MURA_AQUAE
ID MURA_AQUAE Reviewed; 425 AA.
AC O67315;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
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}; OrderedLocusNames=aq_1281;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2] {ECO:0007744|PDB:2YVW}
RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) IN COMPLEX WITH
RP UDP-N-ACETYLGLUCOSAMINE.
RA Kitamura Y., Yokoyama S., Kuramitsu S.;
RT "Crystal structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase
RT from Aquifex aeolicus VF5.";
RL Submitted (APR-2007) to the PDB data bank.
RN [3] {ECO:0007744|PDB:3SWG}
RP X-RAY CRYSTALLOGRAPHY (1.81 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}.
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; AE000657; AAC07268.1; -; Genomic_DNA.
DR PIR; H70410; H70410.
DR RefSeq; NP_213879.1; NC_000918.1.
DR RefSeq; WP_010880817.1; NC_000918.1.
DR PDB; 2YVW; X-ray; 1.81 A; A=1-425.
DR PDB; 3SWG; X-ray; 1.81 A; A=1-425.
DR PDBsum; 2YVW; -.
DR PDBsum; 3SWG; -.
DR AlphaFoldDB; O67315; -.
DR SMR; O67315; -.
DR STRING; 224324.aq_1281; -.
DR EnsemblBacteria; AAC07268; AAC07268; aq_1281.
DR KEGG; aae:aq_1281; -.
DR PATRIC; fig|224324.8.peg.1002; -.
DR eggNOG; COG0766; Bacteria.
DR HOGENOM; CLU_027387_0_0_0; -.
DR InParanoid; O67315; -.
DR OMA; CDPHRAT; -.
DR OrthoDB; 537477at2; -.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; O67315; -.
DR Proteomes; UP000000798; Chromosome.
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; -; 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 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..425
FT /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase"
FT /id="PRO_0000178845"
FT ACT_SITE 124
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111,
FT ECO:0000305|PubMed:22378791"
FT BINDING 31..32
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000305|PubMed:22378791,
FT ECO:0007744|PDB:2YVW, ECO:0007744|PDB:3SWG"
FT BINDING 100
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 129..133
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:22378791,
FT ECO:0007744|PDB:2YVW, ECO:0007744|PDB:3SWG"
FT BINDING 170..172
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:22378791,
FT ECO:0007744|PDB:2YVW, ECO:0007744|PDB:3SWG"
FT BINDING 311
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:22378791,
FT ECO:0007744|PDB:2YVW, ECO:0007744|PDB:3SWG"
FT BINDING 333
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:22378791,
FT ECO:0007744|PDB:2YVW, ECO:0007744|PDB:3SWG"
FT MOD_RES 124
FT /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111,
FT ECO:0000305|PubMed:22378791"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:2YVW"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:2YVW"
FT HELIX 31..40
FT /evidence="ECO:0007829|PDB:2YVW"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:2YVW"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:2YVW"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:2YVW"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:2YVW"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:2YVW"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:2YVW"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:2YVW"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:2YVW"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:2YVW"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:2YVW"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:2YVW"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:2YVW"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:2YVW"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:2YVW"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:2YVW"
FT HELIX 197..208
FT /evidence="ECO:0007829|PDB:2YVW"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:2YVW"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:2YVW"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:2YVW"
FT HELIX 239..251
FT /evidence="ECO:0007829|PDB:2YVW"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:2YVW"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:2YVW"
FT HELIX 267..276
FT /evidence="ECO:0007829|PDB:2YVW"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:2YVW"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:2YVW"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:2YVW"
FT HELIX 310..320
FT /evidence="ECO:0007829|PDB:2YVW"
FT STRAND 323..330
FT /evidence="ECO:0007829|PDB:2YVW"
FT HELIX 339..345
FT /evidence="ECO:0007829|PDB:2YVW"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:2YVW"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:2YVW"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:2YVW"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:2YVW"
FT TURN 376..379
FT /evidence="ECO:0007829|PDB:2YVW"
FT HELIX 380..388
FT /evidence="ECO:0007829|PDB:2YVW"
FT STRAND 389..396
FT /evidence="ECO:0007829|PDB:2YVW"
FT HELIX 399..404
FT /evidence="ECO:0007829|PDB:2YVW"
FT HELIX 408..414
FT /evidence="ECO:0007829|PDB:2YVW"
FT STRAND 419..422
FT /evidence="ECO:0007829|PDB:2YVW"
SQ SEQUENCE 425 AA; 47260 MW; F6E82EDA6CBC0DD5 CRC64;
MKNTTLYTYR DYFVIRGGKP LTGKVKISGA KNAALPIMFA TILTEEPCTI TNVPDLLDVR
NTLLLLRELG AELEFLNNTV FINPSINSFI TNQEIIRRMR ASVLSLGPLL GRFGRAVVGL
PGGCSIGARP IDQHLKFFKE AGADVEVREG YVYVNLKEKR RVHFKFDLVT VTGTENALLY
LASVPEESIL ENIALEPEVM DLIEVLKKMG AHVKVEGRSA YVKGSENLKG FTHSVIPDRI
EAGTFMVGAV LTDGEILLEN ARINHLRAVV EKLKLIGGEV VEENGNLRVF RKESLRACDI
ETQVYPGFPT DMQAQFMALL SVAKGKSRIK ENIFEHRFHH AQELNRLGAN ITVRGNTAYV
EGVERLYGSE VYSTDLRASA SLVLAGLVAQ GETVVRDVYH LDRGYEKLEE KLKKLGADIE
RVSEL
