|
Name |
Accession |
Description |
Interval |
E-value |
| IolC |
COG3892 |
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism]; |
7-645 |
0e+00 |
|
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];
Pssm-ID: 443099 [Multi-domain] Cd Length: 640 Bit Score: 1078.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 7 ASGRQLDLICLGRLGVDLYAQQVGARLEDVSSFAKYLGGSSANIAFGTARLGLKSAMLSRVGDDHMGRFLVESLAREGCD 86
Cdd:COG3892 1 ARMKTLDVICIGRVSVDLYGQQIGGRLEDMSSFAKYLGGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFLREELEREGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 87 VSGIKVDPERLTALVLLGLKDRETFPLVFYRENCADMALRAEDISEAFIASSKALLITGTHFSTDGVYKASLQALDYAAR 166
Cdd:COG3892 81 TSGVVTDPERLTALVLLGIRDDETFPLIFYRENCADMALTEDDIDEAFIASARALLITGTHLSHPRTRAAVLKALRYARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 167 HNVKRVLDIDYRPVLWGLAGKADGETRFVADQNVSQHVQKILPRFDLIVGTEEEFLIAGGSEDLLTALRTVRELTPATLV 246
Cdd:COG3892 161 HGGKVVLDIDYRPVLWGLTGHGDGETRFVASDAVTAHLQEVLPLFDLIVGTEEEFHIAGGSTDTLAALRAVRRVSTATLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 247 VKLGPQGCTVIHGAIPARLEDGAIYPGVRVEVLNVLGAGDAFMSGFLSGWINDASDERCSQLANACGGLVVSRHACAPAM 326
Cdd:COG3892 241 CKRGALGCVVFEGAIPDDLDDGITGPGFPVEVFNVLGAGDAFMSGFLRGWLRGESWETACAYANACGALVVSRHGCAPAM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 327 PTPAELDYLFNSPVPITRPDQDVTLQRLHRVTVPRKAWKQLFVFAFDHRWQLVELAQKGGQAPERISDIKQLFIQAIERV 406
Cdd:COG3892 321 PTWEELDYFLARGSRVPRPDKDAELNHLHRVTTRRRQWDELCVFAFDHRSQFEDMAREAGADEARIPALKRLLLEAAAQV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 407 ERkltEQGVEADVGLLADQRFGQDALNAASGRGWWIARPVEVQNSRPLAFEHGRSIGSNLIAWPQEQIIKCLVQFHPDDE 486
Cdd:COG3892 401 AA---GAGLRGGIGVLIDDRYGQDALNAATGRGWWIGRPVELPGSRPLRFEHGRDIGSQLVEWPQEHVVKCLVFYHPDDP 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 487 PMLRLEQEAQLKAVYEASLVSGHELLLEVIPPKDHPSTyPDVLYRSLKRLYNLGIYPAWWKIETQSAAEWKKLDELIQER 566
Cdd:COG3892 478 AELRLEQEAQLRRLYDACRRSGHELLLEVIPPKDGPVD-DDTVARAIQRFYNLGIKPDWWKLEPMSAAAWQAIDALIAER 556
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 984659657 567 DPYCRGVVLLGLNASPEFLADGFKQASQSSTCRGFAVGRTIFHEPSRAWMAGEIDDETLIQQVQATFEQLINAWLSARR 645
Cdd:COG3892 557 DPYCRGVVLLGLDAPEEELAAGFAAAAGSPLVKGFAVGRTIFAEPARAWLAGEIDDEEAVAEVADNYARLIDLWRAARQ 635
|
|
| DUF2090 |
pfam09863 |
Uncharacterized protein conserved in bacteria (DUF2090); This domain, found in various ... |
331-644 |
2.15e-172 |
|
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: 492.95 E-value: 2.15e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 331 ELDYLFNSPVPITRPDQDVTLQRLHRVTVPRKAWKQLFVFAFDHRWQLVELAQKGGQAPERISDIKQLFIQAIERVERkl 410
Cdd:pfam09863 1 ELDYFLSRGERVPRPDKDAELEHLHRVTTRRRQWDELCVLAFDHRSQLEELAREAGADLARIPALKRLLLRAAEEVAQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 411 tEQGVEADVGLLADQRFGQDALNAASGRGWWIARPVEVQNSRPLAFEHGRSIGSNLIAWPQEQIIKCLVQFHPDDEPMLR 490
Cdd:pfam09863 79 -EAGLQGGAGVLIDGRYGQDALNAATGRGWWIGRPIELPGSRPLRFEHGRSIGSQLIEWPLEHVVKCLVFYHPDDDAALR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 491 LEQEAQLKAVYEASLVSGHELLLEVIPPKDHPSTyPDVLYRSLKRLYNLGIYPAWWKIETQSAAEWKKLDELIQERDPYC 570
Cdd:pfam09863 158 AEQEAQLRELYDACRKSGHELLLEVIPPKDGPVD-DETYARAIRRFYNLGVKPDWWKLPPLSAAAWEQIDALIEERDPYC 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 984659657 571 RGVVLLGLNASPEFLADGFKQASQSSTCRGFAVGRTIFHEPSRAWMAGEIDDETLIQQVQATFEQLINAWLSAR 644
Cdd:pfam09863 237 RGVVILGLDAPEEELAAGFAAAAGFPLVKGFAVGRTIFADPARAWLAGEIDDEELIAEVAANYARLIDLWRQRR 310
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
11-336 |
4.08e-156 |
|
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: 451.67 E-value: 4.08e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 11 QLDLICLGRLGVDLYAQQVGARLEDVSSFAKYLGGSSANIAFGTARLGLKSAMLSRVGDDHMGRFLVESLAREGCDVSGI 90
Cdd:TIGR04382 1 KLDVITIGRVGVDLYPQQIGVPLEDVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 91 KVDPERLTALVLLGLKDRETFPLVFYRENCADMALRAEDISEAFIASSKALLITGTHFSTDGVYKASLQALDYAARHNVK 170
Cdd:TIGR04382 81 VTDPGRRTSLVFLEIKPPDEFPLLFYRENAADLALTPDDVDEDYIASARALLVSGTALSQEPSREAVLKALEYARAAGVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 171 RVLDIDYRPVLWGlagkadgetrfvADQNVSQHVQKILPRFDLIVGTEEEFLIAGGSEDLLTALRTVRELTPATLVVKLG 250
Cdd:TIGR04382 161 VVLDIDYRPYLWK------------SPEEAGIYLRLVLPLVDVIIGTREEFDIAGGEGDDEAAARALLDAGVEILVVKRG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 251 PQGCTVIHGAiparlEDGAIYPGVRVEVLNVLGAGDAFMSGFLSGWINDASDERCSQLANACGGLVVSRHACAPAMPTPA 330
Cdd:TIGR04382 229 PEGSLVYTGD-----GEGVEVPGFPVEVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCSPAMPTLE 303
|
....*.
gi 984659657 331 ELDYLF 336
Cdd:TIGR04382 304 ELEAFL 309
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
13-323 |
7.01e-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: 273.30 E-value: 7.01e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 13 DLICLGRLGVDLYAQQVGaRLEDVSSFAKYLGGSSANIAFGTARLGLKSAMLSRVGDDHMGRFLVESLAREGCDVSGIKV 92
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGG-RLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 93 DPERLTALVLLGLKDRETFPLVFYRENCADMALRAEDISEAFIASSKALLITGTHFS-TDGVYKASLQALDYAARHNVKR 171
Cdd:cd01166 80 DPGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLAlSESAREALLEALEAAKARGVTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 172 VLDIDYRPVLWGLAgkadgETRfvadqnvsQHVQKILPRFDLIVGTEEEFLIAGGSEDLLTALRTVR--ELTPATLVVKL 249
Cdd:cd01166 160 SFDLNYRPKLWSAE-----EAR--------EALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALalALGVKAVVVKL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 984659657 250 GPQGCTVIHGaiparleDGAIY-PGVRVEVLNVLGAGDAFMSGFLSGWINDASDERCSQLANACGGLVVSRHACA 323
Cdd:cd01166 227 GAEGALVYTG-------GGRVFvPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
13-332 |
1.28e-79 |
|
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: 254.42 E-value: 1.28e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 13 DLICLGRLGVDLYAQ----QVGARLEDVSSFAKYLGGSSANIAFGTARLGLKSAMLSRVGDDHMGRFLVESLAREGCDVS 88
Cdd:COG0524 1 DVLVIGEALVDLVARvdrlPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 89 GIKVDPERLTALVLLGLKDRETFPLVFYRenCADMALRAEDISEAFIASSKALLITGTHFSTDGVYKASLQALDYAARHN 168
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYR--GANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 169 VKRVLDIDYRPVLWGLAGKAdgetrfvadqnvsqhVQKILPRFDLIVGTEEEFLIAGGSEDLLTALRTVRELTPATLVVK 248
Cdd:COG0524 159 VPVSLDPNYRPALWEPAREL---------------LRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 249 LGPQGCTVIHGaiparlEDGAIYPGVRVEVLNVLGAGDAFMSGFLSGWINDASDERCSQLANACGGLVVSRHACAPAMPT 328
Cdd:COG0524 224 LGAEGALLYTG------GEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPT 297
|
....
gi 984659657 329 PAEL 332
Cdd:COG0524 298 REEV 301
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
15-319 |
3.50e-48 |
|
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: 170.89 E-value: 3.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 15 ICLGRLGVDLYAQQVGarleDVSSFAKYLGGSSANIAFGTARLGLKSAMLSRVGDDHMGRFLVESLAREGCDVSGIKVDP 94
Cdd:cd01167 3 VCFGEALIDFIPEGSG----APETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 95 ERLTALVLLGLKDR--ETFplVFYRENCADMALRAEDISEAFiaSSKALLITGTH-FSTDGVYKASLQALDYAARHNVKR 171
Cdd:cd01167 79 AAPTTLAFVTLDADgeRSF--EFYRGPAADLLLDTELNPDLL--SEADILHFGSIaLASEPSRSALLELLEAAKKAGVLI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 172 VLDIDYRPVLWglagkADGETRFvadqnvsQHVQKILPRFDLIVGTEEEFLIAGGSEDLLTALRTVRELTPATLVVKLGP 251
Cdd:cd01167 155 SFDPNLRPPLW-----RDEEEAR-------ERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRGA 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 984659657 252 QGCTVIHGaiparlEDGAIYPGVRVEVLNVLGAGDAFMSGFLSG-------WINDASDERCSQLANACGGLVVSR 319
Cdd:cd01167 223 DGALLYTK------GGVGEVPGIPVEVVDTTGAGDAFVAGLLAQllsrgllALDEDELAEALRFANAVGALTCTK 291
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
13-323 |
5.23e-46 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 164.82 E-value: 5.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 13 DLICLGRLGVDLYAQQVGARLED--VSSFAKYLGGSSANIAFGTARLGLKSAMLSRVGDDHMGRFLVESLAREGCDVSGI 90
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPGELvrVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 91 KVDPERLTALVL-LGLKDRETFpLVFYRENCADMALRAEDISEAFIASSKALLITGthFSTDGVYKASLQALDYAARHNV 169
Cdd:pfam00294 81 VIDEDTRTGTALiEVDGDGERT-IVFNRGAAADLTPEELEENEDLLENADLLYISG--SLPLGLPEATLEELIEAAKNGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 170 KRVLdiDYRPVLWGLAGKadgetrfvadqnvsqhVQKILPRFDLIVGTEEEFLIAGGS-----EDLLTALRTVRELTPAT 244
Cdd:pfam00294 158 TFDP--NLLDPLGAAREA----------------LLELLPLADLLKPNEEELEALTGAklddiEEALAALHKLLAKGIKT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 245 LVVKLGPQGCTVIHGaiparlEDGAIYPGVR-VEVLNVLGAGDAFMSGFLSGWINDASDERCSQLANACGGLVVSRHACA 323
Cdd:pfam00294 220 VIVTLGADGALVVEG------DGEVHVPAVPkVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
14-331 |
2.39e-34 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 133.21 E-value: 2.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 14 LICLGRLGVDLYAQQVGARLEDVSSFAKYLGGSSANIAFGTARLGLKSAMLSRVGDDHMGRFLVESLAREGCDVSGIKVD 93
Cdd:PLN02323 13 VVCFGEMLIDFVPTVSGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 94 PERLTALVLLGLKD---REtfpLVFYRENCADMALRAEDISEAFIASSKAL------LIT----GTHFSTDGVYKASLQA 160
Cdd:PLN02323 93 PGARTALAFVTLRSdgeRE---FMFYRNPSADMLLRESELDLDLIRKAKIFhygsisLITepcrSAHLAAMKIAKEAGAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 161 LDYaarhnvkrvlDIDYRPVLWGLAGKADGETRFVADQNvsqhvqkilprfDLIVGTEEE--FLIAGGSEDLLTALRTVR 238
Cdd:PLN02323 170 LSY----------DPNLRLPLWPSAEAAREGIMSIWDEA------------DIIKVSDEEveFLTGGDDPDDDTVVKLWH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 239 ElTPATLVVKLGPQGCT----VIHGAIparledgaiyPGVRVEVLNVLGAGDAFMSGFLSGWINDAS---DE----RCSQ 307
Cdd:PLN02323 228 P-NLKLLLVTEGEEGCRyytkDFKGRV----------EGFKVKAVDTTGAGDAFVGGLLSQLAKDLSlleDEerlrEALR 296
|
330 340
....*....|....*....|....
gi 984659657 308 LANACGGLVVSRHACAPAMPTPAE 331
Cdd:PLN02323 297 FANACGAITTTERGAIPALPTKEA 320
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
37-328 |
3.84e-29 |
|
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: 117.27 E-value: 3.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 37 SSFAKYLGGSSANIAFGTARLGLKSAMLSRVGDDHMGRFLVESLAREGCDVSGIKVDPERLT--ALVLLglkDREtfplv 114
Cdd:cd01174 29 SSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTgtAVITV---DES----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 115 fyRENC------ADMALRAEDISEA--FIASSKALLitgTHFSTDgvYKASLQALDYAARHNVKRVLD----IDYRPVLW 182
Cdd:cd01174 101 --GENRivvvpgANGELTPADVDAAleLIAAADVLL---LQLEIP--LETVLAALRAARRAGVTVILNpapaRPLPAELL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 183 GLAgkadgetrfvadqnvsqhvqkilprfDLIVGTEEEFLIAGG-----SEDLLTALRTVRELTPATLVVKLGPQGCTVI 257
Cdd:cd01174 174 ALV--------------------------DILVPNETEAALLTGievtdEEDAEKAARLLLAKGVKNVIVTLGAKGALLA 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 984659657 258 HGaiparlEDGAIYPGVRVEVLNVLGAGDAFMSGFLSGWINDASDERCSQLANACGGLVVSRHACAPAMPT 328
Cdd:cd01174 228 SG------GEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
34-333 |
1.41e-28 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 116.19 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 34 EDVSSFAKYLGGSSANIAFGTARLGLKSAMLSRVGDDHMGRFLVESLAREGCDVSGIKVDPERLTALVLLGLKDRETFPL 113
Cdd:PRK09434 18 EGENRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERSF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 114 VFYRENCADMALRAEDI-----SEAFIASSKALlitgthfSTDGVYKASLQALDyAARHNVKRVL-DIDYRPVLWglagK 187
Cdd:PRK09434 98 TFMVRPSADLFLQPQDLppfrqGEWLHLCSIAL-------SAEPSRSTTFEAMR-RIKAAGGFVSfDPNLREDLW----Q 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 188 ADGETRFVADQNVSQHvqkilprfDLIVGTEEEFLIAGGSEDLLTALRTVRELTPATLV-VKLGPQGCTVIHGaiparlE 266
Cdd:PRK09434 166 DEAELRECLRQALALA--------DVVKLSEEELCFLSGTSQLEDAIYALADRYPIALLlVTLGAEGVLVHTR------G 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 984659657 267 DGAIYPGVRVEVLNVLGAGDAFMSGFLSG------WINDASDERCSQLANACGGLVVSRHACAPAMPTPAELD 333
Cdd:PRK09434 232 QVQHFPAPSVDPVDTTGAGDAFVAGLLAGlsqaglWTDEAELAEIIAQAQACGALATTAKGAMTALPNRQELE 304
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
13-322 |
2.89e-25 |
|
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: 106.54 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 13 DLICLGRLGVDLYAQ-----------QVG-------ARLEDVSSFAKYL---GGSSANIAFGTARLGLKSAMLSRVGDDH 71
Cdd:cd01168 3 DVLGLGNALVDILAQvddafleklglKKGdmiladmEEQEELLAKLPVKyiaGGSAANTIRGAAALGGSAAFIGRVGDDK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 72 MGRFLVESLAREGCDVSgIKVDPERLTA--LVLLGLKDRETfpLVFYRENCADmaLRAEDISEAFIASSKALLITGTHFS 149
Cdd:cd01168 83 LGDFLLKDLRAAGVDTR-YQVQPDGPTGtcAVLVTPDAERT--MCTYLGAANE--LSPDDLDWSLLAKAKYLYLEGYLLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 150 TDGvyKASLQALDYAARHNVKRVLDIdyrpvlwglagkadgetrfvADQNVSQH----VQKILPRFDLIVGTEEEFLI-- 223
Cdd:cd01168 158 VPP--EAILLAAEHAKENGVKIALNL--------------------SAPFIVQRfkeaLLELLPYVDILFGNEEEAEAla 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 224 -AGGSEDLLTALRTVRELTPaTLVVKLGPQGCTVIHGA----IPARLEDgaiypgvrvEVLNVLGAGDAFMSGFLSGWIN 298
Cdd:cd01168 216 eAETTDDLEAALKLLALRCR-IVVITQGAKGAVVVEGGevypVPAIPVE---------KIVDTNGAGDAFAGGFLYGLVQ 285
|
330 340
....*....|....*....|....
gi 984659657 299 DASDERCSQLANACGGLVVSRHAC 322
Cdd:cd01168 286 GEPLEECIRLGSYAAAEVIQQLGP 309
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
13-322 |
8.97e-24 |
|
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: 101.62 E-value: 8.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 13 DLICLGRLGVDLYAQQVGARLEDVSSFAK----YLGGSSANIAFGTARLGLKSAMLSRVGDDHMGRFLVESLAREGCDVS 88
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKdlrrEFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 89 GIKVDPERLTAL-VLLGLKDRETfplVFYRENCADMALRAEDISEAFiasskallitgthFSTDGVYKASLQALDYAARH 167
Cdd:cd01942 81 HVRVVDEDSTGVaFILTDGDDNQ---IAYFYPGAMDELEPNDEADPD-------------GLADIVHLSSGPGLIELARE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 168 NVKRVLDIDYRP--VLWGLAGKAdgetrfvadqnvsqhVQKILPRFDLIVGTEEEFLIAggseDLLTALRTVRE-LTPAT 244
Cdd:cd01942 145 LAAGGITVSFDPgqELPRLSGEE---------------LEEILERADILFVNDYEAELL----KERTGLSEAELaSGVRV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 245 LVVKLGPQGCTVIHG----AIPARLEdgaiypgvrVEVLNVLGAGDAFMSGFLSGWINDASDERCSQLANACGGLVVSRH 320
Cdd:cd01942 206 VVVTLGPKGAIVFEDgeevEVPAVPA---------VKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERR 276
|
..
gi 984659657 321 AC 322
Cdd:cd01942 277 GA 278
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
14-320 |
4.23e-22 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 96.34 E-value: 4.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 14 LICLGRLGVDLYaQQVGArledvssfaKYLGGSSANIAFGTARLGLKSAMLSRVGDDHMGRFLVESLAREGCDVSGIKVD 93
Cdd:PRK09813 3 LATIGDNCVDIY-PQLGK---------AFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 94 PERlTALVLLGLKDRETfplVF--YRENC-ADMALRAEDIseAFIASSKaLLITGTHFSTDGvykaslqalDYAARHNVK 170
Cdd:PRK09813 73 HGV-TAQTQVELHDNDR---VFgdYTEGVmADFALSEEDY--AWLAQYD-IVHAAIWGHAED---------AFPQLHAAG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 171 RVLDIDYrpvlwglagkadgetrfvADQNVSQHVQKILPRFDLIVGTEEefliaGGSEDLLTALRTVRELTPATLVVKLG 250
Cdd:PRK09813 137 KLTAFDF------------------SDKWDSPLWQTLVPHLDYAFASAP-----QEDEFLRLKMKAIVARGAGVVIVTLG 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 251 PQGCTVIHGaipARLEDGAIYPgvrVEVLNVLGAGDAFMSGFLSGWINDASDERCSQLANACGGLVVSRH 320
Cdd:PRK09813 194 ENGSIAWDG---AQFWRQAPEP---VTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYH 257
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
14-312 |
2.87e-18 |
|
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: 85.10 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 14 LICLGRLGVDLYAQQVGArledvssfakYLGGSSANIAFGTARLGLKSAMLSRVGDDHMGRFLVESLAREGCDVSGIKVD 93
Cdd:cd01940 2 LAAIGDNVVDKYLHLGKM----------YPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 94 P-ERLTALVLLGLKDREtfpLVFYREN-CADMALRAEDIseAFIASSKaLLITGTHfSTDGVYKASLQALDYAarhnvkr 171
Cdd:cd01940 72 EgENAVADVELVDGDRI---FGLSNKGgVAREHPFEADL--EYLSQFD-LVHTGIY-SHEGHLEKALQALVGA------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 172 vldidyrpvlwGLAGKADGETRFVADqnvsqHVQKILPRFDLIVGTEEEFliagGSEDLLTALRTVRELTPATLVVKLGP 251
Cdd:cd01940 138 -----------GALISFDFSDRWDDD-----YLQLVCPYVDFAFFSASDL----SDEEVKAKLKEAVSRGAKLVIVTRGE 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 984659657 252 QGCTVIHGAipaRLEDGAIYPgvrVEVLNVLGAGDAFMSGFLSGWI-NDASDERCSQLANAC 312
Cdd:cd01940 198 DGAIAYDGA---VFYSVAPRP---VEVVDTLGAGDSFIAGFLLSLLaGGTAIAEAMRQGAQF 253
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
36-293 |
3.96e-17 |
|
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: 81.96 E-value: 3.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 36 VSSFAKYLGGSSANIAFGTARLGLKSAMLSRVGDDHMGRFLVESLAREGCDVSGIKVDPERLTAL--VLLGLKDRETfpl 113
Cdd:cd01945 28 ATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPIssITDITGDRAT--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 114 vfYRENCADMALRAEDISEAFIASSKALLITGtHFSTdgvykASLQALDYAARHNVKRVLDIDyrpvlwGLAGKADGEtr 193
Cdd:cd01945 105 --ISITAIDTQAAPDSLPDAILGGADAVLVDG-RQPE-----AALHLAQEARARGIPIPLDLD------GGGLRVLEE-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 194 fvadqnvsqhvqkILPRFDLIVGTEEEFLIAGGSEDLLtALRTVRELTPATLVVKLGPQGCTVIHgaiparlEDGA--IY 271
Cdd:cd01945 169 -------------LLPLADHAICSENFLRPNTGSADDE-ALELLASLGIPFVAVTLGEAGCLWLE-------RDGElfHV 227
|
250 260
....*....|....*....|..
gi 984659657 272 PGVRVEVLNVLGAGDAFMSGFL 293
Cdd:cd01945 228 PAFPVEVVDTTGAGDVFHGAFA 249
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
36-335 |
1.55e-15 |
|
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: 77.62 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 36 VSSFAKYLGGSSANIAFGTARLGLKSAMLSRVGDDHmGRFLVESLAREGCDVSGIKVDPERLTALVLLGLKDRETfplvf 115
Cdd:TIGR03168 27 VAAVRKDAGGKGINVARVLARLGAEVVATGFLGGFT-GEFIEALLAEEGIKNDFVEVKGETRINVKIKESSGEET----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 116 yRENCADMALRAEDIsEAFIASSKALLITGTH--FS-------TDGVYKaslQALDYAARHNVKRVLDIDYRPVLWGLAG 186
Cdd:TIGR03168 101 -ELNEPGPEISEEEL-EQLLEKLRELLASGDIvvISgslppgvPPDFYA---QLIAIARKKGAKVILDTSGEALREALAA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 187 KADgetrFVA--DQNVSQHvqkilprFDLIVGTEEefliaggseDLLTALRTVRELTPATLVVKLGPQGCTVIHGaipar 264
Cdd:TIGR03168 176 KPF----LIKpnHEELEEL-------FGRELKTLE---------EIIEAARELLDRGAENVLVSLGADGALLVTK----- 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 984659657 265 leDGAIYPGV-RVEVLNVLGAGDAFMSGFLSGWINDASDERCSQLANACGGLVVSRHacAPAMPTPAELDYL 335
Cdd:TIGR03168 231 --EGALKATPpKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSP--GTGLPDPEDVEEL 298
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
38-332 |
1.55e-15 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 78.24 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 38 SFAKYLGGSSANIAFGTARLGLKSAMLSRVGDDHMGRFLVESLAREGCDVSGIKVDPERLTALVLLgLKDRETfplvfyR 117
Cdd:PTZ00292 46 SFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTENSSTGLAMI-FVDTKT------G 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 118 ENC------ADMALRAEDISEAF--IASSKALLITGTHFSTDgvykASLQALDYAARHNVKRVLDIDYRPvlwglagkAD 189
Cdd:PTZ00292 119 NNEiviipgANNALTPQMVDAQTdnIQNICKYLICQNEIPLE----TTLDALKEAKERGCYTVFNPAPAP--------KL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 190 GETRFVADqnvsqhvqkILPRFDLIVGTEEEFLIAGGSE--DLLTALRTVRE---LTPATLVVKLGPQGCTVIHGaipar 264
Cdd:PTZ00292 187 AEVEIIKP---------FLKYVSLFCVNEVEAALITGMEvtDTESAFKASKElqqLGVENVIITLGANGCLIVEK----- 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 984659657 265 lEDGAIY-PGVRVEVLNVLGAGDAFMSGFLSGWINDASDERCSQLANACGGLVVSRHACAPAMPTPAEL 332
Cdd:PTZ00292 253 -ENEPVHvPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSEL 320
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
44-318 |
4.32e-15 |
|
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: 76.20 E-value: 4.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 44 GGSSANIAFGTARLGLKSAMLSRVGDDHMGRFLVESLAREGCDVSGIkVDPERLTALVLLGL-KDREtfpLVFyreNCAD 122
Cdd:cd01941 35 GGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRGI-VFEGRSTASYTAILdKDGD---LVV---ALAD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 123 MALrAEDISEAFIASSKALLITGTHFSTDG-VYKASLQAL-DYAARHNVKRVLDIdyrpvlwglagkadgetrfvADQNV 200
Cdd:cd01941 108 MDI-YELLTPDFLRKIREALKEAKPIVVDAnLPEEALEYLlALAAKHGVPVAFEP--------------------TSAPK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 201 SQHVQKILPRFDLIVGTEEEF-----LIAGGSEDLLTALRTVRELTPATLVVKLGPQGCTVIHGAipaRLEDGAIYP-GV 274
Cdd:cd01941 167 LKKLFYLLHAIDLLTPNRAELealagALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSRE---GGVETKLFPaPQ 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 984659657 275 RVEVLNVLGAGDAFMSGFLSGWINDASDERCSQLANACGGLVVS 318
Cdd:cd01941 244 PETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTLE 287
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
41-332 |
9.28e-15 |
|
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: 75.29 E-value: 9.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 41 KYLGGSsANIAFGTARLGLKSAMLSRVGDDHMGRFLVESLAREGCDVSGIkVDPERLTA-----------LVLLglkDRE 109
Cdd:cd01172 37 IRLGGA-ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGI-VDEGRPTTtktrviarnqqLLRV---DRE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 110 TFPLVfyRENCADMALRAediSEAFIASSKALLIT--GTHFSTDGVykasLQALDYAARHNVKRVLdIDyrPvlwglagK 187
Cdd:cd01172 112 DDSPL--SAEEEQRLIER---IAERLPEADVVILSdyGKGVLTPRV----IEALIAAARELGIPVL-VD--P-------K 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 188 ADGETRFvadqnvsqhvqkilPRFDLIVGTEEEFLIAGG-----SEDLLTALRTVRELTPA-TLVVKLGPQGCTVIHGai 261
Cdd:cd01172 173 GRDYSKY--------------RGATLLTPNEKEAREALGdeindDDELEAAGEKLLELLNLeALLVTLGEEGMTLFER-- 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 984659657 262 parleDGAIY--PGVRVEVLNVLGAGDAFMSGFLSGWINDASDERCSQLANACGGLVVSRHACAPAmpTPAEL 332
Cdd:cd01172 237 -----DGEVQhiPALAKEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGTAPV--TPKEL 302
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
36-320 |
1.37e-14 |
|
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: 74.38 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 36 VSSFAKYLGGSSANIAFGTARLGLKSAMLSRVGDDHMGRFLVESLAREG-CDVSGIKVDPERLTALVLLGLKDRETFplv 114
Cdd:cd01947 28 SSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGdKHTVAWRDKPTRKTLSFIDPNGERTIT--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 115 fyrencadmalraeDISEAFIASSKALLITGThfstDGVYKASLQALDYAARHNVKRVLdidyrpVLWGLAGKAdgetRF 194
Cdd:cd01947 105 --------------VPGERLEDDLKWPILDEG----DGVFITAAAVDKEAIRKCRETKL------VILQVTPRV----RV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 195 VADQNVSQHvqkilprFDLIVGTEEEFLIAGGSEDLltALRTVReltpaTLVVKLGPQGCTVIHGAiparlEDGAIyPGV 274
Cdd:cd01947 157 DELNQALIP-------LDILIGSRLDPGELVVAEKI--AGPFPR-----YLIVTEGELGAILYPGG-----RYNHV-PAK 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 984659657 275 RVEVLNVLGAGDAFMSGFLSGWINDASDERCSQLANACGGLVVSRH 320
Cdd:cd01947 217 KAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHF 262
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
36-320 |
2.65e-13 |
|
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: 70.64 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 36 VSSFAKYLGGSSANIAFGTARLGLKSAMLSRVGDDhMGRFLVESLAREGCDVSGIKVDPERLTALVLLGLKDRETfplvf 115
Cdd:cd01164 28 VSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVEVAGETRINVKIKEEDGTET----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 116 yRENCADMALRAEDIsEAFIASSKALLITGTHFS---------TDGVYKaslQALDYAARHNVKRVLDIDYRPVLWGLAG 186
Cdd:cd01164 102 -EINEPGPEISEEEL-EALLEKLKALLKKGDIVVlsgslppgvPADFYA---ELVRLAREKGARVILDTSGEALLAALAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 187 KADgetrfvadqnvsqhvqkilprfdLIVGTEEEF-----LIAGGSEDLLTALRTVRELTPATLVVKLGPQGCTVIHGai 261
Cdd:cd01164 177 KPF-----------------------LIKPNREELeelfgRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTK-- 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 262 parleDGAIY-PGVRVEVLNVLGAGDAFMSGFLSGWINDASDERCSQLANACGGLVVSRH 320
Cdd:cd01164 232 -----DGVYRaSPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSP 286
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
7-314 |
4.23e-13 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 71.79 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 7 ASGRQLDLICLGRLGVDL-----------------YAQQVGARLEDVSSFAkyLGGSsANIAFGTARLGLKSAMLSRVGD 69
Cdd:PLN02341 68 AAGKEIDVATLGNLCVDIvlpvpelpppsreerkaYMEELAASPPDKKSWE--AGGN-CNFAIAAARLGLRCSTIGHVGD 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 70 DHMGRFLVESLAREGCDVSGIKVDP----------ERLTALVLLGLKDRETF---------PLVfyrencADMALRAEDI 130
Cdd:PLN02341 145 EIYGKFLLDVLAEEGISVVGLIEGTdagdsssasyETLLCWVLVDPLQRHGFcsradfgpePAF------SWISKLSAEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 131 SEAfIASSKALLITGTHF---STDGVykasLQALDYAARHNVKRVLDidyrPvlwGLAGKAdgetrFVADQNVSQHVQKI 207
Cdd:PLN02341 219 KMA-IRQSKALFCNGYVFdelSPSAI----ASAVDYAIDVGTAVFFD----P---GPRGKS-----LLVGTPDERRALEH 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 208 LPRF-DLIVGTEEEfliaggsEDLLTALRTVRELTPATL---------VVKLGPQgctvihGAIPARLEDGAIYPGVRVE 277
Cdd:PLN02341 282 LLRMsDVLLLTSEE-------AEALTGIRNPILAGQELLrpgirtkwvVVKMGSK------GSILVTRSSVSCAPAFKVN 348
|
330 340 350
....*....|....*....|....*....|....*..
gi 984659657 278 VLNVLGAGDAFMSGFLSGWINDASDERCSQLANACGG 314
Cdd:PLN02341 349 VVDTVGCGDSFAAAIALGYIHNLPLVNTLTLANAVGA 385
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
36-337 |
8.23e-12 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 66.70 E-value: 8.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 36 VSSFAKYLGGSSANIAFgtarLGlksamlsrvGDDhmGRFLVESLAREGCDVSGIKVDPE-RlTALVLLGLKDRETFPLV 114
Cdd:COG1105 41 VARVLKALGVDVTALGF----LG---------GFT--GEFIEELLDEEGIPTDFVPIEGEtR-INIKIVDPSDGTETEIN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 115 FYRENCADMALRA-EDISEAFIASSKALLITGthfS-----TDGVYKaslQALDYAARHNVKRVLDIDYRPVLWGLAGKA 188
Cdd:COG1105 105 EPGPEISEEELEAlLERLEELLKEGDWVVLSG---SlppgvPPDFYA---ELIRLARARGAKVVLDTSGEALKAALEAGP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 189 DgetrfvadqnvsqhvqkilprfdLIVGTEEEF-LIAGGS----EDLLTALRTVRELTPATLVVKLGPQGCTVIHgaipa 263
Cdd:COG1105 179 D-----------------------LIKPNLEELeELLGRPletlEDIIAAARELLERGAENVVVSLGADGALLVT----- 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 984659657 264 rlEDGAIY-PGVRVEVLNVLGAGDAFMSGFLSGWINDASDERCSQLANACGGLVVSRHacAPAMPTPAELDYLFN 337
Cdd:COG1105 231 --EDGVYRaKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSP--GTGLPDREDVEELLA 301
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
32-335 |
1.11e-11 |
|
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: 66.07 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 32 RLEDVSSFAkylGGSSANIAFGTARLGLKSAMLSRVGDDHmGRFLVESLAREGCDVSGIKVDPERLTALVLLGLKDRETf 111
Cdd:TIGR03828 26 RVESTRIDA---GGKGINVSRVLKNLGVDVVALGFLGGFT-GDFIEALLREEGIKTDFVRVPGETRINVKIKEPSGTET- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 112 plvfyRENCADMALRAEDIsEAFIASSKALLITGTHFSTDGVYKASLQALDY------AARHNVKRVLDIDYRPVLWGLA 185
Cdd:TIGR03828 101 -----KLNGPGPEISEEEL-EALLEKLRAQLAEGDWLVLSGSLPPGVPPDFYaelialAREKGAKVILDTSGEALRDGLK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 186 GKAdgetrFVADQNVSQhvqkilprFDLIVGTEEEfliagGSEDLLTALRTVRELTPATLVVKLGPQGCTVIHGaiparl 265
Cdd:TIGR03828 175 AKP-----FLIKPNDEE--------LEELFGRELK-----TLEEIIEAARELLDLGAENVLISLGADGALLVTK------ 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 984659657 266 eDGAIYP-GVRVEVLNVLGAGDAFMSGFLSGWINDASDERCSQLANACGGLVVSRHacAPAMPTPAELDYL 335
Cdd:TIGR03828 231 -EGALFAqPPKGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSE--GTGLPDPEDIEEL 298
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
36-320 |
2.15e-10 |
|
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: 62.05 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 36 VSSFAKYLGGSSANIAFGTARLGLKSAMLSRVGDDHMGRFLVESLAREGCDVSGIKVDPERLTALVLLGLKDRE-TFpLV 114
Cdd:cd01944 27 EAKSKSYVIGGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEILLPPRGGDDGGCLVALVEPDGErSF-IS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 115 FYRencADMALRAEDISEAFIASSKALLITGTHFSTDGVYKASLqaLDYAARHNVKRVLDIDYRPVLwglagkadgetrf 194
Cdd:cd01944 106 ISG---AEQDWSTEWFATLTVAPYDYVYLSGYTLASENASKVIL--LEWLEALPAGTTLVFDPGPRI------------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 195 vadQNVSQH-VQKILPRFDLIVGTEEEFLIA---GGSEDLLTALRtVRELTPATLVVKLGPQGCTVihgaipaRLEDGA- 269
Cdd:cd01944 168 ---SDIPDTiLQALMAKRPIWSCNREEAAIFaerGDPAAEASALR-IYAKTAAPVVVRLGSNGAWI-------RLPDGNt 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 984659657 270 -IYPGVRVEVLNVLGAGDAFMSGFLSGWINDASDERCSQLANACGGLVVSRH 320
Cdd:cd01944 237 hIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRS 288
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
132-297 |
2.47e-10 |
|
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: 60.19 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 132 EAFIASSKALLITGTHFSTDgvykASLQALDYAARHNVKRVLDIDYRPVLWGLAGKAdgetrfvadqnvsqhvqKILPRF 211
Cdd:cd00287 52 SVTLVGADAVVISGLSPAPE----AVLDALEEARRRGVPVVLDPGPRAVRLDGEELE-----------------KLLPGV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 212 DLIVGTEEEFLIAGGSEDLLT-----ALRTVRELTPATLVVKLGPQGCTV-----IHGAIPArledgaiypgVRVEVLNV 281
Cdd:cd00287 111 DILTPNEEEAEALTGRRDLEVkeaaeAAALLLSKGPKVVIVTLGEKGAIVatrggTEVHVPA----------FPVKVVDT 180
|
170
....*....|....*.
gi 984659657 282 LGAGDAFMSGFLSGWI 297
Cdd:cd00287 181 TGAGDAFLAALAAGLA 196
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
34-317 |
3.27e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 59.03 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 34 EDVSSFAKYLGGSSANIAFG-TARLGLKSAMLSRVGDDHMGRFLVESLAREGCDVSGIKVDPERLTALVLL--GLKDRET 110
Cdd:PLN02379 76 DDLSPIKTMAGGSVANTIRGlSAGFGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSRLRAKKGPTAQCVCLvdALGNRTM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 111 FPlvfyrenCADMALR--AEDISEAFIASSKALLITGTHFSTDGVykasLQALDYAARHNVKRVLDI-------DYRPVL 181
Cdd:PLN02379 156 RP-------CLSSAVKlqADELTKEDFKGSKWLVLRYGFYNLEVI----EAAIRLAKQEGLSVSLDLasfemvrNFRSPL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 182 WGLAgkadgETRFVadqnvsqhvqkilprfDLIVGTEEEF--LIAGGSE-DLLTALRTVRELTPATlVVKLGPQGCTVIH 258
Cdd:PLN02379 225 LQLL-----ESGKI----------------DLCFANEDEAreLLRGEQEsDPEAALEFLAKYCNWA-VVTLGSKGCIARH 282
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 984659657 259 GA----IPARLEDGAIypgvrvevlNVLGAGDAFMSGFLSGWINDASDERCSQLANACGGLVV 317
Cdd:PLN02379 283 GKevvrVPAIGETNAV---------DATGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVV 336
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
44-333 |
4.21e-09 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 58.34 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 44 GGSSANIAFGTARLGLKSAMLSRVGDDHMGRFLVESLAREGCDVSGIKVDPERLTALVLLGLKDREtfplvfyrENC--- 120
Cdd:PRK11142 39 GGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEG--------ENSigi 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 121 ---ADMALRAEDI--SEAFIASSKALLI---TgthfSTDGVykasLQALDYAARHNVKRVLDidyrPvlwglagkadGET 192
Cdd:PRK11142 111 hagANAALTPALVeaHRELIANADALLMqleT----PLETV----LAAAKIAKQHGTKVILN----P----------APA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 193 RFVADQnvsqhvqkILPRFDLIV--GTEEEFLIAGGSEDLLTALRTVREL---TPATLVVKLGPQGCTVihgaipARLED 267
Cdd:PRK11142 169 RELPDE--------LLALVDIITpnETEAEKLTGIRVEDDDDAAKAAQVLhqkGIETVLITLGSRGVWL------SENGE 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 984659657 268 GAIYPGVRVEVLNVLGAGDAFMSGFLSGWINDASDERCSQLANACGGLVVSRHACAPAMPTPAELD 333
Cdd:PRK11142 235 GQRVPGFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEID 300
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
206-327 |
2.26e-06 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 50.03 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 206 KILPRFDLIVGTEEEFLIAG-----GSEDLL-TALRTVREL----TPATLVVklGPQGctvIHGAIPARlEDGAIYPGVR 275
Cdd:PTZ00247 210 QVLPYVDILFGNEEEAKTFAkamkwDTEDLKeIAARIAMLPkysgTRPRLVV--FTQG---PEPTLIAT-KDGVTSVPVP 283
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 984659657 276 V----EVLNVLGAGDAFMSGFLSGWINDASDERCSQLANACGGLVVSRHACA-PAMP 327
Cdd:PTZ00247 284 PldqeKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCTyPEKP 340
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
35-193 |
1.30e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 47.98 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 35 DVSSFAKYLGGSSANIAFGTARLGLKSAMLSRVGDDHMGRFLVESLAREGCDVSGIKVDPERLTALVLLGLKDRETFPLV 114
Cdd:PLN02543 163 DPPEFARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACSRMKIKFRDGGKMV 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 115 FYR-ENCADMALRAEDISEAFIASSKALlitgtHFSTDGVYKASLQ-----ALDYAARHNVKRVLDIDYRPVLWglagKA 188
Cdd:PLN02543 243 AETvKEAAEDSLLASELNLAVLKEARMF-----HFNSEVLTSPSMQstlfrAIELSKKFGGLIFFDLNLPLPLW----RS 313
|
....*
gi 984659657 189 DGETR 193
Cdd:PLN02543 314 RDETR 318
|
|
| PLN02967 |
PLN02967 |
kinase |
11-139 |
2.70e-04 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 43.88 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 11 QLDLICLGRLGVDLYAQQVGARLEDV----SSFAKYLGGSSANIAFGTARLGLKSAMLSRVGDDHMGRFLVESLAREGCD 86
Cdd:PLN02967 206 QHAFVPSGRPANRLLDYEIHERMKDAfwapEKFVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQ 285
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 984659657 87 VSGIKVDPERLTALVLLGLKDRETFPLVFYREnCADMALRAEDISEAFIASSK 139
Cdd:PLN02967 286 TRSVCIDGKRATAVSTMKIAKRGRLKTTCVKP-CAEDSLSKSEINIDVLKEAK 337
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
44-295 |
4.67e-04 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 42.39 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 44 GGSSANIAFGTARLGLKSAMLSRVGDDHMGRFLVEslaregcDVSGIKVdperltalVLLGLKDRETFPLvFYRENCADM 123
Cdd:cd01937 24 GGPATYASLTLSRLGLTVKLVTKVGRDYPDKWSDL-------FDNGIEV--------ISLLSTETTTFEL-NYTNEGRTR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 124 ALRAEDISEAFIASSKALLitgthfSTDGVYKASLQaldyaarHNVKRVLDIDYRPVLWGLAGkadgetrFVADQNVSQH 203
Cdd:cd01937 88 TLLAKCAAIPDTESPLSTI------TAEIVILGPVP-------EEISPSLFRKFAFISLDAQG-------FLRRANQEKL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 204 VQ-KILPRFDLIVGTEEEfliAGGSEDLLTALRTVRELTPATLVVKLGPQGCTVIHGaiparledGAIY--PGVRVEVLN 280
Cdd:cd01937 148 IKcVILKLHDVLKLSRVE---AEVISTPTELARLIKETGVKEIIVTDGEEGGYIFDG--------NGKYtiPASKKDVVD 216
|
250
....*....|....*
gi 984659657 281 VLGAGDAFMSGFLSG 295
Cdd:cd01937 217 PTGAGDVFLAAFLYS 231
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
206-312 |
1.53e-03 |
|
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238921 [Multi-domain] Cd Length: 277 Bit Score: 40.91 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 206 KILPRFDLIVGTEEEFLIAGGSEDLLTALRTVRELTPATLVVKLGPQGCTVIHG----AIPArledgaiYPgvRVEVLNV 281
Cdd:cd01946 159 KVLAKVDVVIINDGEARQLTGAANLVKAARLILAMGPKALIIKRGEYGALLFTDdgyfAAPA-------YP--LESVFDP 229
|
90 100 110
....*....|....*....|....*....|.
gi 984659657 282 LGAGDAFMSGFLsGWINDASDERCSQLANAC 312
Cdd:cd01946 230 TGAGDTFAGGFI-GYLASQKDTSEANMRRAI 259
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
221-318 |
1.97e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 40.95 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 221 FLIAGGSEDLLTALRTVRELTpaTLVVKLGPQGCTVIHG----AIPArledgaiYPGVRVEVLnvlGAGDAFMSGFLSGW 296
Cdd:PLN02630 184 FLKASSEEALFIDVEEVRQKC--CVIVTNGKKGCRIYWKdgemRVPP-------FPAIQVDPT---GAGDSFLGGFVAGL 251
|
90 100
....*....|....*....|..
gi 984659657 297 INDASDERCSQLANACGGLVVS 318
Cdd:PLN02630 252 VQGLAVPDAALLGNYFGSLAVE 273
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
123-335 |
2.00e-03 |
|
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 441841 [Multi-domain] Cd Length: 272 Bit Score: 40.52 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 123 MALRAEDISEaFIASSKALlitGTHFSTDGVY----------KASLQALDY--AARHNVKRVLDidyrPVLwglagkAD- 189
Cdd:COG2240 52 RDLPTDDIAD-ILDGWKEL---GVLLEFDAVLsgylgsaeqgDIIADFVARvkAANPDALYLCD----PVM------GDn 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 190 GETRFVADQNVSQHVQKILPRFDLIV--GTEEEFLiAG----GSEDLLTALRTVRELTPATLVVKlgpqGCTViHGAIPA 263
Cdd:COG2240 118 GKGYYVFPGIAEFIMRRLVPLADIITpnLTELALL-TGrpyeTLEEALAAARALLALGPKIVVVT----SVPL-DDTPAD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984659657 264 RLE------DGAIYpgVRVEVLNVL--GAGDAFMSGFLSGWINDASDERCSQLANA--CGGLVVSRHACAPAMPTPAELD 333
Cdd:COG2240 192 KIGnlavtaDGAWL--VETPLLPFSpnGTGDLFAALLLAHLLRGKSLEEALERAAAfvYEVLERTAAAGSDELLLEAALD 269
|
..
gi 984659657 334 YL 335
Cdd:COG2240 270 EL 271
|
|
| |
