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Database: UniProt
Entry: A0A086XY73_9RHOB
LinkDB: A0A086XY73_9RHOB
Original site: A0A086XY73_9RHOB 
ID   A0A086XY73_9RHOB        Unreviewed;       437 AA.
AC   A0A086XY73;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=CN97_02075 {ECO:0000313|EMBL:KFI26973.1};
OS   Haematobacter massiliensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Haematobacter.
OX   NCBI_TaxID=195105 {ECO:0000313|EMBL:KFI26973.1, ECO:0000313|Proteomes:UP000028826};
RN   [1] {ECO:0000313|EMBL:KFI26973.1, ECO:0000313|Proteomes:UP000028826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 47968 {ECO:0000313|EMBL:KFI26973.1,
RC   ECO:0000313|Proteomes:UP000028826};
RA   Wang D., Wang G.;
RT   "Genome of Haematobacter massiliensis CCUG 47968.";
RL   Submitted (MAR-2014) 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:KFI26973.1}.
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DR   EMBL; JGYG01000013; KFI26973.1; -; Genomic_DNA.
DR   RefSeq; WP_035713485.1; NZ_NIPY01000047.1.
DR   AlphaFoldDB; A0A086XY73; -.
DR   STRING; 195105.CN97_02075; -.
DR   eggNOG; COG0766; Bacteria.
DR   OrthoDB; 9803760at2; -.
DR   Proteomes; UP000028826; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; 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   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   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   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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028826};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFI26973.1}.
FT   DOMAIN          12..421
FT                   /note="Enolpyruvate transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00275"
SQ   SEQUENCE   437 AA;  47046 MW;  92FC2A5F0DBB17CE CRC64;
     MYAIIDGGII PRGHVRVSGA KNSATRLLSA ALLSDEPVTL RNFPTELVDV GHKVNFCRKL
     GAEITLDRET EQASISAQAL KSRLLTRNDY DVPIRTTYLL SAAQVLRSGI ARIPYPGGCP
     IGGGSAGGRG YDQHIMVWKA LGAEVTEKDD HIEITAPQGF QGGEIRFSIS TVGGTETALI
     CTAIAKGRSE IYNAYITPEV EDLIAFLRRM GANIEVFGSS HIVVEGRGQP LGGTHMSVMS
     DRIEALTWIV YGILSGGELT VHNVPFESME VPLLHLQQAG IDFFRNSRSV HVTPGCLTSG
     SVQPFELACG AHPGVISDMQ SFYVILALAA AGTSRVYDYR YPERIAFVGE LAKLVQGDHL
     TAERGKITIN GSARFKPGVA DSTDLRGSMA VVMAALCADG RSIINNVHMA LRGYNDLEGK
     LRTIGGRIEV REDRHAA
//
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