|
Name |
Accession |
Description |
Interval |
E-value |
| trifunc_aldol |
NF041633 |
KHG/KDPG aldolase/sugar kinase fusion protein; The N-terminal region of this protein resembles ... |
1-332 |
6.68e-111 |
|
KHG/KDPG aldolase/sugar kinase fusion protein; The N-terminal region of this protein resembles the bifunctional KHG/KDPG aldolase (4.1.2.14 and 4.1.3.16), while the C-terminal region resembles 2-dehydro-3-deoxygluconokinase and 2-dehydro-3-deoxygalactonokinase.
Pssm-ID: 469516 [Multi-domain] Cd Length: 577 Bit Score: 333.80 E-value: 6.68e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 1 MANILTLGEIMLRLSTTLGDRIAHSSMFAAHYGGGEANVAISLANFGHRVSFASKVPENALGDAVFHHLRSYGVDCRHLL 80
Cdd:NF041633 238 GPKVVTFGEIMLRLSPPGGRRFSQADTFEATFGGAEANVAVSLAQFGLNSRFVTALPDNDIGQAAVNSLRKYGVDTSFIV 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 81 RGGSRLGTYYIETGIGERAARVVYDRAGSSFAQMKENE--WQsDLFDGVDIVHLSGITPALSTTWQTLLLTLIKEAKAAG 158
Cdd:NF041633 318 RGGDRIGIYYLEHGASQRPSKVVYDRAGSAISEISPGDfdWE-KIFEGAGWFHWTGITPALSDSAAEILLEALKAAKEKG 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 159 CKISFDINYRGKLWTTAEARVFLQEVLPYVDYCSAGQLDA-QVFmDVSAPTEEVE------DDYYY--QEMHRKYPnIQL 229
Cdd:NF041633 397 ITVSCDLNYRKKLWSEEKAREVMTELMEYVDVLIGNEEDAaKVF-GIKAKGTDVEagkldeEGYKDvaEQLVERFG-FKK 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 230 FYSTSRQVLSASHNQLTGSLWHNGNYVVSATHEInPIVDRVGGGDAFSAGVLHGLVTKKQDQEIIDFATAASALKHTIHG 309
Cdd:NF041633 475 VAITLRESLSASDNNWSACLYDGKEFYFSPKYHV-HIVDRVGGGDAFAAGLIYALLKGKTDQEALEFAVAASCLKHSIEG 553
|
330 340
....*....|....*....|....
gi 1829055301 310 DCNQFSANEIQEFIA-TGSGKIIR 332
Cdd:NF041633 554 DFNLVSVEEVERLAAgDGSGRVQR 577
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
4-310 |
1.98e-87 |
|
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.
Pssm-ID: 238571 [Multi-domain] Cd Length: 294 Bit Score: 264.44 E-value: 1.98e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 4 ILTLGEIMLRLSTTLGDRIAHSSMFAAHYGGGEANVAISLANFGHRVSFASKVPENALGDAVFHHLRSYGVDCRHLLR-G 82
Cdd:cd01166 2 VVTIGEVMVDLSPPGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVdP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 83 GSRLGTYYIETGiGERAARVVYDRAGSSFAQMKENEWQSDLFDGVDIVHLSGITPALSTTWQTLLLTLIKEAKAAGCKIS 162
Cdd:cd01166 82 GRPTGLYFLEIG-AGGERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLALSESAREALLEALEAAKARGVTVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 163 FDINYRGKLWTTAEARVFLQEVLPYVDYCSAGQLDAQVFMDVSAPTEEVEDdyyYQEMHRKYPNIqlfystsrqVLSASH 242
Cdd:cd01166 161 FDLNYRPKLWSAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAER---ALALALGVKAV---------VVKLGA 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 243 NqltGSLWHNGN--YVVSATHEinPIVDRVGGGDAFSAGVLHGLVTKKQDQEIIDFATAASALKHTIHGD 310
Cdd:cd01166 229 E---GALVYTGGgrVFVPAYPV--EVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGD 293
|
|
| KDG_KDGal_kin_Halo |
NF041332 |
bifunctional 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase; |
1-331 |
2.18e-57 |
|
bifunctional 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase;
Pssm-ID: 469229 [Multi-domain] Cd Length: 318 Bit Score: 188.20 E-value: 2.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 1 MANILTLGEIMLRLSTTLGDRIAHSSMFAAHYGGGEANVAISLANFGHRVSFASKVPENALGDAVFHHLRSYGVDCRHLL 80
Cdd:NF041332 1 MTDLVTFGETMLRLSPPGGERLETADELDVRAGGAESNVAVAAARLGADATWLSKLPDSPLGRRVVGELRSHGVDTDVVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 81 RGGSRLGTYYIETGIGERAARVVYDRAGSSFAQMKENEWQSDLFDGVDIVHLSGITPALSTTWQTLLLTLIKEAKAAGCK 160
Cdd:NF041332 81 DDEGRQGTYYLEHGGEPRGTNVIYDRADAAVTTATPEELPLDRIRDAEVFYTSGITPALSETLAETTAALLEAAQEAGTT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 161 ISFDINYRGKLWTTAEARVFLQEVLPYVDYCSAGQLDAQVFMDVSAPTEEVEDDyyyqemhrkypniqlfystsrqvLSA 240
Cdd:NF041332 161 TAFDLNYRSKLWSPEEARETLESLFPAVDVLVVAERDARTVLGRDGDAEEIAHG-----------------------LAS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 241 SHNQLT--------GSL-WHNGNYVVSATHEiNPIVDRVGGGDAFSAGVLHGLVTKKQDQEIIDFATAASALKHTIHGDC 311
Cdd:NF041332 218 EYDFETvvvtrgeeGALaLHDGEVHEQPAYE-ADTVDPIGTGDAFVGGFLARRLAGGDVPTALEYGAATAALKRTIPGDV 296
|
330 340
....*....|....*....|
gi 1829055301 312 NQFSANEIQEFIATGSGKII 331
Cdd:NF041332 297 AVVTPEEVEAVVEDGGGDGI 316
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
3-312 |
1.81e-56 |
|
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440290 [Multi-domain] Cd Length: 301 Bit Score: 185.09 E-value: 1.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 3 NILTLGEIMLRLSTTL-----GDRIAHSSMFAAHYGGGEANVAISLANFGHRVSFASKVPENALGDAVFHHLRSYGVDCR 77
Cdd:COG0524 1 DVLVIGEALVDLVARVdrlpkGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 78 HLLR-GGSRLGTYYIETGIGERAARVVYdraGSSFAQMKENEWQSDLFDGVDIVHLSGITPAlSTTWQTLLLTLIKEAKA 156
Cdd:COG0524 81 GVRRdPGAPTGLAFILVDPDGERTIVFY---RGANAELTPEDLDEALLAGADILHLGGITLA-SEPPREALLAALEAARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 157 AGCKISFDINYRGKLWttAEARVFLQEVLPYVDYCSAGQLDAQVFMDVSAPTEEVEddyyyqEMHRKYPniqlfystsRQ 236
Cdd:COG0524 157 AGVPVSLDPNYRPALW--EPARELLRELLALVDILFPNEEEAELLTGETDPEEAAA------ALLARGV---------KL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 237 VLsashnqLT----GS-LWHNGNYVVSATHEINpIVDRVGGGDAFSAGVLHGLVTKKQDQEIIDFATAASALKHTIHGDC 311
Cdd:COG0524 220 VV------VTlgaeGAlLYTGGEVVHVPAFPVE-VVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQ 292
|
.
gi 1829055301 312 N 312
Cdd:COG0524 293 P 293
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
3-312 |
4.30e-27 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 107.81 E-value: 4.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 3 NILTLGEIMLRLSTT---LGDRIAHSSMFAAHYGGGEANVAISLANFGHRVSFASKVPENALGDAVFHHLRSYGVDCRHL 79
Cdd:pfam00294 1 KVVVIGEANIDLIGNvegLPGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 80 LR-GGSRLGTYYIE-TGIGERaaRVVYDRAGSSFAQMKENEWQSDLFDGVDIVHLSGITPALSTTWQTLLLTLIkeAKAA 157
Cdd:pfam00294 81 VIdEDTRTGTALIEvDGDGER--TIVFNRGAAADLTPEELEENEDLLENADLLYISGSLPLGLPEATLEELIEA--AKNG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 158 GCkisFDINYRGKLWTTAEArvfLQEVLPYVDYCSAGQLDAQVFMDVSAPTEEVEDDyYYQEMHRKYPNIqLFYSTSRQv 237
Cdd:pfam00294 157 GT---FDPNLLDPLGAAREA---LLELLPLADLLKPNEEELEALTGAKLDDIEEALA-ALHKLLAKGIKT-VIVTLGAD- 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1829055301 238 lsashnqltGSLW--HNGNYVVSATHEINpIVDRVGGGDAFSAGVLHGLVTKKQDQEIIDFATAASALKHTIHGDCN 312
Cdd:pfam00294 228 ---------GALVveGDGEVHVPAVPKVK-VVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
4-309 |
5.24e-08 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 53.47 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 4 ILTLGEIMLR-LSTTLGDRIAHSSMFAAHYGGGEANVAISLANFGHRVSFASKVpenalGDAVFHH-----LRSYGVDCR 77
Cdd:PLN02323 13 VVCFGEMLIDfVPTVSGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKV-----GDDEFGHmladiLKKNGVNNE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 78 HLL-RGGSRLGTYYIE-TGIGERaaRVVYDRAGSSFAQMKENEWQSDLFDGVDIVH---LSGIT-PALSTTWQTllltlI 151
Cdd:PLN02323 88 GVRfDPGARTALAFVTlRSDGER--EFMFYRNPSADMLLRESELDLDLIRKAKIFHygsISLITePCRSAHLAA-----M 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 152 KEAKAAGCKISFDINYRGKLWTTAE-ARVFLQEVLPYVDycsagqldaqvFMDVSapTEEVE---------DDYYYQEMH 221
Cdd:PLN02323 161 KIAKEAGALLSYDPNLRLPLWPSAEaAREGIMSIWDEAD-----------IIKVS--DEEVEfltggddpdDDTVVKLWH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 222 rkyPNIQLFYST-----SRQVLSASHNQLTGslwhngnYVVSAtheinpiVDRVGGGDAFSAGVLHGLVTKK---QDQ-- 291
Cdd:PLN02323 228 ---PNLKLLLVTegeegCRYYTKDFKGRVEG-------FKVKA-------VDTTGAGDAFVGGLLSQLAKDLsllEDEer 290
|
330 340
....*....|....*....|
gi 1829055301 292 --EIIDFATAASALKHTIHG 309
Cdd:PLN02323 291 lrEALRFANACGAITTTERG 310
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| trifunc_aldol |
NF041633 |
KHG/KDPG aldolase/sugar kinase fusion protein; The N-terminal region of this protein resembles ... |
1-332 |
6.68e-111 |
|
KHG/KDPG aldolase/sugar kinase fusion protein; The N-terminal region of this protein resembles the bifunctional KHG/KDPG aldolase (4.1.2.14 and 4.1.3.16), while the C-terminal region resembles 2-dehydro-3-deoxygluconokinase and 2-dehydro-3-deoxygalactonokinase.
Pssm-ID: 469516 [Multi-domain] Cd Length: 577 Bit Score: 333.80 E-value: 6.68e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 1 MANILTLGEIMLRLSTTLGDRIAHSSMFAAHYGGGEANVAISLANFGHRVSFASKVPENALGDAVFHHLRSYGVDCRHLL 80
Cdd:NF041633 238 GPKVVTFGEIMLRLSPPGGRRFSQADTFEATFGGAEANVAVSLAQFGLNSRFVTALPDNDIGQAAVNSLRKYGVDTSFIV 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 81 RGGSRLGTYYIETGIGERAARVVYDRAGSSFAQMKENE--WQsDLFDGVDIVHLSGITPALSTTWQTLLLTLIKEAKAAG 158
Cdd:NF041633 318 RGGDRIGIYYLEHGASQRPSKVVYDRAGSAISEISPGDfdWE-KIFEGAGWFHWTGITPALSDSAAEILLEALKAAKEKG 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 159 CKISFDINYRGKLWTTAEARVFLQEVLPYVDYCSAGQLDA-QVFmDVSAPTEEVE------DDYYY--QEMHRKYPnIQL 229
Cdd:NF041633 397 ITVSCDLNYRKKLWSEEKAREVMTELMEYVDVLIGNEEDAaKVF-GIKAKGTDVEagkldeEGYKDvaEQLVERFG-FKK 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 230 FYSTSRQVLSASHNQLTGSLWHNGNYVVSATHEInPIVDRVGGGDAFSAGVLHGLVTKKQDQEIIDFATAASALKHTIHG 309
Cdd:NF041633 475 VAITLRESLSASDNNWSACLYDGKEFYFSPKYHV-HIVDRVGGGDAFAAGLIYALLKGKTDQEALEFAVAASCLKHSIEG 553
|
330 340
....*....|....*....|....
gi 1829055301 310 DCNQFSANEIQEFIA-TGSGKIIR 332
Cdd:NF041633 554 DFNLVSVEEVERLAAgDGSGRVQR 577
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
4-310 |
1.98e-87 |
|
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.
Pssm-ID: 238571 [Multi-domain] Cd Length: 294 Bit Score: 264.44 E-value: 1.98e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 4 ILTLGEIMLRLSTTLGDRIAHSSMFAAHYGGGEANVAISLANFGHRVSFASKVPENALGDAVFHHLRSYGVDCRHLLR-G 82
Cdd:cd01166 2 VVTIGEVMVDLSPPGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVdP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 83 GSRLGTYYIETGiGERAARVVYDRAGSSFAQMKENEWQSDLFDGVDIVHLSGITPALSTTWQTLLLTLIKEAKAAGCKIS 162
Cdd:cd01166 82 GRPTGLYFLEIG-AGGERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLALSESAREALLEALEAAKARGVTVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 163 FDINYRGKLWTTAEARVFLQEVLPYVDYCSAGQLDAQVFMDVSAPTEEVEDdyyYQEMHRKYPNIqlfystsrqVLSASH 242
Cdd:cd01166 161 FDLNYRPKLWSAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAER---ALALALGVKAV---------VVKLGA 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 243 NqltGSLWHNGN--YVVSATHEinPIVDRVGGGDAFSAGVLHGLVTKKQDQEIIDFATAASALKHTIHGD 310
Cdd:cd01166 229 E---GALVYTGGgrVFVPAYPV--EVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGD 293
|
|
| KDG_KDGal_kin_Halo |
NF041332 |
bifunctional 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase; |
1-331 |
2.18e-57 |
|
bifunctional 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase;
Pssm-ID: 469229 [Multi-domain] Cd Length: 318 Bit Score: 188.20 E-value: 2.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 1 MANILTLGEIMLRLSTTLGDRIAHSSMFAAHYGGGEANVAISLANFGHRVSFASKVPENALGDAVFHHLRSYGVDCRHLL 80
Cdd:NF041332 1 MTDLVTFGETMLRLSPPGGERLETADELDVRAGGAESNVAVAAARLGADATWLSKLPDSPLGRRVVGELRSHGVDTDVVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 81 RGGSRLGTYYIETGIGERAARVVYDRAGSSFAQMKENEWQSDLFDGVDIVHLSGITPALSTTWQTLLLTLIKEAKAAGCK 160
Cdd:NF041332 81 DDEGRQGTYYLEHGGEPRGTNVIYDRADAAVTTATPEELPLDRIRDAEVFYTSGITPALSETLAETTAALLEAAQEAGTT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 161 ISFDINYRGKLWTTAEARVFLQEVLPYVDYCSAGQLDAQVFMDVSAPTEEVEDDyyyqemhrkypniqlfystsrqvLSA 240
Cdd:NF041332 161 TAFDLNYRSKLWSPEEARETLESLFPAVDVLVVAERDARTVLGRDGDAEEIAHG-----------------------LAS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 241 SHNQLT--------GSL-WHNGNYVVSATHEiNPIVDRVGGGDAFSAGVLHGLVTKKQDQEIIDFATAASALKHTIHGDC 311
Cdd:NF041332 218 EYDFETvvvtrgeeGALaLHDGEVHEQPAYE-ADTVDPIGTGDAFVGGFLARRLAGGDVPTALEYGAATAALKRTIPGDV 296
|
330 340
....*....|....*....|
gi 1829055301 312 NQFSANEIQEFIATGSGKII 331
Cdd:NF041332 297 AVVTPEEVEAVVEDGGGDGI 316
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
3-312 |
1.81e-56 |
|
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440290 [Multi-domain] Cd Length: 301 Bit Score: 185.09 E-value: 1.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 3 NILTLGEIMLRLSTTL-----GDRIAHSSMFAAHYGGGEANVAISLANFGHRVSFASKVPENALGDAVFHHLRSYGVDCR 77
Cdd:COG0524 1 DVLVIGEALVDLVARVdrlpkGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 78 HLLR-GGSRLGTYYIETGIGERAARVVYdraGSSFAQMKENEWQSDLFDGVDIVHLSGITPAlSTTWQTLLLTLIKEAKA 156
Cdd:COG0524 81 GVRRdPGAPTGLAFILVDPDGERTIVFY---RGANAELTPEDLDEALLAGADILHLGGITLA-SEPPREALLAALEAARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 157 AGCKISFDINYRGKLWttAEARVFLQEVLPYVDYCSAGQLDAQVFMDVSAPTEEVEddyyyqEMHRKYPniqlfystsRQ 236
Cdd:COG0524 157 AGVPVSLDPNYRPALW--EPARELLRELLALVDILFPNEEEAELLTGETDPEEAAA------ALLARGV---------KL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 237 VLsashnqLT----GS-LWHNGNYVVSATHEINpIVDRVGGGDAFSAGVLHGLVTKKQDQEIIDFATAASALKHTIHGDC 311
Cdd:COG0524 220 VV------VTlgaeGAlLYTGGEVVHVPAFPVE-VVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQ 292
|
.
gi 1829055301 312 N 312
Cdd:COG0524 293 P 293
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
3-309 |
3.74e-29 |
|
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.
Pssm-ID: 238572 [Multi-domain] Cd Length: 295 Bit Score: 113.50 E-value: 3.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 3 NILTLGEImlrlsttLGDRIA----HSSMFAAHYGGGEANVAISLANFGHRVSFASKVPENALGDAVFHHLRSYGVDCRH 78
Cdd:cd01167 1 KVVCFGEA-------LIDFIPegsgAPETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 79 LLRGGSRLgtyyieTGIgeraARVVYDRAGS-SFAQMKENEW--------QSDLFDGVDIVHLSGItPALSTTWQTLLLT 149
Cdd:cd01167 74 IQFDPAAP------TTL----AFVTLDADGErSFEFYRGPAAdllldtelNPDLLSEADILHFGSI-ALASEPSRSALLE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 150 LIKEAKAAGCKISFDINYRGKLWTTA-EARVFLQEVLPYVDYCSAGQLDAQVFMDVSAPTEEVEddyyyqemHRKYPNIQ 228
Cdd:cd01167 143 LLEAAKKAGVLISFDPNLRPPLWRDEeEARERIAELLELADIVKLSDEELELLFGEEDPEEIAA--------LLLLFGLK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 229 LFYST--SRQVLsashnqltgsLWHNGNYVVSATHEINPiVDRVGGGDAFSAGVLHGLVTKKQDQ-------EIIDFATA 299
Cdd:cd01167 215 LVLVTrgADGAL----------LYTKGGVGEVPGIPVEV-VDTTGAGDAFVAGLLAQLLSRGLLAldedelaEALRFANA 283
|
330
....*....|
gi 1829055301 300 ASALKHTIHG 309
Cdd:cd01167 284 VGALTCTKAG 293
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
3-312 |
4.30e-27 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 107.81 E-value: 4.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 3 NILTLGEIMLRLSTT---LGDRIAHSSMFAAHYGGGEANVAISLANFGHRVSFASKVPENALGDAVFHHLRSYGVDCRHL 79
Cdd:pfam00294 1 KVVVIGEANIDLIGNvegLPGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 80 LR-GGSRLGTYYIE-TGIGERaaRVVYDRAGSSFAQMKENEWQSDLFDGVDIVHLSGITPALSTTWQTLLLTLIkeAKAA 157
Cdd:pfam00294 81 VIdEDTRTGTALIEvDGDGER--TIVFNRGAAADLTPEELEENEDLLENADLLYISGSLPLGLPEATLEELIEA--AKNG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 158 GCkisFDINYRGKLWTTAEArvfLQEVLPYVDYCSAGQLDAQVFMDVSAPTEEVEDDyYYQEMHRKYPNIqLFYSTSRQv 237
Cdd:pfam00294 157 GT---FDPNLLDPLGAAREA---LLELLPLADLLKPNEEELEALTGAKLDDIEEALA-ALHKLLAKGIKT-VIVTLGAD- 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1829055301 238 lsashnqltGSLW--HNGNYVVSATHEINpIVDRVGGGDAFSAGVLHGLVTKKQDQEIIDFATAASALKHTIHGDCN 312
Cdd:pfam00294 228 ---------GALVveGDGEVHVPAVPKVK-VVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
24-309 |
4.21e-17 |
|
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238917 [Multi-domain] Cd Length: 279 Bit Score: 80.05 E-value: 4.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 24 HSSMFAAH----YGGGEANVAISLANFGHRVSFASKVPENALGDAVFHHLRSYGVDCRHL--LRGGSRLGTYYIETGIGE 97
Cdd:cd01942 23 FESVLVKDlrreFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSHVrvVDEDSTGVAFILTDGDDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 98 RAarVVYDRAGSSFAQMKENEwqsDLFDGVDIVHLSGITPALSTTwqtllltliKEAKAAGCKISFDINYRGKLWTTAEA 177
Cdd:cd01942 103 QI--AYFYPGAMDELEPNDEA---DPDGLADIVHLSSGPGLIELA---------RELAAGGITVSFDPGQELPRLSGEEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 178 RvflqEVLPYVDYcsagqldaqVFMdvsapteeveDDYYYQEMHRKYPNIQLFYSTSRQVLSASHNQLTGSLWHNGN-YV 256
Cdd:cd01942 169 E----EILERADI---------LFV----------NDYEAELLKERTGLSEAELASGVRVVVVTLGPKGAIVFEDGEeVE 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1829055301 257 VSATHEINpIVDRVGGGDAFSAGVLHGLVTKKQDQEIIDFATAASALKHTIHG 309
Cdd:cd01942 226 VPAVPAVK-VVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRG 277
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
29-309 |
1.41e-13 |
|
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time. .
Pssm-ID: 238920 [Multi-domain] Cd Length: 284 Bit Score: 70.02 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 29 AAHY----GGGEANVAISLANFGHRVSFASKVPENALGDAVFHHLRSYGVDCRHLLRGGSRLGTYYIETGIGERAARVVY 104
Cdd:cd01945 28 ATDYavigGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPISSITDITGDRATISI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 105 DRAGSsfaQMKENEWQSDLFDGVDIVHLSGITPALSTTWQtllltliKEAKAAGCKISFDINyrgklwtTAEARVFLqEV 184
Cdd:cd01945 108 TAIDT---QAAPDSLPDAILGGADAVLVDGRQPEAALHLA-------QEARARGIPIPLDLD-------GGGLRVLE-EL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 185 LPYVDY--CSAGQLdaqvfmdvsAPTEEVEDDYYYQEMHRkypniqlfystsrqvLSASHNQLT----GSLWHNGNyvvs 258
Cdd:cd01945 170 LPLADHaiCSENFL---------RPNTGSADDEALELLAS---------------LGIPFVAVTlgeaGCLWLERD---- 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1829055301 259 ATHEINPI-----VDRVGGGDAFSAGVLHGLVTKKQDQEIIDFATAASALKHTIHG 309
Cdd:cd01945 222 GELFHVPAfpvevVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLG 277
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
33-309 |
3.72e-09 |
|
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.
Pssm-ID: 238914 [Multi-domain] Cd Length: 290 Bit Score: 57.03 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 33 GGGEANVAISLANFGHRVSFASKVPENALGDAVFHHLRSYGVDCRHLLRggsrlgtyyieTGIGERAARVVYD-RAGSS- 110
Cdd:cd01939 36 GGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDISHCYR-----------KDIDEPASSYIIRsRAGGRt 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 111 -------FAQMKENEwqsdlFDGVDI-----VHLSGITPALSTTWQTLLltlikEAKAAGC-----KISFDINYRGKLwt 173
Cdd:cd01939 105 tivndnnLPEVTYDD-----FSKIDLtqygwIHFEGRNPDETLRMMQHI-----EEHNNRRpeiriTISVEVEKPREE-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 174 taearvfLQEVLPYVDYCSAGQLDAQvfmdvsapteeveddyyyqemHRKYPNI-QLFYSTSRQVLSASH------NQLT 246
Cdd:cd01939 173 -------LLELAAYCDVVFVSKDWAQ---------------------SRGYKSPeECLRGEGPRAKKAALlvctwgDQGA 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1829055301 247 GSLWHNGNYVVSATHEINPIVDRVGGGDAFSAGVLHGLVTKKQD-QEIIDFATAASALKHTIHG 309
Cdd:cd01939 225 GALGPDGEYVHSPAHKPIRVVDTLGAGDTFNAAVIYALNKGPDDlSEALDFGNRVASQKCTGVG 288
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
3-309 |
1.32e-08 |
|
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.
Pssm-ID: 238579 [Multi-domain] Cd Length: 292 Bit Score: 55.25 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 3 NILTLGEIMLRLSTTLgDRI------AHSSMFAAHYGGGEANVAISLANFGHRVSFASKVPENALGDAVFHHLRSYGVDC 76
Cdd:cd01174 1 KVVVVGSINVDLVTRV-DRLpkpgetVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 77 RHLLR-GGSRLGTYYI---ETG---IgeraarVVYDRAGSSFAQMKENEwQSDLFDGVDIVHLSGITPALSTTWQtlllt 149
Cdd:cd01174 80 SYVEVvVGAPTGTAVItvdESGenrI------VVVPGANGELTPADVDA-ALELIAAADVLLLQLEIPLETVLAA----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 150 lIKEAKAAGCKISFDinyrgklwtTAEARVFLQEVLPYVDYCSAGQLDAQVFMDVSAPTEEVEDDYYyQEMHRKYPniql 229
Cdd:cd01174 148 -LRAARRAGVTVILN---------PAPARPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAA-RLLLAKGV---- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 230 fystsRQVLsashnqLT----GSLWHNGNYV--VSATHEinPIVDRVGGGDAFSAGVLHGLVTKKQDQEIIDFATAASAL 303
Cdd:cd01174 213 -----KNVI------VTlgakGALLASGGEVehVPAFKV--KAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAAL 279
|
....*.
gi 1829055301 304 KHTIHG 309
Cdd:cd01174 280 SVTRPG 285
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
4-309 |
5.24e-08 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 53.47 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 4 ILTLGEIMLR-LSTTLGDRIAHSSMFAAHYGGGEANVAISLANFGHRVSFASKVpenalGDAVFHH-----LRSYGVDCR 77
Cdd:PLN02323 13 VVCFGEMLIDfVPTVSGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKV-----GDDEFGHmladiLKKNGVNNE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 78 HLL-RGGSRLGTYYIE-TGIGERaaRVVYDRAGSSFAQMKENEWQSDLFDGVDIVH---LSGIT-PALSTTWQTllltlI 151
Cdd:PLN02323 88 GVRfDPGARTALAFVTlRSDGER--EFMFYRNPSADMLLRESELDLDLIRKAKIFHygsISLITePCRSAHLAA-----M 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 152 KEAKAAGCKISFDINYRGKLWTTAE-ARVFLQEVLPYVDycsagqldaqvFMDVSapTEEVE---------DDYYYQEMH 221
Cdd:PLN02323 161 KIAKEAGALLSYDPNLRLPLWPSAEaAREGIMSIWDEAD-----------IIKVS--DEEVEfltggddpdDDTVVKLWH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 222 rkyPNIQLFYST-----SRQVLSASHNQLTGslwhngnYVVSAtheinpiVDRVGGGDAFSAGVLHGLVTKK---QDQ-- 291
Cdd:PLN02323 228 ---PNLKLLLVTegeegCRYYTKDFKGRVEG-------FKVKA-------VDTTGAGDAFVGGLLSQLAKDLsllEDEer 290
|
330 340
....*....|....*....|
gi 1829055301 292 --EIIDFATAASALKHTIHG 309
Cdd:PLN02323 291 lrEALRFANACGAITTTERG 310
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
33-309 |
7.70e-08 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 53.02 E-value: 7.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 33 GGGEANVAISLANFGHRVSFASKVPENALGDAVFHHLRSYGVDCRHL-LRGGSRLGTYYIE-TGIGERaarvvydragsS 110
Cdd:PRK09434 28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLrLDPAHRTSTVVVDlDDQGER-----------S 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 111 FAQM-----------------KENEWqsdlfdgvdiVHLSGIT----PALSTTWQTllltlIKEAKAAGCKISFDINYRG 169
Cdd:PRK09434 97 FTFMvrpsadlflqpqdlppfRQGEW----------LHLCSIAlsaePSRSTTFEA-----MRRIKAAGGFVSFDPNLRE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 170 KLW-TTAEARVFLQEVLPYVDYC--SAGQLDaqvFMdvsAPTEEVEDDYYYqeMHRKYPnIQLFYST--SRQVLsashnq 244
Cdd:PRK09434 162 DLWqDEAELRECLRQALALADVVklSEEELC---FL---SGTSQLEDAIYA--LADRYP-IALLLVTlgAEGVL------ 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1829055301 245 ltgsLWHNGNYVVSATHEINPiVDRVGGGDAFSAGVLHGLV------TKKQDQEIIDFATAASALKHTIHG 309
Cdd:PRK09434 227 ----VHTRGQVQHFPAPSVDP-VDTTGAGDAFVAGLLAGLSqaglwtDEAELAEIIAQAQACGALATTAKG 292
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
28-300 |
1.47e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 52.60 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 28 FAAHYGGGEANVAISLANFGHRVSFASKVPENALGDAVFHHLRSYGVDCRHL-LRGGSRLGTYYIETGI---GERAARVV 103
Cdd:PLN02543 167 FARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVkFDENAKTACSRMKIKFrdgGKMVAETV 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 104 YDRAGSSfaqMKENEWQSDLFDGVDIVHLSG---ITPAlsttWQTLLLTLIKEAKAAGCKISFDINYRGKLWTTA-EARV 179
Cdd:PLN02543 247 KEAAEDS---LLASELNLAVLKEARMFHFNSevlTSPS----MQSTLFRAIELSKKFGGLIFFDLNLPLPLWRSRdETRE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 180 FLQEVLPYVDYCSAGQLDAQVFMDvsapteeveDDYYyqEMHRKYP------------NIQLFYSTSRQVLSashnqltg 247
Cdd:PLN02543 320 LIKKAWNEADIIEVSRQELEFLLD---------EDYY--ERKRNYPpqyyaesfeqtkNWRDYYHYTPEEIA-------- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 248 SLWHNG-------------NY-------VVSATHE--INPIV-DRVGGGDAFSAGVLHGLVT---KKQDQEIID----FA 297
Cdd:PLN02543 381 PLWHDGlklllvtdgtlriHYytpkfdgVVVGTEDvlITPFTcDRTGSGDAVVAAIMRKLTTcpeMFEDQDVLErqlrFA 460
|
...
gi 1829055301 298 TAA 300
Cdd:PLN02543 461 VAA 463
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
126-285 |
2.19e-07 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 50.56 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 126 GVDIVHLSGITPALSTTWQTllltlIKEAKAAGCKISFDINYRGKLWTTAEarvfLQEVLPYVDYCSAGQLDAQVFMDVS 205
Cdd:cd00287 57 GADAVVISGLSPAPEAVLDA-----LEEARRRGVPVVLDPGPRAVRLDGEE----LEKLLPGVDILTPNEEEAEALTGRR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 206 APtEEVEDDYYYQEMHRKYPNIQLFYSTSRQVLsashnqltgsLWHNGNYVVSATHEINPIVDRVGGGDAFSAGVLHGLV 285
Cdd:cd00287 128 DL-EVKEAAEAAALLLSKGPKVVIVTLGEKGAI----------VATRGGTEVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
29-302 |
9.16e-07 |
|
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.
Pssm-ID: 238573 [Multi-domain] Cd Length: 312 Bit Score: 49.92 E-value: 9.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 29 AAHYGGGEANVAISLANFGHRVSFASKVPENALGDAVFHHLRSYGVDCRHLLRGGSRLGTYYIETGIGERAARVVYDRAG 108
Cdd:cd01168 51 KYIAGGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDAERTMCTYLGAA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 109 SSFAQmkenewQSDLFDGVDIVHLSGITPALSTTWQTLLLTLIKEAKAAGCKISFDI-------NYRGKLWttaearvfl 181
Cdd:cd01168 131 NELSP------DDLDWSLLAKAKYLYLEGYLLTVPPEAILLAAEHAKENGVKIALNLsapfivqRFKEALL--------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 182 qEVLPYVDYCSAGQLDAQVFMDvSAPTEEVEDDYYYQEMHrkypniqlfystSRQVLsashnqLTGSlwHNGNYVVSATH 261
Cdd:cd01168 196 -ELLPYVDILFGNEEEAEALAE-AETTDDLEAALKLLALR------------CRIVV------ITQG--AKGAVVVEGGE 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1829055301 262 EI-------NPIVDRVGGGDAFSAGVLHGLVTKKQDQEIIDFATAASA 302
Cdd:cd01168 254 VYpvpaipvEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAA 301
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
33-284 |
1.12e-06 |
|
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.
Pssm-ID: 238915 [Multi-domain] Cd Length: 264 Bit Score: 49.27 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 33 GGGEANVAISLANFGHRVSFASKVPENALGDAVFHHLRSYGVDCRHLLrggsrlgTYYIETGI-------GERAArVVYD 105
Cdd:cd01940 22 GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCR-------VKEGENAVadvelvdGDRIF-GLSN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 106 RAGSsfaqMKENEWQSDL--FDGVDIVHLSgitpalSTTWQTLLLTLIKEAKAAGCKISFDINYRgklWTTAEarvfLQE 183
Cdd:cd01940 94 KGGV----AREHPFEADLeyLSQFDLVHTG------IYSHEGHLEKALQALVGAGALISFDFSDR---WDDDY----LQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 184 VLPYVDYC--SAGQLDaqvfmdvsapTEEVEddyyyQEMHRkypniqlFYSTSRQVLSASHNQLTGSLWHNGNYVVSATH 261
Cdd:cd01940 157 VCPYVDFAffSASDLS----------DEEVK-----AKLKE-------AVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPR 214
|
250 260
....*....|....*....|...
gi 1829055301 262 EINpIVDRVGGGDAFSAGVLHGL 284
Cdd:cd01940 215 PVE-VVDTLGAGDSFIAGFLLSL 236
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
30-309 |
8.42e-06 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 46.65 E-value: 8.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 30 AHYGGGEANVAISLANFGHRVSFASKVPENALGDAVFHHLRSYGVDCRHLLRGGSRLGTYYIETGIGEraaRVVYDRAGS 109
Cdd:PRK09813 20 AFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGVTAQTQVELHDND---RVFGDYTEG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 110 SFAQMKENEWQSDLFDGVDIVHlSGItpalsttwQTLLLTLIKEAKAAGCKISFDINYR--GKLWTTAearvflqevLPY 187
Cdd:PRK09813 97 VMADFALSEEDYAWLAQYDIVH-AAI--------WGHAEDAFPQLHAAGKLTAFDFSDKwdSPLWQTL---------VPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 188 VDYcsagqldaqVFMDVSAPTEEVEDdyYYQEMHRKYPniqlfystsrQVLSASHNQlTGSLWHNGNYVVsaTHEINP-- 265
Cdd:PRK09813 159 LDY---------AFASAPQEDEFLRL--KMKAIVARGA----------GVVIVTLGE-NGSIAWDGAQFW--RQAPEPvt 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1829055301 266 IVDRVGGGDAFSAGVLHGLVTKKQDQEIIDFATAASALKHTIHG 309
Cdd:PRK09813 215 VVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
24-321 |
2.40e-05 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 45.50 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 24 HSSMFAAHYGGGEANVAISLANFGHRVSFASKVPENALGDAVFHHLRSYGVDCRHLLRGG---SRLGTYYIETGIGERAA 100
Cdd:PTZ00292 43 HGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTEnssTGLAMIFVDTKTGNNEI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 101 RVVYDRAGSSFAQMKENEWqSDLFDGVDIVHLSGITPalsttwQTLLLTLIKEAKAAGCKISFDINYRGKLWTTAEARvf 180
Cdd:PTZ00292 123 VIIPGANNALTPQMVDAQT-DNIQNICKYLICQNEIP------LETTLDALKEAKERGCYTVFNPAPAPKLAEVEIIK-- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 181 lqEVLPYVDYCSAGQLDAQVFMDVSAPTEEVEDDyYYQEMhrkypniqlfystsrQVLSASHNQLT-GS----LWHNGNY 255
Cdd:PTZ00292 194 --PFLKYVSLFCVNEVEAALITGMEVTDTESAFK-ASKEL---------------QQLGVENVIITlGAngclIVEKENE 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1829055301 256 VVSATHEINPIVDRVGGGDAFSAGVLHGLVTKKQDQEIIDFATAASALKHTIHGdcNQFSANEIQE 321
Cdd:PTZ00292 256 PVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHG--TQSSYPHPSE 319
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
247-303 |
2.48e-05 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 45.46 E-value: 2.48e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1829055301 247 GSLWHNGNYVVSATHEINPIVDRVGGGDAFSAGVLHGLVTKKQDQEIIDFATAASAL 303
Cdd:PRK09513 228 GALWVNASGEWIAKPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSAL 284
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
33-303 |
6.91e-05 |
|
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238916 [Multi-domain] Cd Length: 288 Bit Score: 43.84 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 33 GGGEANVAISLANFGHRVSFASKVPENALGDAVFHHLRSYGVDCRHLLRGGSRLGTYyieTGIGERAARVVYdragsSFA 112
Cdd:cd01941 35 GGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRGIVFEGRSTASY---TAILDKDGDLVV-----ALA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 113 QMkenewqsDLFDGVDIVHLSGITPAlsttwqtllltlIKEAKAagckISFDIN-------YRGKLWTTAEARVF----- 180
Cdd:cd01941 107 DM-------DIYELLTPDFLRKIREA------------LKEAKP----IVVDANlpeealeYLLALAAKHGVPVAfepts 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 181 ------LQEVLPYVDYCSAGQLDAQVFMDvsAPTEEVEDDyyyqemhRKYPNIQLFYSTSRQVLSASHNqltGSLWHNGN 254
Cdd:cd01941 164 apklkkLFYLLHAIDLLTPNRAELEALAG--ALIENNEDE-------NKAAKILLLPGIKNVIVTLGAK---GVLLSSRE 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1829055301 255 YVVSATHEINPIVDRV----GGGDAFSAGVLHGLVTKKQDQEIIDFATAASAL 303
Cdd:cd01941 232 GGVETKLFPAPQPETVvnvtGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAAL 284
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
247-304 |
5.20e-04 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 41.27 E-value: 5.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1829055301 247 GSLWHNGNYVVSATHEINPIVDRVGGGDAFSAGVLHGLVTKKQDQEIIDFATAASALK 304
Cdd:COG1105 225 GALLVTEDGVYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAA 282
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
20-297 |
1.16e-03 |
|
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238922 [Multi-domain] Cd Length: 265 Bit Score: 40.09 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 20 DRIAHSSMFAAHYGGGEANVAISLANFGHRVSFASKVPENALGDAVFHHLRSYGvDCRHLLR--GGSRLGTYYIEtGIGE 97
Cdd:cd01947 23 GGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGG-DKHTVAWrdKPTRKTLSFID-PNGE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 98 RAARVVYDRagssfaQMKENEWQSdlFDGVDIVHLSGITPalsttwqtlLLTLIKEAKAAGCKISfDINYRGKLWTTAEA 177
Cdd:cd01947 101 RTITVPGER------LEDDLKWPI--LDEGDGVFITAAAV---------DKEAIRKCRETKLVIL-QVTPRVRVDELNQA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829055301 178 RVFLQEVLpyvdyCSAGQLDAQVFMDVSApteeveddyyyqemhrkYPNIQLFystsrqVLSASHNqltGSLWHNGNYVV 257
Cdd:cd01947 163 LIPLDILI-----GSRLDPGELVVAEKIA-----------------GPFPRYL------IVTEGEL---GAILYPGGRYN 211
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1829055301 258 SATHEINPIVDRVGGGDAFSAGVLHGLVTKKQDQEIIDFA 297
Cdd:cd01947 212 HVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELG 251
|
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