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Conserved domains on  [gi|488391868|ref|WP_002461253|]
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MULTISPECIES: UDP-N-acetylglucosamine 1-carboxyvinyltransferase [Staphylococcus]

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
3-421 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed


:

Pssm-ID: 183779  Cd Length: 417  Bit Score: 742.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868   3 QEVIKIRGGQTLKGEVNISGAKNSAVAIIPATLLAQGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDTVLEVDTTEIKN 82
Cdd:PRK12830   1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDTLEIDPTGIQS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  83 APLPNNKVESLRASYYMMGAMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSDtSMKIEAKELIGTTIFLD 162
Cdd:PRK12830  81 MPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGG-AIYLKADELKGAHIYLD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 163 MVSVGATINIMLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTSTLKIKGVDALHGSEYQVIPDRIEAGTYM 242
Cdd:PRK12830 160 VVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAGTYM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 243 CMAAACGQEVKINNIVPKHVEALMVKLQELGVDITVEDEYAIIKGKAKYKNVDIKTLVYPGFATDLQQPITPLLFKASGP 322
Cdd:PRK12830 240 ILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGNLKAVDIKTLPYPGFATDLQQPLTPLLLKANGR 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 323 SFVTETIYPARFKHVEELQHMGANIEADEvtGTATIK-PSTLHGTEVYASDLRAGACLIIAGLIAEGVTTIYNVKHIYRG 401
Cdd:PRK12830 320 SVVTDTIYEKRFKHVDELKRMGANIKVEG--RSAIITgPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDRG 397
                        410       420
                 ....*....|....*....|
gi 488391868 402 YTDIVEHLEQLGADIWTEKV 421
Cdd:PRK12830 398 YSNIIEKLKALGADIWREED 417
 
Name Accession Description Interval E-value
PRK12830 PRK12830
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
3-421 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed


Pssm-ID: 183779  Cd Length: 417  Bit Score: 742.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868   3 QEVIKIRGGQTLKGEVNISGAKNSAVAIIPATLLAQGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDTVLEVDTTEIKN 82
Cdd:PRK12830   1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDTLEIDPTGIQS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  83 APLPNNKVESLRASYYMMGAMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSDtSMKIEAKELIGTTIFLD 162
Cdd:PRK12830  81 MPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGG-AIYLKADELKGAHIYLD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 163 MVSVGATINIMLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTSTLKIKGVDALHGSEYQVIPDRIEAGTYM 242
Cdd:PRK12830 160 VVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAGTYM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 243 CMAAACGQEVKINNIVPKHVEALMVKLQELGVDITVEDEYAIIKGKAKYKNVDIKTLVYPGFATDLQQPITPLLFKASGP 322
Cdd:PRK12830 240 ILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGNLKAVDIKTLPYPGFATDLQQPLTPLLLKANGR 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 323 SFVTETIYPARFKHVEELQHMGANIEADEvtGTATIK-PSTLHGTEVYASDLRAGACLIIAGLIAEGVTTIYNVKHIYRG 401
Cdd:PRK12830 320 SVVTDTIYEKRFKHVDELKRMGANIKVEG--RSAIITgPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDRG 397
                        410       420
                 ....*....|....*....|
gi 488391868 402 YTDIVEHLEQLGADIWTEKV 421
Cdd:PRK12830 398 YSNIIEKLKALGADIWREED 417
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
4-417 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: 620.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868   4 EVIKIRGGQTLKGEVNISGAKNSAVAIIPATLLAQGKVQLDGLPQISDVETLVSLLEDLNIK-TQLNDTVLEVDTTEIKN 82
Cdd:COG0766    2 DKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKvERDDGGTLTIDASNINS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  83 APLPNNKVESLRASYYMMGAMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSDtSMKIEAKELIGTTIFLD 162
Cdd:COG0766   82 TEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHG-YIEARAGRLKGARIYLD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 163 MVSVGATINIMLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTSTLKIKGVDALHGSEYQVIPDRIEAGTYM 242
Cdd:COG0766  161 FPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGTFL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 243 CMAAACGQEVKINNIVPKHVEALMVKLQELGVDITVEDEYAIIKGKAKYKNVDIKTLVYPGFATDLQQPITPLLFKASGP 322
Cdd:COG0766  241 VAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQAEGT 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 323 SFVTETIYPARFKHVEELQHMGANIEADEvtGTATIK-PSTLHGTEVYASDLRAGACLIIAGLIAEGVTTIYNVKHIYRG 401
Cdd:COG0766  321 SVITETVFENRFMHVDELNRMGADIKLDG--HTAIVRgVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDRG 398
                        410
                 ....*....|....*.
gi 488391868 402 YTDIVEHLEQLGADIW 417
Cdd:COG0766  399 YENLEEKLRALGADIE 414
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
14-412 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: 578.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  14 LKGEVNISGAKNSAVAIIPATLLAQGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDT-VLEVDTTEIKNAPLPNNKVES 92
Cdd:cd01555    1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGEnTLVIDASNINSTEAPYELVRK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  93 LRASYYMMGAMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSDTSMKIEAKELIGTTIFLDMVSVGATINI 172
Cdd:cd01555   81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAAGRLKGARIYLDFPSVGATENI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 173 MLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTSTLKIKGVDALHGSEYQVIPDRIEAGTYMCMAAACGQEV 252
Cdd:cd01555  161 MMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGDI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 253 KINNIVPKHVEALMVKLQELGVDITVEDEYAIIKGKAK-YKNVDIKTLVYPGFATDLQQPITPLLFKASGPSFVTETIYP 331
Cdd:cd01555  241 TVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGGrLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIFE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 332 ARFKHVEELQHMGANIEADEvtGTATIK-PSTLHGTEVYASDLRAGACLIIAGLIAEGVTTIYNVKHIYRGYTDIVEHLE 410
Cdd:cd01555  321 NRFMHVDELNRMGADIKVEG--NTAIIRgVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLR 398

                 ..
gi 488391868 411 QL 412
Cdd:cd01555  399 AL 400
murA TIGR01072
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ...
3-417 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: 517.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868    3 QEVIKIRGGQTLKGEVNISGAKNSAVAIIPATLLAQGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDTVLEVDTTEIKN 82
Cdd:TIGR01072   1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNINS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868   83 APLPNNKVESLRASYYMMGAMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIdESSDTSMKIEAKE-LIGTTIFL 161
Cdd:TIGR01072  81 TEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEI-VIEDGYVYASAKGrLVGAHIVL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  162 DMVSVGATINIMLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTSTLKIKGVDALHGSEYQVIPDRIEAGTY 241
Cdd:TIGR01072 160 DKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  242 MCMAAACGQEVKINNIVPKHVEALMVKLQELGVDITV-EDEYAIIKGKAKYKNVDIKTLVYPGFATDLQQPITPLLFKAS 320
Cdd:TIGR01072 240 LVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVdENGIRVDMRQKRLKAVDIETLPYPGFPTDLQAQFMALLSQAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  321 GPSFVTETIYPARFKHVEELQHMGANIEADevTGTATIK-PSTLHGTEVYASDLRAGACLIIAGLIAEGVTTIYNVKHIY 399
Cdd:TIGR01072 320 GTSVITETVFENRFMHVDELIRMGANIKLE--GNTAVIHgVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLD 397
                         410
                  ....*....|....*...
gi 488391868  400 RGYTDIVEHLEQLGADIW 417
Cdd:TIGR01072 398 RGYEDLEEKLRALGAKIE 415
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
9-409 3.38e-91

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 281.49  E-value: 3.38e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868    9 RGGQTLKGEVNISG-AKNSAVAIIPATLLAqGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDTVLEVDTTE--IKNAPL 85
Cdd:pfam00275   1 TGGSRLSGEVKIPGsKSNSHRALILAALAA-GESTITNLLDSDDTLTMLEALRALGAEIIKLDDEKSVVIVEglGGSFEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868   86 PNNKVESLRASYYMMGAMLGRF--KKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSD---TSMKIEAKELIGTTIF 160
Cdd:pfam00275  80 PEDLVLDMGNSGTALRPLTGRLalQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGynyAPLKVRGLRLGGIHID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  161 LDMVSVGATINIMLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTST-LKIKGVDALHGSEYQVIPDRIEAG 239
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLPGQEYRVEGDRSSAA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  240 TYMCMAAACGQEVKINNIVPKHV---EALMVKLQELGVDITVEDEYAIIKGKAKY--KNVDIKTLVYPGFATDLQQPITP 314
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDADIVVGPPGLrgKAVDIRTAPDPAPTTAVLAAFAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  315 LLFKASGPSFVTETIYPARFKHVEELQHMGANIEADEVTGTATIKPSTLHGTEVYAS-DLRAGACLIIAGLIAEGVTTIY 393
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKELKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
                         410
                  ....*....|....*.
gi 488391868  394 NVKHIYRGYTDIVEHL 409
Cdd:pfam00275 400 DIECTDRSFPDFEEKL 415
 
Name Accession Description Interval E-value
PRK12830 PRK12830
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
3-421 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed


Pssm-ID: 183779  Cd Length: 417  Bit Score: 742.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868   3 QEVIKIRGGQTLKGEVNISGAKNSAVAIIPATLLAQGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDTVLEVDTTEIKN 82
Cdd:PRK12830   1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDTLEIDPTGIQS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  83 APLPNNKVESLRASYYMMGAMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSDtSMKIEAKELIGTTIFLD 162
Cdd:PRK12830  81 MPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGG-AIYLKADELKGAHIYLD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 163 MVSVGATINIMLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTSTLKIKGVDALHGSEYQVIPDRIEAGTYM 242
Cdd:PRK12830 160 VVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAGTYM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 243 CMAAACGQEVKINNIVPKHVEALMVKLQELGVDITVEDEYAIIKGKAKYKNVDIKTLVYPGFATDLQQPITPLLFKASGP 322
Cdd:PRK12830 240 ILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGNLKAVDIKTLPYPGFATDLQQPLTPLLLKANGR 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 323 SFVTETIYPARFKHVEELQHMGANIEADEvtGTATIK-PSTLHGTEVYASDLRAGACLIIAGLIAEGVTTIYNVKHIYRG 401
Cdd:PRK12830 320 SVVTDTIYEKRFKHVDELKRMGANIKVEG--RSAIITgPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDRG 397
                        410       420
                 ....*....|....*....|
gi 488391868 402 YTDIVEHLEQLGADIWTEKV 421
Cdd:PRK12830 398 YSNIIEKLKALGADIWREED 417
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
4-417 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: 620.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868   4 EVIKIRGGQTLKGEVNISGAKNSAVAIIPATLLAQGKVQLDGLPQISDVETLVSLLEDLNIK-TQLNDTVLEVDTTEIKN 82
Cdd:COG0766    2 DKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKvERDDGGTLTIDASNINS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  83 APLPNNKVESLRASYYMMGAMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSDtSMKIEAKELIGTTIFLD 162
Cdd:COG0766   82 TEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHG-YIEARAGRLKGARIYLD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 163 MVSVGATINIMLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTSTLKIKGVDALHGSEYQVIPDRIEAGTYM 242
Cdd:COG0766  161 FPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGTFL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 243 CMAAACGQEVKINNIVPKHVEALMVKLQELGVDITVEDEYAIIKGKAKYKNVDIKTLVYPGFATDLQQPITPLLFKASGP 322
Cdd:COG0766  241 VAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQAEGT 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 323 SFVTETIYPARFKHVEELQHMGANIEADEvtGTATIK-PSTLHGTEVYASDLRAGACLIIAGLIAEGVTTIYNVKHIYRG 401
Cdd:COG0766  321 SVITETVFENRFMHVDELNRMGADIKLDG--HTAIVRgVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDRG 398
                        410
                 ....*....|....*.
gi 488391868 402 YTDIVEHLEQLGADIW 417
Cdd:COG0766  399 YENLEEKLRALGADIE 414
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
4-417 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 580.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868   4 EVIKIRGGQTLKGEVNISGAKNSAVAIIPATLLAQGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDT-VLEVDTTEIKN 82
Cdd:PRK09369   2 DKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNgTVTIDASNINN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  83 APLPNNKVESLRASYYMMGAMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSDTsmkIEAK---ELIGTTI 159
Cdd:PRK09369  82 TEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGY---VEAKadgRLKGAHI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 160 FLDMVSVGATINIMLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTSTLKIKGVDALHGSEYQVIPDRIEAG 239
Cdd:PRK09369 159 VLDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 240 TYMCMAAACGQEVKINNIVPKHVEALMVKLQELGVDITVEDEYAIIKGKAKYKNVDIKTLVYPGFATDLQQPITPLLFKA 319
Cdd:PRK09369 239 TFLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQA 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 320 SGPSFVTETIYPARFKHVEELQHMGANIEADEvtGTATIK-PSTLHGTEVYASDLRAGACLIIAGLIAEGVTTIYNVKHI 398
Cdd:PRK09369 319 EGTSVITETIFENRFMHVPELIRMGADIEVDG--HTAVVRgVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHL 396
                        410
                 ....*....|....*....
gi 488391868 399 YRGYTDIVEHLEQLGADIW 417
Cdd:PRK09369 397 DRGYERIEEKLRALGADIE 415
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
14-412 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: 578.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  14 LKGEVNISGAKNSAVAIIPATLLAQGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDT-VLEVDTTEIKNAPLPNNKVES 92
Cdd:cd01555    1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGEnTLVIDASNINSTEAPYELVRK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  93 LRASYYMMGAMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSDTSMKIEAKELIGTTIFLDMVSVGATINI 172
Cdd:cd01555   81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAAGRLKGARIYLDFPSVGATENI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 173 MLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTSTLKIKGVDALHGSEYQVIPDRIEAGTYMCMAAACGQEV 252
Cdd:cd01555  161 MMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGDI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 253 KINNIVPKHVEALMVKLQELGVDITVEDEYAIIKGKAK-YKNVDIKTLVYPGFATDLQQPITPLLFKASGPSFVTETIYP 331
Cdd:cd01555  241 TVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGGrLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIFE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 332 ARFKHVEELQHMGANIEADEvtGTATIK-PSTLHGTEVYASDLRAGACLIIAGLIAEGVTTIYNVKHIYRGYTDIVEHLE 410
Cdd:cd01555  321 NRFMHVDELNRMGADIKVEG--NTAIIRgVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLR 398

                 ..
gi 488391868 411 QL 412
Cdd:cd01555  399 AL 400
murA TIGR01072
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ...
3-417 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: 517.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868    3 QEVIKIRGGQTLKGEVNISGAKNSAVAIIPATLLAQGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDTVLEVDTTEIKN 82
Cdd:TIGR01072   1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNINS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868   83 APLPNNKVESLRASYYMMGAMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIdESSDTSMKIEAKE-LIGTTIFL 161
Cdd:TIGR01072  81 TEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEI-VIEDGYVYASAKGrLVGAHIVL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  162 DMVSVGATINIMLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTSTLKIKGVDALHGSEYQVIPDRIEAGTY 241
Cdd:TIGR01072 160 DKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  242 MCMAAACGQEVKINNIVPKHVEALMVKLQELGVDITV-EDEYAIIKGKAKYKNVDIKTLVYPGFATDLQQPITPLLFKAS 320
Cdd:TIGR01072 240 LVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVdENGIRVDMRQKRLKAVDIETLPYPGFPTDLQAQFMALLSQAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  321 GPSFVTETIYPARFKHVEELQHMGANIEADevTGTATIK-PSTLHGTEVYASDLRAGACLIIAGLIAEGVTTIYNVKHIY 399
Cdd:TIGR01072 320 GTSVITETVFENRFMHVDELIRMGANIKLE--GNTAVIHgVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLD 397
                         410
                  ....*....|....*...
gi 488391868  400 RGYTDIVEHLEQLGADIW 417
Cdd:TIGR01072 398 RGYEDLEEKLRALGAKIE 415
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
9-409 3.38e-91

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 281.49  E-value: 3.38e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868    9 RGGQTLKGEVNISG-AKNSAVAIIPATLLAqGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDTVLEVDTTE--IKNAPL 85
Cdd:pfam00275   1 TGGSRLSGEVKIPGsKSNSHRALILAALAA-GESTITNLLDSDDTLTMLEALRALGAEIIKLDDEKSVVIVEglGGSFEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868   86 PNNKVESLRASYYMMGAMLGRF--KKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSD---TSMKIEAKELIGTTIF 160
Cdd:pfam00275  80 PEDLVLDMGNSGTALRPLTGRLalQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGynyAPLKVRGLRLGGIHID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  161 LDMVSVGATINIMLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTST-LKIKGVDALHGSEYQVIPDRIEAG 239
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLPGQEYRVEGDRSSAA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  240 TYMCMAAACGQEVKINNIVPKHV---EALMVKLQELGVDITVEDEYAIIKGKAKY--KNVDIKTLVYPGFATDLQQPITP 314
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDADIVVGPPGLrgKAVDIRTAPDPAPTTAVLAAFAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  315 LLFKASGPSFVTETIYPARFKHVEELQHMGANIEADEVTGTATIKPSTLHGTEVYAS-DLRAGACLIIAGLIAEGVTTIY 393
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKELKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
                         410
                  ....*....|....*.
gi 488391868  394 NVKHIYRGYTDIVEHL 409
Cdd:pfam00275 400 DIECTDRSFPDFEEKL 415
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
14-412 5.82e-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: 237.12  E-value: 5.82e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  14 LKGEVNISGAKNSAVAIIPATLLAQGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDTVLEVDTTEI---KNAPLPNNKV 90
Cdd:cd01554    1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKDGVITIQGVGMaglKAPQNALNLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  91 ESLRASYYMMGAMLGRFKKcvIGLPGGCPLGPRPIDQHIKGFKALGAEI---DESSDTSMKIEAKELIGTTIFLDMVSVG 167
Cdd:cd01554   81 NSGTAIRLISGVLAGADFE--VELFGDDSLSKRPMDRVTLPLKKMGASIsgqEERDLPPLLKGGKNLGPIHYEDPIASAQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 168 ATINIMLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTSTLKIKGVDALHGSEYQVIPDRIEAGTYMCMAAA 247
Cdd:cd01554  159 VKSALMFAALLAKGETVIIEAAKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQKYVVPGDISSAAFFLVAAAI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 248 CGQEVKINNIVPKHVE-ALMVKLQELGVDITVEDEYaIIKGKAKYKNVDIKTLVYPgFATDLQQPITPLLFKASGPSFVT 326
Cdd:cd01554  239 APGRLVLQNVGINETRtGIIDVLRAMGAKIEIGEDT-ISVESSDLKATEICGALIP-RLIDELPIIALLALQAQGTTVIK 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 327 ETIYPA------RFKHVEELQHMGANIEadEVTGTATIK-PSTLHGTEVYA-SDLRAGACLIIAGLIAEGVTTIYNVKHI 398
Cdd:cd01554  317 DAEELKvketdrIFVVADELNSMGADIE--PTADGMIIKgKEKLHGARVNTfGDHRIGMMTALAALVADGEVELDRAEAI 394
                        410
                 ....*....|....
gi 488391868 399 YRGYTDIVEHLEQL 412
Cdd:cd01554  395 NTSYPSFFDDLESL 408
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
14-412 1.67e-25

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: 107.26  E-value: 1.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  14 LKGEVNISGAKN-SAVAIIPAtLLAQGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDTVLEVdtTEIKNAPLPNNKV-- 90
Cdd:cd01556    1 LSGEITVPGSKSiSHRALLLA-ALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVEI--VGGGGLGLPPEAVld 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  91 --ESLRASYYMMGAMLGRFKKCVIGlpGGCPLGPRPIDQHIKGFKALGAEID--ESSDTSMKIEAKELIGTTIFLDM-VS 165
Cdd:cd01556   78 cgNSGTTMRLLTGLLALQGGDSVLT--GDESLRKRPMGRLVDALRQLGAEIEgrEGGGYPPLIGGGGLKGGEVEIPGaVS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 166 ---VGAtinIMLAAVHAKGQTIIENAAKEPEV-VDV-ANFLMSMGANIKGAGTSTLKIKGVDALHGSEYQVIPDrIEAGT 240
Cdd:cd01556  156 sqfKSA---LLLAAPLAEGPTTIIIGELESKPyIDHtERMLRAFGAEVEVDGYRTITVKGGQKYKGPEYTVEGD-ASSAA 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 241 YMcMAAAC--GQEVKINNIVPKHVEALMVK-LQELGVDITVEDE-YAIIKGKAKYKNVDIKtlvyPGFATDLQQPITPLL 316
Cdd:cd01556  232 FF-LAAAAitGSEIVIKNVGLNSGDTGIIDvLKEMGADIEIGNEdTVVVESGGKLKGIDID----GNDIPDEAPTLAVLA 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 317 FKASGPSFVTeTIYPARFKH-------VEELQHMGANIEadEVTGTATIKPSTLH--GTEVYAS-DLRAGACLIIAGLIA 386
Cdd:cd01556  307 AFAEGPTRIR-NAAELRVKEsdriaamATELRKLGADVE--ETEDGLIIEGGPLKgaGVEVYTYgDHRIAMSFAIAGLVA 383
                        410       420
                 ....*....|....*....|....*.
gi 488391868 387 EGVTTIYNVKHIYRGYTDIVEHLEQL 412
Cdd:cd01556  384 EGGVTIEDPECVAKSFPNFFEDLESL 409
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
16-415 8.85e-19

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: 87.72  E-value: 8.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868   16 GEVNISGAKNSAVAIIPATLLAQGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDTVLEVD--TTEIKNAPL-PNNKVES 92
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAVIEgvGGKEPQAELdLGNSGTT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868   93 LRasyYMMGAM-LGRFKKCVIGLPGgcpLGPRPIDQHIKGFKALGAEIDESSDTS---MKIEAKELIGTTIFLDMVSVGA 168
Cdd:TIGR01356  81 AR---LLTGVLaLADGEVVLTGDES---LRKRPMGRLVDALRQLGAEISSLEGGGslpLTISGPLPGGIVYISGSASSQY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  169 TINIMLAAVHAKGQTIIENAAKEPEV--VDVANFLMSM-GANIKGAGTSTLKIKGVDALHGSEYQVIPDRIEAGTYMCMA 245
Cdd:TIGR01356 155 KSALLLAAPALQAVGITIVGEPLKSRpyIEITLDLLGSfGVEVERSDGRKIVVPGGQKYGPQGYDVPGDYSSAAFFLAAA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  246 AACGQEVKINNIVPKHVE---ALMVKLQELGVDITVEDEYAIIKGKAKYK--NVDIKTLvypgfaTDLQQPITPLLFKAS 320
Cdd:TIGR01356 235 AITGGRVTLENLGINPTQgdkAIIIVLEEMGADIEVEEDDLIVEGASGLKgiKIDMDDM------IDELPTLAVLAAFAE 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  321 GPSFVTEtIYPARFKH-------VEELQHMGANIE--AD--EVTGTATIKPSTLHGtevYAsDLRAGACLIIAGLIAEGV 389
Cdd:TIGR01356 309 GVTRITG-AEELRVKEsdriaaiAEELRKLGVDVEefEDglYIRGKKELKGAVVDT---FG-DHRIAMAFAVAGLVAEGE 383
                         410       420
                  ....*....|....*....|....*.
gi 488391868  390 TTIYNVKHIYRGYTDIVEHLEQLGAD 415
Cdd:TIGR01356 384 VLIDDPECVAKSFPSFFDVLERLGAN 409
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
4-412 1.94e-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: 83.60  E-value: 1.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868   4 EVIKIRGGQTLKGEVNISGAKN-SAVAIIPAtLLAQGKVQLDGLPQISDVETLVSLLEDLNIK-TQLNDTVLEVdttEIK 81
Cdd:COG0128    2 SSLTIAPPSPLKGTVRVPGSKSiSHRALLLA-ALAEGESTIRNLLESDDTLATLEALRALGAEiEELDGGTLRV---TGV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  82 NAPLPNNKVE--------SLRasyYMMGAM-LGRFKKCVIGLPGgcpLGPRPIDQHIKGFKALGAEIDESSDTS--MKIE 150
Cdd:COG0128   78 GGGLKEPDAVldcgnsgtTMR---LLTGLLaLQPGEVVLTGDES---LRKRPMGRLLDPLRQLGARIESRGGGYlpLTIR 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 151 AKELIGTTIFLD-MVS---VGAtinIMLAAVHAKGQTIIENAAKEPEV--VDVA-NFLMSMGANIKGAGTSTLKIKGVDA 223
Cdd:COG0128  152 GGPLKGGEYEIPgSASsqfKSA---LLLAGPLAEGGLEITVTGELESKpyRDHTeRMLRAFGVEVEVEGYRRFTVPGGQR 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 224 LHGSEYQVIPDRIEAGTYMCMAAACGQEVKINN--IVPKHVEALMVK-LQELGVDITVEDEYAIIKGkAKYKNVDIKtlv 300
Cdd:COG0128  229 YRPGDYTVPGDISSAAFFLAAAAITGSEVTVEGvgLNSTQGDTGILDiLKEMGADIEIENDGITVRG-SPLKGIDID--- 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 301 yPGFATDLQQPITPLLFKASGPSFVTeTIYPARFKH-------VEELQHMGANIEADE----VTGTATIKPSTLHGtevY 369
Cdd:COG0128  305 -LSDIPDEAPTLAVLAAFAEGTTRIR-GAAELRVKEsdriaamATELRKLGADVEETEdgliIEGGPKLKGAEVDS---Y 379
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 488391868 370 AsDLRAGACLIIAGLIAEGVTTIYNVKHIYRGYTDIVEHLEQL 412
Cdd:COG0128  380 G-DHRIAMAFAVAGLRAEGPVTIDDAECVAKSFPDFFELLESL 421
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
6-416 3.73e-13

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 70.56  E-value: 3.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868   6 IKIRGGQTLKGEVNISGAKN-SAVAIIPAtLLAQGKVQLDGLPQISDVETLVSLLEDLNIKtqLNDTVLEVDTTEIKNAP 84
Cdd:PRK02427   5 LLIIPPSPLSGTVRVPGSKSiSHRALLLA-ALAEGETTITNLLRSEDTLATLNALRALGVE--IEDDEVVVEGVGGGGLK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  85 LPNNKVE------SLRasyYMMGAM-LGRFKKCVIGLPGgcpLGPRPIDQHIKGFKALGAEIDESSDTS--MKIE-AKEL 154
Cdd:PRK02427  82 EPEDVLDcgnsgtTMR---LLTGLLaLQPGEVVLTGDES---LRKRPMGRLLDPLRQMGAKIEGRDEGYlpLTIRgGKKG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 155 IGTTIFLDM----VSvGAtinIMLAAVHAKGQTIIEnaAKEPEV----VDV-ANFLMSMGANIK---GAGTSTLKIKGVD 222
Cdd:PRK02427 156 GPIEYDGPVssqfVK-SL---LLLAPLFAEGDTETT--VIEPLPsrphTEItLRMLRAFGVEVEnveGWGYRRIVIKGGQ 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 223 ALHGSEYQVIPDrIEAGTYMcMAAAC---GQEVKINNI--VPKHVEALMVK-LQELGVDITVEDEYAIIKGKAkykNVDI 296
Cdd:PRK02427 230 RLRGQDITVPGD-PSSAAFF-LAAAAitgGSEVTITNVglNSTQGGKAIIDvLEKMGADIEIENEREGGEPVG---DIRV 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 297 KTLVYPGF------ATDLQQPITPL-LFkASGPSfvteTIYPA---RFKH-------VEELQHMGANIEADEvtGTATIK 359
Cdd:PRK02427 305 RSSELKGIdidipdIIDEAPTLAVLaAF-AEGTT----VIRNAeelRVKEtdriaamATELRKLGAEVEETE--DGLIIT 377
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488391868 360 PSTLHGT-EVYAsDLRAGACLIIAGLIAEGVTTIYNVKHIYRGYTDIVEHLEQLGADI 416
Cdd:PRK02427 378 GGPLAGVvDSYG-DHRIAMAFAIAGLAAEGPVTIDDPECVAKSFPDFFEDLASLGANI 434
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
129-416 6.05e-13

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: 70.12  E-value: 6.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 129 IKGFKALGAEIDESSDTSMKIE--AKELIGTTIFLDMVSVGATINIMLAAV-HAKGQTII---ENAAKEP--EVVDVanf 200
Cdd:COG0128   54 LEALRALGAEIEELDGGTLRVTgvGGGLKEPDAVLDCGNSGTTMRLLTGLLaLQPGEVVLtgdESLRKRPmgRLLDP--- 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 201 LMSMGANIKGAGTST--LKIKGvDALHGSEY--------QVIpdrieagTYMCMAAAC---GQEVKI-NNIVPK----HV 262
Cdd:COG0128  131 LRQLGARIESRGGGYlpLTIRG-GPLKGGEYeipgsassQFK-------SALLLAGPLaegGLEITVtGELESKpyrdHT 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 263 EALMvklQELGVDITVEDEYAI-IKGKAKYKNVDIKtlVyPGfatDLQQPITPLLFKASGPSFVT------ETIYP-ARF 334
Cdd:COG0128  203 ERML---RAFGVEVEVEGYRRFtVPGGQRYRPGDYT--V-PG---DISSAAFFLAAAAITGSEVTvegvglNSTQGdTGI 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 335 khVEELQHMGANIEADEvtGTATIKPSTLHGTEVyasDLRAGACLI----IAGLIAEGVTTIYNVKHIyRGY-TD----I 405
Cdd:COG0128  274 --LDILKEMGADIEIEN--DGITVRGSPLKGIDI---DLSDIPDEAptlaVLAAFAEGTTRIRGAAEL-RVKeSDriaaM 345
                        330
                 ....*....|.
gi 488391868 406 VEHLEQLGADI 416
Cdd:COG0128  346 ATELRKLGADV 356
EPT_RTPC-like cd01553
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ...
233-412 3.29e-12

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: 65.38  E-value: 3.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 233 PDRIEAGTYMCMAAACGQEVKINNIVP---------KHVEALMVKLQELGVDITV--EDEYAIIKGKAKYKNVDIKTLVY 301
Cdd:cd01553    8 GGGQILRSFLVLAAISGGPITVTGIRPdrakpgllrQHLTFLKALEKICGATVEGgeLGSDRISFRPGTVRGGDVRFAIG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 302 P-GFATDLQQPITPLLFKASGPSFVTETIYPA----------RFKHVEELQHMGANIEADEVTGTATIKPSTLHGTEVY- 369
Cdd:cd01553   88 SaGSCTDVLQTILPLLLFAKGPTRLTVTGGTDnpsappadfiRFVLEPELAKIGAHQEETLLRHGFYPAGGGVVATEVSp 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 488391868 370 -----ASDLRAGACLIIAGliaeGVTTIYNVKHIYRGYTDIVEHLEQL 412
Cdd:cd01553  168 veklnTAQLRQLVLPMLLA----SGAVEFTVAHPSCHLLTNFAVLEAL 211
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
129-422 2.71e-09

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: 58.44  E-value: 2.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  129 IKGFKALGAEIDESSDTsMKIEAKELIGTTIFLDMVSVGATINIMLAAVHAKGQTII----ENAAKEPeVVDVANFLMSM 204
Cdd:TIGR01356  41 LDALRALGAKIEDGGEV-AVIEGVGGKEPQAELDLGNSGTTARLLTGVLALADGEVVltgdESLRKRP-MGRLVDALRQL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  205 GANI---KGAGTSTLKIKGvdALHGSEYQVIPDR-IEAGTYMCMAAACGQ----EVKINNIVPK-HVEaLMVKLQE-LGV 274
Cdd:TIGR01356 119 GAEIsslEGGGSLPLTISG--PLPGGIVYISGSAsSQYKSALLLAAPALQavgiTIVGEPLKSRpYIE-ITLDLLGsFGV 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  275 DITVEDEYAI-IKGKAKYKNVDIKTlvyPGfatDLQQPITPLLFKASGPSFVTET---IYPARF--KHVEELQHMGANIE 348
Cdd:TIGR01356 196 EVERSDGRKIvVPGGQKYGPQGYDV---PG---DYSSAAFFLAAAAITGGRVTLEnlgINPTQGdkAIIIVLEEMGADIE 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  349 AD----EVTGtatikPSTLHGTEVYASDLrAGACLIIAGL--IAEGVTTIYNVKHIYRGYTD----IVEHLEQLGADIwT 418
Cdd:TIGR01356 270 VEeddlIVEG-----ASGLKGIKIDMDDM-IDELPTLAVLaaFAEGVTRITGAEELRVKESDriaaIAEELRKLGVDV-E 342

                  ....
gi 488391868  419 EKVD 422
Cdd:TIGR01356 343 EFED 346
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
269-416 3.24e-08

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: 55.26  E-value: 3.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 269 LQELGVDITVEDEYAIIKGKAKYKNVDIKTLvYPGFATDLQQPITPLLFKASGPSFVTETIYPAR--FKH-VEELQHMGA 345
Cdd:cd01556   46 LRALGAKIEEEGGTVEIVGGGGLGLPPEAVL-DCGNSGTTMRLLTGLLALQGGDSVLTGDESLRKrpMGRlVDALRQLGA 124
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488391868 346 NIEADEVTGTA-TIKPSTLHGTEVyasDLRAGA------CLIIAGLIAEGVTTIYNVKHIYRGYTDIVEH-LEQLGADI 416
Cdd:cd01556  125 EIEGREGGGYPpLIGGGGLKGGEV---EIPGAVssqfksALLLAAPLAEGPTTIIIGELESKPYIDHTERmLRAFGAEV 200
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
172-416 2.26e-07

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: 52.78  E-value: 2.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 172 IMLAAVhAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTSTLKIKGVdalhGSEYQVIPDRI---EAGT--YMCMAA 246
Cdd:COG0128   29 LLLAAL-AEGESTIRNLLESDDTLATLEALRALGAEIEELDGGTLRVTGV----GGGLKEPDAVLdcgNSGTtmRLLTGL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 247 ACGQevkinnivPKHVE----ALMVK---------LQELGVDIT-VEDEYA--IIKGkAKYKNVDIKTlvyPGFATDlqQ 310
Cdd:COG0128  104 LALQ--------PGEVVltgdESLRKrpmgrlldpLRQLGARIEsRGGGYLplTIRG-GPLKGGEYEI---PGSASS--Q 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 311 PITPLLFkaSGPSF-------VTETIYPARF-KHVEE-LQHMGANIEADEvTGTATIK-PSTLHGTEVY-ASDLRAGACL 379
Cdd:COG0128  170 FKSALLL--AGPLAeggleitVTGELESKPYrDHTERmLRAFGVEVEVEG-YRRFTVPgGQRYRPGDYTvPGDISSAAFF 246
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 488391868 380 IIAGLIAEGVTTIYNV-KHIYRGYTDIVEHLEQLGADI 416
Cdd:COG0128  247 LAAAAITGSEVTVEGVgLNSTQGDTGILDILKEMGADI 284
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
133-288 4.35e-04

bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 42.67  E-value: 4.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 133 KALGAEIDESSDTSMKIEAKELIGTTIFL--DMVSvgATINIMLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIK- 209
Cdd:PRK14806 503 RGFGYPVKVEGNTISVEGGGKLTATDIEVpaDISS--AAFFLVAASIAEGSELTLEHVGINPTRTGVIDILKLMGADITl 580
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 210 -------GAGTSTLKIKGVDaLHG---SEYQViPDRIEAGTYMCMAAACGQEVKinniVPKHVEALMVK----------- 268
Cdd:PRK14806 581 enerevgGEPVADIRVRGAR-LKGidiPEDQV-PLAIDEFPVLFVAAACAEGRT----VLTGAEELRVKesdriqvmadg 654
                        170       180
                 ....*....|....*....|
gi 488391868 269 LQELGVDITVEDEYAIIKGK 288
Cdd:PRK14806 655 LKTLGIDCEPTPDGIIIEGG 674
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
262-416 1.61e-03

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: 40.34  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  262 VEALMVKLQELGVDITVEDEYAIIKGKA-KYKNVDIktlvYPGFATDLQQPITPLLFKASGPsfvTETIYPARFKH---- 336
Cdd:TIGR01356  37 TLATLDALRALGAKIEDGGEVAVIEGVGgKEPQAEL----DLGNSGTTARLLTGVLALADGE---VVLTGDESLRKrpmg 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868  337 --VEELQHMGANIEADEVTGTA--TIKpSTLHGTEVYASDLRA---GACLIIAGLIAEGVT-TIYNVKHIYRGYTDIVeh 408
Cdd:TIGR01356 110 rlVDALRQLGAEISSLEGGGSLplTIS-GPLPGGIVYISGSASsqyKSALLLAAPALQAVGiTIVGEPLKSRPYIEIT-- 186

                  ....*...
gi 488391868  409 LEQLGADI 416
Cdd:TIGR01356 187 LDLLGSFG 194
 
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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