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Multifunctional fusion protein [Includes: UDP-N-acetylglucosamine 1-carboxyvinyltransferase (EC 2.5.1.7) (Enoylpyruvate transferase) (UDP-N-acetylglucosamine enolpyruvyl transferase) (EPT); ATP phosphoribosyltransferase (ATP-PRT) (ATP-PRTase) (EC 2.4.2.17)]

 A0A1Q7X5H0_9BACT        Unreviewed;       613 AA.
A0A1Q7X5H0;
12-APR-2017, integrated into UniProtKB/TrEMBL.
12-APR-2017, sequence version 1.
28-MAR-2018, entry version 12.
RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|HAMAP-Rule:MF_01018};
Includes:
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};
Includes:
RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01018};
Short=ATP-PRT {ECO:0000256|HAMAP-Rule:MF_01018};
Short=ATP-PRTase {ECO:0000256|HAMAP-Rule:MF_01018};
EC=2.4.2.17 {ECO:0000256|HAMAP-Rule:MF_01018};
Name=murA {ECO:0000256|HAMAP-Rule:MF_00111};
Synonyms=hisG {ECO:0000256|HAMAP-Rule:MF_01018};
ORFNames=AUG00_05740 {ECO:0000313|EMBL:OLE38257.1};
Candidatus Rokubacteria bacterium 13_1_20CM_2_70_7.
Bacteria; Candidatus Rokubacteria.
NCBI_TaxID=1805343 {ECO:0000313|EMBL:OLE38257.1, ECO:0000313|Proteomes:UP000186129};
[1] {ECO:0000313|EMBL:OLE38257.1, ECO:0000313|Proteomes:UP000186129}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=27843720;
Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C.,
Singh A., Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G.,
Northen T., Pan C., Banfield J.F.;
"Proteogenomic analyses indicate bacterial methylotrophy and archaeal
heterotrophy are prevalent below the grass root zone.";
PeerJ 4:E2687-E2687(2016).
-!- FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1-
diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a
crucial role in the pathway because the rate of histidine
biosynthesis seems to be controlled primarily by regulation of
HisG enzymatic activity. {ECO:0000256|HAMAP-Rule:MF_01018}.
-!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111,
ECO:0000256|SAAS:SAAS00767217}.
-!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
= ATP + 5-phospho-alpha-D-ribose 1-diphosphate.
{ECO:0000256|HAMAP-Rule:MF_01018}.
-!- 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: Amino-acid biosynthesis; L-histidine biosynthesis; L-
histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
{ECO:0000256|HAMAP-Rule:MF_01018}.
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
{ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767283}.
-!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
{ECO:0000256|HAMAP-Rule:MF_01018}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00111,
ECO:0000256|SAAS:SAAS00767211}.
-!- DOMAIN: Lacks the C-terminal regulatory region which is replaced
by HisZ. {ECO:0000256|HAMAP-Rule:MF_01018}.
-!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family.
Short subfamily. {ECO:0000256|HAMAP-Rule:MF_01018}.
-!- 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:OLE38257.1}.
-----------------------------------------------------------------------
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EMBL; MNJV01000086; OLE38257.1; -; Genomic_DNA.
UniPathway; UPA00031; UER00006.
UniPathway; UPA00219; -.
Proteomes; UP000186129; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
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:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
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; cd13595; PBP2_HisGs; 1.
CDD; cd01555; UdpNAET; 1.
Gene3D; 3.65.10.10; -; 3.
HAMAP; MF_01018; HisG_Short; 1.
HAMAP; MF_00111; MurA; 1.
InterPro; IPR013820; ATP_PRibTrfase_cat.
InterPro; IPR018198; ATP_PRibTrfase_CS.
InterPro; IPR024893; ATP_PRibTrfase_HisG_short.
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.
Pfam; PF01634; HisG; 1.
SUPFAM; SSF55205; SSF55205; 1.
TIGRFAMs; TIGR00070; hisG; 1.
TIGRFAMs; TIGR01072; murA; 1.
PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01018};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01018};
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:UP000186129};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00111,
ECO:0000256|SAAS:SAAS00767234};
Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01018};
Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01018};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01018};
Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00111,
ECO:0000256|SAAS:SAAS00767219};
Pyruvate {ECO:0000256|HAMAP-Rule:MF_00111};
Reference proteome {ECO:0000313|Proteomes:UP000186129};
Transferase {ECO:0000256|HAMAP-Rule:MF_01018}.
DOMAIN 8 396 EPSP_synthase.
{ECO:0000259|Pfam:PF00275}.
DOMAIN 450 605 HisG. {ECO:0000259|Pfam:PF01634}.
REGION 23 24 Phosphoenolpyruvate binding.
{ECO:0000256|HAMAP-Rule:MF_00111}.
REGION 122 126 UDP-N-acetylglucosamine binding.
{ECO:0000256|HAMAP-Rule:MF_00111}.
ACT_SITE 117 117 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_00111}.
BINDING 93 93 UDP-N-acetylglucosamine.
{ECO:0000256|HAMAP-Rule:MF_00111}.
BINDING 305 305 UDP-N-acetylglucosamine.
{ECO:0000256|HAMAP-Rule:MF_00111}.
BINDING 327 327 UDP-N-acetylglucosamine; via carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_00111}.
MOD_RES 117 117 2-(S-cysteinyl)pyruvic acid O-
phosphothioketal. {ECO:0000256|HAMAP-
Rule:MF_00111}.
SEQUENCE 613 AA; 65426 MW; 28470648369116CF CRC64;
MPARLVIEGG VPLRGSVAVS AAKNAALPAL TAGLLTVEPL VFTNVPDLQD VRTMIRLLET
LGAAVDRAGA RVRVRVERVT SEVAPYELVS TMRASVLVLG PLVARHGTAR VALPGGCAIG
VRPIDQHLKG LTRLGAEITI ENGYVVARAS RLKGARIATD LVTVTGTENL MMAAALAEGT
TVIENAAREP EVVDLADVLN AMGARIHGAG TVRIEIEGVA DLGGTTHTIV PDRIEAGTVI
VAGAITGGDV TVTGLVPDHV SAVLAKLEEC GVALEVGPGR VRVCGPERPR PADVTTSPFP
GFPTDMQAQL MTLLGLADGQ SRVTETIFEN RFMHAAELVR MGASIETEGS TAIIRGVPFY
QGAPVMASDL RASAALVLAG LAARGRTEVS RVYHLAARMR ERLTLALPKG RLLDGALGLL
RELGVDGVDA ESRRLIFTDT RRGLRMLFLK PADIPAYVTY GAADLGIVGR DILLEQEPDV
YEPLDLGFGF CRLVVAEPRE LWERDDPAKW SWVRVATKYP RMAERYFSER GIQVEIVRLD
GSIELAPLVG LAERIVDLVQ SGETLRVNGL VEVAEIARST ARVIVNRASM KTEHAAVTGL
IEEMRARTTK VGR


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