|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06555 |
PRK06555 |
pyrophosphate--fructose-6-phosphate 1-phosphotransferase; Validated |
1-403 |
0e+00 |
|
pyrophosphate--fructose-6-phosphate 1-phosphotransferase; Validated
Pssm-ID: 180620 [Multi-domain] Cd Length: 403 Bit Score: 818.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 1 MAKQKVAMLTAGGLAPCLSSAVGGLIERYSDVAPELEIVAYKSGYQGVLLGDSIEITPAIREKAPLLHRYGGSPIGNSRV 80
Cdd:PRK06555 1 MAVKKVALLTAGGLAPCLSSAVGGLIERYTEIAPEVEIIAYRSGYQGLLLGDSIEITPAVRANAGLLHRYGGSPIGNSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 81 KLTNAADCVKRGLVKEGENPLRIAAERLANDGITILHTIGGDDTNTTAADLAAYLAANGYDLTVVGLPKTVDNDVVPIRQ 160
Cdd:PRK06555 81 KLTNVADCVKRGLVKEGENPLKVAAERLAADGVDILHTIGGDDTNTTAADLAAYLAENGYDLTVVGLPKTIDNDVVPIRQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 161 SLGAWTAAEVGAHFFDNVGNEQTAAPRTLVIHEVMGRHCGWLTAATARAYLQRTSRNQYVDGLMMDAHLKSIDAVYLPEM 240
Cdd:PRK06555 161 SLGAWTAAEQGARFFDNVINEHSANPRMLIIHEVMGRNCGWLTAATARAYREWLDRQEYVPGFGLSAERWDIHAVYLPEM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 241 AFDLDAEAARLKESMDRNGHATVFVSEGACLDAIVAEREAAGETVKRDAFGHVKIDTINVGAWFQKQFANLLDAERSLVQ 320
Cdd:PRK06555 241 AFDLEAEAERLKAVMDEVGNVNIFLSEGAGLDAIVAEMEAAGEEVKRDAFGHVKLDTINPGAWFAKQFAELLGAEKVMVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 321 KSGYFARSAPANADDLRLIQSMVDLAVESALNKVSGVTGHDEGQNGKLRTIEFPRIKGGKAFDLSTAWFAEVMDNIGQKY 400
Cdd:PRK06555 321 KSGYFARSAPANAEDLRLIKSMVDLAVECALRGVSGVIGHDEEQGGKLRAIEFPRIKGGKAFDTSTPWFTELLDEIGQPY 400
|
...
gi 502306579 401 KEA 403
Cdd:PRK06555 401 GPA 403
|
|
| PfkA |
COG0205 |
6-phosphofructokinase [Carbohydrate transport and metabolism]; 6-phosphofructokinase is part ... |
3-393 |
4.23e-81 |
|
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: 252.30 E-value: 4.23e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 3 KQKVAMLTAGGLAPCLSSAVGGLIERYsdVAPELEIVAYKSGYQGVLLGDSIEITpaiREKAPLLHRYGGSPIGNSRVKL 82
Cdd:COG0205 1 MKRIGILTSGGDAPGLNAAIRAVVRTA--IKYGIEVYGIRDGYEGLLEGDIIDLT---REDVSGILQRGGTILGSSRSKP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 83 TNAADCVKRglvkegenplriAAERLANDGITILHTIGGDDTNTTAADLAAYlaangYDLTVVGLPKTVDNDVVPIRQSL 162
Cdd:COG0205 76 FKTEEGREK------------ALENLKKLGIDALVVIGGDGSLDGAAKLAEE-----YGIPVVGIPKTIDNDLPGTDYTI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 163 GAWTAAEVGAHFFDNVGNEQTAAPRTLVIhEVMGRHCGWLTAATARAYlqrtsrnqyvdglmmDAHLksidaVYLPEMAF 242
Cdd:COG0205 139 GFDTAVNTAAEAIDRLRDTAASHERVFVV-EVMGRHAGWLALAAGLAG---------------GADL-----ILIPEVPF 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 243 DLDAEAARLKESMDR-NGHATVFVSEGACLDAIVAEREAAgetvkRDAFGHVKidTINVGAWFQKQFANLLDAErSLVQK 321
Cdd:COG0205 198 DLDKLLEKLKERRKRgKGYSIIVVAEGAGDEDGEAVLEAD-----TDAFGHVR--LGGIGEYLAKEIEERTGIE-TRVTV 269
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502306579 322 SGYFARSAPANADDLRLIQSMVDLAVESALNKVSGVTGHDegQNGKLRTIEFPRIKGG-KAFDLSTAWFAEVM 393
Cdd:COG0205 270 LGHLQRGGSPSAFDRVLASRLGAAAVELLLEGKTGVMVGI--RRGEIVLVPLEEVANKeKPVDPDSPLIQLAR 340
|
|
| PFK |
pfam00365 |
Phosphofructokinase; |
5-293 |
5.38e-30 |
|
Phosphofructokinase;
Pssm-ID: 459783 [Multi-domain] Cd Length: 271 Bit Score: 116.67 E-value: 5.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 5 KVAMLTAGGLAP----CLSSAVGGLIERYsdvapeLEIVAYKSGYQGVLLGDSIEITPaiREKAPLLHRyGGSPIGNSRV 80
Cdd:pfam00365 1 RIGILTSGGDAPgmnaAIRAVVRTAIYRG------HEVYGIRNGYEGLVEGDIDELTW--RDVSGILNR-GGTILGTSRS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 81 KLTNAADCVKRglvkegenplriAAERLANDGITILHTIGGDDTNTTAADLAAYlaangYDLTVVGLPKTVDNDVVPIRQ 160
Cdd:pfam00365 72 KPFKTEEGREK------------IAENLKKLGIDALVVIGGDGSLTGANKLSEE-----RGIPVVGIPKTIDNDIPGTDY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 161 SLGAWTAAEVGAHFFDNVgnEQTAA--PRTLVIhEVMGRHCGWLTAATARAylqrtsrnqyvdglmmdahlKSIDAVYLP 238
Cdd:pfam00365 135 TIGFDTALNTIVEAIDRI--RDTASshNRVFVV-EVMGRHCGWLALMAGLA--------------------GGADAILIP 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 502306579 239 EMAFDLDAEAARLKESMDRNGHATVFVSEGACLDAIVAER--EAAGETVKRDAFGHV 293
Cdd:pfam00365 192 EIPFDIEELCEKIKELRKGKRFSIIVVAEGASDGEFLAKLieEGTGIETRVTVLGHV 248
|
|
| PFK_mixed |
TIGR02483 |
phosphofructokinase; Members of this family that are characterized, save one, are ... |
5-319 |
1.61e-23 |
|
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: 100.07 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 5 KVAMLTAGGLAPCLSSAVGGL----IERYSDvapelEIVAYKSGYQGVLLGDSIeITPAIREKAPLLHRyGGSPIGNSRv 80
Cdd:TIGR02483 1 RIGVLTGGGDCPGLNAVIRGVvrraIAEYGW-----EVIGIRDGWRGLLEGDTV-PLLDLEDVRGILPR-GGTILGSSR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 81 klTNAADCVKRGLVKegenplriAAERLANDGITILHTIGGDDTNTtaadLAAYLAANGydLTVVGLPKTVDNDVVPIRQ 160
Cdd:TIGR02483 73 --TNPFKYEEDGDDK--------IVANLKELGLDALIAIGGDGTLG----IARRLADKG--LPVVGVPKTIDNDLEATDY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 161 SLGAWTAAEVGAHFFDNVGNEQTAAPRTLVIhEVMGRHCGWLTAATaraylqrtsrnqyvdGLMMDAhlksiDAVYLPEM 240
Cdd:TIGR02483 137 TFGFDTAVEIATEALDRLHTTAESHHRVMVV-EVMGRHAGWIALHS---------------GIAGGA-----DVILIPEI 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 241 AFDLDAEAARLKESMDRNG-HATVFVSEGAcldaivaeREAAGETVKR----DAFGHVKIDTInvGAWFQKQFANLLDAE 315
Cdd:TIGR02483 196 PFDIDSVCEKVRERFARGKrFAIVVVAEGA--------KPKGGEMVVQegvkDAFGHVRLGGI--GNWLAEEIERRTGIE 265
|
....*
gi 502306579 316 -RSLV 319
Cdd:TIGR02483 266 tRATV 270
|
|
| PFK |
cd00363 |
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ... |
5-270 |
3.04e-21 |
|
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: 93.52 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 5 KVAMLTAGGLAPCLSSAVGGLIeRYSdVAPELEIVAYKSGYQGVLLGDSIEITpaIREKAPLLHRyGGSPIGNSRVKltn 84
Cdd:cd00363 2 KIGVLTSGGDAPGMNAAIRGVV-RSA-IAEGLEVYGIYEGYAGLVEGDIKELD--WESVSDIINR-GGTIIGSARCK--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 85 aadcvkrglVKEGENPLRIAAERLANDGITILHTIGGDDTNTTAADLAAYLAANGYDLTVVGLPKTVDNDVVPIRQSLGA 164
Cdd:cd00363 74 ---------EFRTEEGRAKAAENLKKHGIDALVVIGGDGSYTGADLLTEEWPSKYQGFNVIGLPGTIDNDIKGTDYTIGF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 165 WTAAEVGAHFFDNVGNEQTAAPRTLVIhEVMGRHCGWLTAATARAylqrtsrnqyvdglmmdahlKSIDAVYLPEMAFDL 244
Cdd:cd00363 145 DTALKTIVEAIDRIRDTASSHQRTFVV-EVMGRHCGDIALEAGLA--------------------TGADIIFIPEEPAAD 203
|
250 260 270
....*....|....*....|....*....|
gi 502306579 245 DAE---AARLKESMDR-NGHATVFVSEGAC 270
Cdd:cd00363 204 EWEeemVDVIKKRRERgKRHGIVIVAEGAI 233
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06555 |
PRK06555 |
pyrophosphate--fructose-6-phosphate 1-phosphotransferase; Validated |
1-403 |
0e+00 |
|
pyrophosphate--fructose-6-phosphate 1-phosphotransferase; Validated
Pssm-ID: 180620 [Multi-domain] Cd Length: 403 Bit Score: 818.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 1 MAKQKVAMLTAGGLAPCLSSAVGGLIERYSDVAPELEIVAYKSGYQGVLLGDSIEITPAIREKAPLLHRYGGSPIGNSRV 80
Cdd:PRK06555 1 MAVKKVALLTAGGLAPCLSSAVGGLIERYTEIAPEVEIIAYRSGYQGLLLGDSIEITPAVRANAGLLHRYGGSPIGNSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 81 KLTNAADCVKRGLVKEGENPLRIAAERLANDGITILHTIGGDDTNTTAADLAAYLAANGYDLTVVGLPKTVDNDVVPIRQ 160
Cdd:PRK06555 81 KLTNVADCVKRGLVKEGENPLKVAAERLAADGVDILHTIGGDDTNTTAADLAAYLAENGYDLTVVGLPKTIDNDVVPIRQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 161 SLGAWTAAEVGAHFFDNVGNEQTAAPRTLVIHEVMGRHCGWLTAATARAYLQRTSRNQYVDGLMMDAHLKSIDAVYLPEM 240
Cdd:PRK06555 161 SLGAWTAAEQGARFFDNVINEHSANPRMLIIHEVMGRNCGWLTAATARAYREWLDRQEYVPGFGLSAERWDIHAVYLPEM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 241 AFDLDAEAARLKESMDRNGHATVFVSEGACLDAIVAEREAAGETVKRDAFGHVKIDTINVGAWFQKQFANLLDAERSLVQ 320
Cdd:PRK06555 241 AFDLEAEAERLKAVMDEVGNVNIFLSEGAGLDAIVAEMEAAGEEVKRDAFGHVKLDTINPGAWFAKQFAELLGAEKVMVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 321 KSGYFARSAPANADDLRLIQSMVDLAVESALNKVSGVTGHDEGQNGKLRTIEFPRIKGGKAFDLSTAWFAEVMDNIGQKY 400
Cdd:PRK06555 321 KSGYFARSAPANAEDLRLIKSMVDLAVECALRGVSGVIGHDEEQGGKLRAIEFPRIKGGKAFDTSTPWFTELLDEIGQPY 400
|
...
gi 502306579 401 KEA 403
Cdd:PRK06555 401 GPA 403
|
|
| PfkA |
COG0205 |
6-phosphofructokinase [Carbohydrate transport and metabolism]; 6-phosphofructokinase is part ... |
3-393 |
4.23e-81 |
|
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: 252.30 E-value: 4.23e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 3 KQKVAMLTAGGLAPCLSSAVGGLIERYsdVAPELEIVAYKSGYQGVLLGDSIEITpaiREKAPLLHRYGGSPIGNSRVKL 82
Cdd:COG0205 1 MKRIGILTSGGDAPGLNAAIRAVVRTA--IKYGIEVYGIRDGYEGLLEGDIIDLT---REDVSGILQRGGTILGSSRSKP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 83 TNAADCVKRglvkegenplriAAERLANDGITILHTIGGDDTNTTAADLAAYlaangYDLTVVGLPKTVDNDVVPIRQSL 162
Cdd:COG0205 76 FKTEEGREK------------ALENLKKLGIDALVVIGGDGSLDGAAKLAEE-----YGIPVVGIPKTIDNDLPGTDYTI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 163 GAWTAAEVGAHFFDNVGNEQTAAPRTLVIhEVMGRHCGWLTAATARAYlqrtsrnqyvdglmmDAHLksidaVYLPEMAF 242
Cdd:COG0205 139 GFDTAVNTAAEAIDRLRDTAASHERVFVV-EVMGRHAGWLALAAGLAG---------------GADL-----ILIPEVPF 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 243 DLDAEAARLKESMDR-NGHATVFVSEGACLDAIVAEREAAgetvkRDAFGHVKidTINVGAWFQKQFANLLDAErSLVQK 321
Cdd:COG0205 198 DLDKLLEKLKERRKRgKGYSIIVVAEGAGDEDGEAVLEAD-----TDAFGHVR--LGGIGEYLAKEIEERTGIE-TRVTV 269
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502306579 322 SGYFARSAPANADDLRLIQSMVDLAVESALNKVSGVTGHDegQNGKLRTIEFPRIKGG-KAFDLSTAWFAEVM 393
Cdd:COG0205 270 LGHLQRGGSPSAFDRVLASRLGAAAVELLLEGKTGVMVGI--RRGEIVLVPLEEVANKeKPVDPDSPLIQLAR 340
|
|
| PTZ00286 |
PTZ00286 |
6-phospho-1-fructokinase; Provisional |
5-399 |
1.16e-31 |
|
6-phospho-1-fructokinase; Provisional
Pssm-ID: 185539 Cd Length: 459 Bit Score: 125.16 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 5 KVAMLTAGGLAPCLSSAVGGLIERYSDVAPELEIVAYKSGYQGVLLGDSIEITPAIREKaplLHRYGGSPIGNSRvkltn 84
Cdd:PTZ00286 89 KAGIVTCGGLCPGLNVVIRELVMNLINNYGVKTIYGAKYGYKGLYKEDWIKLDPKDVKT---IHRLGGTILGSSR----- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 85 aadcvkrglvkeGENPLRIAAERLANDGITILHTIGGDDTNTTAADLAAYLAANGYDLTVVGLPKTVDNDVVPIRQSLGA 164
Cdd:PTZ00286 161 ------------GGFDPKVMVDTLIRHGINILFTLGGDGTHRGALAIYKELRRRKLNISVVGIPKTIDNDIPIIDESFGF 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 165 WTAAEVGAHFFDNVGNEQTAAPRTLVIHEVMGRHCGWLTAATARAylqrtSRnqyvdglmmDAHLksidaVYLPEMAFDL 244
Cdd:PTZ00286 229 QTAVEEAQNAIRAAYVEAKSAKNGVGIVKLMGRDSGFIALHASVA-----SA---------DVNV-----CLIPEFDIPL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 245 DAEAARLKESMDRNGHATVFVSEGACldaivAEREAAGETVKRDAFGHVKIdtINVGAWFQKQFANLLDAERSLVQ---- 320
Cdd:PTZ00286 290 EGVLEYIEQRLQKKGHCVIVVAEGAG-----QSLKDADLDLGTDASGNKKL--WDIGVYLKDEITKYLKKKKPEHTvkyi 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 321 KSGYFARSAPANADDLRLIQSMVDLAVESALNKVSGVT-GHdegQNGKLRTIEFPRIKGG--KAFDLSTAWFAEVMDNIG 397
Cdd:PTZ00286 363 DPSYMIRAVPANAADAKFCTQLAQNAVHGAMAGFTGFIiGH---VHNNYVMIPIKEMSGNyrRRVNPEGRLWQRMLAITG 439
|
..
gi 502306579 398 QK 399
Cdd:PTZ00286 440 QP 441
|
|
| PFK |
pfam00365 |
Phosphofructokinase; |
5-293 |
5.38e-30 |
|
Phosphofructokinase;
Pssm-ID: 459783 [Multi-domain] Cd Length: 271 Bit Score: 116.67 E-value: 5.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 5 KVAMLTAGGLAP----CLSSAVGGLIERYsdvapeLEIVAYKSGYQGVLLGDSIEITPaiREKAPLLHRyGGSPIGNSRV 80
Cdd:pfam00365 1 RIGILTSGGDAPgmnaAIRAVVRTAIYRG------HEVYGIRNGYEGLVEGDIDELTW--RDVSGILNR-GGTILGTSRS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 81 KLTNAADCVKRglvkegenplriAAERLANDGITILHTIGGDDTNTTAADLAAYlaangYDLTVVGLPKTVDNDVVPIRQ 160
Cdd:pfam00365 72 KPFKTEEGREK------------IAENLKKLGIDALVVIGGDGSLTGANKLSEE-----RGIPVVGIPKTIDNDIPGTDY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 161 SLGAWTAAEVGAHFFDNVgnEQTAA--PRTLVIhEVMGRHCGWLTAATARAylqrtsrnqyvdglmmdahlKSIDAVYLP 238
Cdd:pfam00365 135 TIGFDTALNTIVEAIDRI--RDTASshNRVFVV-EVMGRHCGWLALMAGLA--------------------GGADAILIP 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 502306579 239 EMAFDLDAEAARLKESMDRNGHATVFVSEGACLDAIVAER--EAAGETVKRDAFGHV 293
Cdd:pfam00365 192 EIPFDIEELCEKIKELRKGKRFSIIVVAEGASDGEFLAKLieEGTGIETRVTVLGHV 248
|
|
| PRK06830 |
PRK06830 |
ATP-dependent 6-phosphofructokinase; |
2-335 |
2.52e-25 |
|
ATP-dependent 6-phosphofructokinase;
Pssm-ID: 235869 Cd Length: 443 Bit Score: 106.88 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 2 AKQKVAMLTAGGLAPCLSSAVGGLI----ERYSdVApelEIVAYKSGYQGVL--LG-DSIEITPairEKAPLLHRYGGSP 74
Cdd:PRK06830 79 SKVKAAIVTCGGLCPGLNDVIRAIVlelhHHYG-VR---RILGIRYGYQGLIprYGhDPVELTP---EVVADIHEFGGTI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 75 IGNSRvkltnaadcvkrGlvkeGENPLRI--AAERLandGITILHTIGGDDTNTTAADLAAYLAANGYDLTVVGLPKTVD 152
Cdd:PRK06830 152 LGSSR------------G----PQDPEEIvdTLERM---NINILFVIGGDGTLRGASAIAEEIERRGLKISVIGIPKTID 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 153 NDVVPIRQSLGAWTAAEV------GAHffdnvgNEQTAAPRTLVIHEVMGRHCGWLTAATARAylqrtsrnqyvdglmmd 226
Cdd:PRK06830 213 NDINFIQKSFGFETAVEKateairCAH------VEANGAPNGIGLVKLMGRHSGFIAAYAALA----------------- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 227 ahLKSIDAVYLPEMAFDLDAEA---ARLKESMDRNGHATVFVSEGacldaivAEREAAGETVKRDAFGHVKI-------- 295
Cdd:PRK06830 270 --SKDVNFVLIPEVPFDLEGPNgllAALEKRLAERGHAVIVVAEG-------AGQELFDDTGETDASGNPKLgdiglflk 340
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 502306579 296 DTINvgAWFQKQfanllDAERSL--VQKSgYFARSAPANADD 335
Cdd:PRK06830 341 DRIK--EYFKAR-----GIPINLkyIDPS-YIIRSVPANAND 374
|
|
| PFK_mixed |
TIGR02483 |
phosphofructokinase; Members of this family that are characterized, save one, are ... |
5-319 |
1.61e-23 |
|
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: 100.07 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 5 KVAMLTAGGLAPCLSSAVGGL----IERYSDvapelEIVAYKSGYQGVLLGDSIeITPAIREKAPLLHRyGGSPIGNSRv 80
Cdd:TIGR02483 1 RIGVLTGGGDCPGLNAVIRGVvrraIAEYGW-----EVIGIRDGWRGLLEGDTV-PLLDLEDVRGILPR-GGTILGSSR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 81 klTNAADCVKRGLVKegenplriAAERLANDGITILHTIGGDDTNTtaadLAAYLAANGydLTVVGLPKTVDNDVVPIRQ 160
Cdd:TIGR02483 73 --TNPFKYEEDGDDK--------IVANLKELGLDALIAIGGDGTLG----IARRLADKG--LPVVGVPKTIDNDLEATDY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 161 SLGAWTAAEVGAHFFDNVGNEQTAAPRTLVIhEVMGRHCGWLTAATaraylqrtsrnqyvdGLMMDAhlksiDAVYLPEM 240
Cdd:TIGR02483 137 TFGFDTAVEIATEALDRLHTTAESHHRVMVV-EVMGRHAGWIALHS---------------GIAGGA-----DVILIPEI 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 241 AFDLDAEAARLKESMDRNG-HATVFVSEGAcldaivaeREAAGETVKR----DAFGHVKIDTInvGAWFQKQFANLLDAE 315
Cdd:TIGR02483 196 PFDIDSVCEKVRERFARGKrFAIVVVAEGA--------KPKGGEMVVQegvkDAFGHVRLGGI--GNWLAEEIERRTGIE 265
|
....*
gi 502306579 316 -RSLV 319
Cdd:TIGR02483 266 tRATV 270
|
|
| PRK14072 |
PRK14072 |
diphosphate--fructose-6-phosphate 1-phosphotransferase; |
1-372 |
5.25e-23 |
|
diphosphate--fructose-6-phosphate 1-phosphotransferase;
Pssm-ID: 237600 [Multi-domain] Cd Length: 416 Bit Score: 99.93 E-value: 5.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 1 MAKQKVAMLTAGGLAPCLSSAVGGLIERYSDVAPELEIVAYKSGYQGVLLGDSIEITPAIREKAPLLHRYGGSPIGNSRV 80
Cdd:PRK14072 1 MMKGNALYAQSGGPTAVINASAAGVIEEARKHKKIGKVYGARNGIIGILDEDLIDLSKESDEALAALAHTPSGALGSCRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 81 KL----TNAADCVKrgLVkegenplriaaERLANDGITILHTIGGDDTNTTAADLAAYLAANGYDLTVVGLPKTVDNDVV 156
Cdd:PRK14072 81 KLksleEDRAEYER--LL-----------EVFKAHDIGYFFYNGGNDSMDTALKVSQLAKKMGYPIRCIGIPKTIDNDLP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 157 PIRQSLGAWTAAEVGAHFFDNVGNEQTAAPRTLVIH--EVMGRHCGWLTAATARAylqrtsrnQYVDGlmMDAHLksida 234
Cdd:PRK14072 148 GTDHCPGFGSAAKYIATSVLEAALDVAAMANTSKVFilEVMGRHAGWLAAAAALA--------KQNPD--DAPHL----- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 235 VYLPEMAFDLDAEAARLKESMDRNGHATVFVSEGAcldaivaeREAAG----ETVKR-DAFGHVKIDtiNVGAWfqkqFA 309
Cdd:PRK14072 213 IYLPERPFDEEKFLADVRAIVKRYGYCVVVVSEGI--------RDADGkfiaEAGLAeDAFGHAQLG--GVAPV----LA 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 310 NLLDAE-----RSLVqkSGYFARSAP--ANADDLRLIQSMVDLAVESALNkvsgvtghdeGQNGKLRTIE 372
Cdd:PRK14072 279 NLIKEKlgkkvHWAV--LDYLQRAARhiASKTDVEEAYAVGKAAVEYALA----------GKNGVMPAIR 336
|
|
| PFK |
cd00363 |
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ... |
5-270 |
3.04e-21 |
|
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: 93.52 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 5 KVAMLTAGGLAPCLSSAVGGLIeRYSdVAPELEIVAYKSGYQGVLLGDSIEITpaIREKAPLLHRyGGSPIGNSRVKltn 84
Cdd:cd00363 2 KIGVLTSGGDAPGMNAAIRGVV-RSA-IAEGLEVYGIYEGYAGLVEGDIKELD--WESVSDIINR-GGTIIGSARCK--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 85 aadcvkrglVKEGENPLRIAAERLANDGITILHTIGGDDTNTTAADLAAYLAANGYDLTVVGLPKTVDNDVVPIRQSLGA 164
Cdd:cd00363 74 ---------EFRTEEGRAKAAENLKKHGIDALVVIGGDGSYTGADLLTEEWPSKYQGFNVIGLPGTIDNDIKGTDYTIGF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 165 WTAAEVGAHFFDNVGNEQTAAPRTLVIhEVMGRHCGWLTAATARAylqrtsrnqyvdglmmdahlKSIDAVYLPEMAFDL 244
Cdd:cd00363 145 DTALKTIVEAIDRIRDTASSHQRTFVV-EVMGRHCGDIALEAGLA--------------------TGADIIFIPEEPAAD 203
|
250 260 270
....*....|....*....|....*....|
gi 502306579 245 DAE---AARLKESMDR-NGHATVFVSEGAC 270
Cdd:cd00363 204 EWEeemVDVIKKRRERgKRHGIVIVAEGAI 233
|
|
| PRK03202 |
PRK03202 |
ATP-dependent 6-phosphofructokinase; |
5-293 |
4.58e-18 |
|
ATP-dependent 6-phosphofructokinase;
Pssm-ID: 235111 [Multi-domain] Cd Length: 320 Bit Score: 84.36 E-value: 4.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 5 KVAMLTAGGLAPCLSSAVGGLIeRYSdVAPELEIVAYKSGYQGVLLGDSIEITpaIREKAPLLHRyGGSPIGNSRVKLTN 84
Cdd:PRK03202 3 RIGVLTSGGDAPGMNAAIRAVV-RTA-ISEGLEVYGIYDGYAGLLEGDIVKLD--LKSVSDIINR-GGTILGSARFPEFK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 85 AADCVKRglvkegenplriAAERLANDGITILHTIGGDDTNTtaadlaaylaaNGYDLT-----VVGLPKTVDNDVVPIR 159
Cdd:PRK03202 78 DEEGRAK------------AIENLKKLGIDALVVIGGDGSYM-----------GAKRLTehgipVIGLPGTIDNDIAGTD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 160 QSLGAWTAAE--VGA----HFfdnvgneqTAAP--RTLVIhEVMGRHCGWLT-----AATAraylqrtsrnqyvdglmmd 226
Cdd:PRK03202 135 YTIGFDTALNtaVEAidrlRD--------TASSheRVFIV-EVMGRHAGDLAlhagiAGGA------------------- 186
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 227 ahlksiDAVYLPEMAFDLDAEAARLKESMDRNG-HATVFVSEGACLDAIVAER--EAAGETVKRDAFGHV 293
Cdd:PRK03202 187 ------EVILIPEVPFDIEELCAKIKKGRERGKkHAIIVVAEGVMPAEELAKEieERTGLETRVTVLGHI 250
|
|
| PLN02564 |
PLN02564 |
6-phosphofructokinase |
5-376 |
7.79e-17 |
|
6-phosphofructokinase
Pssm-ID: 178178 Cd Length: 484 Bit Score: 82.10 E-value: 7.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 5 KVAMLTAGGLAPCLSSAVGGLIERYSDVAPELEIVAYKSGYQGVLLGDSIEITPAIREKaplLHRYGGSPIGNSRvkltn 84
Cdd:PLN02564 89 RACIVTCGGLCPGLNTVIREIVCGLSYMYGVTRILGIDGGYRGFYSRNTIPLTPKVVND---IHKRGGTILGTSR----- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 85 aadcvkrglvkEGENPLRIAaERLANDGITILHTIGGDDTNTTAADLAAYLAANGYDLTVVGLPKTVDNDVVPIRQSLGA 164
Cdd:PLN02564 161 -----------GGHDTSKIV-DSIQDRGINQVYIIGGDGTQKGASVIYEEIRRRGLKVAVAGIPKTIDNDIPVIDKSFGF 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 165 WTAAEVGAHFFDNVGNEQTAAPRTLVIHEVMGRHCGWLTaataraylqrtsrnqyvdglmMDAHLKS--IDAVYLPEMAF 242
Cdd:PLN02564 229 DTAVEEAQRAINAAHVEAESVENGIGLVKLMGRYSGFIA---------------------MYATLASrdVDCCLIPESPF 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 243 DLDAEAA-------RLKEsmdrNGHATVFVSEGACLDAIVaerEAAGETVKRDAFGHVKIdtINVGAWFQKQFANLLDAE 315
Cdd:PLN02564 288 YLEGKGGlfefiekRLKE----NGHMVIVVAEGAGQDLIA---ESMESSDLQDASGNKLL--LDVGLWLSQKIKDHFTKV 358
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502306579 316 RSLVQK-----SGYFARSAPANADD----LRLIQSmvdlAVESALnkvSGVTGHDEGQ-NGKLRTIEFPRI 376
Cdd:PLN02564 359 KKMPINlkyidPTYMIRAIPSNASDnvycTLLAHS----AVHGAM---AGYTGFTVGPvNGRHAYIPFYRI 422
|
|
| Bacterial_PFK |
cd00763 |
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ... |
4-294 |
2.57e-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 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: 76.29 E-value: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 4 QKVAMLTAGGLAPCLSSAVGGLIErySDVAPELEIVAYKSGYQGVLLGDSIEITpaIREKAPLLHRyGGSPIGNSRvkLT 83
Cdd:cd00763 1 KRIGVLTSGGDAPGMNAAIRGVVR--SAIAEGLEVYGIRDGYAGLIAGDIVPLD--RYSVSDIINR-GGTFLGSAR--FP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 84 NAADcvkrglvkegENPLRIAAERLANDGITILHTIGGDDTnttaADLAAYLAANGYDltVVGLPKTVDNDVVPIRQSLG 163
Cdd:cd00763 74 EFKD----------EEGQAKAIEQLKKHGIDALVVIGGDGS----YMGAMRLTEHGFP--CVGLPGTIDNDIPGTDYTIG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 164 AWTAAEVGAHFFDNVGNEQTAAPRTLVIhEVMGRHCGWLTAATARAylqrtsrnqyvdglmmdahlKSIDAVYLPEMAFD 243
Cdd:cd00763 138 FDTALNTVVEAIDRIRDTSSSHQRISVV-EVMGRHCGDIALAAGIA--------------------GGAEFIVIPEAEFD 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 502306579 244 LDAEAARLKESMDR-NGHATVFVSEGAC-LDAIVAE-REAAGETVKRDAFGHVK 294
Cdd:cd00763 197 REEVANRIKAGIERgKKHAIVVVAEGVYdVDELAKEiEEATGFETRATVLGHIQ 250
|
|
| PLN02884 |
PLN02884 |
6-phosphofructokinase |
5-358 |
1.21e-14 |
|
6-phosphofructokinase
Pssm-ID: 178472 [Multi-domain] Cd Length: 411 Bit Score: 74.85 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 5 KVAMLTAGGLAPCLSSAVGGLI---ERYSdvapELEIVAYKSGYQGvLLGDSIEITPAIREKAPLLHRYGGSPIGNSR-- 79
Cdd:PLN02884 55 KAAIVTCGGLCPGLNDVIRQIVftlEIYG----VKNIVGIPFGYRG-FFEKGLSEMPLSRKVVQNIHLSGGSLLGVSRgg 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 80 VKLTNAADCVKRglvkegenplriaaerlanDGITILHTIGGDDTNTTAADLAAYLAANGYDLTVVGLPKTVDNDVVPIR 159
Cdd:PLN02884 130 AKTSDIVDSIEA-------------------RGINMLFVLGGNGTHAGANAIHNECRKRKMKVSVVGVPKTIDNDILLMD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 160 QSLGAWTAAEVGAHFFDNVGNEQTAAPRTLVIHEVMGRHCGWLTaataraylqrtsrnqyvdglmMDAHLKS--IDAVYL 237
Cdd:PLN02884 191 KTFGFDTAVEEAQRAINSAYIEAHSAYHGIGLVKLMGRSSGFIA---------------------MHASLASgqVDICLI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 238 PEMAFDLDAEAA---RLKESMDRNGHATVFVSEGACLDAIvaereaaGETVKRDAFGHVKIDTInvGAWFQKQFANLLD- 313
Cdd:PLN02884 250 PEVPFTLDGPNGvlrHLEHLIETKGSAVVCVAEGAGQDLL-------QKTNATDASGNPVLGDI--GVHLQQEIKKHFKd 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 502306579 314 ----AERSLVQKSgYFARSAPANADDLRLIQSMVDLAVESALNKVSGVT 358
Cdd:PLN02884 321 igvpADVKYIDPT-YMIRACRANASDAILCTVLGQNAVHGAFAGFSGIT 368
|
|
| PFKA_ATP |
TIGR02482 |
6-phosphofructokinase; 6-phosphofructokinase (EC 2.7.1.11) catalyzes the addition of phosphate ... |
5-294 |
9.07e-14 |
|
6-phosphofructokinase; 6-phosphofructokinase (EC 2.7.1.11) catalyzes the addition of phosphate from ATP to fructose 6-phosphate to give fructose 1,6-bisphosphate. This represents a key control step in glycolysis. This model hits bacterial ATP-dependent 6-phosphofructokinases which lack a beta-hairpin loop present in TIGR02483 family members. TIGR02483 contains members that are ATP-dependent as well as members that are pyrophosphate-dependent. TIGR02477 represents the pyrophosphate-dependent phosphofructokinase, diphosphate--fructose-6-phosphate 1-phosphotransferase (EC 2.7.1.90). [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 213713 [Multi-domain] Cd Length: 301 Bit Score: 71.23 E-value: 9.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 5 KVAMLTAGGLAPCLSSAVGGLIeRYSdVAPELEIVAYKSGYQGVLLGDSIEITPaiREKAPLLHRyGGSPIGNSRVKLTN 84
Cdd:TIGR02482 1 KIGILTSGGDAPGMNAAIRAVV-RTA-IYHGFEVYGIRRGYKGLINGKIEPLES--KNVSGIIHR-GGTILGTARCPEFK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 85 AadcvkrglvKEGENplrIAAERLANDGITILHTIGGDDTNTTAADLAAYlaangYDLTVVGLPKTVDNDVVPIRQSLGA 164
Cdd:TIGR02482 76 T---------EEVRE---KAVENLKKLGIEGLVVIGGDGSYTGAQKLYEE-----GGIPVIGLPGTIDNDIPGTDYTIGF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 165 WTAAEVGAHFFDNVGNEQTAAPRTLVIhEVMGRHCGWLTaataraylqrtsrnqyvdglMMDAHLKSIDAVYLPEMAFDL 244
Cdd:TIGR02482 139 DTALNTIIDAVDKIRDTATSHERAFVI-EVMGRHAGDLA--------------------LYAGIATGAEIIIIPEFDYDI 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 502306579 245 DAEAARLKESMDRNG-HATVFVSEGACLDAI--VAER--EAAGETVKRDAFGHVK 294
Cdd:TIGR02482 198 DELIQRLKEQHEAGKkHSIIIVAEGNIVGSAkeVAKKieEKTGIETRVTVLGHTQ 252
|
|
| 6PF1K_euk |
TIGR02478 |
6-phosphofructokinase, eukaryotic type; Members of this family are eukaryotic (with one ... |
5-269 |
8.37e-11 |
|
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: 63.90 E-value: 8.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 5 KVAMLTAGGLAPCLSSAVGGLIErySDVAPELEIVAYKSGYQG-VLLGDSIEitPAIREK-APLLHRyGGSPIGNSRVKL 82
Cdd:TIGR02478 2 RIAVLTSGGDAQGMNAAVRAVVR--MAIYVGCRVYAIREGYQGlVDGGDNIE--EAQWEDvRGILSL-GGTIIGTARCKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 83 tnaadcvkrglVKEGENPLRiAAERLANDGITILHTIGGDDTNT-----------------TAADLAAYLAANGYDLTVV 145
Cdd:TIGR02478 77 -----------FRERPGRLK-AARNLVSNGIDALVVIGGDGSLTgadlfreewpslleelvDTGKITAEQAEEHRHLTIV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 146 GLPKTVDNDVVPIRQSLGAWTAAEVGAHFFDNVGNEQTAAPRTLVIhEVMGRHCGWL--TAATARAylqrtsrnqyvdgl 223
Cdd:TIGR02478 145 GLVGSIDNDMCGTDMTIGADSALHRICEAIDAISSTAQSHQRAFVV-EVMGRHCGYLalMAAIATG-------------- 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 502306579 224 mmdahlksIDAVYLPEMAFDlDAEAARLKESMDRNGHA-----TVFVSEGA 269
Cdd:TIGR02478 210 --------ADYVFIPERPPE-EGWEDQLCHKLKRNRKAgkrktIVIVAEGA 251
|
|
| Eukaryotic_PFK |
cd00764 |
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ... |
2-269 |
1.42e-10 |
|
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: 62.92 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 2 AKQKVAMLTAGGLAPCLSSAVGGLIErySDVAPELEIVAYKSGYQGVLLGDSiEITPAIREKAPLLHRYGGSPIGNSRVK 81
Cdd:cd00764 2 AGKAIAVLTSGGDAQGMNAAVRAVVR--MGIYVGAKVFFVYEGYEGLVKGGD-YIKQAEWESVSNWLQEGGTIIGSARCK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 82 LtnaadcvkrglVKEGENPLRiAAERLANDGITILHTIGGDDTNTTA-------ADLAAYLAANG----------YDLTV 144
Cdd:cd00764 79 E-----------FREREGRLQ-AAYNLIQRGITNLCVIGGDGSLTGAdlfrsewPSLLEELVKDGkiteeevakyQHLNI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 145 VGLPKTVDNDVVPIRQSLGAWTAAEVGAHFFDNVGNEQTAAPRTLVIhEVMGRHCGWLTAATARAylqrtsrnqyvdglm 224
Cdd:cd00764 147 VGMVGSIDNDFCGTDMTIGTDSALHRICEVVDAITTTAQSHQRTFVL-EVMGRHCGYLALVSGLA--------------- 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 502306579 225 mdahlKSIDAVYLPEMAFDLDAE---AARLKESMDRNGHAT-VFVSEGA 269
Cdd:cd00764 211 -----TGADWIFIPERPPEDGWEdqmCRRLSEHRSRGKRLNiIIVAEGA 254
|
|
| Pyrophosphate_PFK |
cd00765 |
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ... |
3-197 |
2.45e-10 |
|
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: 62.20 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 3 KQKVAMLTAGGLAPCLSSAVGGLIERYSDVAPELEIVAYKSGYQGVLLGDSIEITpairekAPLLHRY----GGSPIGNS 78
Cdd:cd00765 72 KLKIGIVLSGGQAPGGHNVISGLFDYLKERAKGSTLYGFKGGPAGILKCDYIELN------AEYIQPYrntgGFDMICSG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 79 RVKLtnaadcvkrglvkEGENPLRIAAE---RLANDGITIlhtIGGDDTNTTAADLAAYLAANGYDLTVVGLPKTVD--- 152
Cdd:cd00765 146 RTKI-------------ETEDQFKQAEEtakKLDLDALVV---IGGDDSNTNAALLAENFRSKGLKTRVIGVPKTIDgdl 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502306579 153 -NDVVPIrqSLGAWTAAEVGAHFFDNVGNEQTAAPRTLVIHEVMGR 197
Cdd:cd00765 210 kNKEIET--SFGFDTATKIYSELIGNVMRDARSTGKYWHFVKLMGR 253
|
|
| PRK07085 |
PRK07085 |
diphosphate--fructose-6-phosphate 1-phosphotransferase; Provisional |
5-154 |
5.15e-08 |
|
diphosphate--fructose-6-phosphate 1-phosphotransferase; Provisional
Pssm-ID: 235930 Cd Length: 555 Bit Score: 54.93 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 5 KVAMLTAGGLAPCLSSAVGGLIERYSDVAPELEIVAYKSGYQGVLLGDSIEITPAIrekaplLHRY---GG-SPIGNSRV 80
Cdd:PRK07085 72 KVGVILSGGQAPGGHNVIAGLFDGLKKLNPDSKLFGFIGGPLGLLNGKYIEITEEV------IDEYrntGGfDMIGSGRT 145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502306579 81 KLTNaadcvkrglvKEGENPLRIAAERLANDGITIlhtIGGDDTNTTAADLAAYLAANGYDLTVVGLPKTVDND 154
Cdd:PRK07085 146 KIET----------EEQKEACLETVKKLKLDGLVI---IGGDDSNTNAAILAEYFAKHGCKTQVIGVPKTIDGD 206
|
|
| PRK14071 |
PRK14071 |
ATP-dependent 6-phosphofructokinase; |
141-348 |
3.92e-07 |
|
ATP-dependent 6-phosphofructokinase;
Pssm-ID: 184487 [Multi-domain] Cd Length: 360 Bit Score: 51.61 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 141 DLTVVGLPKTVDNDVVPIRQSLGAWTAAEVGAHFFDNVgnEQTAAPRTLV-IHEVMGRHCGWLtAATAraylqrtsrnqy 219
Cdd:PRK14071 131 GINLVGIPKTIDNDVGATEVSIGFDTAVNIATEALDRL--HFTAASHNRVmILEVMGRDAGHI-ALAA------------ 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 220 vdGLMMDAHLksidaVYLPEMAFDLDAEAARLKESMDR-NGHATVFVSEgacldaivAEREAAGETVKR-DAFGHVKIDT 297
Cdd:PRK14071 196 --GIAGGADV-----ILIPEIPYTLENVCKKIRERQEEgKNFCLVVVSE--------AVRTEEGEQVTKtQALGEDRYGG 260
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502306579 298 InvGAWFQKQFANLLDAErSLVQKSGYFARSAPANADDlRLIQSM-----VDLAVE 348
Cdd:PRK14071 261 I--GQYLAEQIAERTGAE-TRVTVLGHIQRGGIPSPRD-RLLASAfgvaaVDLIAQ 312
|
|
| PLN02251 |
PLN02251 |
pyrophosphate-dependent phosphofructokinase |
3-178 |
3.51e-06 |
|
pyrophosphate-dependent phosphofructokinase
Pssm-ID: 215140 Cd Length: 568 Bit Score: 49.02 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 3 KQKVAMLTAGGLAPCLSSAVGGLIERYSDVAPELEIVAYKSGYQGVLLGDSIEITpairekAPLLHRY----GGSPIGNS 78
Cdd:PLN02251 96 KLKIGVVLSGGQAPGGHNVISGIFDYLQEHAKGSVLYGFKGGPAGIMKCKYVELT------AEFIYPYrnqgGFDMICSG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 79 RVKLTNAADcvkrglVKEGENplriAAERLANDGITIlhtIGGDDTNTTAADLAAYLAANGYDLTVVGLPKTVDNDV--- 155
Cdd:PLN02251 170 RDKIETPEQ------FKQAEE----TATKLDLDGLVV---IGGDDSNTNACLLAEYFRAKNLKTRVIGCPKTIDGDLksk 236
|
170 180
....*....|....*....|....
gi 502306579 156 -VPIrqSLGAWTAAEVGAHFFDNV 178
Cdd:PLN02251 237 eVPT--SFGFDTACKIYSEMIGNV 258
|
|
| 6PF1K_euk |
TIGR02478 |
6-phosphofructokinase, eukaryotic type; Members of this family are eukaryotic (with one ... |
145-258 |
9.65e-06 |
|
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: 47.72 E-value: 9.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 145 VGLPKTVDNDVVPIRQSLGAWTAAEVGAHFFDNVGNEQTAAPRTLVIHEVMGRHCGWLtaATaraylqrtsrnqyVDGLM 224
Cdd:TIGR02478 512 VVIPATISNNVPGTEYSLGSDTALNEITEYCDNIKQSASASKRRVFVVETMGGYSGYL--AT-------------MAGLA 576
|
90 100 110
....*....|....*....|....*....|....*..
gi 502306579 225 MDAhlksiDAVYLPEMAFDLD---AEAARLKESMDRN 258
Cdd:TIGR02478 577 TGA-----DAAYIPEEGISLKdlqEDIEHLKETFAEG 608
|
|
| PTZ00287 |
PTZ00287 |
6-phosphofructokinase; Provisional |
5-197 |
1.63e-04 |
|
6-phosphofructokinase; Provisional
Pssm-ID: 240345 [Multi-domain] Cd Length: 1419 Bit Score: 43.87 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 5 KVAMLTAGGLAPCLSSAVGGLIERYSDVAPELEIVAYKSGYQGVLLGDSIEITPAirekapLLHRY----GGSPIGNSRV 80
Cdd:PTZ00287 179 KIGIILSGGPAPGGHNVISGIYDYAKRYNEQSQVIGFLGGIDGLYSKNYVTITDS------LMNRFrnlgGFNMLWSGRG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 81 KLTNAADCVKRglvkegENplrIAAeRLANDGITIlhtIGGDDTNTTAADLAAYLAANGYDLTVVGLPKTVDNDVV--PI 158
Cdd:PTZ00287 253 KVRNKDDLIAI------EN---IVA-KLKLNGLVI---IGGDGSNSNAALISEYFAERQIPISIIGIPKTIDGDLKseAI 319
|
170 180 190
....*....|....*....|....*....|....*....
gi 502306579 159 RQSLGAWTAAEVGAHFFDNVGNEQTAAPRTLVIHEVMGR 197
Cdd:PTZ00287 320 EISFGFDTATKTYSEVIGNLCTDVKTGHNVYHVVRVMGR 358
|
|
| Eukaryotic_PFK |
cd00764 |
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ... |
147-255 |
1.65e-04 |
|
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: 44.04 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 147 LPKTVDNDVVPIRQSLGAWTAAEVGAHFFDNVGNEQTAAPRTLVIHEVMGRHCGWLTAATaraylqrtsrnqyvdGLMMD 226
Cdd:cd00764 514 IPATVSNNVPGTDFSLGSDTALNALMKYCDRIKQSASGTKRRVFIVETMGGYCGYLATMT---------------GLAVG 578
|
90 100 110
....*....|....*....|....*....|..
gi 502306579 227 AhlksiDAVYLPEMAF---DLDAEAARLKESM 255
Cdd:cd00764 579 A-----DAAYVFEEPFnirDLQENVEHLTEKM 605
|
|
| PTZ00468 |
PTZ00468 |
phosphofructokinase family protein; Provisional |
4-170 |
2.94e-04 |
|
phosphofructokinase family protein; Provisional
Pssm-ID: 185647 [Multi-domain] Cd Length: 1328 Bit Score: 43.04 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 4 QKVAMLTAGGLAPCLSSAVGGLIERYSDVAPELEIVAYKSGYQGVLLGDSIEITPAIREKapLLHRYGGSPIGNSRVKLt 83
Cdd:PTZ00468 103 RRIGVVLSGGQASGGHNVIAGLMSYIKLCNQSSQLFGFLGGPEGVYSERYRELTEDDING--ILNQGGFNIICSGRHKI- 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306579 84 naadcvkrglvkEGENPLRIA---AERLANDGITIlhtIGGDDTNTTAADLAAYLAANGYDLTVVGLPKTVDNDVVP--I 158
Cdd:PTZ00468 180 ------------ETEEQMRASleiCEKLKLHGLVV---IGGDDSNTNAAVLAEYFKRNSSSTVVVGCPKTIDGDLKNevI 244
|
170
....*....|..
gi 502306579 159 RQSLGAWTAAEV 170
Cdd:PTZ00468 245 ETSFGYDTAVKT 256
|
|
| |
