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Conserved domains on  [gi|616915692|gb|KAH06841|]
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UDP-N-acetylglucosamine 1-carboxyvinyltransferase 2 [Staphylococcus aureus VET1738S]

Protein Classification

UDP-N-acetylglucosamine 1-carboxyvinyltransferase( domain architecture ID 10793701)

UDP-N-acetylglucosamine 1-carboxyvinyltransferase catalyzes enolpyruvyl transfer as part of the first step in the biosynthesis of peptidoglycan

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK12830 PRK12830
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
3-419 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed


:

Pssm-ID: 183779  Cd Length: 417  Bit Score: 744.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692   3 QEVIKIRGGRTLNGEVNISGAKNSAVAIIPATLLAQGHVKLEGLPQISDVKTLVSLLEDLNIKASLNGTELEVDTTEIQN 82
Cdd:PRK12830   1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDTLEIDPTGIQS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  83 AALPNNKVESLRASYYMMGTMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSTtSMKIEAKELKGAHIFLD 162
Cdd:PRK12830  81 MPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGG-AIYLKADELKGAHIYLD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 163 MVSVGATINIMLAAVYATGQTVIENAAKEPEVVDVANFLTSMGANIKGAGTSTIKINGVKELHGSEYQVIPDRIEAGTYM 242
Cdd:PRK12830 160 VVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAGTYM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 243 CIAAACGENVILNNIVPKHVETLTAKFSELGVNVDVRDERIRINNNAPYQFVDIKTLVYPGFATDLQQPITPLLFMANGP 322
Cdd:PRK12830 240 ILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGNLKAVDIKTLPYPGFATDLQQPLTPLLLKANGR 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 323 SFVTDTIYPERFKHVEELKRMGANIEVDEGTATIK-PSTLHGADVYASDLRAGACLIIAGLIAEGVTTIYNVKHIYRGYT 401
Cdd:PRK12830 320 SVVTDTIYEKRFKHVDELKRMGANIKVEGRSAIITgPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDRGYS 399
                        410
                 ....*....|....*...
gi 616915692 402 DIVEHLKALGADIWTETV 419
Cdd:PRK12830 400 NIIEKLKALGADIWREED 417
 
Name Accession Description Interval E-value
PRK12830 PRK12830
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
3-419 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed


Pssm-ID: 183779  Cd Length: 417  Bit Score: 744.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692   3 QEVIKIRGGRTLNGEVNISGAKNSAVAIIPATLLAQGHVKLEGLPQISDVKTLVSLLEDLNIKASLNGTELEVDTTEIQN 82
Cdd:PRK12830   1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDTLEIDPTGIQS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  83 AALPNNKVESLRASYYMMGTMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSTtSMKIEAKELKGAHIFLD 162
Cdd:PRK12830  81 MPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGG-AIYLKADELKGAHIYLD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 163 MVSVGATINIMLAAVYATGQTVIENAAKEPEVVDVANFLTSMGANIKGAGTSTIKINGVKELHGSEYQVIPDRIEAGTYM 242
Cdd:PRK12830 160 VVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAGTYM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 243 CIAAACGENVILNNIVPKHVETLTAKFSELGVNVDVRDERIRINNNAPYQFVDIKTLVYPGFATDLQQPITPLLFMANGP 322
Cdd:PRK12830 240 ILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGNLKAVDIKTLPYPGFATDLQQPLTPLLLKANGR 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 323 SFVTDTIYPERFKHVEELKRMGANIEVDEGTATIK-PSTLHGADVYASDLRAGACLIIAGLIAEGVTTIYNVKHIYRGYT 401
Cdd:PRK12830 320 SVVTDTIYEKRFKHVDELKRMGANIKVEGRSAIITgPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDRGYS 399
                        410
                 ....*....|....*...
gi 616915692 402 DIVEHLKALGADIWTETV 419
Cdd:PRK12830 400 NIIEKLKALGADIWREED 417
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
4-415 0e+00

UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine enolpyruvyl transferase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440529  Cd Length: 416  Bit Score: 624.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692   4 EVIKIRGGRTLNGEVNISGAKNSAVAIIPATLLAQGHVKLEGLPQISDVKTLVSLLEDLNIKAS-LNGTELEVDTTEIQN 82
Cdd:COG0766    2 DKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVErDDGGTLTIDASNINS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  83 AALPNNKVESLRASYYMMGTMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSTtSMKIEAKELKGAHIFLD 162
Cdd:COG0766   82 TEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHG-YIEARAGRLKGARIYLD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 163 MVSVGATINIMLAAVYATGQTVIENAAKEPEVVDVANFLTSMGANIKGAGTSTIKINGVKELHGSEYQVIPDRIEAGTYM 242
Cdd:COG0766  161 FPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGTFL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 243 CIAAACGENVILNNIVPKHVETLTAKFSELGVNVDVRDERIRINNNAPYQFVDIKTLVYPGFATDLQQPITPLLFMANGP 322
Cdd:COG0766  241 VAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQAEGT 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 323 SFVTDTIYPERFKHVEELKRMGANIEVDEGTATIK-PSTLHGADVYASDLRAGACLIIAGLIAEGVTTIYNVKHIYRGYT 401
Cdd:COG0766  321 SVITETVFENRFMHVDELNRMGADIKLDGHTAIVRgVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDRGYE 400
                        410
                 ....*....|....
gi 616915692 402 DIVEHLKALGADIW 415
Cdd:COG0766  401 NLEEKLRALGADIE 414
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
14-410 0e+00

UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the first step in the biosynthesis of peptidoglycan, a component of the bacterial cell wall. The reaction is phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine = phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine. This enzyme is of interest as a potential target for anti-bacterial agents. The only other known enolpyruvyl transferase is the related 5-enolpyruvylshikimate-3-phosphate synthase.


Pssm-ID: 238796  Cd Length: 400  Bit Score: 591.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  14 LNGEVNISGAKNSAVAIIPATLLAQGHVKLEGLPQISDVKTLVSLLEDLNIKASLNGT-ELEVDTTEIQNAALPNNKVES 92
Cdd:cd01555    1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGEnTLVIDASNINSTEAPYELVRK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  93 LRASYYMMGTMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSTTSMKIEAKELKGAHIFLDMVSVGATINI 172
Cdd:cd01555   81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAAGRLKGARIYLDFPSVGATENI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 173 MLAAVYATGQTVIENAAKEPEVVDVANFLTSMGANIKGAGTSTIKINGVKELHGSEYQVIPDRIEAGTYMCIAAACGENV 252
Cdd:cd01555  161 MMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGDI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 253 ILNNIVPKHVETLTAKFSELGVNVDVRDERIRI-NNNAPYQFVDIKTLVYPGFATDLQQPITPLLFMANGPSFVTDTIYP 331
Cdd:cd01555  241 TVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVdGDGGRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIFE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 332 ERFKHVEELKRMGANIEVDEGTATIK-PSTLHGADVYASDLRAGACLIIAGLIAEGVTTIYNVKHIYRGYTDIVEHLKAL 410
Cdd:cd01555  321 NRFMHVDELNRMGADIKVEGNTAIIRgVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLRAL 400
murA TIGR01072
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ...
3-415 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 162190 [Multi-domain]  Cd Length: 416  Bit Score: 530.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692    3 QEVIKIRGGRTLNGEVNISGAKNSAVAIIPATLLAQGHVKLEGLPQISDVKTLVSLLEDLNIKASLNGTELEVDTTEIQN 82
Cdd:TIGR01072   1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNINS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692   83 AALPNNKVESLRASYYMMGTMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEID-ESSTTSMKIEAKeLKGAHIFL 161
Cdd:TIGR01072  81 TEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIViEDGYVYASAKGR-LVGAHIVL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  162 DMVSVGATINIMLAAVYATGQTVIENAAKEPEVVDVANFLTSMGANIKGAGTSTIKINGVKELHGSEYQVIPDRIEAGTY 241
Cdd:TIGR01072 160 DKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  242 MCIAAACGENVILNNIVPKHVETLTAKFSELGVNVDVRDERIRINNNAP-YQFVDIKTLVYPGFATDLQQPITPLLFMAN 320
Cdd:TIGR01072 240 LVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQKrLKAVDIETLPYPGFPTDLQAQFMALLSQAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  321 GPSFVTDTIYPERFKHVEELKRMGANIEVDEGTATIK-PSTLHGADVYASDLRAGACLIIAGLIAEGVTTIYNVKHIYRG 399
Cdd:TIGR01072 320 GTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHgVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDRG 399
                         410
                  ....*....|....*.
gi 616915692  400 YTDIVEHLKALGADIW 415
Cdd:TIGR01072 400 YEDLEEKLRALGAKIE 415
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
9-407 6.31e-89

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 275.72  E-value: 6.31e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692    9 RGGRTLNGEVNISG-AKNSAVAIIPATLLAqGHVKLEGLPQISDVKTLVSLLEDL---NIKASLNGTELEVDTTEIQNAA 84
Cdd:pfam00275   1 TGGSRLSGEVKIPGsKSNSHRALILAALAA-GESTITNLLDSDDTLTMLEALRALgaeIIKLDDEKSVVIVEGLGGSFEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692   85 lPNNKVESLRASYYMMGTMLGRF--KKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESS---TTSMKIEAKELKGAHI 159
Cdd:pfam00275  80 -PEDLVLDMGNSGTALRPLTGRLalQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREgynYAPLKVRGLRLGGIHI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  160 FLDMVSVGATINIMLAAVYATGQTVIENAAKEPEVVDVANFLTSMGANIKGAGTST-IKINGVKELHGSEYQVIPDRIEA 238
Cdd:pfam00275 159 DGDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLPGQEYRVEGDRSSA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  239 GTYMCIAAACGENVILNNIVPKHVETLTA---KFSELGVNVDVRDERIRINNNAPYQF--VDIKTLVYPGFATDLQQPIT 313
Cdd:pfam00275 239 AYFLVAAAITGGTVTVENVGINSLQGDEAlleILEKMGAEITQEEDADIVVGPPGLRGkaVDIRTAPDPAPTTAVLAAFA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  314 PLLFMANGPSFVTDTIYPERFKHVEELKRMGANIEVDEGTATIKPST--LHGADVYAS-DLRAGACLIIAGLIAEGVTTI 390
Cdd:pfam00275 319 EGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVkeLKGAEVDSYgDHRIAMALALAGLVAEGETII 398
                         410
                  ....*....|....*..
gi 616915692  391 YNVKHIYRGYTDIVEHL 407
Cdd:pfam00275 399 DDIECTDRSFPDFEEKL 415
 
Name Accession Description Interval E-value
PRK12830 PRK12830
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
3-419 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed


Pssm-ID: 183779  Cd Length: 417  Bit Score: 744.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692   3 QEVIKIRGGRTLNGEVNISGAKNSAVAIIPATLLAQGHVKLEGLPQISDVKTLVSLLEDLNIKASLNGTELEVDTTEIQN 82
Cdd:PRK12830   1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDTLEIDPTGIQS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  83 AALPNNKVESLRASYYMMGTMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSTtSMKIEAKELKGAHIFLD 162
Cdd:PRK12830  81 MPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGG-AIYLKADELKGAHIYLD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 163 MVSVGATINIMLAAVYATGQTVIENAAKEPEVVDVANFLTSMGANIKGAGTSTIKINGVKELHGSEYQVIPDRIEAGTYM 242
Cdd:PRK12830 160 VVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAGTYM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 243 CIAAACGENVILNNIVPKHVETLTAKFSELGVNVDVRDERIRINNNAPYQFVDIKTLVYPGFATDLQQPITPLLFMANGP 322
Cdd:PRK12830 240 ILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGNLKAVDIKTLPYPGFATDLQQPLTPLLLKANGR 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 323 SFVTDTIYPERFKHVEELKRMGANIEVDEGTATIK-PSTLHGADVYASDLRAGACLIIAGLIAEGVTTIYNVKHIYRGYT 401
Cdd:PRK12830 320 SVVTDTIYEKRFKHVDELKRMGANIKVEGRSAIITgPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDRGYS 399
                        410
                 ....*....|....*...
gi 616915692 402 DIVEHLKALGADIWTETV 419
Cdd:PRK12830 400 NIIEKLKALGADIWREED 417
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
4-415 0e+00

UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine enolpyruvyl transferase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440529  Cd Length: 416  Bit Score: 624.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692   4 EVIKIRGGRTLNGEVNISGAKNSAVAIIPATLLAQGHVKLEGLPQISDVKTLVSLLEDLNIKAS-LNGTELEVDTTEIQN 82
Cdd:COG0766    2 DKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVErDDGGTLTIDASNINS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  83 AALPNNKVESLRASYYMMGTMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSTtSMKIEAKELKGAHIFLD 162
Cdd:COG0766   82 TEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHG-YIEARAGRLKGARIYLD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 163 MVSVGATINIMLAAVYATGQTVIENAAKEPEVVDVANFLTSMGANIKGAGTSTIKINGVKELHGSEYQVIPDRIEAGTYM 242
Cdd:COG0766  161 FPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGTFL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 243 CIAAACGENVILNNIVPKHVETLTAKFSELGVNVDVRDERIRINNNAPYQFVDIKTLVYPGFATDLQQPITPLLFMANGP 322
Cdd:COG0766  241 VAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQAEGT 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 323 SFVTDTIYPERFKHVEELKRMGANIEVDEGTATIK-PSTLHGADVYASDLRAGACLIIAGLIAEGVTTIYNVKHIYRGYT 401
Cdd:COG0766  321 SVITETVFENRFMHVDELNRMGADIKLDGHTAIVRgVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDRGYE 400
                        410
                 ....*....|....
gi 616915692 402 DIVEHLKALGADIW 415
Cdd:COG0766  401 NLEEKLRALGADIE 414
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
14-410 0e+00

UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the first step in the biosynthesis of peptidoglycan, a component of the bacterial cell wall. The reaction is phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine = phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine. This enzyme is of interest as a potential target for anti-bacterial agents. The only other known enolpyruvyl transferase is the related 5-enolpyruvylshikimate-3-phosphate synthase.


Pssm-ID: 238796  Cd Length: 400  Bit Score: 591.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  14 LNGEVNISGAKNSAVAIIPATLLAQGHVKLEGLPQISDVKTLVSLLEDLNIKASLNGT-ELEVDTTEIQNAALPNNKVES 92
Cdd:cd01555    1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGEnTLVIDASNINSTEAPYELVRK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  93 LRASYYMMGTMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSTTSMKIEAKELKGAHIFLDMVSVGATINI 172
Cdd:cd01555   81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAAGRLKGARIYLDFPSVGATENI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 173 MLAAVYATGQTVIENAAKEPEVVDVANFLTSMGANIKGAGTSTIKINGVKELHGSEYQVIPDRIEAGTYMCIAAACGENV 252
Cdd:cd01555  161 MMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGDI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 253 ILNNIVPKHVETLTAKFSELGVNVDVRDERIRI-NNNAPYQFVDIKTLVYPGFATDLQQPITPLLFMANGPSFVTDTIYP 331
Cdd:cd01555  241 TVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVdGDGGRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIFE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 332 ERFKHVEELKRMGANIEVDEGTATIK-PSTLHGADVYASDLRAGACLIIAGLIAEGVTTIYNVKHIYRGYTDIVEHLKAL 410
Cdd:cd01555  321 NRFMHVDELNRMGADIKVEGNTAIIRgVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLRAL 400
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
4-415 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 585.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692   4 EVIKIRGGRTLNGEVNISGAKNSAVAIIPATLLAQGHVKLEGLPQISDVKTLVSLLEDLNIKASLNGT-ELEVDTTEIQN 82
Cdd:PRK09369   2 DKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNgTVTIDASNINN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  83 AALPNNKVESLRASYYMMGTMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSTTsmkIEAK---ELKGAHI 159
Cdd:PRK09369  82 TEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGY---VEAKadgRLKGAHI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 160 FLDMVSVGATINIMLAAVYATGQTVIENAAKEPEVVDVANFLTSMGANIKGAGTSTIKINGVKELHGSEYQVIPDRIEAG 239
Cdd:PRK09369 159 VLDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 240 TYMCIAAACGENVILNNIVPKHVETLTAKFSELGVNVDVRDERIRINNNAPYQFVDIKTLVYPGFATDLQQPITPLLFMA 319
Cdd:PRK09369 239 TFLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQA 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 320 NGPSFVTDTIYPERFKHVEELKRMGANIEVDEGTATIK-PSTLHGADVYASDLRAGACLIIAGLIAEGVTTIYNVKHIYR 398
Cdd:PRK09369 319 EGTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRgVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDR 398
                        410
                 ....*....|....*..
gi 616915692 399 GYTDIVEHLKALGADIW 415
Cdd:PRK09369 399 GYERIEEKLRALGADIE 415
murA TIGR01072
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ...
3-415 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 162190 [Multi-domain]  Cd Length: 416  Bit Score: 530.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692    3 QEVIKIRGGRTLNGEVNISGAKNSAVAIIPATLLAQGHVKLEGLPQISDVKTLVSLLEDLNIKASLNGTELEVDTTEIQN 82
Cdd:TIGR01072   1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNINS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692   83 AALPNNKVESLRASYYMMGTMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEID-ESSTTSMKIEAKeLKGAHIFL 161
Cdd:TIGR01072  81 TEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIViEDGYVYASAKGR-LVGAHIVL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  162 DMVSVGATINIMLAAVYATGQTVIENAAKEPEVVDVANFLTSMGANIKGAGTSTIKINGVKELHGSEYQVIPDRIEAGTY 241
Cdd:TIGR01072 160 DKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  242 MCIAAACGENVILNNIVPKHVETLTAKFSELGVNVDVRDERIRINNNAP-YQFVDIKTLVYPGFATDLQQPITPLLFMAN 320
Cdd:TIGR01072 240 LVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQKrLKAVDIETLPYPGFPTDLQAQFMALLSQAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  321 GPSFVTDTIYPERFKHVEELKRMGANIEVDEGTATIK-PSTLHGADVYASDLRAGACLIIAGLIAEGVTTIYNVKHIYRG 399
Cdd:TIGR01072 320 GTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHgVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDRG 399
                         410
                  ....*....|....*.
gi 616915692  400 YTDIVEHLKALGADIW 415
Cdd:TIGR01072 400 YEDLEEKLRALGAKIE 415
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
9-407 6.31e-89

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 275.72  E-value: 6.31e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692    9 RGGRTLNGEVNISG-AKNSAVAIIPATLLAqGHVKLEGLPQISDVKTLVSLLEDL---NIKASLNGTELEVDTTEIQNAA 84
Cdd:pfam00275   1 TGGSRLSGEVKIPGsKSNSHRALILAALAA-GESTITNLLDSDDTLTMLEALRALgaeIIKLDDEKSVVIVEGLGGSFEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692   85 lPNNKVESLRASYYMMGTMLGRF--KKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESS---TTSMKIEAKELKGAHI 159
Cdd:pfam00275  80 -PEDLVLDMGNSGTALRPLTGRLalQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREgynYAPLKVRGLRLGGIHI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  160 FLDMVSVGATINIMLAAVYATGQTVIENAAKEPEVVDVANFLTSMGANIKGAGTST-IKINGVKELHGSEYQVIPDRIEA 238
Cdd:pfam00275 159 DGDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLPGQEYRVEGDRSSA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  239 GTYMCIAAACGENVILNNIVPKHVETLTA---KFSELGVNVDVRDERIRINNNAPYQF--VDIKTLVYPGFATDLQQPIT 313
Cdd:pfam00275 239 AYFLVAAAITGGTVTVENVGINSLQGDEAlleILEKMGAEITQEEDADIVVGPPGLRGkaVDIRTAPDPAPTTAVLAAFA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  314 PLLFMANGPSFVTDTIYPERFKHVEELKRMGANIEVDEGTATIKPST--LHGADVYAS-DLRAGACLIIAGLIAEGVTTI 390
Cdd:pfam00275 319 EGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVkeLKGAEVDSYgDHRIAMALALAGLVAEGETII 398
                         410
                  ....*....|....*..
gi 616915692  391 YNVKHIYRGYTDIVEHL 407
Cdd:pfam00275 399 DDIECTDRSFPDFEEKL 415
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
14-410 1.05e-74

Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine enolpyruvyl transferase. Both enzymes catalyze the reaction of enolpyruvyl transfer.


Pssm-ID: 238795  Cd Length: 408  Bit Score: 238.66  E-value: 1.05e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  14 LNGEVNISGAKNSAVAIIPATLLAQGHVKLEGLPQISDVKTLVSLLEDLNIKASLNGTELEVDTTEI---QNAALPNNKV 90
Cdd:cd01554    1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKDGVITIQGVGMaglKAPQNALNLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  91 ESLRASYYMMGTMLGRFKKcvIGLPGGCPLGPRPIDQHIKGFKALGAEI---DESSTTSMKIEAKELKGAHIFLDMVSVG 167
Cdd:cd01554   81 NSGTAIRLISGVLAGADFE--VELFGDDSLSKRPMDRVTLPLKKMGASIsgqEERDLPPLLKGGKNLGPIHYEDPIASAQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 168 ATINIMLAAVYATGQTVIENAAKEPEVVDVANFLTSMGANIKGAGTSTIKINGVKELHGSEYQVIPDRIEAGTYMCIAAA 247
Cdd:cd01554  159 VKSALMFAALLAKGETVIIEAAKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQKYVVPGDISSAAFFLVAAAI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 248 CGENVILNNIVPKHVET-LTAKFSELGVNVDVRDERIRINNNAPyQFVDIKTLVYPgFATDLQQPITPLLFMANGPSFVT 326
Cdd:cd01554  239 APGRLVLQNVGINETRTgIIDVLRAMGAKIEIGEDTISVESSDL-KATEICGALIP-RLIDELPIIALLALQAQGTTVIK 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 327 DTIYPE------RFKHVEELKRMGANIEVDEGTATIK-PSTLHGADVYA-SDLRAGACLIIAGLIAEGVTTIYNVKHIYR 398
Cdd:cd01554  317 DAEELKvketdrIFVVADELNSMGADIEPTADGMIIKgKEKLHGARVNTfGDHRIGMMTALAALVADGEVELDRAEAINT 396
                        410
                 ....*....|..
gi 616915692 399 GYTDIVEHLKAL 410
Cdd:cd01554  397 SYPSFFDDLESL 408
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
14-410 1.46e-22

EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase (5-enolpyruvylshikimate-3-phosphate synthase) (EC 2.5.1.19) catalyses the reaction between shikimate-3-phosphate (S3P) and phosphoenolpyruvate (PEP) to form 5-enolpyruvylshkimate-3-phosphate (EPSP), an intermediate in the shikimate pathway leading to aromatic amino acid biosynthesis. The reaction is phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. It is found in bacteria and plants but not animals. The enzyme is the target of the widely used herbicide glyphosate, which has been shown to occupy the active site. In bacteria and plants, it is a single domain protein, while in fungi, the domain is found as part of a multidomain protein with functions that are all part of the shikimate pathway.


Pssm-ID: 238797  Cd Length: 409  Bit Score: 98.78  E-value: 1.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  14 LNGEVNISGAKN-SAVAIIPAtLLAQGHVKLEGLPQISDVKTLVSLLEDLNIKASLNGTELEVDTTEIQNaaLPNNKV-- 90
Cdd:cd01556    1 LSGEITVPGSKSiSHRALLLA-ALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVEIVGGGGLG--LPPEAVld 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  91 --ESLRASYYMMGTMLGRFKKCVIGlpGGCPLGPRPIDQHIKGFKALGAEID--ESSTTSMKIEAKELKGAHIFLDM-VS 165
Cdd:cd01556   78 cgNSGTTMRLLTGLLALQGGDSVLT--GDESLRKRPMGRLVDALRQLGAEIEgrEGGGYPPLIGGGGLKGGEVEIPGaVS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 166 ---VGAtinIMLAAVYATGQTVIENAAKEPEV-VDV-ANFLTSMGANIKGAGTSTIKINGVKELHGSEYQVIPDrIEAGT 240
Cdd:cd01556  156 sqfKSA---LLLAAPLAEGPTTIIIGELESKPyIDHtERMLRAFGAEVEVDGYRTITVKGGQKYKGPEYTVEGD-ASSAA 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 241 YMcIAAAC--GENVILNNIVPKHVETLTAK-FSELGVNVDVRDER-IRINNNAPYQFVDIKtlvyPGFATDLQQPITPLL 316
Cdd:cd01556  232 FF-LAAAAitGSEIVIKNVGLNSGDTGIIDvLKEMGADIEIGNEDtVVVESGGKLKGIDID----GNDIPDEAPTLAVLA 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 317 FMANGPSFVTDtIYPERFKH-------VEELKRMGANIEVDEGTATIKPSTLHGADVYAS---DLRAGACLIIAGLIAEG 386
Cdd:cd01556  307 AFAEGPTRIRN-AAELRVKEsdriaamATELRKLGADVEETEDGLIIEGGPLKGAGVEVYtygDHRIAMSFAIAGLVAEG 385
                        410       420
                 ....*....|....*....|....
gi 616915692 387 VTTIYNVKHIYRGYTDIVEHLKAL 410
Cdd:cd01556  386 GVTIEDPECVAKSFPNFFEDLESL 409
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
4-410 6.81e-17

5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; 5-enolpyruvylshikimate-3-phosphate synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439898  Cd Length: 421  Bit Score: 82.06  E-value: 6.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692   4 EVIKIRGGRTLNGEVNISGAKN-SAVAIIPAtLLAQGHVKLEGLPQISDVKTLVSLLEDLNIKAS-LNGTELEVdttEIQ 81
Cdd:COG0128    2 SSLTIAPPSPLKGTVRVPGSKSiSHRALLLA-ALAEGESTIRNLLESDDTLATLEALRALGAEIEeLDGGTLRV---TGV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  82 NAALPNNKV-----ESlrasyymmGTMLgRFkkcVIGLPGGCP----------LGPRPIDQHIKGFKALGAEIDESSTTS 146
Cdd:COG0128   78 GGGLKEPDAvldcgNS--------GTTM-RL---LTGLLALQPgevvltgdesLRKRPMGRLLDPLRQLGARIESRGGGY 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 147 --MKIEAKELKGAHIFLD-MVS---VGAtinIMLAAVYATGQTVIENAAKEPEV--VDVA-NFLTSMGANIKGAGTSTIK 217
Cdd:COG0128  146 lpLTIRGGPLKGGEYEIPgSASsqfKSA---LLLAGPLAEGGLEITVTGELESKpyRDHTeRMLRAFGVEVEVEGYRRFT 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 218 INGVKELHGSEYQVIPDRIEAGTYMCIAAACGENVILNNiVPKH--------VETLTakfsELGVNVDVRDERIRINNnA 289
Cdd:COG0128  223 VPGGQRYRPGDYTVPGDISSAAFFLAAAAITGSEVTVEG-VGLNstqgdtgiLDILK----EMGADIEIENDGITVRG-S 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 290 PYQFVDIKtlvyPGFATDLQQPITPLLFMANGPSFVTDtIYPERFKH-------VEELKRMGANIEVDEGTATIKPST-L 361
Cdd:COG0128  297 PLKGIDID----LSDIPDEAPTLAVLAAFAEGTTRIRG-AAELRVKEsdriaamATELRKLGADVEETEDGLIIEGGPkL 371
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 616915692 362 HGADV--YAsDLRAGACLIIAGLIAEGVTTIYNVKHIYRGYTDIVEHLKAL 410
Cdd:COG0128  372 KGAEVdsYG-DHRIAMAFAVAGLRAEGPVTIDDAECVAKSFPDFFELLESL 421
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
16-413 3.54e-16

3-phosphoshikimate 1-carboxyvinyltransferase; This model represents 3-phosphoshikimate-1-carboxyvinyltransferase (aroA), which catalyzes the sixth of seven steps in the shikimate pathway of the biosynthesis of chorimate. Chorismate is last common precursor of all three aromatic amino acids. Sequences scoring between the trusted and noise cutoffs include fragmentary and aberrant sequences in which generally well-conserved motifs are missing or altererd, but no example of a protein known to have a different function. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 273574  Cd Length: 409  Bit Score: 79.63  E-value: 3.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692   16 GEVNISGAKNSAVAIIPATLLAQGHVKLEGLPQISDVKTLVSLLEDLNIKASLNGTELEVD--TTEIQNAAL-PNNKVES 92
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAVIEgvGGKEPQAELdLGNSGTT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692   93 LRasyYMMGTM-LGRFKKCVIGLPGgcpLGPRPIDQHIKGFKALGAEIDESSTTS---MKIEAKeLKGAHIFLD-MVSVG 167
Cdd:TIGR01356  81 AR---LLTGVLaLADGEVVLTGDES---LRKRPMGRLVDALRQLGAEISSLEGGGslpLTISGP-LPGGIVYISgSASSQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  168 ATINIMLAAVYATGQT---VIENAAKEPEVVDVANFLTSMGANIKGAGTSTIKINGVKELHGSEYQVIPDRIEAGTYMCI 244
Cdd:TIGR01356 154 YKSALLLAAPALQAVGitiVGEPLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKYGPQGYDVPGDYSSAAFFLAA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  245 AAACGENVILNNIVPKHVET---LTAKFSELGVNVDVRDERIRINNNAPYQFV--DIKTLvypgfaTDLQQPITPLLFMA 319
Cdd:TIGR01356 234 AAITGGRVTLENLGINPTQGdkaIIIVLEEMGADIEVEEDDLIVEGASGLKGIkiDMDDM------IDELPTLAVLAAFA 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  320 NGPSFVTDtIYPERFKH-------VEELKRMGANIEVDEGTATIKPS-TLHGADVYA-SDLRAGACLIIAGLIAEGVTTI 390
Cdd:TIGR01356 308 EGVTRITG-AEELRVKEsdriaaiAEELRKLGVDVEEFEDGLYIRGKkELKGAVVDTfGDHRIAMAFAVAGLVAEGEVLI 386
                         410       420
                  ....*....|....*....|...
gi 616915692  391 YNVKHIYRGYTDIVEHLKALGAD 413
Cdd:TIGR01356 387 DDPECVAKSFPSFFDVLERLGAN 409
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
6-414 1.17e-15

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 78.26  E-value: 1.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692   6 IKIRGGRTLNGEVNISGAKN-SAVAIIPAtLLAQGHVKLEGLPQISDVKTLVSLLEDLnikaslnGTELEVDTTEIQNAA 84
Cdd:PRK02427   5 LLIIPPSPLSGTVRVPGSKSiSHRALLLA-ALAEGETTITNLLRSEDTLATLNALRAL-------GVEIEDDEVVVEGVG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  85 LPNNKVeslRASYYMMG----TMlgRFkkcVIGLPGGCP----------LGPRPIDQHIKGFKALGAEID--ESSTTSMK 148
Cdd:PRK02427  77 GGGLKE---PEDVLDCGnsgtTM--RL---LTGLLALQPgevvltgdesLRKRPMGRLLDPLRQMGAKIEgrDEGYLPLT 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 149 IE-AKELKGAHIFLDM----VSvGAtinIMLAAVYATGQTVIEnaAKEPEV----VDV-ANFLTSMGANIK---GAGTST 215
Cdd:PRK02427 149 IRgGKKGGPIEYDGPVssqfVK-SL---LLLAPLFAEGDTETT--VIEPLPsrphTEItLRMLRAFGVEVEnveGWGYRR 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 216 IKINGVKELHGSEYQVIPDrIEAGTYMcIAAAC---GENVILNNiVPKH--------VETLTakfsELGVNVDVRDERIR 284
Cdd:PRK02427 223 IVIKGGQRLRGQDITVPGD-PSSAAFF-LAAAAitgGSEVTITN-VGLNstqggkaiIDVLE----KMGADIEIENEREG 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 285 INNNAPyqfVDIKTLVYPGF------ATDLQQPITPLLFMANGPSFVTDtIYPERFKH-------VEELKRMGANIEVDE 351
Cdd:PRK02427 296 GEPVGD---IRVRSSELKGIdidipdIIDEAPTLAVLAAFAEGTTVIRN-AEELRVKEtdriaamATELRKLGAEVEETE 371
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616915692 352 GTATIKPSTLHGA-DVYAsDLRAGACLIIAGLIAEGVTTIYNVKHIYRGYTDIVEHLKALGADI 414
Cdd:PRK02427 372 DGLIITGGPLAGVvDSYG-DHRIAMAFAIAGLAAEGPVTIDDPECVAKSFPDFFEDLASLGANI 434
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
129-418 2.20e-14

5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; 5-enolpyruvylshikimate-3-phosphate synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439898  Cd Length: 421  Bit Score: 74.35  E-value: 2.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 129 IKGFKALGAEIDESSTTSMKIE--AKELKGAHIFLDMVSVGATINIMLAAVYATGQTVI----ENAAKEP--EVVDVanf 200
Cdd:COG0128   54 LEALRALGAEIEELDGGTLRVTgvGGGLKEPDAVLDCGNSGTTMRLLTGLLALQPGEVVltgdESLRKRPmgRLLDP--- 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 201 LTSMGANIKGAGTST--IKINGVKeLHGSEY--------QVIpdrieagTYMCIAAACGEN----VILNNIVPK----HV 262
Cdd:COG0128  131 LRQLGARIESRGGGYlpLTIRGGP-LKGGEYeipgsassQFK-------SALLLAGPLAEGgleiTVTGELESKpyrdHT 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 263 ETLTAKFselGVNVDVRDE-RIRINNNAPYQFVDIKtlVyPG------FatdlqqpitpllFMANG---PSFVT------ 326
Cdd:COG0128  203 ERMLRAF---GVEVEVEGYrRFTVPGGQRYRPGDYT--V-PGdissaaF------------FLAAAaitGSEVTvegvgl 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 327 DTIYPE-RFkhVEELKRMGANIEVDEGTATIKPSTLHGADVyasDLRAGACLI----IAGLIAEGVTTIYNVKHIyRGY- 400
Cdd:COG0128  265 NSTQGDtGI--LDILKEMGADIEIENDGITVRGSPLKGIDI---DLSDIPDEAptlaVLAAFAEGTTRIRGAAEL-RVKe 338
                        330       340
                 ....*....|....*....|..
gi 616915692 401 TD----IVEHLKALGADIwTET 418
Cdd:COG0128  339 SDriaaMATELRKLGADV-EET 359
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
129-414 6.66e-13

3-phosphoshikimate 1-carboxyvinyltransferase; This model represents 3-phosphoshikimate-1-carboxyvinyltransferase (aroA), which catalyzes the sixth of seven steps in the shikimate pathway of the biosynthesis of chorimate. Chorismate is last common precursor of all three aromatic amino acids. Sequences scoring between the trusted and noise cutoffs include fragmentary and aberrant sequences in which generally well-conserved motifs are missing or altererd, but no example of a protein known to have a different function. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 273574  Cd Length: 409  Bit Score: 69.61  E-value: 6.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  129 IKGFKALGAEIdESSTTSMKIEAKELKGAHIFLDMVSVGATINIMLAAVYATGQTVI----ENAAKEPeVVDVANFLTSM 204
Cdd:TIGR01356  41 LDALRALGAKI-EDGGEVAVIEGVGGKEPQAELDLGNSGTTARLLTGVLALADGEVVltgdESLRKRP-MGRLVDALRQL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  205 GANI---KGAGTSTIKINGVKELhGSEY-------QVIpdrieagTYMCIAAAC----GENVILNNIVPK-HVETLTAKF 269
Cdd:TIGR01356 119 GAEIsslEGGGSLPLTISGPLPG-GIVYisgsassQYK-------SALLLAAPAlqavGITIVGEPLKSRpYIEITLDLL 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692  270 SELGVNVDVRDER-IRINNNAPYQFVDIKTlvyPGfatDLQQPITPLLFMANGPSFVT------DTIYPERfKHVEELKR 342
Cdd:TIGR01356 191 GSFGVEVERSDGRkIVVPGGQKYGPQGYDV---PG---DYSSAAFFLAAAAITGGRVTlenlgiNPTQGDK-AIIIVLEE 263
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616915692  343 MGANIEVDEGTATIK-PSTLHGADVYASDLrAGACLIIAGL--IAEGVTTIYNVKHIYRGYTD----IVEHLKALGADI 414
Cdd:TIGR01356 264 MGADIEVEEDDLIVEgASGLKGIKIDMDDM-IDELPTLAVLaaFAEGVTRITGAEELRVKESDriaaIAEELRKLGVDV 341
EPT_RTPC-like cd01553
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ...
233-410 5.34e-10

This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate cyclase family (RTPC). These 2 families differ in that EPT is formed by 3 repeats of an alpha-beta structural domain while RTPC has 3 similar repeats with a 4th slightly different domain inserted between the 2nd and 3rd repeat. They evidently share the same active site location, although the catalytic residues differ.


Pssm-ID: 238794  Cd Length: 211  Bit Score: 58.83  E-value: 5.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 233 PDRIEAGTYMCIAAACGENVILNNIVP---------KHVETLTAKFSELGVNVDV---RDERIRINNNAPyQFVDIKTLV 300
Cdd:cd01553    8 GGGQILRSFLVLAAISGGPITVTGIRPdrakpgllrQHLTFLKALEKICGATVEGgelGSDRISFRPGTV-RGGDVRFAI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915692 301 YP-GFATDLQQPITPLLFMANGPSFVTDTIYPE----------RFKHVEELKRMGANIEVDEGTATIKPSTLHG------ 363
Cdd:cd01553   87 GSaGSCTDVLQTILPLLLFAKGPTRLTVTGGTDnpsappadfiRFVLEPELAKIGAHQEETLLRHGFYPAGGGVvatevs 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 616915692 364 --ADVYASDLRAGACLIIAGliaeGVTTIYNVKHIYRGYTDIVEHLKAL 410
Cdd:cd01553  167 pvEKLNTAQLRQLVLPMLLA----SGAVEFTVAHPSCHLLTNFAVLEAL 211
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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