|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00286 |
PTZ00286 |
6-phospho-1-fructokinase; Provisional |
1-470 |
0e+00 |
|
6-phospho-1-fructokinase; Provisional
Pssm-ID: 185539 Cd Length: 459 Bit Score: 691.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 1 MENRLRDTSRVVRSHAAPLNEVTQEDLKVERLHGRKYMNpskKHVMREEFSDKIEHIMHDPRPQEGVHSElpvsiSPLLC 80
Cdd:PTZ00286 1 TCEIERVNNLIIDLPDAPLPSVVNPDLGECNLRGVFGGN---GFLPREAFVDTNSYILSTPRFGPDDVIV-----NTKRW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 81 ELAAPRQRIHFNPPETVVGIVTCGGICPGLNDVIRSLTLTAVNAYRVKRVIGFRFGYWGLSKKGShtaMELYRTSVTSIH 160
Cdd:PTZ00286 73 LRAGPRKHLYFNPKEVKAGIVTCGGLCPGLNVVIRELVMNLINNYGVKTIYGAKYGYKGLYKEDW---IKLDPKDVKTIH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 161 RYGGTILGSSRGPQDTSEMVDTLERLGVNILFTVGGDGTQRGALKIAEEAKRRGANLAVFGIPKTIDNDLSFSHRTFGFE 240
Cdd:PTZ00286 150 RLGGTILGSSRGGFDPKVMVDTLIRHGINILFTLGGDGTHRGALAIYKELRRRKLNISVVGIPKTIDNDIPIIDESFGFQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 241 TAVDKAVEAVRAAYAEAISLNYGVGVVKLMGRDSGFIAAEAAVASAQANICLVPENPISEDIVMALIQRRFETSRSCVII 320
Cdd:PTZ00286 230 TAVEEAQNAIRAAYVEAKSAKNGVGIVKLMGRDSGFIALHASVASADVNVCLIPEFDIPLEGVLEYIEQRLQKKGHCVIV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 321 VAEGFGQDWEGGT--GGHDASGNKKLTDIGVVLTKRIQAWLRKNKeryPNGTVKYIDPSYMIRACPPSANDALFCATLST 398
Cdd:PTZ00286 310 VAEGAGQSLKDADldLGTDASGNKKLWDIGVYLKDEITKYLKKKK---PEHTVKYIDPSYMIRAVPANAADAKFCTQLAQ 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 122047336 399 LAMHEAMAGATNCIIALRYNSYILVPIKV-ATSVRRVLDLRGQLWRQVREITVGLQDDVRAFKEAEVRRELEA 470
Cdd:PTZ00286 387 NAVHGAMAGFTGFIIGHVHNNYVMIPIKEmSGNYRRRVNPEGRLWQRMLAITGQPSFLNNEEIERHQRRQLES 459
|
|
| PfkA |
COG0205 |
6-phosphofructokinase [Carbohydrate transport and metabolism]; 6-phosphofructokinase is part ... |
98-450 |
6.06e-96 |
|
6-phosphofructokinase [Carbohydrate transport and metabolism]; 6-phosphofructokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 439975 [Multi-domain] Cd Length: 344 Bit Score: 293.52 E-value: 6.06e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 98 VGIVTCGGICPGLNDVIRSLTLTAVNaYRVkRVIGFRFGYWGLSKKgshTAMELYRTSVTSIHRYGGTILGSSRGPQ--- 174
Cdd:COG0205 4 IGILTSGGDAPGLNAAIRAVVRTAIK-YGI-EVYGIRDGYEGLLEG---DIIDLTREDVSGILQRGGTILGSSRSKPfkt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 175 --DTSEMVDTLERLGVNILFTVGGDGTQRGALKIAEEAKrrganLAVFGIPKTIDNDLSFSHRTFGFETAVDKAVEAVRA 252
Cdd:COG0205 79 eeGREKALENLKKLGIDALVVIGGDGSLDGAAKLAEEYG-----IPVVGIPKTIDNDLPGTDYTIGFDTAVNTAAEAIDR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 253 AYAEAISLNyGVGVVKLMGRDSGFIaaeaavasaqaNICLVPENPISEDIVMALIQRRFETSR-SCVIIVAEGFGQDWEG 331
Cdd:COG0205 154 LRDTAASHE-RVFVVEVMGRHAGWLalaag-laggaDLILIPEVPFDLDKLLEKLKERRKRGKgYSIIVVAEGAGDEDGE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 332 --GTGGHDASGNKKLTDIGVVLTKRIqawlrknkERYPNGTVKYIDPSYMIRACPPSANDALFCATLSTLAMHEAMAGAT 409
Cdd:COG0205 232 avLEADTDAFGHVRLGGIGEYLAKEI--------EERTGIETRVTVLGHLQRGGSPSAFDRVLASRLGAAAVELLLEGKT 303
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 122047336 410 NCIIALRYNSYILVPIKVATSVRRVLDLRGQLWRQVREITV 450
Cdd:COG0205 304 GVMVGIRRGEIVLVPLEEVANKEKPVDPDSPLIQLARELGI 344
|
|
| PFK |
pfam00365 |
Phosphofructokinase; |
98-402 |
3.20e-56 |
|
Phosphofructokinase;
Pssm-ID: 459783 [Multi-domain] Cd Length: 271 Bit Score: 187.93 E-value: 3.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 98 VGIVTCGGICPGLNDVIRSLTLTAVNAYRvkRVIGFRFGYWGLSKKGshtAMELYRTSVTSIHRYGGTILGSSRG-PQDT 176
Cdd:pfam00365 2 IGILTSGGDAPGMNAAIRAVVRTAIYRGH--EVYGIRNGYEGLVEGD---IDELTWRDVSGILNRGGTILGTSRSkPFKT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 177 SE----MVDTLERLGVNILFTVGGDGTQRGALKIAEEAkrrgaNLAVFGIPKTIDNDLSFSHRTFGFETAVDKAVEAVRA 252
Cdd:pfam00365 77 EEgrekIAENLKKLGIDALVVIGGDGSLTGANKLSEER-----GIPVVGIPKTIDNDIPGTDYTIGFDTALNTIVEAIDR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 253 AYAEAISLNyGVGVVKLMGRDSGFIaaeaavasaqaNICLVPENPISEDIVMALIQRRFETSRSCVIIVAEGfgqdwegg 332
Cdd:pfam00365 152 IRDTASSHN-RVFVVEVMGRHCGWLalmag-laggaDAILIPEIPFDIEELCEKIKELRKGKRFSIIVVAEG-------- 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 333 tgghdASGnkkltdiGVVLTKRIQAwlRKNKErypngtVKYIDPSYMIRACPPSANDALFCATLSTLAMH 402
Cdd:pfam00365 222 -----ASD-------GEFLAKLIEE--GTGIE------TRVTVLGHVQRGGTPSAFDRILATRLGVKAVE 271
|
|
| PFK_mixed |
TIGR02483 |
phosphofructokinase; Members of this family that are characterized, save one, are ... |
98-429 |
2.16e-51 |
|
phosphofructokinase; Members of this family that are characterized, save one, are phosphofructokinases dependent on pyrophosphate (EC 2.7.1.90) rather than ATP (EC 2.7.1.11). The exception is one of three phosphofructokinases from Streptomyces coelicolor. Family members are both bacterial and archaeal. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 274155 [Multi-domain] Cd Length: 324 Bit Score: 177.11 E-value: 2.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 98 VGIVTCGGICPGLNDVIRSLTLTAVNAYRVKrVIGFRFGYWGLSKKGshTAMELYRTSVTSIHRYGGTILGSSRG-PQDT 176
Cdd:TIGR02483 2 IGVLTGGGDCPGLNAVIRGVVRRAIAEYGWE-VIGIRDGWRGLLEGD--TVPLLDLEDVRGILPRGGTILGSSRTnPFKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 177 SEM-----VDTLERLGVNILFTVGGDGTqrgaLKIAEEAKRRGanLAVFGIPKTIDNDLSFSHRTFGFETAVDKAVEAVR 251
Cdd:TIGR02483 79 EEDgddkiVANLKELGLDALIAIGGDGT----LGIARRLADKG--LPVVGVPKTIDNDLEATDYTFGFDTAVEIATEALD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 252 AAYAEAISLNYgVGVVKLMGRDSGFIaAEAAVASAQANICLVPENPISEDIVMALIQRRFETSRS-CVIIVAEGF---GQ 327
Cdd:TIGR02483 153 RLHTTAESHHR-VMVVEVMGRHAGWI-ALHSGIAGGADVILIPEIPFDIDSVCEKVRERFARGKRfAIVVVAEGAkpkGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 328 DWEGGTGGHDASGNKKLTDIGVVLTKRIQAwlRKNKERYPngTVKyidpSYMIRACPPSANDALFCATLSTLAMHEAMAG 407
Cdd:TIGR02483 231 EMVVQEGVKDAFGHVRLGGIGNWLAEEIER--RTGIETRA--TVL----GHLQRGGSPSAFDRVLATRFGVAAVDLVHEG 302
|
330 340
....*....|....*....|..
gi 122047336 408 ATNCIIALRYNSYILVPIKVAT 429
Cdd:TIGR02483 303 QFGHMVALRGTDIVYVPIAEAV 324
|
|
| PFK |
cd00363 |
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ... |
98-443 |
3.46e-42 |
|
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate. The members belong to PFK family that includes ATP- and pyrophosphate (PPi)- dependent phosphofructokinases. Some members evolved by gene duplication and thus have a large C-terminal/N-terminal extension comprising a second PFK domain. Generally, ATP-PFKs are allosteric homotetramers, and PPi-PFKs are dimeric and nonallosteric except for plant PPi-PFKs which are allosteric heterotetramers.
Pssm-ID: 238216 [Multi-domain] Cd Length: 338 Bit Score: 152.84 E-value: 3.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 98 VGIVTCGGICPGLNDVIRSLTLTAVnaYRVKRVIGFRFGYWGLSKkGSHtaMELYRTSVTSIHRYGGTILGSSRGPQDTS 177
Cdd:cd00363 3 IGVLTSGGDAPGMNAAIRGVVRSAI--AEGLEVYGIYEGYAGLVE-GDI--KELDWESVSDIINRGGTIIGSARCKEFRT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 178 E-----MVDTLERLGVNILFTVGGDGTQRGALKIAEEAKRRGANLAVFGIPKTIDNDLSFSHRTFGFETAVDKAVEAVRA 252
Cdd:cd00363 78 EegrakAAENLKKHGIDALVVIGGDGSYTGADLLTEEWPSKYQGFNVIGLPGTIDNDIKGTDYTIGFDTALKTIVEAIDR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 253 AYAEAISLNYgVGVVKLMGRDSGFIaAEAAVASAQANICLVPENP----ISEDIVMALIQRRFETSRSCVIIVAEGFGQD 328
Cdd:cd00363 158 IRDTASSHQR-TFVVEVMGRHCGDI-ALEAGLATGADIIFIPEEPaadeWEEEMVDVIKKRRERGKRHGIVIVAEGAIDF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 329 WEGGTGGHdasgnkkltDIGVVLTKRIQAWLRknkerypnGTVKyidpSYMIRACPPSANDALFCATLSTLAMHEAMAGA 408
Cdd:cd00363 236 IPKPITEK---------LLAKLVEERLGFDTR--------ATVL----GHVQRGGTPTAFDRILASRLGAEAVELLLEGT 294
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 122047336 409 TN---CIIALRYNSYILVPIKVATSVRR--VLDLRGQLWR 443
Cdd:cd00363 295 GGtpvGIQNLNENQVVRHPLTEAVNMTKrvGVDLEGRPFK 334
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00286 |
PTZ00286 |
6-phospho-1-fructokinase; Provisional |
1-470 |
0e+00 |
|
6-phospho-1-fructokinase; Provisional
Pssm-ID: 185539 Cd Length: 459 Bit Score: 691.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 1 MENRLRDTSRVVRSHAAPLNEVTQEDLKVERLHGRKYMNpskKHVMREEFSDKIEHIMHDPRPQEGVHSElpvsiSPLLC 80
Cdd:PTZ00286 1 TCEIERVNNLIIDLPDAPLPSVVNPDLGECNLRGVFGGN---GFLPREAFVDTNSYILSTPRFGPDDVIV-----NTKRW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 81 ELAAPRQRIHFNPPETVVGIVTCGGICPGLNDVIRSLTLTAVNAYRVKRVIGFRFGYWGLSKKGShtaMELYRTSVTSIH 160
Cdd:PTZ00286 73 LRAGPRKHLYFNPKEVKAGIVTCGGLCPGLNVVIRELVMNLINNYGVKTIYGAKYGYKGLYKEDW---IKLDPKDVKTIH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 161 RYGGTILGSSRGPQDTSEMVDTLERLGVNILFTVGGDGTQRGALKIAEEAKRRGANLAVFGIPKTIDNDLSFSHRTFGFE 240
Cdd:PTZ00286 150 RLGGTILGSSRGGFDPKVMVDTLIRHGINILFTLGGDGTHRGALAIYKELRRRKLNISVVGIPKTIDNDIPIIDESFGFQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 241 TAVDKAVEAVRAAYAEAISLNYGVGVVKLMGRDSGFIAAEAAVASAQANICLVPENPISEDIVMALIQRRFETSRSCVII 320
Cdd:PTZ00286 230 TAVEEAQNAIRAAYVEAKSAKNGVGIVKLMGRDSGFIALHASVASADVNVCLIPEFDIPLEGVLEYIEQRLQKKGHCVIV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 321 VAEGFGQDWEGGT--GGHDASGNKKLTDIGVVLTKRIQAWLRKNKeryPNGTVKYIDPSYMIRACPPSANDALFCATLST 398
Cdd:PTZ00286 310 VAEGAGQSLKDADldLGTDASGNKKLWDIGVYLKDEITKYLKKKK---PEHTVKYIDPSYMIRAVPANAADAKFCTQLAQ 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 122047336 399 LAMHEAMAGATNCIIALRYNSYILVPIKV-ATSVRRVLDLRGQLWRQVREITVGLQDDVRAFKEAEVRRELEA 470
Cdd:PTZ00286 387 NAVHGAMAGFTGFIIGHVHNNYVMIPIKEmSGNYRRRVNPEGRLWQRMLAITGQPSFLNNEEIERHQRRQLES 459
|
|
| PRK06830 |
PRK06830 |
ATP-dependent 6-phosphofructokinase; |
22-449 |
3.04e-180 |
|
ATP-dependent 6-phosphofructokinase;
Pssm-ID: 235869 Cd Length: 443 Bit Score: 512.11 E-value: 3.04e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 22 VTQEDLKVERLHGRKYMNP---SKKHVMREEFSDKIEHIMHDPRPQEGVHSELPVSISPLLcELAAPRQRIHFNPPETVV 98
Cdd:PRK06830 5 VTELDFAIETLGECKIPSPliySLAAGDTTHFVSDSDRVLFDVSLSLIKEEDAPGTEPPSF-EKAGPREKIYFDPSKVKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 99 GIVTCGGICPGLNDVIRSLTLTAVNAYRVKRVIGFRFGYWGLSKKGSHTAMELYRTSVTSIHRYGGTILGSSRGPQDTSE 178
Cdd:PRK06830 84 AIVTCGGLCPGLNDVIRAIVLELHHHYGVRRILGIRYGYQGLIPRYGHDPVELTPEVVADIHEFGGTILGSSRGPQDPEE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 179 MVDTLERLGVNILFTVGGDGTQRGALKIAEEAKRRGANLAVFGIPKTIDNDLSFSHRTFGFETAVDKAVEAVRAAYAEAI 258
Cdd:PRK06830 164 IVDTLERMNINILFVIGGDGTLRGASAIAEEIERRGLKISVIGIPKTIDNDINFIQKSFGFETAVEKATEAIRCAHVEAN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 259 SLNYGVGVVKLMGRDSGFIAAEAAVASAQANICLVPENPIS---EDIVMALIQRRFETSRSCVIIVAEGFGQDWEGGTGG 335
Cdd:PRK06830 244 GAPNGIGLVKLMGRHSGFIAAYAALASKDVNFVLIPEVPFDlegPNGLLAALEKRLAERGHAVIVVAEGAGQELFDDTGE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 336 HDASGNKKLTDIGVVLTKRIQAWLRknKERYPNgTVKYIDPSYMIRACPPSANDALFCATLSTLAMHEAMAGATNCIIAL 415
Cdd:PRK06830 324 TDASGNPKLGDIGLFLKDRIKEYFK--ARGIPI-NLKYIDPSYIIRSVPANANDSVYCGFLGQNAVHAAMAGKTGMVVGR 400
|
410 420 430
....*....|....*....|....*....|....
gi 122047336 416 RYNSYILVPIKVATSVRRVLDLRGQLWRQVREIT 449
Cdd:PRK06830 401 WNNRFVHLPIDLAVSKRKKVNPEGDLWRSVLEST 434
|
|
| PLN02884 |
PLN02884 |
6-phosphofructokinase |
83-442 |
7.26e-115 |
|
6-phosphofructokinase
Pssm-ID: 178472 [Multi-domain] Cd Length: 411 Bit Score: 344.49 E-value: 7.26e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 83 AAPRQRIHFNPPETVVGIVTCGGICPGLNDVIRSLTLTaVNAYRVKRVIGFRFGYWGLSKKGSHTaMELYRTSVTSIHRY 162
Cdd:PLN02884 41 AGPRKKIYFEPEEVKAAIVTCGGLCPGLNDVIRQIVFT-LEIYGVKNIVGIPFGYRGFFEKGLSE-MPLSRKVVQNIHLS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 163 GGTILGSSRGPQDTSEMVDTLERLGVNILFTVGGDGTQRGALKIAEEAKRRGANLAVFGIPKTIDNDLSFSHRTFGFETA 242
Cdd:PLN02884 119 GGSLLGVSRGGAKTSDIVDSIEARGINMLFVLGGNGTHAGANAIHNECRKRKMKVSVVGVPKTIDNDILLMDKTFGFDTA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 243 VDKAVEAVRAAYAEAISLNYGVGVVKLMGRDSGFIAAEAAVASAQANICLVPENPIS---EDIVMALIQRRFETSRSCVI 319
Cdd:PLN02884 199 VEEAQRAINSAYIEAHSAYHGIGLVKLMGRSSGFIAMHASLASGQVDICLIPEVPFTldgPNGVLRHLEHLIETKGSAVV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 320 IVAEGFGQDWEGGTGGHDASGNKKLTDIGVVLTKRIQAWLrknKERYPNGTVKYIDPSYMIRACPPSANDALFCATLSTL 399
Cdd:PLN02884 279 CVAEGAGQDLLQKTNATDASGNPVLGDIGVHLQQEIKKHF---KDIGVPADVKYIDPTYMIRACRANASDAILCTVLGQN 355
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 122047336 400 AMHEAMAGATNCIIALRYNSYILVPIKVATSVRRVLDLRGQLW 442
Cdd:PLN02884 356 AVHGAFAGFSGITVGICNTHYVYLPIPEVIAYPRRVDPNSRMW 398
|
|
| PLN02564 |
PLN02564 |
6-phosphofructokinase |
83-442 |
2.60e-108 |
|
6-phosphofructokinase
Pssm-ID: 178178 Cd Length: 484 Bit Score: 330.17 E-value: 2.60e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 83 AAPRQRIHFNPPETVVGIVTCGGICPGLNDVIRSLTLTAVNAYRVKRVIGFRFGYWGLSKKGShtaMELYRTSVTSIHRY 162
Cdd:PLN02564 75 AGPRQKVYFESDEVRACIVTCGGLCPGLNTVIREIVCGLSYMYGVTRILGIDGGYRGFYSRNT---IPLTPKVVNDIHKR 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 163 GGTILGSSRGPQDTSEMVDTLERLGVNILFTVGGDGTQRGALKIAEEAKRRGANLAVFGIPKTIDNDLSFSHRTFGFETA 242
Cdd:PLN02564 152 GGTILGTSRGGHDTSKIVDSIQDRGINQVYIIGGDGTQKGASVIYEEIRRRGLKVAVAGIPKTIDNDIPVIDKSFGFDTA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 243 VDKAVEAVRAAYAEAISLNYGVGVVKLMGRDSGFIAAEAAVASAQANICLVPENPI---SEDIVMALIQRRFETSRSCVI 319
Cdd:PLN02564 232 VEEAQRAINAAHVEAESVENGIGLVKLMGRYSGFIAMYATLASRDVDCCLIPESPFyleGKGGLFEFIEKRLKENGHMVI 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 320 IVAEGFGQDWEG----GTGGHDASGNKKLTDIGVVLTKRIQAWLRKNKERypNGTVKYIDPSYMIRACPPSANDALFCAT 395
Cdd:PLN02564 312 VVAEGAGQDLIAesmeSSDLQDASGNKLLLDVGLWLSQKIKDHFTKVKKM--PINLKYIDPTYMIRAIPSNASDNVYCTL 389
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 122047336 396 LSTLAMHEAMAGATNCIIALRYNSYILVPIKVATSVRRVLDLRGQLW 442
Cdd:PLN02564 390 LAHSAVHGAMAGYTGFTVGPVNGRHAYIPFYRITEKQNKVVITDRMW 436
|
|
| PfkA |
COG0205 |
6-phosphofructokinase [Carbohydrate transport and metabolism]; 6-phosphofructokinase is part ... |
98-450 |
6.06e-96 |
|
6-phosphofructokinase [Carbohydrate transport and metabolism]; 6-phosphofructokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 439975 [Multi-domain] Cd Length: 344 Bit Score: 293.52 E-value: 6.06e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 98 VGIVTCGGICPGLNDVIRSLTLTAVNaYRVkRVIGFRFGYWGLSKKgshTAMELYRTSVTSIHRYGGTILGSSRGPQ--- 174
Cdd:COG0205 4 IGILTSGGDAPGLNAAIRAVVRTAIK-YGI-EVYGIRDGYEGLLEG---DIIDLTREDVSGILQRGGTILGSSRSKPfkt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 175 --DTSEMVDTLERLGVNILFTVGGDGTQRGALKIAEEAKrrganLAVFGIPKTIDNDLSFSHRTFGFETAVDKAVEAVRA 252
Cdd:COG0205 79 eeGREKALENLKKLGIDALVVIGGDGSLDGAAKLAEEYG-----IPVVGIPKTIDNDLPGTDYTIGFDTAVNTAAEAIDR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 253 AYAEAISLNyGVGVVKLMGRDSGFIaaeaavasaqaNICLVPENPISEDIVMALIQRRFETSR-SCVIIVAEGFGQDWEG 331
Cdd:COG0205 154 LRDTAASHE-RVFVVEVMGRHAGWLalaag-laggaDLILIPEVPFDLDKLLEKLKERRKRGKgYSIIVVAEGAGDEDGE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 332 --GTGGHDASGNKKLTDIGVVLTKRIqawlrknkERYPNGTVKYIDPSYMIRACPPSANDALFCATLSTLAMHEAMAGAT 409
Cdd:COG0205 232 avLEADTDAFGHVRLGGIGEYLAKEI--------EERTGIETRVTVLGHLQRGGSPSAFDRVLASRLGAAAVELLLEGKT 303
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 122047336 410 NCIIALRYNSYILVPIKVATSVRRVLDLRGQLWRQVREITV 450
Cdd:COG0205 304 GVMVGIRRGEIVLVPLEEVANKEKPVDPDSPLIQLARELGI 344
|
|
| PFK |
pfam00365 |
Phosphofructokinase; |
98-402 |
3.20e-56 |
|
Phosphofructokinase;
Pssm-ID: 459783 [Multi-domain] Cd Length: 271 Bit Score: 187.93 E-value: 3.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 98 VGIVTCGGICPGLNDVIRSLTLTAVNAYRvkRVIGFRFGYWGLSKKGshtAMELYRTSVTSIHRYGGTILGSSRG-PQDT 176
Cdd:pfam00365 2 IGILTSGGDAPGMNAAIRAVVRTAIYRGH--EVYGIRNGYEGLVEGD---IDELTWRDVSGILNRGGTILGTSRSkPFKT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 177 SE----MVDTLERLGVNILFTVGGDGTQRGALKIAEEAkrrgaNLAVFGIPKTIDNDLSFSHRTFGFETAVDKAVEAVRA 252
Cdd:pfam00365 77 EEgrekIAENLKKLGIDALVVIGGDGSLTGANKLSEER-----GIPVVGIPKTIDNDIPGTDYTIGFDTALNTIVEAIDR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 253 AYAEAISLNyGVGVVKLMGRDSGFIaaeaavasaqaNICLVPENPISEDIVMALIQRRFETSRSCVIIVAEGfgqdwegg 332
Cdd:pfam00365 152 IRDTASSHN-RVFVVEVMGRHCGWLalmag-laggaDAILIPEIPFDIEELCEKIKELRKGKRFSIIVVAEG-------- 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 333 tgghdASGnkkltdiGVVLTKRIQAwlRKNKErypngtVKYIDPSYMIRACPPSANDALFCATLSTLAMH 402
Cdd:pfam00365 222 -----ASD-------GEFLAKLIEE--GTGIE------TRVTVLGHVQRGGTPSAFDRILATRLGVKAVE 271
|
|
| PFK_mixed |
TIGR02483 |
phosphofructokinase; Members of this family that are characterized, save one, are ... |
98-429 |
2.16e-51 |
|
phosphofructokinase; Members of this family that are characterized, save one, are phosphofructokinases dependent on pyrophosphate (EC 2.7.1.90) rather than ATP (EC 2.7.1.11). The exception is one of three phosphofructokinases from Streptomyces coelicolor. Family members are both bacterial and archaeal. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 274155 [Multi-domain] Cd Length: 324 Bit Score: 177.11 E-value: 2.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 98 VGIVTCGGICPGLNDVIRSLTLTAVNAYRVKrVIGFRFGYWGLSKKGshTAMELYRTSVTSIHRYGGTILGSSRG-PQDT 176
Cdd:TIGR02483 2 IGVLTGGGDCPGLNAVIRGVVRRAIAEYGWE-VIGIRDGWRGLLEGD--TVPLLDLEDVRGILPRGGTILGSSRTnPFKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 177 SEM-----VDTLERLGVNILFTVGGDGTqrgaLKIAEEAKRRGanLAVFGIPKTIDNDLSFSHRTFGFETAVDKAVEAVR 251
Cdd:TIGR02483 79 EEDgddkiVANLKELGLDALIAIGGDGT----LGIARRLADKG--LPVVGVPKTIDNDLEATDYTFGFDTAVEIATEALD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 252 AAYAEAISLNYgVGVVKLMGRDSGFIaAEAAVASAQANICLVPENPISEDIVMALIQRRFETSRS-CVIIVAEGF---GQ 327
Cdd:TIGR02483 153 RLHTTAESHHR-VMVVEVMGRHAGWI-ALHSGIAGGADVILIPEIPFDIDSVCEKVRERFARGKRfAIVVVAEGAkpkGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 328 DWEGGTGGHDASGNKKLTDIGVVLTKRIQAwlRKNKERYPngTVKyidpSYMIRACPPSANDALFCATLSTLAMHEAMAG 407
Cdd:TIGR02483 231 EMVVQEGVKDAFGHVRLGGIGNWLAEEIER--RTGIETRA--TVL----GHLQRGGSPSAFDRVLATRFGVAAVDLVHEG 302
|
330 340
....*....|....*....|..
gi 122047336 408 ATNCIIALRYNSYILVPIKVAT 429
Cdd:TIGR02483 303 QFGHMVALRGTDIVYVPIAEAV 324
|
|
| PFK |
cd00363 |
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ... |
98-443 |
3.46e-42 |
|
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate. The members belong to PFK family that includes ATP- and pyrophosphate (PPi)- dependent phosphofructokinases. Some members evolved by gene duplication and thus have a large C-terminal/N-terminal extension comprising a second PFK domain. Generally, ATP-PFKs are allosteric homotetramers, and PPi-PFKs are dimeric and nonallosteric except for plant PPi-PFKs which are allosteric heterotetramers.
Pssm-ID: 238216 [Multi-domain] Cd Length: 338 Bit Score: 152.84 E-value: 3.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 98 VGIVTCGGICPGLNDVIRSLTLTAVnaYRVKRVIGFRFGYWGLSKkGSHtaMELYRTSVTSIHRYGGTILGSSRGPQDTS 177
Cdd:cd00363 3 IGVLTSGGDAPGMNAAIRGVVRSAI--AEGLEVYGIYEGYAGLVE-GDI--KELDWESVSDIINRGGTIIGSARCKEFRT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 178 E-----MVDTLERLGVNILFTVGGDGTQRGALKIAEEAKRRGANLAVFGIPKTIDNDLSFSHRTFGFETAVDKAVEAVRA 252
Cdd:cd00363 78 EegrakAAENLKKHGIDALVVIGGDGSYTGADLLTEEWPSKYQGFNVIGLPGTIDNDIKGTDYTIGFDTALKTIVEAIDR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 253 AYAEAISLNYgVGVVKLMGRDSGFIaAEAAVASAQANICLVPENP----ISEDIVMALIQRRFETSRSCVIIVAEGFGQD 328
Cdd:cd00363 158 IRDTASSHQR-TFVVEVMGRHCGDI-ALEAGLATGADIIFIPEEPaadeWEEEMVDVIKKRRERGKRHGIVIVAEGAIDF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 329 WEGGTGGHdasgnkkltDIGVVLTKRIQAWLRknkerypnGTVKyidpSYMIRACPPSANDALFCATLSTLAMHEAMAGA 408
Cdd:cd00363 236 IPKPITEK---------LLAKLVEERLGFDTR--------ATVL----GHVQRGGTPTAFDRILASRLGAEAVELLLEGT 294
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 122047336 409 TN---CIIALRYNSYILVPIKVATSVRR--VLDLRGQLWR 443
Cdd:cd00363 295 GGtpvGIQNLNENQVVRHPLTEAVNMTKrvGVDLEGRPFK 334
|
|
| PRK03202 |
PRK03202 |
ATP-dependent 6-phosphofructokinase; |
98-324 |
1.96e-41 |
|
ATP-dependent 6-phosphofructokinase;
Pssm-ID: 235111 [Multi-domain] Cd Length: 320 Bit Score: 150.23 E-value: 1.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 98 VGIVTCGGICPGLNDVIRSLTLTAVnaYRVKRVIGFRFGYWGLSKKgshTAMELYRTSVTSIHRYGGTILGSSRGPQDTS 177
Cdd:PRK03202 4 IGVLTSGGDAPGMNAAIRAVVRTAI--SEGLEVYGIYDGYAGLLEG---DIVKLDLKSVSDIINRGGTILGSARFPEFKD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 178 E-----MVDTLERLGVNILFTVGGDGTQRGALKIAEEakrrgaNLAVFGIPKTIDNDLSFSHRTFGFETAVDKAVEAVRA 252
Cdd:PRK03202 79 EegrakAIENLKKLGIDALVVIGGDGSYMGAKRLTEH------GIPVIGLPGTIDNDIAGTDYTIGFDTALNTAVEAIDR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 122047336 253 AYAEAISLNYgVGVVKLMGRDSGFIaaeaavasaqaNICLVPENPISEDIVMALIQRRFET-SRSCVIIVAEG 324
Cdd:PRK03202 153 LRDTASSHER-VFIVEVMGRHAGDLalhag-iaggaEVILIPEVPFDIEELCAKIKKGRERgKKHAIIVVAEG 223
|
|
| PRK14071 |
PRK14071 |
ATP-dependent 6-phosphofructokinase; |
98-446 |
3.45e-36 |
|
ATP-dependent 6-phosphofructokinase;
Pssm-ID: 184487 [Multi-domain] Cd Length: 360 Bit Score: 137.12 E-value: 3.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 98 VGIVTCGGICPGLNDVIRSLTLTAVNAYRVKrVIGFRFGYWGLSKKGSHtAMELYRTSVTSIHRYGGTILGSS-RG---- 172
Cdd:PRK14071 7 IGILTSGGDCAGLNAVIRAVVHRARGTYGWE-VIGIRDATQGLMARPPQ-YIELDLDQVDDLLRMGGTILGTTnKGdpfa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 173 -P------QDTS-EMVDTLERLGVNILFTVGGDGTQRGALKIAEEAkrrGANLAvfGIPKTIDNDLSFSHRTFGFETAVD 244
Cdd:PRK14071 85 fPmpdgslRDRSqEIIDGYHSLGLDALIGIGGDGSLAILRRLAQQG---GINLV--GIPKTIDNDVGATEVSIGFDTAVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 245 KAVEAVRAAYAEAISLNYgVGVVKLMGRDSGFIaAEAAVASAQANICLVPENPISEDIVMALIQRRFETSRS-CVIIVAE 323
Cdd:PRK14071 160 IATEALDRLHFTAASHNR-VMILEVMGRDAGHI-ALAAGIAGGADVILIPEIPYTLENVCKKIRERQEEGKNfCLVVVSE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 324 G--------------FGQDWEGGTGGHdasgnkkltdIGVVLTKRIQAWLRKnkerypngTVKyidpSYMIRACPPSAND 389
Cdd:PRK14071 238 AvrteegeqvtktqaLGEDRYGGIGQY----------LAEQIAERTGAETRV--------TVL----GHIQRGGIPSPRD 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 122047336 390 ALFCATLSTLAMHEAMAGATNCIIALRYNSYILVPIKVATSVRRVLDLRGQLWRQVR 446
Cdd:PRK14071 296 RLLASAFGVAAVDLIAQGKFDRMVAWQNRQVVSVPIAEAIATYRAVDPEGTLVKTAR 352
|
|
| Bacterial_PFK |
cd00763 |
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ... |
98-324 |
8.90e-29 |
|
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate. The members belong to a subfamily of the PFKA family (cd00363) and include bacterial ATP-dependent phosphofructokinases. These are allosrterically regulated homotetramers; the subunits are of about 320 amino acids.
Pssm-ID: 238388 [Multi-domain] Cd Length: 317 Bit Score: 115.58 E-value: 8.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 98 VGIVTCGGICPGLNDVIRSLTLTAVnaYRVKRVIGFRFGYWGLSkkgSHTAMELYRTSVTSIHRYGGTILGSSRGPQDTS 177
Cdd:cd00763 3 IGVLTSGGDAPGMNAAIRGVVRSAI--AEGLEVYGIRDGYAGLI---AGDIVPLDRYSVSDIINRGGTFLGSARFPEFKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 178 E-----MVDTLERLGVNILFTVGGDGTQRGALKIAEEAkrrganLAVFGIPKTIDNDLSFSHRTFGFETAVDKAVEAVRA 252
Cdd:cd00763 78 EegqakAIEQLKKHGIDALVVIGGDGSYMGAMRLTEHG------FPCVGLPGTIDNDIPGTDYTIGFDTALNTVVEAIDR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 122047336 253 AYAEAISLNYgVGVVKLMGRDSGFIAAEAAVASAQANIClVPENPISEDIVMALIQRRFET-SRSCVIIVAEG 324
Cdd:cd00763 152 IRDTSSSHQR-ISVVEVMGRHCGDIALAAGIAGGAEFIV-IPEAEFDREEVANRIKAGIERgKKHAIVVVAEG 222
|
|
| PRK14072 |
PRK14072 |
diphosphate--fructose-6-phosphate 1-phosphotransferase; |
167-434 |
7.98e-20 |
|
diphosphate--fructose-6-phosphate 1-phosphotransferase;
Pssm-ID: 237600 [Multi-domain] Cd Length: 416 Bit Score: 91.46 E-value: 7.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 167 LGSSR--------GPQDTSEMVDTLERLGVNILFTVGGDGTQRGALKIAEEAKRRGANLAVFGIPKTIDNDLSFSHRTFG 238
Cdd:PRK14072 75 LGSCRyklksleeDRAEYERLLEVFKAHDIGYFFYNGGNDSMDTALKVSQLAKKMGYPIRCIGIPKTIDNDLPGTDHCPG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 239 FETAVDKAVEAVRAAY--AEAISLNYGVGVVKLMGRDSGFIAAEAAVASAQAN----ICLVPENPISEDIVMALIQRRFE 312
Cdd:PRK14072 155 FGSAAKYIATSVLEAAldVAAMANTSKVFILEVMGRHAGWLAAAAALAKQNPDdaphLIYLPERPFDEEKFLADVRAIVK 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 313 TSRSCVIIVAEGFgQDWEGG----TGGH-DASGNKKLTDIGVVLTKRIqawlrKNKERYPngtVKYIDPSYMIRACP--P 385
Cdd:PRK14072 235 RYGYCVVVVSEGI-RDADGKfiaeAGLAeDAFGHAQLGGVAPVLANLI-----KEKLGKK---VHWAVLDYLQRAARhiA 305
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 122047336 386 SANDALFCATLSTLAMHEAMAGATNCIIALR------YN-SYILVPI-KVATSVRRV 434
Cdd:PRK14072 306 SKTDVEEAYAVGKAAVEYALAGKNGVMPAIRrtsddpYKwKIGLVPLsKVANKEKKM 362
|
|
| 6PF1K_euk |
TIGR02478 |
6-phosphofructokinase, eukaryotic type; Members of this family are eukaryotic (with one ... |
98-324 |
4.07e-19 |
|
6-phosphofructokinase, eukaryotic type; Members of this family are eukaryotic (with one exception) ATP-dependent 6-phosphofructokinases (EC 2.7.1.11) in which two tandem copies of the phosphofructokinase are found. Members are found, often including several isozymes, in animals and fungi and in the bacterium Propionibacterium acnes KPA171202 (a human skin commensal).
Pssm-ID: 274152 [Multi-domain] Cd Length: 746 Bit Score: 90.48 E-value: 4.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 98 VGIVTCGGICPGLNDVIRSLTLTAVnaYRVKRVIGFRFGYWGLSKKGSHTAmELYRTSVTSIHRYGGTILGSSRgpqdTS 177
Cdd:TIGR02478 3 IAVLTSGGDAQGMNAAVRAVVRMAI--YVGCRVYAIREGYQGLVDGGDNIE-EAQWEDVRGILSLGGTIIGTAR----CK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 178 EMVDTLERL---------GVNILFTVGGDGTQRGA-----------------LKIAEEAKRRGANLAVFGIPKTIDNDLS 231
Cdd:TIGR02478 76 EFRERPGRLkaarnlvsnGIDALVVIGGDGSLTGAdlfreewpslleelvdtGKITAEQAEEHRHLTIVGLVGSIDNDMC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 232 FSHRTFGFETAVDKAVEAVRAAYAEAISLNYGVgVVKLMGRDSGFIAAEAAVASAQANIcLVPENPIS----EDIVMALI 307
Cdd:TIGR02478 156 GTDMTIGADSALHRICEAIDAISSTAQSHQRAF-VVEVMGRHCGYLALMAAIATGADYV-FIPERPPEegweDQLCHKLK 233
|
250
....*....|....*..
gi 122047336 308 QRRFETSRSCVIIVAEG 324
Cdd:TIGR02478 234 RNRKAGKRKTIVIVAEG 250
|
|
| Eukaryotic_PFK |
cd00764 |
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ... |
98-324 |
1.03e-18 |
|
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate. The members belong to a subfamily of the PFKA family (cd00363) and include eukaryotic ATP-dependent phosphofructokinases. These have evolved from the bacterial PFKs by gene duplication and fusion events and exhibit complex allosteric behavior.
Pssm-ID: 238389 [Multi-domain] Cd Length: 762 Bit Score: 89.50 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 98 VGIVTCGGICPGLNDVIRSLTLTAVnaYRVKRVIGFRFGYWGLSKKGSHTAmELYRTSVTSIHRYGGTILGSSRGP---- 173
Cdd:cd00764 6 IAVLTSGGDAQGMNAAVRAVVRMGI--YVGAKVFFVYEGYEGLVKGGDYIK-QAEWESVSNWLQEGGTIIGSARCKefre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 174 -----QDTSEMVDTlerlGVNILFTVGGDGTQRGAL-----------------KIAEEAKRRGANLAVFGIPKTIDNDLS 231
Cdd:cd00764 83 regrlQAAYNLIQR----GITNLCVIGGDGSLTGADlfrsewpslleelvkdgKITEEEVAKYQHLNIVGMVGSIDNDFC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 232 FSHRTFGFETAVDKAVEAVRAAYAEAISLNYGVgVVKLMGRDSGFIAAEAAVASAQANIcLVPENPIS---EDIVMALIQ 308
Cdd:cd00764 159 GTDMTIGTDSALHRICEVVDAITTTAQSHQRTF-VLEVMGRHCGYLALVSGLATGADWI-FIPERPPEdgwEDQMCRRLS 236
|
250
....*....|....*..
gi 122047336 309 R-RFETSRSCVIIVAEG 324
Cdd:cd00764 237 EhRSRGKRLNIIIVAEG 253
|
|
| PRK06555 |
PRK06555 |
pyrophosphate--fructose-6-phosphate 1-phosphotransferase; Validated |
98-277 |
1.46e-16 |
|
pyrophosphate--fructose-6-phosphate 1-phosphotransferase; Validated
Pssm-ID: 180620 [Multi-domain] Cd Length: 403 Bit Score: 81.59 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 98 VGIVTCGGICPGLNDVIRSLtltaVNAYRVK----RVIGFRFGYWGLSKKGSHTAMELYRTSVTSIHRYGGTILGSSR-- 171
Cdd:PRK06555 6 VALLTAGGLAPCLSSAVGGL----IERYTEIapevEIIAYRSGYQGLLLGDSIEITPAVRANAGLLHRYGGSPIGNSRvk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 172 --GPQD------TSEMVDTL----ERL---GVNILFTVGGDGTQRGALKIAEEAKRRGANLAVFGIPKTIDNDLSFSHRT 236
Cdd:PRK06555 82 ltNVADcvkrglVKEGENPLkvaaERLaadGVDILHTIGGDDTNTTAADLAAYLAENGYDLTVVGLPKTIDNDVVPIRQS 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 122047336 237 FGFETAVDKAveavrAAYAEAISLNYGVG-----VVKLMGRDSGFI 277
Cdd:PRK06555 162 LGAWTAAEQG-----ARFFDNVINEHSANprmliIHEVMGRNCGWL 202
|
|
| PRK07085 |
PRK07085 |
diphosphate--fructose-6-phosphate 1-phosphotransferase; Provisional |
98-324 |
1.32e-15 |
|
diphosphate--fructose-6-phosphate 1-phosphotransferase; Provisional
Pssm-ID: 235930 Cd Length: 555 Bit Score: 79.19 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 98 VGIVTCGGICPGLNDVIRSL--TLTAVNAYrvKRVIGFRFGYWGLSKkgsHTAMELYRTSVTSIHRYGG-TILGSSRGPQ 174
Cdd:PRK07085 73 VGVILSGGQAPGGHNVIAGLfdGLKKLNPD--SKLFGFIGGPLGLLN---GKYIEITEEVIDEYRNTGGfDMIGSGRTKI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 175 DTSE----MVDTLERLGVNILFTVGGDGTQRGALKIAEEAKRRGANLAVFGIPKTIDNDLSFSH--RTFGFETAVDkave 248
Cdd:PRK07085 148 ETEEqkeaCLETVKKLKLDGLVIIGGDDSNTNAAILAEYFAKHGCKTQVIGVPKTIDGDLKNEFieTSFGFDTATK---- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 249 avraAYAEAIS-----LNYGVG---VVKLMGRDSGFIaAEAAVASAQANICLVPE---------NPISEDIVMALIQRRF 311
Cdd:PRK07085 224 ----TYSEMIGnisrdALSAKKywhFIKLMGRSASHI-ALECALQTHPNICLISEevaekkmslQDIVHYIASVIADRAA 298
|
250
....*....|...
gi 122047336 312 ETSRSCVIIVAEG 324
Cdd:PRK07085 299 KGKNYGVILIPEG 311
|
|
| PTZ00287 |
PTZ00287 |
6-phosphofructokinase; Provisional |
98-325 |
3.30e-15 |
|
6-phosphofructokinase; Provisional
Pssm-ID: 240345 [Multi-domain] Cd Length: 1419 Bit Score: 78.54 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 98 VGIVTCGGICPGLNDVIRSLTLTAVNAYRVKRVIGFRFGYWGLSKKGSHTAMElyrTSVTSIHRYGG-TILGSSRGP--- 173
Cdd:PTZ00287 180 IGIILSGGPAPGGHNVISGIYDYAKRYNEQSQVIGFLGGIDGLYSKNYVTITD---SLMNRFRNLGGfNMLWSGRGKvrn 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 174 -QDTSEMVDTLERLGVNILFTVGGDGTQRGALKIAEEAKRRGANLAVFGIPKTIDNDLSFS--HRTFGFETAVDKAVEAV 250
Cdd:PTZ00287 257 kDDLIAIENIVAKLKLNGLVIIGGDGSNSNAALISEYFAERQIPISIIGIPKTIDGDLKSEaiEISFGFDTATKTYSEVI 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 251 RAAYAEAISLNYGVGVVKLMGRDSGFIaAEAAVASAQANICLVPE---------NPISEDIVMALIQRRFETSRSCVIIV 321
Cdd:PTZ00287 337 GNLCTDVKTGHNVYHVVRVMGRSASHV-VLECALQTRPNIVLIGEevekenlslKDIVSNIVNTILKRRSLNKNYGVILI 415
|
....
gi 122047336 322 AEGF 325
Cdd:PTZ00287 416 PEGL 419
|
|
| Pyrophosphate_PFK |
cd00765 |
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ... |
93-324 |
4.95e-15 |
|
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate. The members belong to a subfamily of the PFKA family (cd00363) and include pyrophosphate-dependent phosphofructokinases. These are found in bacteria as well as plants. These may be dimeric nonallosteric enzymes as in bacteria or allosteric heterotetramers as in plants.
Pssm-ID: 238390 Cd Length: 550 Bit Score: 77.60 E-value: 4.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 93 PPETVVGIVTCGGICPGLNDVIRSLTLTAVNAYRVKRVIGFRFGYWGLsKKGSHtaMELYRTSVTSIHRYGG-TILGSSR 171
Cdd:cd00765 70 APKLKIGIVLSGGQAPGGHNVISGLFDYLKERAKGSTLYGFKGGPAGI-LKCDY--IELNAEYIQPYRNTGGfDMICSGR 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 172 GPQDTSEM----VDTLERLGVNILFTVGGDGTQRGALKIAEEAKRRGANLAVFGIPKTIDNDLSFSH--RTFGFETAVDK 245
Cdd:cd00765 147 TKIETEDQfkqaEETAKKLDLDALVVIGGDDSNTNAALLAENFRSKGLKTRVIGVPKTIDGDLKNKEieTSFGFDTATKI 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 246 AVEAVRAAYAEAISLNYGVGVVKLMGRDSGFIaAEAAVASAQANICLVPE---------NPISEDIVMALIQRRFETSRS 316
Cdd:cd00765 227 YSELIGNVMRDARSTGKYWHFVKLMGRSASHI-ALECALKTHPNICIISEevsaqkqtlKNITDYMVDVICKRAELGYNF 305
|
....*...
gi 122047336 317 CVIIVAEG 324
Cdd:cd00765 306 GVVLVPEG 313
|
|
| PTZ00468 |
PTZ00468 |
phosphofructokinase family protein; Provisional |
35-277 |
3.13e-14 |
|
phosphofructokinase family protein; Provisional
Pssm-ID: 185647 [Multi-domain] Cd Length: 1328 Bit Score: 75.78 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 35 RKYMNPSKKHVMREEFS----DKIEHIMHDPRpqEGVHSELPVSISPLLCELAAPRQRI----HFnpPETVVGIVTCGGI 106
Cdd:PTZ00468 38 RRRWEPCLPHILRSPLSikevSAFEGMGKMER--SDVSSYFPLTSGNSLVKFEAISDGSsswkKF--PARRIGVVLSGGQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 107 CPGLNDVIRSLTLTAVNAYRVKRVIGFRFGYWGLSkkgSHTAMELYRTSVTSIHRYGG-TILGSSRGPQDTSEM----VD 181
Cdd:PTZ00468 114 ASGGHNVIAGLMSYIKLCNQSSQLFGFLGGPEGVY---SERYRELTEDDINGILNQGGfNIICSGRHKIETEEQmrasLE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 182 TLERLGVNILFTVGGDGTQRGALKIAEEAKRRGANLAVFGIPKTIDNDLSFS--HRTFGFETAVDKAVEAVRAAYAEAIS 259
Cdd:PTZ00468 191 ICEKLKLHGLVVIGGDDSNTNAAVLAEYFKRNSSSTVVVGCPKTIDGDLKNEviETSFGYDTAVKTYSEQIGSIMDAIKT 270
|
250
....*....|....*...
gi 122047336 260 LNYGVGVVKLMGRDSGFI 277
Cdd:PTZ00468 271 EGYGYYFVRLMGRSASHI 288
|
|
| 6PF1K_euk |
TIGR02478 |
6-phosphofructokinase, eukaryotic type; Members of this family are eukaryotic (with one ... |
81-321 |
1.48e-13 |
|
6-phosphofructokinase, eukaryotic type; Members of this family are eukaryotic (with one exception) ATP-dependent 6-phosphofructokinases (EC 2.7.1.11) in which two tandem copies of the phosphofructokinase are found. Members are found, often including several isozymes, in animals and fungi and in the bacterium Propionibacterium acnes KPA171202 (a human skin commensal).
Pssm-ID: 274152 [Multi-domain] Cd Length: 746 Bit Score: 73.14 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 81 ELAAPRQRIHFNPPET---VVGIVTCGGICPGLNDVIRSLTLTAVnaYRVKRVIGFRFGYWGLSKKGSHtamELYRTSVT 157
Cdd:TIGR02478 372 FLSIPDDDKKLVPSEAsrlRIAIIHVGAPAGGMNAATRSAVRYAL--ARGHTVIAIHNGFSGLARHDVR---ELTWSDVE 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 158 SIHRYGGTILGSSRG-PQDTSEMVDT-LERLGVNILFTVGGDGTQRGALKIAEEAKRRGA-NLAVFGIPKTIDNDLSFSH 234
Cdd:TIGR02478 447 GWVGEGGSELGTNRSlPGDDLGTIAYyFQQHKIDGLIIIGGFEAFEALYQLDAAREKYPAfRIPMVVIPATISNNVPGTE 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 235 RTFGFETAVDKAVEAVRAAYAEAISLNYGVGVVKLMGRDSGFIAAEAAVASAQANIcLVPENPISEDIVMALI---QRRF 311
Cdd:TIGR02478 527 YSLGSDTALNEITEYCDNIKQSASASKRRVFVVETMGGYSGYLATMAGLATGADAA-YIPEEGISLKDLQEDIehlKETF 605
|
250
....*....|
gi 122047336 312 ETSRSCVIIV 321
Cdd:TIGR02478 606 AEGRAGKLIL 615
|
|
| PLN02251 |
PLN02251 |
pyrophosphate-dependent phosphofructokinase |
98-277 |
5.15e-08 |
|
pyrophosphate-dependent phosphofructokinase
Pssm-ID: 215140 Cd Length: 568 Bit Score: 55.18 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 98 VGIVTCGGICPGLNDVIRSLTLTAVNAYRVKRVIGFRFGYWGLSKkgsHTAMELYRTSVTSIHRYGG-TILGSSRGPQDT 176
Cdd:PLN02251 99 IGVVLSGGQAPGGHNVISGIFDYLQEHAKGSVLYGFKGGPAGIMK---CKYVELTAEFIYPYRNQGGfDMICSGRDKIET 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 177 SEM----VDTLERLGVNILFTVGGDGTQRGALKIAEEAKRRGANLAVFGIPKTIDNDLSFSH--RTFGFETAVDKAVEAV 250
Cdd:PLN02251 176 PEQfkqaEETATKLDLDGLVVIGGDDSNTNACLLAEYFRAKNLKTRVIGCPKTIDGDLKSKEvpTSFGFDTACKIYSEMI 255
|
170 180
....*....|....*....|....*..
gi 122047336 251 RAAYAEAISLNYGVGVVKLMGRDSGFI 277
Cdd:PLN02251 256 GNVMIDARSTGKYYHFVRLMGRAASHI 282
|
|
| PLN03028 |
PLN03028 |
pyrophosphate--fructose-6-phosphate 1-phosphotransferase; Provisional |
27-272 |
9.79e-08 |
|
pyrophosphate--fructose-6-phosphate 1-phosphotransferase; Provisional
Pssm-ID: 215543 Cd Length: 610 Bit Score: 54.40 E-value: 9.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 27 LKVERLHGRKYMNPSKKHVMREEFSdkieHIMHDPRpqegVHSELPVSISPllcelaaPRQRIHFNPPeTVVGIVTCGGI 106
Cdd:PLN03028 27 VRVELGDATTAADPADAHAISRAFP----HTYGQPL----AHFLRATAKVP-------DAQVITEHPA-VRVGVVFCGRQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 107 CPGLNDVIRSL--TLTAVNAYRVkrVIGFRFGYWGLSKKGShtaMELYRTSVTSIHRYGG-TILGSSRGPQDTSEMVD-- 181
Cdd:PLN03028 91 SPGGHNVIWGLhdALKAHNPNSV--LLGFLGGTEGLFAQKT---LEITDDVLSTYKNQGGyDLLGRTKDQIRTTEQVNaa 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 182 --TLERLGVNILFTVGGDGTQRGALKIAEEAKRRGANLAVFGIPKTIDNDL--SFSHRTFGFETAVDKAVEAVRAAYAEA 257
Cdd:PLN03028 166 laACEALKLDGLVIIGGVTSNTDAAQLAETFAEAKCKTKVVGVPVTLNGDLknQFVETNVGFDTICKVNSQLISNVCTDA 245
|
250
....*....|....*
gi 122047336 258 ISLNYGVGVVKLMGR 272
Cdd:PLN03028 246 LSAEKYYYFIRLMGR 260
|
|
| Eukaryotic_PFK |
cd00764 |
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ... |
98-299 |
4.15e-06 |
|
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate. The members belong to a subfamily of the PFKA family (cd00363) and include eukaryotic ATP-dependent phosphofructokinases. These have evolved from the bacterial PFKs by gene duplication and fusion events and exhibit complex allosteric behavior.
Pssm-ID: 238389 [Multi-domain] Cd Length: 762 Bit Score: 49.44 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 98 VGIVTCGGICPGLNDVIRSLTLTAVNayRVKRVIGFRFGYWGLSKKGShtaMELYRTSVTSIHRYGGTILGSSR--GPQD 175
Cdd:cd00764 392 IAIVNVGAPAAGMNAAVRSAVRYGLA--HGHRPYAIYDGFEGLAKGQI---VELGWIDVGGWTGRGGSELGTKRtlPKKD 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 176 TSEMVDTLERLGVNILFTVGGDGTQRGALKIAEEAKRRGA-NLAVFGIPKTIDNDLSFSHRTFGFETAVDKAVEAVRAAY 254
Cdd:cd00764 467 LETIAYNFQKYGIDGLIIVGGFEAYKGLLQLREAREQYEEfCIPMVLIPATVSNNVPGTDFSLGSDTALNALMKYCDRIK 546
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 122047336 255 AEAISLNYGVGVVKLMGRDSGFIAAeAAVASAQANICLVPENPIS 299
Cdd:cd00764 547 QSASGTKRRVFIVETMGGYCGYLAT-MTGLAVGADAAYVFEEPFN 590
|
|
| DAGK_cat |
pfam00781 |
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ... |
172-260 |
1.10e-03 |
|
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologs. YegS is the Escherichia coli protein in this family whose crystal structure reveals an active site in the inter-domain cleft formed by four conserved sequence motifs, revealing a novel metal-binding site. The residues of this site are conserved across the family.
Pssm-ID: 425868 [Multi-domain] Cd Length: 125 Bit Score: 39.11 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122047336 172 GPQDTSEMVDTLERLGVNILFTVGGDGTQRGALKIAEEAKRRGAnLAVfgIPKTIDNDLSfshRTFGFETAVDKAVEAVR 251
Cdd:pfam00781 40 GPGDALELAREAAEDGYDRIVVAGGDGTVNEVLNGLAGLATRPP-LGI--IPLGTGNDFA---RALGIPGDPEEALEAIL 113
|
....*....
gi 122047336 252 AAYAEAISL 260
Cdd:pfam00781 114 KGQTRPVDV 122
|
|
|