50943"
SQ   SEQUENCE   508 AA;  55637 MW;  20F8641E5145EF45 CRC64;
     MTETSLDRIG SLIRDARKHR GLTQTQLASV LGTSQSAVHR IEAGNQNLSL EMVNRIAAAL
     DSPLISVGPS GPVHLRVRGG AKLSGSIEVR SSKNAAVALL CASLLNRGRT VFRGIARIEE
     VNRILEVLTS VGVQATWLNG GADLELVRPA ELDLNAMKVD AARRTRSVIM FLGPLLHSFD
     DFQLPYAGGC DLGARTIEPH LQVLRRFGLE VIATDGFYRC TVDTEVEPTR PITLTERGDT
     VTENALLAAA LSPGETVLRN ASPNYMVQDL CVFLTHLGVE IDGIGTTTLR IRGVHQINTD
     VEFSPSEDPI EAMSLLTAAI VTESEVTIQR VPIEFLEIEL AILEEMGLDF TLSDEYVAAN
     GHTRLVDLTV RPSKLKSPID KIHPMPFPGL NIDNLPFFAV IAATAEGKTV IHDWVYDNRA
     IYMTELNKLG ARVQLLDPYR IIVEGPTRWR GQQVVCPPAL RPAVCILICM LAARGESMLR
     DVYVINRGYE DLANRLNALG ANIEVFRD
//
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