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Database: UniProt
Entry: D3E575_GEOS4
LinkDB: D3E575_GEOS4
Original site: D3E575_GEOS4 
ID   D3E575_GEOS4            Unreviewed;       427 AA.
AC   D3E575;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 79.
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   OrderedLocusNames=GYMC10_1819 {ECO:0000313|EMBL:ACX64102.1};
OS   Geobacillus sp. (strain Y412MC10).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=481743 {ECO:0000313|EMBL:ACX64102.1, ECO:0000313|Proteomes:UP000002381};
RN   [1] {ECO:0000313|Proteomes:UP000002381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y412MC10 {ECO:0000313|Proteomes:UP000002381};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Brumm P., Mead D.;
RT   "Complete sequence of Geobacillus sp. Y412MC10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACX64102.1, ECO:0000313|Proteomes:UP000002381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y412MC10 {ECO:0000313|EMBL:ACX64102.1,
RC   ECO:0000313|Proteomes:UP000002381};
RX   PubMed=23408395; DOI=10.4056/sigs.2605792;
RA   Mead D.A., Lucas S., Copeland A., Lapidus A., Cheng J.F., Bruce D.C.,
RA   Goodwin L.A., Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C.S.,
RA   Tapia R., Land M., Hauser L.J., Chang Y.J., Kyrpides N.C., Ivanova N.N.,
RA   Ovchinnikova G., Woyke T., Brumm C., Hochstein R., Schoenfeld T., Brumm P.;
RT   "Complete Genome Sequence of Paenibacillus strain Y4.12MC10, a Novel
RT   Paenibacillus lautus strain Isolated from Obsidian Hot Spring in
RT   Yellowstone National Park.";
RL   Stand. Genomic Sci. 6:381-400(2012).
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; CP001793; ACX64102.1; -; Genomic_DNA.
DR   RefSeq; WP_015734238.1; NC_013406.1.
DR   AlphaFoldDB; D3E575; -.
DR   STRING; 481743.GYMC10_1819; -.
DR   KEGG; gym:GYMC10_1819; -.
DR   HOGENOM; CLU_027387_0_0_9; -.
DR   OMA; TTHYYPG; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002381; 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; 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          7..404
FT                   /note="Enolpyruvate transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00275"
FT   ACT_SITE        116
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         92
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT   BINDING         305
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT   BINDING         327
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         116
FT                   /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
SQ   SEQUENCE   427 AA;  46103 MW;  C2BB23956A020A52 CRC64;
     MDKLVIEGGR PLSGTIRIHG AKNAALPILA ASLLAEGTVR LSNVPHLLDI EVMLSILGRL
     GSKCKHELET VTVDTSSANS FHVPEDLMKQ MRSSIFLMGP LLARFGEVTI YQPGGCAIGE
     RKIDLHLKGL QALGAEIEES NDKIHCRASR LIGTDIHLDF ASVGATENIM MAAATALGTT
     VLTNAAREPE IQDLQHFLNK MGANIIGAGT DTITIHGVER LEPCEYEIIP DRIVAGTVMI
     AAAVTRGSVT LTKTNPSHLT SLIHVLKRAG VQTSICNDII NISCMSRPKA VERIVTSPYP
     SFPTDLQSQV MVLLSLADGF SVMKETVFEG RFKHVEELSR MGADISTDLN YAFIRGVQRI
     YGATVEATDL RAGAALVIAG LAAQGTTVVE QVHHIDRGYD RIENMFQGLG ARIYRQTPVP
     KPLDLAN
//
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