ID MURA_HAEIN Reviewed; 424 AA.
AC P45025;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 27-MAR-2024, entry version 153.
DE RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00111};
DE EC=2.5.1.7 {ECO:0000255|HAMAP-Rule:MF_00111};
DE AltName: Full=Enoylpyruvate transferase {ECO:0000255|HAMAP-Rule:MF_00111};
DE AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000255|HAMAP-Rule:MF_00111};
DE Short=EPT {ECO:0000255|HAMAP-Rule:MF_00111};
GN Name=murA {ECO:0000255|HAMAP-Rule:MF_00111}; Synonyms=murZ;
GN OrderedLocusNames=HI_1081;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2] {ECO:0007744|PDB:3SWE}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP ACTIVE SITE, AND FORMATION OF COVALENT REACTION INTERMEDIATE.
RX PubMed=22378791; DOI=10.1074/jbc.m112.342725;
RA Zhu J.Y., Yang Y., Han H., Betzi S., Olesen S.H., Marsilio F.,
RA Schoenbrunn E.;
RT "Functional consequence of covalent reaction of phosphoenolpyruvate with
RT UDP-N-acetylglucosamine 1-carboxyvinyltransferase (MurA).";
RL J. Biol. Chem. 287:12657-12667(2012).
CC -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
CC acetylglucosamine. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00111};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00111}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00111}.
CC -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00111}.
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DR EMBL; L42023; AAC22737.1; -; Genomic_DNA.
DR PIR; A64182; A64182.
DR RefSeq; NP_439238.1; NC_000907.1.
DR PDB; 2RL1; X-ray; 2.20 A; A=1-424.
DR PDB; 2RL2; X-ray; 2.30 A; A=1-424.
DR PDB; 3SWE; X-ray; 2.20 A; A=1-424.
DR PDBsum; 2RL1; -.
DR PDBsum; 2RL2; -.
DR PDBsum; 3SWE; -.
DR AlphaFoldDB; P45025; -.
DR SMR; P45025; -.
DR STRING; 71421.HI_1081; -.
DR EnsemblBacteria; AAC22737; AAC22737; HI_1081.
DR KEGG; hin:HI_1081; -.
DR PATRIC; fig|71421.8.peg.1126; -.
DR eggNOG; COG0766; Bacteria.
DR HOGENOM; CLU_027387_0_0_6; -.
DR OrthoDB; 9803760at2; -.
DR PhylomeDB; P45025; -.
DR BioCyc; HINF71421:G1GJ1-1116-MONOMER; -.
DR BRENDA; 2.5.1.7; 2529.
DR SABIO-RK; P45025; -.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; P45025; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IBA:GO_Central.
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; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Peptidoglycan synthesis;
KW Pyruvate; Reference proteome; Transferase.
FT CHAIN 1..424
FT /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase"
FT /id="PRO_0000178876"
FT ACT_SITE 117
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111,
FT ECO:0000305|PubMed:22378791"
FT BINDING 22..23
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000305|PubMed:22378791,
FT ECO:0007744|PDB:3SWE"
FT BINDING 93
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|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:0000269|PubMed:22378791,
FT ECO:0007744|PDB:3SWE"
FT BINDING 164..166
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:22378791,
FT ECO:0007744|PDB:3SWE"
FT BINDING 307
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:22378791,
FT ECO:0007744|PDB:3SWE"
FT BINDING 329
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:22378791,
FT ECO:0007744|PDB:3SWE"
FT MOD_RES 117
FT /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111,
FT ECO:0000305|PubMed:22378791"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:2RL1"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:2RL1"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:2RL1"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:2RL1"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2RL1"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:2RL1"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:2RL1"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:2RL2"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2RL1"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:2RL1"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:2RL1"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:2RL1"
FT HELIX 234..245
FT /evidence="ECO:0007829|PDB:2RL1"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:2RL1"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:2RL1"
FT HELIX 262..270
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:2RL1"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:2RL1"
FT HELIX 309..317
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 319..326
FT /evidence="ECO:0007829|PDB:2RL1"
FT HELIX 336..341
FT /evidence="ECO:0007829|PDB:2RL1"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:2RL1"
FT TURN 372..375
FT /evidence="ECO:0007829|PDB:2RL1"
FT HELIX 376..384
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 385..392
FT /evidence="ECO:0007829|PDB:2RL1"
FT HELIX 395..400
FT /evidence="ECO:0007829|PDB:2RL1"
FT HELIX 404..409
FT /evidence="ECO:0007829|PDB:2RL1"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:2RL1"
FT STRAND 415..419
FT /evidence="ECO:0007829|PDB:2RL1"
SQ SEQUENCE 424 AA; 45187 MW; EAB3170DF91F17C3 CRC64;
MDKFRVYGQS RLSGSVNISG AKNAALPILF AAILATEPVK LTNVPELKDI ETTLKILRQL
GVVVDRDATG AVLLDASNIN HFTAPYELVK TMRASIWALA PLVARFHQGQ VSLPGGCSIG
ARPVDLHISG LEKLGADIVL EEGYVKAQVS DRLVGTRIVI EKVSVGATLS IMMAATLAKG
TTVIENAARE PEIVDTADFL NKMGAKITGA GSAHITIEGV ERLTGCEHSV VPDRIETGTF
LIAAAISGGC VVCQNTKADT LDAVIDKLRE AGAQVDVTEN SITLDMLGNR PKAVNIRTAP
HPGFPTDMQA QFTLLNMVAE GTSIITETIF ENRFMHIPEL IRMGGKAEIE GNTAVCHGVE
QLSGTEVIAT DLRASISLVL AGCIATGETI VDRIYHIDRG YEHIEDKLRG LGAKIERFSG
SDEA
//
