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UDP-N-acetylglucosamine 1-carboxyvinyltransferase (EC 2.5.1.7) (Enoylpyruvate transferase) (UDP-N-acetylglucosamine enolpyruvyl transferase) (EPT)

 A0A076JGE3_BIFAD        Unreviewed;       441 AA.
A0A076JGE3;
29-OCT-2014, integrated into UniProtKB/TrEMBL.
29-OCT-2014, sequence version 1.
20-JUN-2018, entry version 35.
RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase {ECO:0000256|HAMAP-Rule:MF_00111};
EC=2.5.1.7 {ECO:0000256|HAMAP-Rule:MF_00111};
AltName: Full=Enoylpyruvate transferase {ECO:0000256|HAMAP-Rule:MF_00111};
AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000256|HAMAP-Rule:MF_00111};
Short=EPT {ECO:0000256|HAMAP-Rule:MF_00111};
Name=murA {ECO:0000256|HAMAP-Rule:MF_00111,
ECO:0000313|EMBL:AVT46061.1};
ORFNames=AAX71_01105 {ECO:0000313|EMBL:KLE28579.1},
AL0124_0202 {ECO:0000313|EMBL:OSG92518.1},
AL0467_0225 {ECO:0000313|EMBL:OSH01170.1},
B0042_0132 {ECO:0000313|EMBL:OSG90070.1},
B0703_0215 {ECO:0000313|EMBL:OSG94963.1},
BADO_0191 {ECO:0000313|EMBL:AII75617.1},
BBK15_01990 {ECO:0000313|EMBL:OFA36285.1},
BBMN23_0209 {ECO:0000313|EMBL:AJE05181.1},
C8077_01015 {ECO:0000313|EMBL:AVT46061.1},
ERS852382_00443 {ECO:0000313|EMBL:CUN46029.1},
ERS852419_00816 {ECO:0000313|EMBL:CUN59844.1},
LU08_05985 {ECO:0000313|EMBL:KIM01412.1};
Bifidobacterium adolescentis.
Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
Bifidobacterium.
NCBI_TaxID=1680 {ECO:0000313|EMBL:AII75617.1, ECO:0000313|Proteomes:UP000028581};
[1] {ECO:0000313|EMBL:AII75617.1, ECO:0000313|Proteomes:UP000028581}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=22L {ECO:0000313|EMBL:AII75617.1,
ECO:0000313|Proteomes:UP000028581};
PubMed=25063659; DOI=10.1128/AEM.01993-14;
Duranti S., Turroni F., Lugli G.A., Milani C., Viappiani A.,
Mangifesta M., Gioiosa L., Palanza P., van Sinderen D., Ventura M.;
"Genomic Characterization and Transcriptional Studies of the Starch-
Utilizing Strain Bifidobacterium adolescentis 22L.";
Appl. Environ. Microbiol. 80:6080-6090(2014).
[2] {ECO:0000313|EMBL:KIM01412.1, ECO:0000313|Proteomes:UP000031974}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IVS-1 {ECO:0000313|EMBL:KIM01412.1,
ECO:0000313|Proteomes:UP000031974};
Frese S.A., Hutkins R.W., Walter J.;
Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|EMBL:AJE05181.1, ECO:0000313|Proteomes:UP000031405}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=BBMN23 {ECO:0000313|EMBL:AJE05181.1,
ECO:0000313|Proteomes:UP000031405};
Ren F., Liu S., Sun E., Wang R.;
"The genome sequence of Bifidobacterium adolescentis BBMN23 reveals
adaptations for complex carbohydrates utilization from the adult
microbiome.";
Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|EMBL:KIM01412.1, ECO:0000313|Proteomes:UP000031974}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IVS-1 {ECO:0000313|EMBL:KIM01412.1,
ECO:0000313|Proteomes:UP000031974};
Krumbeck J.A., Maldonado-Gomez M.X., Martinez I., Burkey T.E.,
Ramer-Tait A., Harris E.N.;
"Introducing the concept of In Vivo Selection to identify probiotic
stains for synergistic synbiotic applications.";
Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000313|EMBL:KLE28579.1, ECO:0000313|Proteomes:UP000035571}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=150 {ECO:0000313|EMBL:KLE28579.1,
ECO:0000313|Proteomes:UP000035571};
Dyachkova M.S., Klimina K.M., Kovtun A.S., Zakharevich N.V.,
Nezametdinova V.Z., Averina O.V., Danilenko V.N.;
"Draft genome sequences of Bifidobacterium angulatum strain 102 and
Bifidobacterium adolescentis strain 150: focusing on the genes
responsible for communication with the host organism.";
Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000313|EMBL:CUN46029.1, ECO:0000313|Proteomes:UP000078409, ECO:0000313|Proteomes:UP000095647}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=2789STDY5608824 {ECO:0000313|EMBL:CUN46029.1,
ECO:0000313|Proteomes:UP000095647}, and
2789STDY5608862 {ECO:0000313|EMBL:CUN59844.1,
ECO:0000313|Proteomes:UP000078409};
Pathogen Informatics;
Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
[7] {ECO:0000313|Proteomes:UP000193179, ECO:0000313|Proteomes:UP000193208, ECO:0000313|Proteomes:UP000193823}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=42B {ECO:0000313|EMBL:OSG90070.1,
ECO:0000313|Proteomes:UP000193823}, 703B {ECO:0000313|EMBL:OSG94963.1,
ECO:0000313|Proteomes:UP000193179},
AL12-4 {ECO:0000313|EMBL:OSG92518.1,
ECO:0000313|Proteomes:UP000193901}, and
AL46-7 {ECO:0000313|EMBL:OSH01170.1,
ECO:0000313|Proteomes:UP000193208};
PubMed=27035119; DOI=.1038/srep23971;
Duranti S., Milani C., Lugli G.A., Mancabelli L., Turroni F.,
Ferrario C., Mangifesta M., Viappiani A., Sanchez B., Margolles A.,
van Sinderen D., Ventura M.;
"Evaluation of genetic diversity among strains of the human gut
commensal Bifidobacterium adolescentis.";
Sci. Rep. 6:23971-23971(2016).
[8] {ECO:0000313|EMBL:OFA36285.1, ECO:0000313|Proteomes:UP000175684}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Km 4 {ECO:0000313|EMBL:OFA36285.1,
ECO:0000313|Proteomes:UP000175684};
Danilenko V.N.;
"Draft Genome Sequence of Bifidobacterium adolescentis strain Km 4.";
Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
[9] {ECO:0000313|EMBL:AVT46061.1, ECO:0000313|Proteomes:UP000241454}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=1-11 {ECO:0000313|EMBL:AVT46061.1,
ECO:0000313|Proteomes:UP000241454};
Keele B.F.;
Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111,
ECO:0000256|SAAS:SAAS00767217}.
-!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + UDP-N-acetyl-alpha-D-
glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-
D-glucosamine. {ECO:0000256|HAMAP-Rule:MF_00111,
ECO:0000256|SAAS:SAAS00767208}.
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
{ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767283}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00111,
ECO:0000256|SAAS:SAAS00767211}.
-!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
{ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767202}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00111}.
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EMBL; CP007443; AII75617.1; -; Genomic_DNA.
EMBL; CP010437; AJE05181.1; -; Genomic_DNA.
EMBL; CP028341; AVT46061.1; -; Genomic_DNA.
EMBL; CYYI01000002; CUN46029.1; -; Genomic_DNA.
EMBL; CYYG01000003; CUN59844.1; -; Genomic_DNA.
EMBL; JRNZ01000027; KIM01412.1; -; Genomic_DNA.
EMBL; LBHQ01000001; KLE28579.1; -; Genomic_DNA.
EMBL; MAXD01000001; OFA36285.1; -; Genomic_DNA.
EMBL; LNKB01000001; OSG90070.1; -; Genomic_DNA.
EMBL; LNKG01000001; OSG92518.1; -; Genomic_DNA.
EMBL; LNKE01000003; OSG94963.1; -; Genomic_DNA.
EMBL; LNKI01000001; OSH01170.1; -; Genomic_DNA.
RefSeq; WP_011742717.1; NZ_MAXD01000001.1.
EnsemblBacteria; AII75617; AII75617; BADO_0191.
EnsemblBacteria; AJE05181; AJE05181; BBMN23_0209.
EnsemblBacteria; KIM01412; KIM01412; LU08_05985.
EnsemblBacteria; KLE28579; KLE28579; AAX71_01105.
EnsemblBacteria; OFA36285; OFA36285; BBK15_01990.
GeneID; 4556371; -.
KEGG; badl:BADO_0191; -.
KEGG; bado:BBMN23_0209; -.
PATRIC; fig|1680.5.peg.214; -.
eggNOG; ENOG4105CDF; Bacteria.
eggNOG; COG0766; LUCA.
KO; K00790; -.
UniPathway; UPA00219; -.
Proteomes; UP000028581; Chromosome.
Proteomes; UP000031405; Chromosome.
Proteomes; UP000031974; Unassembled WGS sequence.
Proteomes; UP000035571; Unassembled WGS sequence.
Proteomes; UP000078409; Unassembled WGS sequence.
Proteomes; UP000095647; Unassembled WGS sequence.
Proteomes; UP000175684; Unassembled WGS sequence.
Proteomes; UP000193179; Unassembled WGS sequence.
Proteomes; UP000193208; Unassembled WGS sequence.
Proteomes; UP000193823; Unassembled WGS sequence.
Proteomes; UP000193901; Unassembled WGS sequence.
Proteomes; UP000241454; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
GO; GO:0019277; P:UDP-N-acetylgalactosamine biosynthetic process; IEA:InterPro.
CDD; cd01555; UdpNAET; 1.
Gene3D; 3.65.10.10; -; 3.
HAMAP; MF_00111; MurA; 1.
InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
InterPro; IPR005750; UDP_GlcNAc_COvinyl_MurA.
Pfam; PF00275; EPSP_synthase; 1.
SUPFAM; SSF55205; SSF55205; 1.
TIGRFAMs; TIGR01072; murA; 1.
3: Inferred from homology;
Cell cycle {ECO:0000256|HAMAP-Rule:MF_00111,
ECO:0000256|SAAS:SAAS00767191};
Cell division {ECO:0000256|HAMAP-Rule:MF_00111,
ECO:0000256|SAAS:SAAS00767191};
Cell shape {ECO:0000256|HAMAP-Rule:MF_00111,
ECO:0000256|SAAS:SAAS00767219};
Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00111,
ECO:0000256|SAAS:SAAS00767261};
Complete proteome {ECO:0000313|Proteomes:UP000028581,
ECO:0000313|Proteomes:UP000031405, ECO:0000313|Proteomes:UP000031974,
ECO:0000313|Proteomes:UP000035571};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00111,
ECO:0000256|SAAS:SAAS00767234};
Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00111,
ECO:0000256|SAAS:SAAS00767219};
Pyruvate {ECO:0000256|HAMAP-Rule:MF_00111};
Transferase {ECO:0000256|HAMAP-Rule:MF_00111,
ECO:0000256|SAAS:SAAS00767179, ECO:0000313|EMBL:AII75617.1}.
DOMAIN 11 433 EPSP_synthase.
{ECO:0000259|Pfam:PF00275}.
REGION 27 28 Phosphoenolpyruvate binding.
{ECO:0000256|HAMAP-Rule:MF_00111}.
ACT_SITE 125 125 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_00111}.
BINDING 101 101 UDP-N-acetylglucosamine.
{ECO:0000256|HAMAP-Rule:MF_00111}.
BINDING 316 316 UDP-N-acetylglucosamine.
{ECO:0000256|HAMAP-Rule:MF_00111}.
BINDING 338 338 UDP-N-acetylglucosamine; via carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_00111}.
MOD_RES 125 125 2-(S-cysteinyl)pyruvic acid O-
phosphothioketal. {ECO:0000256|HAMAP-
Rule:MF_00111}.
SEQUENCE 441 AA; 47303 MW; D826C142BEF63643 CRC64;
MSDNKNDILH VEGGKPLNGT IKVRGAKNFV SKAMVAALLA PGTSVLKNVP EIRDVHVVSD
LLRLHGVDVT VDGANGVVTI DATNVQLADV ADVDTLSGSS RIPILFSGPL LHRLGEAFIP
ALGGCNIGGR PIDFHLETLR KLGANVDKEH KDGIHITAPN GLHGAKIHLP YPSVGATEQT
LLAAVLAEGK TELSGAAIEP EIMDLVSVLQ KMGAIISVDV DRTFRIEGVK ELKGYTHTSL
TDRIEAASWA SAALATHGDI FVKGATQPEM MTFLNVFRKI GGEFDITDKG IRFWHPGGDL
KPVAIETDVH PGFMTDWQQP LVVALTQANG LSIVHETVYE NRFGFTKPLV QMGATIQLYR
ECLGSLPCRF QQRNYKHSAV IFGPTPLTGR DIDVPDLRGG FSHLIAALAA KGPSNVQGIS
LIDRGYADFR GKLEALGADF D


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