ID A0A150L422_9BACI Unreviewed; 436 AA.
AC A0A150L422;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=B4102_1983 {ECO:0000313|EMBL:KYD07038.1}, B5V89_11905
GN {ECO:0000313|EMBL:PTY78172.1};
OS Heyndrickxia sporothermodurans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX NCBI_TaxID=46224 {ECO:0000313|EMBL:KYD07038.1, ECO:0000313|Proteomes:UP000075666};
RN [1] {ECO:0000313|EMBL:KYD07038.1, ECO:0000313|Proteomes:UP000075666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4102 {ECO:0000313|EMBL:KYD07038.1,
RC ECO:0000313|Proteomes:UP000075666};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Genome Sequences of Twelve Sporeforming Bacillus Species Isolated from
RT Foods.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PTY78172.1, ECO:0000313|Proteomes:UP000244181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAD {ECO:0000313|EMBL:PTY78172.1,
RC ECO:0000313|Proteomes:UP000244181};
RA Owusu-Darko R., Allam M., Ismail A., Buys E.;
RT "Whole genome sequence of Bacillus sporothermodurans.";
RL Submitted (MAR-2017) 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 -!- 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, ECO:0000256|HAMAP-
CC Rule:MF_00111};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00111}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00111}.
CC -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
CC {ECO:0000256|ARBA:ARBA00038367, ECO:0000256|HAMAP-Rule:MF_00111}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00111}.
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:KYD07038.1}.
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DR EMBL; LQYN01000046; KYD07038.1; -; Genomic_DNA.
DR EMBL; NAZB01000023; PTY78172.1; -; Genomic_DNA.
DR RefSeq; WP_066231178.1; NZ_NAZB01000023.1.
DR AlphaFoldDB; A0A150L422; -.
DR STRING; 46224.B4102_1983; -.
DR GeneID; 62499126; -.
DR PATRIC; fig|46224.3.peg.2931; -.
DR OrthoDB; 9803760at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000075666; Unassembled WGS sequence.
DR Proteomes; UP000244181; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IEA:UniProtKB-UniRule.
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-UniRule.
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 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 NCBIfam; TIGR01072; murA; 1.
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, ECO:0000256|HAMAP-
KW Rule:MF_00111};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_00111};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_00111};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_00111};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00111};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_00111}; Pyruvate {ECO:0000256|HAMAP-Rule:MF_00111};
KW Reference proteome {ECO:0000313|Proteomes:UP000075666};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00111}.
FT DOMAIN 6..407
FT /note="Enolpyruvate transferase"
FT /evidence="ECO:0000259|Pfam:PF00275"
FT ACT_SITE 117
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT BINDING 22..23
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT BINDING 93
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT BINDING 122..126
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT BINDING 306
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT BINDING 328
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT MOD_RES 117
FT /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
SQ SEQUENCE 436 AA; 47146 MW; 82F08F6ED9D55828 CRC64;
MEKIIVRGGK RLNGTVQVEG AKNAVLPVIA ASLLASEGRS IIRDVPSLSD VYTIGEVLRY
LNADVTFQEN KISVDASREL LIEAPFEYVR KMRASVLVMG PLLARMGRAR VALPGGCAIG
SRPIDLHLKG FEAMGAKVKV GNGFIEAETE GRLKGAKIYL DFPSVGATQN IMMAATLAEG
TSTIENCAKE PEIVDLANYL NKMGASVKGA GTGTIRIEGV ERLYAADHTI IPDRIEAGTF
MIAAAITGGN VLVKGAVPEH LTSLIAKLEE MGVTIIEEEQ GLRVIGPEKL KAVDIKTMPH
PGFPTDMQSQ MMSLLVVAEG TGMITETVFE NRFMHVEEFR RMNSDIKIEG RSVIINGPCQ
LQGAEVSATD LRAAAALIIA GLRADGYTRV TELKHLDRGY LNFHQKLASL GADIERVNDE
VEVTTTNRKE FLSEQL
//