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

 K1A8C3_9STRE            Unreviewed;       427 AA.
K1A8C3;
28-NOV-2012, integrated into UniProtKB/TrEMBL.
28-NOV-2012, sequence version 1.
25-OCT-2017, entry version 31.
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};
ORFNames=GMD4S_02149 {ECO:0000313|EMBL:EKA11767.1};
Streptococcus sp. GMD4S.
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=1169673 {ECO:0000313|EMBL:EKA11767.1, ECO:0000313|Proteomes:UP000004724};
[1] {ECO:0000313|EMBL:EKA11767.1, ECO:0000313|Proteomes:UP000004724}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=GMD4S {ECO:0000313|EMBL:EKA11767.1,
ECO:0000313|Proteomes:UP000004724};
PubMed=23493677; DOI=10.1101/gr.142208.112;
Fitzsimons M.S., Novotny M., Lo C.C., Dichosa A.E.,
Yee-Greenbaum J.L., Snook J.P., Gu W., Chertkov O., Davenport K.W.,
McMurry K., Reitenga K.G., Daughton A.R., He J., Johnson S.L.,
Gleasner C.D., Wills P.L., Parson-Quintana B., Chain P.S.,
Detter J.C., Lasken R.S., Han C.S.;
"Nearly finished genomes produced using gel microdroplet culturing
reveal substantial intraspecies genomic diversity within the human
microbiome.";
Genome Res. 23:878-888(2013).
-!- 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}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EKA11767.1}.
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EMBL; AJRE01000031; EKA11767.1; -; Genomic_DNA.
RefSeq; WP_000411919.1; NZ_AJRE01000031.1.
EnsemblBacteria; EKA11767; EKA11767; GMD4S_02149.
PATRIC; fig|1169673.3.peg.407; -.
UniPathway; UPA00219; -.
Proteomes; UP000004724; Unassembled WGS sequence.
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; -; 2.
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:UP000004724};
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:EKA11767.1}.
DOMAIN 11 410 EPSP_synthase.
{ECO:0000259|Pfam:PF00275}.
REGION 23 24 Phosphoenolpyruvate binding.
{ECO:0000256|HAMAP-Rule:MF_00111}.
REGION 125 129 UDP-N-acetylglucosamine binding.
{ECO:0000256|HAMAP-Rule:MF_00111}.
ACT_SITE 120 120 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_00111}.
BINDING 96 96 UDP-N-acetylglucosamine.
{ECO:0000256|HAMAP-Rule:MF_00111}.
BINDING 309 309 UDP-N-acetylglucosamine.
{ECO:0000256|HAMAP-Rule:MF_00111}.
BINDING 331 331 UDP-N-acetylglucosamine; via carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_00111}.
MOD_RES 120 120 2-(S-cysteinyl)pyruvic acid O-
phosphothioketal. {ECO:0000256|HAMAP-
Rule:MF_00111}.
SEQUENCE 427 AA; 46048 MW; D14B2E9A713C5891 CRC64;
MEKIVVQGGD NRLVGSVTIE GAKNAVLPLL AATILASKGK TVLQNVPILS DVFTMNQVVR
GLNAKVDFDE EAHVVEVDAT GDITEEAPYK YVSKMRASIV VLGPILARVG HAKVSMPGGC
TIGSRPIDLH LKGLEAMGAK ITQTAGYIEA KAERLHGAHI YMDFPSVGAT QNLMMAATLA
DGVTVIENAA REPEIVDLAI LLNEMGAKVK GAGTETITVT GVEELHGTTH NVVQDRIEAG
TFMVAAAMTG GDVLVRDAVW EHNRPLISKL LEMGVEVTEE SEGIRVRSQL ENLKAVHVKT
LPHPGFPTDM QAQFTALMTV AKGESTMVET VFENRFQHLE EMRRMGLHSE IIRDTARIVG
GQALQGAEVL STDLRASASL ILTGLVVQGE TVVGKLVHLD RGYYRFHEKL AQLGAKIQRI
EANDEEE


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