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Database: UniProt
Entry: A0A0H4VY52_9BORD
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ID   A0A0H4VY52_9BORD        Unreviewed;       433 AA.
AC   A0A0H4VY52;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
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_1 {ECO:0000313|EMBL:AKQ55452.1};
GN   ORFNames=ACR54_02137 {ECO:0000313|EMBL:AKQ55452.1}, CS347_20360
GN   {ECO:0000313|EMBL:AZW18941.1};
OS   Bordetella hinzii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=103855 {ECO:0000313|EMBL:AKQ55452.1, ECO:0000313|Proteomes:UP000036382};
RN   [1] {ECO:0000313|EMBL:AKQ55452.1, ECO:0000313|Proteomes:UP000036382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F582 {ECO:0000313|EMBL:AKQ55452.1,
RC   ECO:0000313|Proteomes:UP000036382};
RX   PubMed=26316634;
RA   Weigand M.R., Changayil S., Kulasekarapandian Y., Tondella M.L.;
RT   "Complete Genome Sequences of Two Bordetella hinzii Strains Isolated from
RT   Humans.";
RL   Genome Announc. 3:e00965-e00915(2015).
RN   [2] {ECO:0000313|Proteomes:UP000036382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F582 {ECO:0000313|Proteomes:UP000036382};
RA   Weigand M.R., Changayil S., Kulasekarapandian Y., Batra D., Williams M.M.,
RA   Tondella M.L.;
RT   "Complete Genome Sequences of Two Bordetella hinzii Isolated from Humans.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000282741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H720 {ECO:0000313|Proteomes:UP000282741};
RA   Weigand M.R., Loparev V., Peng Y., Bowden K.E., Tondella M.L.,
RA   Williams M.M.;
RT   "Whole genome sequencing of various Bordetella species.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AZW18941.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=H720 {ECO:0000313|EMBL:AZW18941.1};
RX   PubMed=31744907;
RA   Weigand M.R., Peng Y., Batra D., Burroughs M., Davis J.K., Knipe K.,
RA   Loparev V.N., Johnson T., Juieng P., Rowe L.A., Sheth M., Tang K.,
RA   Unoarumhi Y., Williams M.M., Tondella M.L.;
RT   "Conserved Patterns of Symmetric Inversion in the Genome Evolution of
RT   Bordetella Respiratory Pathogens.";
RL   mSystems 4:e00702-19(2019).
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; CP012076; AKQ55452.1; -; Genomic_DNA.
DR   EMBL; CP024172; AZW18941.1; -; Genomic_DNA.
DR   RefSeq; WP_029580718.1; NZ_LT906461.1.
DR   STRING; 103855.ACR54_02137; -.
DR   KEGG; bhz:ACR54_02137; -.
DR   PATRIC; fig|103855.14.peg.2066; -.
DR   eggNOG; COG0766; Bacteria.
DR   OrthoDB; 9803760at2; -.
DR   Proteomes; UP000036382; Chromosome.
DR   Proteomes; UP000282741; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   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: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};
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:UP000036382};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AKQ55452.1}.
FT   DOMAIN          7..420
FT                   /note="Enolpyruvate transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00275"
SQ   SEQUENCE   433 AA;  47262 MW;  F9C4A3D378EC02ED CRC64;
     MSHLIVHGGT ALRGKIVPSA NKNAVLPILC ATLLTDQPLR LIGVPEITDV KKILEIFRLL
     GSDVSVDFST GVLELHHRAT AFDPARHHLP EEMRSSIMLV PPLLARFGVA RLENDVKGCT
     LGVREIDPHV EVFERFGARI ERAPASLIVR ADGQMAANDH WLDYASVTTT ENFALCAASA
     RGVSTLVNAA SEPHVQEFCR FLEMLGVPIS GIGTSHLRIE GGRRLGGGEF RFDEDFHEIA
     TFLALGAITG GSITVKNSAP GQFPLIDRTF AKFGVEVEHR DGWSQAHCDG PLRVRRPFTQ
     NILTKVEAAP WPYLPVDLLP IFIALGVRAE GSAMFWNKVY DGAMGWSVEL SKFGAHVFLS
     DPHRLITFGG LPLSPAKVES PYIIRVAIAL LMVAASIEGR SEIINALPIR RAHPNFVENL
     CSVGARVEWA EGE
//
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