|
Name |
Accession |
Description |
Interval |
E-value |
| IolC |
COG3892 |
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism]; |
3-640 |
0e+00 |
|
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];
Pssm-ID: 443099 [Multi-domain] Cd Length: 640 Bit Score: 1113.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 3 TQQKPLDVICIGRIAVDLYGQQIGARLEDETTFAKYLGGSSGNVAYGTAIQGLKSAMLARVGDEHMGRFLREELQRAGCD 82
Cdd:COG3892 1 ARMKTLDVICIGRVSVDLYGQQIGGRLEDMSSFAKYLGGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFLREELEREGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 83 TQSLITDKKRLTGLVILGIKDRETFPLVFYRDNCADMGLVPDDIREEYIASARAVAVTGTHLSHADTRAAVLKALDIARR 162
Cdd:COG3892 81 TSGVVTDPERLTALVLLGIRDDETFPLIFYRENCADMALTEDDIDEAFIASARALLITGTHLSHPRTRAAVLKALRYARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 163 HGLRSALDIDYRPVLWGLTSLGDGETRFVESARVTQQLQDVLHYFDLVVGTEEEFHIAGGSTDSLTALKNVRQATKATLV 242
Cdd:COG3892 161 HGGKVVLDIDYRPVLWGLTGHGDGETRFVASDAVTAHLQEVLPLFDLIVGTEEEFHIAGGSTDTLAALRAVRRVSTATLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 243 CKRGALGCVVFEGEIPDTWQQTKLHPGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHGCAPAM 322
Cdd:COG3892 241 CKRGALGCVVFEGAIPDDLDDGITGPGFPVEVFNVLGAGDAFMSGFLRGWLRGESWETACAYANACGALVVSRHGCAPAM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 323 PTKEELDDFLGRQHAVKRPDLDGRLNHLHRVTTRKQHWHELNIFAFDHRKQLVDMAAEAGADDTRIPELKSLLLRAAREA 402
Cdd:COG3892 321 PTWEELDYFLARGSRVPRPDKDAELNHLHRVTTRRRQWDELCVFAFDHRSQFEDMAREAGADEARIPALKRLLLEAAAQV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 403 AKEAGLdDGRCGILADTTYGQPALNEITGRGWWIARPIELPGSRPLRLEHG-NIGSQLVDWPQEHVVKCLTFYHPQDGKE 481
Cdd:COG3892 401 AAGAGL-RGGIGVLIDDRYGQDALNAATGRGWWIGRPVELPGSRPLRFEHGrDIGSQLVEWPQEHVVKCLVFYHPDDPAE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 482 MRQAQDELLLDVWQSCNRSGHELLLEVILPESNPDKDEkYYVQILNHFYHMGIKPDWWKLPPLSRDSWAAIGRLIEDHDQ 561
Cdd:COG3892 480 LRLEQEAQLRRLYDACRRSGHELLLEVIPPKDGPVDDD-TVARAIQRFYNLGIKPDWWKLEPMSAAAWQAIDALIAERDP 558
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1353436328 562 HCRGILLLGLDAPEAELKTGFAAAASSPWVKGFAVGRTIFGQPSRQWLQNELDDNTLINKVKTNYLTLIGYWREARPAQ 640
Cdd:COG3892 559 YCRGVVLLGLDAPEEELAAGFAAAAGSPLVKGFAVGRTIFAEPARAWLAGEIDDEEAVAEVADNYARLIDLWRAARQAA 637
|
|
| DUF2090 |
pfam09863 |
Uncharacterized protein conserved in bacteria (DUF2090); This domain, found in various ... |
327-637 |
1.14e-170 |
|
Uncharacterized protein conserved in bacteria (DUF2090); This domain, found in various prokaryotic carbohydrate kinases, has no known function.
Pssm-ID: 430888 Cd Length: 310 Bit Score: 488.72 E-value: 1.14e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 327 ELDDFLGRQHAVKRPDLDGRLNHLHRVTTRKQHWHELNIFAFDHRKQLVDMAAEAGADDTRIPELKSLLLRAAREAAKEA 406
Cdd:pfam09863 1 ELDYFLSRGERVPRPDKDAELEHLHRVTTRRRQWDELCVLAFDHRSQLEELAREAGADLARIPALKRLLLRAAEEVAQEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 407 GLDdGRCGILADTTYGQPALNEITGRGWWIARPIELPGSRPLRLEHG-NIGSQLVDWPQEHVVKCLTFYHPQDGKEMRQA 485
Cdd:pfam09863 81 GLQ-GGAGVLIDGRYGQDALNAATGRGWWIGRPIELPGSRPLRFEHGrSIGSQLIEWPLEHVVKCLVFYHPDDDAALRAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 486 QDELLLDVWQSCNRSGHELLLEVILPESNPDKDEkYYVQILNHFYHMGIKPDWWKLPPLSRDSWAAIGRLIEDHDQHCRG 565
Cdd:pfam09863 160 QEAQLRELYDACRKSGHELLLEVIPPKDGPVDDE-TYARAIRRFYNLGVKPDWWKLPPLSAAAWEQIDALIEERDPYCRG 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1353436328 566 ILLLGLDAPEAELKTGFAAAASSPWVKGFAVGRTIFGQPSRQWLQNELDDNTLINKVKTNYLTLIGYWREAR 637
Cdd:pfam09863 239 VVILGLDAPEEELAAGFAAAAGFPLVKGFAVGRTIFADPARAWLAGEIDDEELIAEVAANYARLIDLWRQRR 310
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
7-332 |
3.39e-161 |
|
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are translated from the iolC gene of known or putative inositol catabolism operons. Members with characterized function are 5-dehydro-2-deoxygluconokinase, the enzyme catalyzing the fifth step in degradation from myo-inositol or closely related compounds. Note that many members of this family are fusion proteins with an additional C-terminal domain, of unknown function, described by pfam09863. [Energy metabolism, Sugars]
Pssm-ID: 275175 [Multi-domain] Cd Length: 309 Bit Score: 464.38 E-value: 3.39e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 7 PLDVICIGRIAVDLYGQQIGARLEDETTFAKYLGGSSGNVAYGTAIQGLKSAMLARVGDEHMGRFLREELQRAGCDTQSL 86
Cdd:TIGR04382 1 KLDVITIGRVGVDLYPQQIGVPLEDVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 87 ITDKKRLTGLVILGIKDRETFPLVFYRDNCADMGLVPDDIREEYIASARAVAVTGTHLSHADTRAAVLKALDIARRHGLR 166
Cdd:TIGR04382 81 VTDPGRRTSLVFLEIKPPDEFPLLFYRENAADLALTPDDVDEDYIASARALLVSGTALSQEPSREAVLKALEYARAAGVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 167 SALDIDYRPVLWGltslgdgetrfvESARVTQQLQDVLHYFDLVVGTEEEFHIAGGSTDSLTALKNVRQATKATLVCKRG 246
Cdd:TIGR04382 161 VVLDIDYRPYLWK------------SPEEAGIYLRLVLPLVDVIIGTREEFDIAGGEGDDEAAARALLDAGVEILVVKRG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 247 ALGCVVFEGEiPDTWQQtklhPGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHGCAPAMPTKE 326
Cdd:TIGR04382 229 PEGSLVYTGD-GEGVEV----PGFPVEVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCSPAMPTLE 303
|
....*.
gi 1353436328 327 ELDDFL 332
Cdd:TIGR04382 304 ELEAFL 309
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
9-328 |
1.33e-82 |
|
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: 262.13 E-value: 1.33e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 9 DVICIGRIAVDLYGQ----QIGARLEDETTFAKYLGGSSGNVAYGTAIQGLKSAMLARVGDEHMGRFLREELQRAGCDTQ 84
Cdd:COG0524 1 DVLVIGEALVDLVARvdrlPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 85 SLITDKKRLTGLVILGIKDRETFPLVFYRdnCADMGLVPDDIREEYIASARAVAVTGTHLSHADTRAAVLKALDIARRHG 164
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYR--GANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 165 LRSALDIDYRPVLWgltslgdgetrfvesARVTQQLQDVLHYFDLVVGTEEEFHIAGGSTDSLTALKNVRQATKATLVCK 244
Cdd:COG0524 159 VPVSLDPNYRPALW---------------EPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 245 RGALGCVVFEGEipdtwqQTKLHPGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHGCAPAMPT 324
Cdd:COG0524 224 LGAEGALLYTGG------EVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPT 297
|
....
gi 1353436328 325 KEEL 328
Cdd:COG0524 298 REEV 301
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
9-319 |
5.03e-82 |
|
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: 260.59 E-value: 5.03e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 9 DVICIGRIAVDLYGQQIGaRLEDETTFAKYLGGSSGNVAYGTAIQGLKSAMLARVGDEHMGRFLREELQRAGCDTQSLIT 88
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGG-RLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 89 DKKRLTGLVILGIKDRETFPLVFYRDNCADMGLVPDDIREEYIASARAVAVTGTHLS-HADTRAAVLKALDIARRHGLRS 167
Cdd:cd01166 80 DPGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLAlSESAREALLEALEAAKARGVTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 168 ALDIDYRPVLWGLtslgdgetrfvESARvtQQLQDVLHYFDLVVGTEEEFHIAGGSTDSLTALKNVRQ--ATKATLVCKR 245
Cdd:cd01166 160 SFDLNYRPKLWSA-----------EEAR--EALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALAlaLGVKAVVVKL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1353436328 246 GALGCVVFEGEipdtwQQTKLhPGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHGCA 319
Cdd:cd01166 227 GAEGALVYTGG-----GRVFV-PAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
10-317 |
7.03e-49 |
|
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: 172.44 E-value: 7.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 10 VICIGRIAVDLYGQQIGarleDETTFAKYLGGSSGNVAYGTAIQGLKSAMLARVGDEHMGRFLREELQRAGCDTQSLITD 89
Cdd:cd01167 2 VVCFGEALIDFIPEGSG----APETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 90 KKRLTGLVILGIKDR--ETFplVFYRDNCADMgLVPDDIREEYIASARAVaVTGTH-LSHADTRAAVLKALDIARRHGLR 166
Cdd:cd01167 78 PAAPTTLAFVTLDADgeRSF--EFYRGPAADL-LLDTELNPDLLSEADIL-HFGSIaLASEPSRSALLELLEAAKKAGVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 167 SALDIDYRPVLWgltslgdgetRFVESARVTqqLQDVLHYFDLVVGTEEEFHIAGGSTDSLTALKNVRQATKATLVCKRG 246
Cdd:cd01167 154 ISFDPNLRPPLW----------RDEEEARER--IAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRG 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1353436328 247 ALGCVVFEGEipdtwqQTKLHPGVRVEVLNVLGAGDAFMSGLLRG-------WLNDESWEQACRYANACGALVVSRHG 317
Cdd:cd01167 222 ADGALLYTKG------GVGEVPGIPVEVVDTTGAGDAFVAGLLAQllsrgllALDEDELAEALRFANAVGALTCTKAG 293
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
9-319 |
1.58e-43 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 157.89 E-value: 1.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 9 DVICIGRIAVDLYGQQIGARLED--ETTFAKYLGGSSGNVAYGTAIQGLKSAMLARVGDEHMGRFLREELQRAGCDTQSL 86
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPGELvrVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 87 ITDKKRLTGL-VILGIKDRETFpLVFYRDNCADMGLVPDDIREEYIASARAVAVTGTHLSHADTrAAVLKALDIARRHGl 165
Cdd:pfam00294 81 VIDEDTRTGTaLIEVDGDGERT-IVFNRGAAADLTPEELEENEDLLENADLLYISGSLPLGLPE-ATLEELIEAAKNGG- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 166 rsALDIDYRPVLWgltslgdgetrfvesaRVTQQLQDVLHYFDLVVGTEEEF----HIAGGSTDSLT-ALKNVRQATKAT 240
Cdd:pfam00294 158 --TFDPNLLDPLG----------------AAREALLELLPLADLLKPNEEELealtGAKLDDIEEALaALHKLLAKGIKT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 241 LVCKRGALGCVVFEGEipdtwqQTKLHPGVR-VEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHGCA 319
Cdd:pfam00294 220 VIVTLGADGALVVEGD------GEVHVPAVPkVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
1-337 |
7.38e-32 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 126.27 E-value: 7.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 1 MGTQQKPLdVICIGRIAVDLYGQQIGARLEDETTFAKYLGGSSGNVAYGTAIQGLKSAMLARVGDEHMGRFLREELQRAG 80
Cdd:PLN02323 5 PSTAESSL-VVCFGEMLIDFVPTVSGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 81 CDTQSLITDKKRLTGLVILGIKD---REtfpLVFYRDNCADMGLVPDDIREEYIASARAVAVTGTHLSHADTRAAVLKAL 157
Cdd:PLN02323 84 VNNEGVRFDPGARTALAFVTLRSdgeRE---FMFYRNPSADMLLRESELDLDLIRKAKIFHYGSISLITEPCRSAHLAAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 158 DIARRHGLRSALDIDYRPVLWGLTslgdgetrfvESARvtQQLQDVLHYFDLVVGTEEE--FHIAGGSTDSLTALKNVRQ 235
Cdd:PLN02323 161 KIAKEAGALLSYDPNLRLPLWPSA----------EAAR--EGIMSIWDEADIIKVSDEEveFLTGGDDPDDDTVVKLWHP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 236 ATKATLVCKrGALGCV----VFEGEIPdtwqqtklhpGVRVEVLNVLGAGDAFMSGLL------RGWLNDES-WEQACRY 304
Cdd:PLN02323 229 NLKLLLVTE-GEEGCRyytkDFKGRVE----------GFKVKAVDTTGAGDAFVGGLLsqlakdLSLLEDEErLREALRF 297
|
330 340 350
....*....|....*....|....*....|...
gi 1353436328 305 ANACGALVVSRHGCAPAMPTKEELDDFLGRQHA 337
Cdd:PLN02323 298 ANACGAITTTERGAIPALPTKEAVLKLLKKAVA 330
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
30-329 |
1.29e-27 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 113.49 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 30 EDETTFAKYLGGSSGNVAYGTAIQGLKSAMLARVGDEHMGRFLREELQRAGCDTQSLITDKKRLTGLVILGIKDRETFPL 109
Cdd:PRK09434 18 EGENRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERSF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 110 VFYRDNCADMGLVPDDI----REEY-----IAsaravavtgthLSHADTRAAVLKALDIARRHGLRSALDIDYRPVLWGL 180
Cdd:PRK09434 98 TFMVRPSADLFLQPQDLppfrQGEWlhlcsIA-----------LSAEPSRSTTFEAMRRIKAAGGFVSFDPNLREDLWQD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 181 TSlgdgETRFVesarVTQ--QLQDVLHYfdlvvgTEEEFHIAGGSTDSLTALKNVRQATKATLV-CKRGALG-CVVFEGe 256
Cdd:PRK09434 167 EA----ELREC----LRQalALADVVKL------SEEELCFLSGTSQLEDAIYALADRYPIALLlVTLGAEGvLVHTRG- 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1353436328 257 ipdtwqQTKLHPGVRVEVLNVLGAGDAFMSGLLRG------WLNDESWEQACRYANACGALVVSRHGCAPAMPTKEELD 329
Cdd:PRK09434 232 ------QVQHFPAPSVDPVDTTGAGDAFVAGLLAGlsqaglWTDEAELAEIIAQAQACGALATTAKGAMTALPNRQELE 304
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
9-318 |
2.91e-27 |
|
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: 111.63 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 9 DVICIGRIAVDLYGQQIGARLEDETTFAK----YLGGSSGNVAYGTAIQGLKSAMLARVGDEHMGRFLREELQRAGCDTQ 84
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKdlrrEFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 85 SLITDKKRLTGL-VILGIKDRETfplVFYRDNCADMGLVPDDIrEEYIASARAVavtgtHLSHADtrAAVLKALDIARRh 163
Cdd:cd01942 81 HVRVVDEDSTGVaFILTDGDDNQ---IAYFYPGAMDELEPNDE-ADPDGLADIV-----HLSSGP--GLIELARELAAG- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 164 glrsALDIDYRP--VLWGLTslGDGETRFVESArvtqqlqdvlhyfDLVVGTEEEFHIAggstDSLTALKNVRQATKA-T 240
Cdd:cd01942 149 ----GITVSFDPgqELPRLS--GEELEEILERA-------------DILFVNDYEAELL----KERTGLSEAELASGVrV 205
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1353436328 241 LVCKRGALGCVVFEGEipdtwqQTKLHPGV-RVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHGC 318
Cdd:cd01942 206 VVVTLGPKGAIVFEDG------EEVEVPAVpAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGA 278
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
7-318 |
3.09e-26 |
|
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: 109.63 E-value: 3.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 7 PLDVICIGRIAVDL-----------YGQQIG-ARLEDETTF--------AKYL-GGSSGNVAYGTAIQGLKSAMLARVGD 65
Cdd:cd01168 1 RYDVLGLGNALVDIlaqvddaflekLGLKKGdMILADMEEQeellaklpVKYIaGGSAANTIRGAAALGGSAAFIGRVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 66 EHMGRFLREELQRAGCDTQSLiTDKKRLTG--LVILGIKDRETfpLVFYRDNCADmgLVPDDIREEYIASARAVAVTGTH 143
Cdd:cd01168 81 DKLGDFLLKDLRAAGVDTRYQ-VQPDGPTGtcAVLVTPDAERT--MCTYLGAANE--LSPDDLDWSLLAKAKYLYLEGYL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 144 LSHADtrAAVLKALDIARRHGLRSALDIdyrpvlwgltSLGDGETRFvesarvTQQLQDVLHYFDLVVGTEEEFHIAGGS 223
Cdd:cd01168 156 LTVPP--EAILLAAEHAKENGVKIALNL----------SAPFIVQRF------KEALLELLPYVDILFGNEEEAEALAEA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 224 --TDSLTALKNVRQATKATLVCKRGALGCVVFEGEipdtwQQTKLHPGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQA 301
Cdd:cd01168 218 etTDDLEAALKLLALRCRIVVITQGAKGAVVVEGG-----EVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEEC 292
|
330
....*....|....*..
gi 1353436328 302 CRYANACGALVVSRHGC 318
Cdd:cd01168 293 IRLGSYAAAEVIQQLGP 309
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
9-324 |
1.62e-25 |
|
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: 106.87 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 9 DVICIGRIAVDLYgqqigARLED-----ET----TFAKYLGGSSGNVAYGTAIQGLKSAMLARVGDEHMGRFLREELQRA 79
Cdd:cd01174 1 KVVVVGSINVDLV-----TRVDRlpkpgETvlgsSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 80 GCDTQSLITDKKRLTGL-VILGIKDREtfplvfyrdNC------ADMGLVPDDIR--EEYIASARAVaVTGTHLSHadtr 150
Cdd:cd01174 76 GIDVSYVEVVVGAPTGTaVITVDESGE---------NRivvvpgANGELTPADVDaaLELIAAADVL-LLQLEIPL---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 151 AAVLKALDIARRHGLRSALDidyrpvlwgltslgdgetrfveSARVTQQLQDVLHYFDLVVGTEEEF----HIAGGSTDS 226
Cdd:cd01174 142 ETVLAALRAARRAGVTVILN----------------------PAPARPLPAELLALVDILVPNETEAalltGIEVTDEED 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 227 LTALKNVRQATKA-TLVCKRGALGCVVFEGEipdtwqQTKLHPGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYA 305
Cdd:cd01174 200 AEKAARLLLAKGVkNVIVTLGAKGALLASGG------EVEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFA 273
|
330
....*....|....*....
gi 1353436328 306 NACGALVVSRHGCAPAMPT 324
Cdd:cd01174 274 NAAAALSVTRPGAQPSIPT 292
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
9-324 |
1.36e-16 |
|
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: 80.42 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 9 DVICIGRIAVDLYGQQIGARLEDE----TTFAKYLGGSSGNVAYGTAIQGLKSAMLARVGDEHMGRFLREELQRAGCDTQ 84
Cdd:cd01945 1 RVLGVGLAVLDLIYLVASFPGGDGkivaTDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 85 SLITDKKRLT--GLVILGIKDRETfPLVFYRDNCADMGLVPDDIreeyIASARAVavtgthlsHADTR--AAVLKALDIA 160
Cdd:cd01945 81 FIVVAPGARSpiSSITDITGDRAT-ISITAIDTQAAPDSLPDAI----LGGADAV--------LVDGRqpEAALHLAQEA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 161 RRHGLRSALDIDyrpvlwgltslgdgetrfVESARVTQQLqdvLHYFDLVVGTEEEFHIAGGSTDSLtALKNVRQATKAT 240
Cdd:cd01945 148 RARGIPIPLDLD------------------GGGLRVLEEL---LPLADHAICSENFLRPNTGSADDE-ALELLASLGIPF 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 241 LVCKRGALGCVVFE--GEipdTWQQtklhPGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHGC 318
Cdd:cd01945 206 VAVTLGEAGCLWLErdGE---LFHV----PAFPVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGG 278
|
....*.
gi 1353436328 319 APAMPT 324
Cdd:cd01945 279 RAGLPT 284
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
1-328 |
4.93e-16 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 79.78 E-value: 4.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 1 MGTQQKplDVICIGRIAVDLYG-----QQIGARLEDeTTFAKYLGGSSGNVAYGTAIQGLKSAMLARVGDEHMGRFLREE 75
Cdd:PTZ00292 11 GGEAEP--DVVVVGSSNTDLIGyvdrmPQVGETLHG-TSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 76 LQRAGCDTQSLITDKKRLTGLVILgIKDRETfplvfyRDNC------ADMGLVPDDIREEY--IASARAVAVTGTHLSHA 147
Cdd:PTZ00292 88 FKRNGVNTSFVSRTENSSTGLAMI-FVDTKT------GNNEiviipgANNALTPQMVDAQTdnIQNICKYLICQNEIPLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 148 DTraavLKALDIARRHGLRSALDIDYRPvlwgltslgdgetrfveSARVTQQLQDVLHYFDLVVGTEEEFHIAGGSTdsL 227
Cdd:PTZ00292 161 TT----LDALKEAKERGCYTVFNPAPAP-----------------KLAEVEIIKPFLKYVSLFCVNEVEAALITGME--V 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 228 TALKNVRQATKATL-------VCKRGALGCVVFEGEipdtwqQTKLH-PGVRVEVLNVLGAGDAFMSGLLRGWLNDESWE 299
Cdd:PTZ00292 218 TDTESAFKASKELQqlgvenvIITLGANGCLIVEKE------NEPVHvPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLK 291
|
330 340
....*....|....*....|....*....
gi 1353436328 300 QACRYANACGALVVSRHGCAPAMPTKEEL 328
Cdd:PTZ00292 292 ESCKRANRIAAISVTRHGTQSSYPHPSEL 320
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
10-314 |
2.89e-14 |
|
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: 73.50 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 10 VICIGRIAVDLYGQ-----QIGARLEDETTFAkyLGGSSGNVAYGTAIQGLKSAMLARVGDEHMGRFLREELQRAGCDTQ 84
Cdd:cd01941 2 IVVIGAANIDLRGKvsgslVPGTSNPGHVKQS--PGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 85 SLITDKKRlTGlvilgikdreTFPLVFYRDN-----CADMGLVpDDIREEYIASARAVavtgthLSHADT--------RA 151
Cdd:cd01941 80 GIVFEGRS-TA----------SYTAILDKDGdlvvaLADMDIY-ELLTPDFLRKIREA------LKEAKPivvdanlpEE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 152 AVLKALDIARRHGLRSALDidyrPVlwgltslgdgetrfveSARVTQQLQDVLHYFDLVVGTEEEF-----HIAGGSTDS 226
Cdd:cd01941 142 ALEYLLALAAKHGVPVAFE----PT----------------SAPKLKKLFYLLHAIDLLTPNRAELealagALIENNEDE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 227 LTALKNVRQATKATLVCKRGALGCVVFEGEIPDTwqqTKLHP-GVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYA 305
Cdd:cd01941 202 NKAAKILLLPGIKNVIVTLGAKGVLLSSREGGVE---TKLFPaPQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFA 278
|
....*....
gi 1353436328 306 NACGALVVS 314
Cdd:cd01941 279 QAAAALTLE 287
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
10-328 |
1.24e-13 |
|
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.
Pssm-ID: 238577 [Multi-domain] Cd Length: 304 Bit Score: 72.21 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 10 VICIGRIAVD--LYGQQIG---------ARLEDETTFakyLGGSsGNVAYGTAIQGLKSAMLARVGDEHMGRFLREELQR 78
Cdd:cd01172 2 VLVVGDVILDeyLYGDVERispeapvpvVKVEREEIR---LGGA-ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 79 AGCDTQsLITDKKRLT---------GLVILGIkDRETFPLVfyrdncadmglvPDDIREEYIASARAvavtgtHLSHAD- 148
Cdd:cd01172 78 EGIDTD-GIVDEGRPTttktrviarNQQLLRV-DREDDSPL------------SAEEEQRLIERIAE------RLPEADv 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 149 -----------TRAAVLKALDIARRHGLRSALDidyrpvlwgltSLGDGETRFVEsarvtqqlqdvlhyFDLVVGTEEEF 217
Cdd:cd01172 138 vilsdygkgvlTPRVIEALIAAARELGIPVLVD-----------PKGRDYSKYRG--------------ATLLTPNEKEA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 218 HIAGGSTDS-----LTALKNVRQATKATLVC-KRGALGCVVFEGEipdtwQQTKLHPGVRVEVLNVLGAGDAFMSGLLRG 291
Cdd:cd01172 193 REALGDEINdddelEAAGEKLLELLNLEALLvTLGEEGMTLFERD-----GEVQHIPALAKEVYDVTGAGDTVIATLALA 267
|
330 340 350
....*....|....*....|....*....|....*..
gi 1353436328 292 WLNDESWEQACRYANACGALVVSRHGCAPAmpTKEEL 328
Cdd:cd01172 268 LAAGADLEEAAFLANAAAGVVVGKVGTAPV--TPKEL 302
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
40-335 |
4.79e-12 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 67.20 E-value: 4.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 40 GGSSGNVAYGTAIQGLKSAMLARVGDEHMGRFLREELQRAGCDTQSLITDKKRLTGLVilgikdretfpLVFYRDNC--- 116
Cdd:PRK11142 39 GGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVA-----------LIFVNDEGens 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 117 ------ADMGLVPDDIREEY--IASARAVavtgthLSHADT-RAAVLKALDIARRHGLRSALDidyrPvlwgltslgdge 187
Cdd:PRK11142 108 igihagANAALTPALVEAHRelIANADAL------LMQLETpLETVLAAAKIAKQHGTKVILN----P------------ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 188 trfvesARVTQQLQDVLHYFDLVVGTEEEFHIAGG--STDSLTAlknvRQATK-------ATLVCKRGALGCVVFEGEip 258
Cdd:PRK11142 166 ------APARELPDELLALVDIITPNETEAEKLTGirVEDDDDA----AKAAQvlhqkgiETVLITLGSRGVWLSENG-- 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1353436328 259 dtwqQTKLHPGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHGCAPAMPTKEELDDFLGRQ 335
Cdd:PRK11142 234 ----EGQRVPGFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQEQ 306
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
271-334 |
5.90e-12 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 67.08 E-value: 5.90e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1353436328 271 RVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHGcaPAMPTKEELDDFLGR 334
Cdd:COG1105 241 KVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPG--TGLPDREDVEELLAQ 302
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
10-317 |
6.22e-12 |
|
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: 66.22 E-value: 6.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 10 VICIGRIAVDLYGQQIGArledettfakYLGGSSGNVAYGTAIQGLKSAMLARVGDEHMGRFLREELQRAGCDTqSLITD 89
Cdd:cd01940 2 LAAIGDNVVDKYLHLGKM----------YPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDI-SHCRV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 90 KKRLTGLVILGIK--DREtfpLVFYRDNcADMGLVPDDIREEYIASARAVavtgtHLSHADTRAAVLKALDIARRHGLRS 167
Cdd:cd01940 71 KEGENAVADVELVdgDRI---FGLSNKG-GVAREHPFEADLEYLSQFDLV-----HTGIYSHEGHLEKALQALVGAGALI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 168 ALDIDYRpvlwgltslgdgetrfvesaRVTQQLQDVLHYFDLVVGTEEEFhiagGSTDSLTALKNVRQATKATLVCKRGA 247
Cdd:cd01940 142 SFDFSDR--------------------WDDDYLQLVCPYVDFAFFSASDL----SDEEVKAKLKEAVSRGAKLVIVTRGE 197
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1353436328 248 LGCVVFEGEipDTWQQtklhPGVRVEVLNVLGAGDAFMSGLLRGWL-NDESWEQACRYANACGALVVSRHG 317
Cdd:cd01940 198 DGAIAYDGA--VFYSV----APRPVEVVDTLGAGDSFIAGFLLSLLaGGTAIAEAMRQGAQFAAKTCGHEG 262
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
131-293 |
1.30e-11 |
|
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: 64.04 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 131 IASARAVAVTGThlshADTRAAVLKALDIARRHGLRSALDidyrpvlwgltsLGDGETRFVEsarvtQQLQDVLHYFDLV 210
Cdd:cd00287 55 LVGADAVVISGL----SPAPEAVLDALEEARRRGVPVVLD------------PGPRAVRLDG-----EELEKLLPGVDIL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 211 VGTEEEFHIAGGSTDSLTALKNVRQATKA-----TLVCKRGALGCVVFegeipdTWQQTKLH-PGVRVEVLNVLGAGDAF 284
Cdd:cd00287 114 TPNEEEAEALTGRRDLEVKEAAEAAALLLskgpkVVIVTLGEKGAIVA------TRGGTEVHvPAFPVKVVDTTGAGDAF 187
|
....*....
gi 1353436328 285 MSGLLRGWL 293
Cdd:cd00287 188 LAALAAGLA 196
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
245-334 |
3.99e-11 |
|
hexose kinase, 1-phosphofructokinase family; This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases.
Pssm-ID: 274464 [Multi-domain] Cd Length: 303 Bit Score: 64.52 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 245 RGALGCVVFEGEipDTWQQTklhpGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHGcaPAMPT 324
Cdd:TIGR03168 220 LGADGALLVTKE--GALKAT----PPKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPG--TGLPD 291
|
90
....*....|
gi 1353436328 325 KEELDDFLGR 334
Cdd:TIGR03168 292 PEDVEELLDQ 301
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
34-317 |
4.46e-11 |
|
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: 63.98 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 34 TFAKYLGGSSGNVAYGTAIQGLKSAMLARVGDEHMGRFLREELQRAGCDTQSLITDKK-RLTGLVILGIKDRETFplVFY 112
Cdd:cd01947 30 DSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHTVAWRDKPtRKTLSFIDPNGERTIT--VPG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 113 RDNCADMGLV-PDDIREEYIASAravAVTGTHLSHADTRAAVLKALdiarrhGLRSALDIdyrpvlwgltslgdgetrfv 191
Cdd:cd01947 108 ERLEDDLKWPiLDEGDGVFITAA---AVDKEAIRKCRETKLVILQV------TPRVRVDE-------------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 192 esarvtqqLQDVLHYFDLVVGTEEEFHIAGGSTDSltALKNVRqatkaTLVCKRGALGCVVFEGeipdtwQQTKLHPGVR 271
Cdd:cd01947 159 --------LNQALIPLDILIGSRLDPGELVVAEKI--AGPFPR-----YLIVTEGELGAILYPG------GRYNHVPAKK 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1353436328 272 VEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHG 317
Cdd:cd01947 218 AKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFG 263
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
6-310 |
4.15e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 59.07 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 6 KPLDVICIGRIAVD--LYGQQIGARLEDETTfaKYLG--------------GSSGNVAYGTAIQGLKSAMLARVGDEHMG 69
Cdd:PLN02341 71 KEIDVATLGNLCVDivLPVPELPPPSREERK--AYMEelaasppdkksweaGGNCNFAIAAARLGLRCSTIGHVGDEIYG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 70 RFLREELQRAGCDTQSLITDkkrlTGLVILGIKDRET---FPLV--FYRDN-C--ADMGLVP--DDIRE------EYIAS 133
Cdd:PLN02341 149 KFLLDVLAEEGISVVGLIEG----TDAGDSSSASYETllcWVLVdpLQRHGfCsrADFGPEPafSWISKlsaeakMAIRQ 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 134 ARAVAVTGTHLSHADTrAAVLKALDIARRHGlrSALDIDYRPvlwgltslgDGETRFVESARVTQQLQDVLHYFDLVVGT 213
Cdd:PLN02341 225 SKALFCNGYVFDELSP-SAIASAVDYAIDVG--TAVFFDPGP---------RGKSLLVGTPDERRALEHLLRMSDVLLLT 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 214 EEEFHiaggstdSLTALKNVRQATKATL---------VCKRGALGCVVFegeipdTWQQTKLHPGVRVEVLNVLGAGDAF 284
Cdd:PLN02341 293 SEEAE-------ALTGIRNPILAGQELLrpgirtkwvVVKMGSKGSILV------TRSSVSCAPAFKVNVVDTVGCGDSF 359
|
330 340
....*....|....*....|....*.
gi 1353436328 285 MSGLLRGWLNDESWEQACRYANACGA 310
Cdd:PLN02341 360 AAAIALGYIHNLPLVNTLTLANAVGA 385
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
245-329 |
2.16e-08 |
|
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific phosphotransferase system (PTS) which imports fructose as fructose-1-phosphate. The action of 1-phosphofructokinase results in beta-D-fructose-1,6-bisphosphate and is an entry point into glycolysis (GenProp0688).
Pssm-ID: 274804 [Multi-domain] Cd Length: 304 Bit Score: 56.06 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 245 RGALGCVVFEGEipDTWQQTklhpGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHGcaPAMPT 324
Cdd:TIGR03828 220 LGADGALLVTKE--GALFAQ----PPKGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEG--TGLPD 291
|
....*
gi 1353436328 325 KEELD 329
Cdd:TIGR03828 292 PEDIE 296
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
10-317 |
3.89e-08 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 54.74 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 10 VICIGRIAVDLYgQQIGArledettfaKYLGGSSGNVAYGTAIQGLKSAMLARVGDEHMGRFLREELQRAGCDTQSLITD 89
Cdd:PRK09813 3 LATIGDNCVDIY-PQLGK---------AFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 90 KKRlTGLVILGIKDRETfplVF--YRDNC-ADMGLVPDDIReeyIASARAVAVTGThLSHADtraAVLKALdiaRRHGLR 166
Cdd:PRK09813 73 HGV-TAQTQVELHDNDR---VFgdYTEGVmADFALSEEDYA---WLAQYDIVHAAI-WGHAE---DAFPQL---HAAGKL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 167 SALDIDYRPvlwgltslgdgETRFVESArvtqqlqdvLHYFDLVvgteeeFHIAGGSTDSL-TALKNVRQATKATLVCKR 245
Cdd:PRK09813 139 TAFDFSDKW-----------DSPLWQTL---------VPHLDYA------FASAPQEDEFLrLKMKAIVARGAGVVIVTL 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1353436328 246 GALGCVVFEGEipdtwqQTKLHPGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHG 317
Cdd:PRK09813 193 GENGSIAWDGA------QFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
157-317 |
3.98e-08 |
|
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.
Pssm-ID: 238570 [Multi-domain] Cd Length: 289 Bit Score: 55.23 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 157 LDIARRHGLRSALDIDYRPvlwgltslgdgetrfvesarvtqqLQDVLHYF-DLVVGTEEEFH-IAGGSTDSLT----AL 230
Cdd:cd01164 151 VRLAREKGARVILDTSGEA------------------------LLAALAAKpFLIKPNREELEeLFGRPLGDEEdviaAA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 231 KNVRQATKATLVCKRGALGCVVFEGEipDTWQQTklhpGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGA 310
Cdd:cd01164 207 RKLIERGAENVLVSLGADGALLVTKD--GVYRAS----PPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGS 280
|
....*..
gi 1353436328 311 LVVSRHG 317
Cdd:cd01164 281 ATAFSPG 287
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
237-317 |
4.44e-08 |
|
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238919 [Multi-domain] Cd Length: 289 Bit Score: 55.12 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 237 TKATLVCKRGALGCVVFEgeiPDtwQQTKLHPGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRH 316
Cdd:cd01944 214 TAAPVVVRLGSNGAWIRL---PD--GNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRS 288
|
.
gi 1353436328 317 G 317
Cdd:cd01944 289 G 289
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
40-324 |
1.13e-07 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 54.17 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 40 GGSSGNVAYGTAIQGLKSAMLARVGDEHMGRFLREELQRAGCDTQSLItdkkRLTGlvilgiKDRETFplvfyrdncadm 119
Cdd:PRK09954 93 GGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGCI----RLHG------QSTSTY------------ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 120 gLVPDDIREEYIasaraVAVTGTHLSHADTRAAVLKALDIARRHGLRSAlDIDYRP--VLWGLTsLGDGETRFVE--SAR 195
Cdd:PRK09954 151 -LAIANRQDETV-----LAINDTHILQQLTPQLLNGSRDLIRHAGVVLA-DCNLTAeaLEWVFT-LADEIPVFVDtvSEF 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 196 VTQQLQDVLHYFDLVVGTEEEFHIAGGS-----TDSLTALKNV-RQATKATLVC-KRGALGCVVFEGEipdtwqQTKLHP 268
Cdd:PRK09954 223 KAGKIKHWLAHIHTLKPTQPELEILWGQaitsdADRNAAVNALhQQGVQQIFVYlPDESVFCSEKDGE------QFLLTA 296
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1353436328 269 GVRVeVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALvvSRHGCAPAMPT 324
Cdd:PRK09954 297 PAHT-TVDSFGADDGFMAGLVYSFLEGYSFRDSARFAMACAAI--SRASGSLNNPT 349
|
|
| PLN02967 |
PLN02967 |
kinase |
14-178 |
2.46e-07 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 53.90 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 14 GRIAVDLYGQQIGARLEDE----TTFAKYLGGSSGNVAYGTAIQGLKSAMLARVGDEHMGRFLREELQRAGCDTQSLITD 89
Cdd:PLN02967 213 GRPANRLLDYEIHERMKDAfwapEKFVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQTRSVCID 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 90 KKRLTGLVILGIKDRETFPLVFYRDnCADMGLVPDDIREEYIASARAVAVTGTHLSHADTRAAVLKALDIARRHGLRSAL 169
Cdd:PLN02967 293 GKRATAVSTMKIAKRGRLKTTCVKP-CAEDSLSKSEINIDVLKEAKMFYFNTHSLLDPTMRSTTLRAIKISKKLGGVIFY 371
|
....*....
gi 1353436328 170 DIDYRPVLW 178
Cdd:PLN02967 372 DLNLPLPLW 380
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
223-336 |
1.64e-05 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 47.34 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 223 STDSLTALKNVRQATKAT--LVCKRGALGCVV-FEGEIPDTW------QQTKlhpgvrveVLNVLGAGDAFMSGLLRGWL 293
Cdd:cd01943 208 KEAVLQALLFSGILQDPGggVVLRCGKLGCYVgSADSGPELWlpayhtKSTK--------VVDPTGGGNSFLGGFAAGLA 279
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1353436328 294 NDESWEQACRYANACGALVVSRHGcapaMPtkeELDDFLGRQH 336
Cdd:cd01943 280 LTKSIDEACIYGSVAASFAIEQVG----LP---RLTKVEGEEL 315
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
268-314 |
1.53e-04 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 44.21 E-value: 1.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1353436328 268 PGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVS 314
Cdd:PRK09850 242 APIKTNVINVTGAGDAMMAGLASCWVDGMPFAESVRFAQGCSSMALS 288
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
197-323 |
2.14e-04 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 43.86 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353436328 197 TQQLQDVLHYFDLVVGTEEEFHIAGGSTD-SLTALKNV--RQATKATLVCKRGALgcVVFEGEIPDTWQQTKLH------ 267
Cdd:PTZ00247 205 FERLLQVLPYVDILFGNEEEAKTFAKAMKwDTEDLKEIaaRIAMLPKYSGTRPRL--VVFTQGPEPTLIATKDGvtsvpv 282
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1353436328 268 PGVRVE-VLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHGCA-PAMP 323
Cdd:PTZ00247 283 PPLDQEkIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCTyPEKP 340
|
|
| |
