ID   A0A414E3H3_9FIRM        Unreviewed;       430 AA.
AC   A0A414E3H3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   05-JUN-2019, entry version 2.
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   ORFNames=DW802_02875 {ECO:0000313|EMBL:RHD24463.1};
OS   Ruminococcus bromii.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Ruminococcus.
OX   NCBI_TaxID=40518 {ECO:0000313|EMBL:RHD24463.1, ECO:0000313|Proteomes:UP000284544};
RN   [1] {ECO:0000313|EMBL:RHD24463.1, ECO:0000313|Proteomes:UP000284544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM32-13AC {ECO:0000313|EMBL:RHD24463.1,
RC   ECO:0000313|Proteomes:UP000284544};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut
RT   microbiota.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
CC       acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111,
CC       ECO:0000256|SAAS:SAAS00767217}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine =
CC         phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-
CC         glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483;
CC         EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111,
CC         ECO:0000256|SAAS:SAAS01124343};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767283}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00111,
CC       ECO:0000256|SAAS:SAAS00767211}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767202}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00111}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:RHD24463.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QSIY01000001; RHD24463.1; -; Genomic_DNA.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000284544; Unassembled WGS sequence.
DR   CDD; cd01555; UdpNAET; 1.
DR   Gene3D; 3.65.10.10; -; 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   Pfam; PF00275; EPSP_synthase; 1.
DR   SUPFAM; SSF55205; SSF55205; 1.
DR   TIGRFAMs; TIGR01072; murA; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767221};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767191};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767246};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767261};
KW   Complete proteome {ECO:0000313|Proteomes:UP000284544};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767234};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767219};
KW   Pyruvate {ECO:0000256|HAMAP-Rule:MF_00111};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767179, ECO:0000313|EMBL:RHD24463.1}.
FT   DOMAIN        6    407       EPSP_synthase. {ECO:0000259|Pfam:
FT                                PF00275}.
FT   REGION       22     23       Phosphoenolpyruvate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   REGION      122    126       UDP-N-acetylglucosamine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   ACT_SITE    117    117       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00111}.
FT   BINDING      93     93       UDP-N-acetylglucosamine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   BINDING     307    307       UDP-N-acetylglucosamine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   BINDING     329    329       UDP-N-acetylglucosamine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00111}.
FT   MOD_RES     117    117       2-(S-cysteinyl)pyruvic acid O-
FT                                phosphothioketal. {ECO:0000256|HAMAP-
FT                                Rule:MF_00111}.
SQ   SEQUENCE   430 AA;  46109 MW;  D88DEDA4E0068359 CRC64;
     MEKFVVTGGK PLSGEVTISG AKNAAVAIIP AVILCDEPCQ IENIPNISDV SLISRILQQM
     GANVRRINRS SLYIDPTKIR TCNAVTDLVR GMRASYYLLG ALLGKYGKAK VALPGGCNFG
     VRPIDQHLKG FEALGATTQL VDGAIIEAEC DRLVGTHVYL DVVSVGATMN IMLAASKAKG
     QTIIENAARE PHIVDLANFL NSMGADVRGA GTDVIKIRGV EYLHGITYSI IPDQIEAGTY
     MCAAAATRGC ITVKNITPKH LESISAKLRE MGVKITEYDE ALKVDASSAP LKRCNIKTMP
     HPGFPTDCQP QFAALLMSVP GTSIINENVW DNRYQYVSEL IRMGAQISVE GRLAIIEGGV
     PLTAAPVKAT DLRAGAAMII AALEINGTTE ISNIQFIERG YEDVVEKFRG LGADIKKVYF
     TGDNEQELGA
//