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Database: UniProt
Entry: B6AKN9_9BACT
LinkDB: B6AKN9_9BACT
Original site: B6AKN9_9BACT 
ID   B6AKN9_9BACT            Unreviewed;       442 AA.
AC   B6AKN9;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   24-JAN-2024, entry version 68.
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=CGL2_11364005 {ECO:0000313|EMBL:EDZ40143.1};
OS   Leptospirillum sp. Group II '5-way CG'.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Leptospirillum.
OX   NCBI_TaxID=419541 {ECO:0000313|EMBL:EDZ40143.1};
RN   [1] {ECO:0000313|EMBL:EDZ40143.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14961025; DOI=10.1038/nature02340;
RA   Tyson G.W., Chapman J., Hugenholtz P., Allen E.E., Ram R.J.,
RA   Richardson P.M., Solovyev V.V., Rubin E.M., Rokhsar D.S., Banfield J.F.;
RT   "Community structure and metabolism through reconstruction of microbial
RT   genomes from the environment.";
RL   Nature 428:37-43(2004).
RN   [2] {ECO:0000313|EMBL:EDZ40143.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18651792; DOI=10.1371/journal.pbio.0060177;
RA   Simmons S.L., Dibartolo G., Denef V.J., Goltsman D.S., Thelen M.P.,
RA   Banfield J.F.;
RT   "Population genomic analysis of strain variation in Leptospirillum group II
RT   bacteria involved in acid mine drainage formation.";
RL   PLoS Biol. 6:E177-E177(2008).
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}.
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DR   EMBL; DS995259; EDZ40143.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6AKN9; -.
DR   UniPathway; UPA00219; -.
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|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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00111}.
FT   DOMAIN          8..426
FT                   /note="Enolpyruvate transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00275"
FT   ACT_SITE        137
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         113
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT   BINDING         325
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT   BINDING         347
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         137
FT                   /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
SQ   SEQUENCE   442 AA;  47480 MW;  9D3BD4E7DEEFB2C8 CRC64;
     MDRFHIVGGS PLRGEVIVSG SKNSALPILF SSLLGGGLEI SNVPSLRDIR TAFSLLSQLG
     IRAEPLVSAD PEKTDLTNGT SYHTNDGWPG KYRLVEESIE AHEAPYDLVR TMRASILCLG
     PLLARRKRGR VSLPGGCLIG ARPVDIHLNA FVRMGAKISI DHGYIDAHTS GLTGCDIHLP
     YPTVTGTENI LMAATLARGT TRIFNAAQEP EVSDLAFSLI ARGARIEGIG TSSIKVTGVD
     SLFEAPYTVM SDRIEAGTFL VAGALLGEDL TIRNVDVSCL DSLLGTLRDI GADFQEKNGS
     VSISRIRKPR GTSARTEPYP GFPTDMQAQI LPLMAIAEGP STVVETVFEN RFTHVMEMNR
     MGANIDIHGS RAFVRGGASL EGASVMASDL RASAGLVLAA LIAKGESEIQ RVYHIDRGYE
     RIETKLESIG ARIKRVRGEE IS
//
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