|
Name |
Accession |
Description |
Interval |
E-value |
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
3-312 |
8.30e-90 |
|
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: 270.60 E-value: 8.30e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 3 KLLLVGEPLIRVSPNQFQPLTNACEAQLFFGGSEVNIARTLGGFGLEARLFTALPDNPVGHAFHQFLKQSGVDMSL-TAW 81
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHvRVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 82 QGHRVGLYYLENGFGcRASQVYYDRCGSSFSALDKDSLDLAAiFEGISHFHFSGISLALGKKTQDLIEILAREAKKRDIC 161
Cdd:cd01166 81 PGRPTGLYFLEIGAG-GERRVLYYRAGSAASRLTPEDLDEAA-LAGADHLHLSGITLALSESAREALLEALEAAKARGVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 162 ISFDLNFRSSMIAVADAKRLFSHFAQYADIIFGMEpllldsDDFDMFDRKKADTTMIRErlaglYQRYQLQAIYHTERsN 241
Cdd:cd01166 159 VSFDLNYRPKLWSAEEAREALEELLPYVDIVLPSE------EEAEALLGDEDPTDAAER-----ALALALGVKAVVVK-L 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1731567761 242 DAQGsnhfkAYAYD-GQFYESCEVTTPVLQRVGSGDAFVAGLLYQLLEGNEKQRNLDFAVATASLKCTVVED 312
Cdd:cd01166 227 GAEG-----ALVYTgGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGD 293
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
3-313 |
2.01e-40 |
|
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: 143.49 E-value: 2.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 3 KLLLVGEPLIRVSPN-----QFQPLTNACEAQLFFGGSEVNIARTLGGFGLEARLFTALPDNPVGHAFHQFLKQSGVDMS 77
Cdd:COG0524 1 DVLVIGEALVDLVARvdrlpKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 78 LTAW-QGHRVGLYYLENGFGCRASQVYYdrcGSSFSALDKDSLDlAAIFEGISHFHFSGISLAlGKKTQDLIEILAREAK 156
Cdd:COG0524 81 GVRRdPGAPTGLAFILVDPDGERTIVFY---RGANAELTPEDLD-EALLAGADILHLGGITLA-SEPPREALLAALEAAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 157 KRDICISFDLNFRSSMIavADAKRLFSHFAQYADIIFGMEP---LLLDSDDFdmfdrkkadttmirERLAGLYQRYQLQA 233
Cdd:COG0524 156 AAGVPVSLDPNYRPALW--EPARELLRELLALVDILFPNEEeaeLLTGETDP--------------EEAAAALLARGVKL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 234 IYHTERsndAQGSnhfkAYAYDGQFYESCEVTTPVLQRVGSGDAFVAGLLYQLLEGNEKQRNLDFAVATASLKCTVVEDQ 313
Cdd:COG0524 220 VVVTLG---AEGA----LLYTGGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQ 292
|
|
| KDG_KDGal_kin_Halo |
NF041332 |
bifunctional 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase; |
1-333 |
3.88e-40 |
|
bifunctional 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase;
Pssm-ID: 469229 [Multi-domain] Cd Length: 318 Bit Score: 143.13 E-value: 3.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 1 MSKLLLVGEPLIRVSPNQFQPLTNACEAQLFFGGSEVNIARTLGGFGLEARLFTALPDNPVGHAFHQFLKQSGVDMSLTA 80
Cdd:NF041332 1 MTDLVTFGETMLRLSPPGGERLETADELDVRAGGAESNVAVAAARLGADATWLSKLPDSPLGRRVVGELRSHGVDTDVVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 81 WQGHRVGLYYLENGFGCRASQVYYDRCGSSFSALDKDSLDLAAIfEGISHFHFSGISLALGKKTQDLIEILAREAKKRDI 160
Cdd:NF041332 81 DDEGRQGTYYLEHGGEPRGTNVIYDRADAAVTTATPEELPLDRI-RDAEVFYTSGITPALSETLAETTAALLEAAQEAGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 161 CISFDLNFRSSMIAVADAKRLFSHFAQYADIIFGMEpllldSDDFDMFDRkKADTTMIRERLAglyQRYQLQAIYHTers 240
Cdd:NF041332 160 TTAFDLNYRSKLWSPEEARETLESLFPAVDVLVVAE-----RDARTVLGR-DGDAEEIAHGLA---SEYDFETVVVT--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 241 ndaQGSNHFKAYAyDGQFYESCEVTTPVLQRVGSGDAFVAGLLYQLLEGNEKQRNLDFAVATASLKCTVVEDQLYHSVQQ 320
Cdd:NF041332 228 ---RGEEGALALH-DGEVHEQPAYEADTVDPIGTGDAFVGGFLARRLAGGDVPTALEYGAATAALKRTIPGDVAVVTPEE 303
|
330
....*....|....*
gi 1731567761 321 VEAVLANQR--DIQR 333
Cdd:NF041332 304 VEAVVEDGGgdGISR 318
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
3-314 |
9.54e-22 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 93.18 E-value: 9.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 3 KLLLVGEPLIRVSPNQFQPLTNACEAQ---LFFGGSEVNIARTLGGFGLEARLFTALPDNPVGHAFHQFLKQSGVDMSLT 79
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPGELVRVStveKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 80 AWQGH-RVGLYYLENGFGCRASQVYYDrcGSSFSALDKDSLDLAAIFEGISHFHFSGI-SLALGKKTQDLIEILAREAKK 157
Cdd:pfam00294 81 VIDEDtRTGTALIEVDGDGERTIVFNR--GAAADLTPEELEENEDLLENADLLYISGSlPLGLPEATLEELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 158 rdicisFDLNFRSSMIAVADAkrlFSHFAQYADIIFGMEpllldsDDFD-MFDRKKADTTMIRERLAGLYQRYQLQAIYh 236
Cdd:pfam00294 159 ------FDPNLLDPLGAAREA---LLELLPLADLLKPNE------EELEaLTGAKLDDIEEALAALHKLLAKGIKTVIV- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 237 terSNDAQGsnhfkAYAYDGQFyESCEVTTP---VLQRVGSGDAFVAGLLYQLLEGNEKQRNLDFAVATASLKCTVVEDQ 313
Cdd:pfam00294 223 ---TLGADG-----ALVVEGDG-EVHVPAVPkvkVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
|
.
gi 1731567761 314 L 314
Cdd:pfam00294 294 T 294
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
31-305 |
2.01e-12 |
|
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: 66.85 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 31 FFGGSEVNIARTLGGFGLEARLFTALPDNPVGHAFHQFLKQSGVDMS-LTAWQGHRVGLYYLENGFGCRASQVYYdRCGS 109
Cdd:TIGR04382 32 YLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTShVVTDPGRRTSLVFLEIKPPDEFPLLFY-RENA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 110 SFSALDKDSLDLAAIFEGiSHFHFSGISLAlGKKTQDLIEILAREAKKRDICISFDLNFRS-SMIAVADAKRLFSHFAQY 188
Cdd:TIGR04382 111 ADLALTPDDVDEDYIASA-RALLVSGTALS-QEPSREAVLKALEYARAAGVRVVLDIDYRPyLWKSPEEAGIYLRLVLPL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 189 ADIIFGMEpllldsDDFDMFDRKKADttmirERLAGLYQRY--QLQAIYHTERsndaqGSNhfkAYAYDGQFYESCEVTT 266
Cdd:TIGR04382 189 VDVIIGTR------EEFDIAGGEGDD-----EAAARALLDAgvEILVVKRGPE-----GSL---VYTGDGEGVEVPGFPV 249
|
250 260 270
....*....|....*....|....*....|....*....
gi 1731567761 267 PVLQRVGSGDAFVAGLLYQLLEGNEKQRNLDFAVATASL 305
Cdd:TIGR04382 250 EVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAI 288
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
37-303 |
1.57e-04 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 43.00 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 37 VNIARtLGGfglEARLFTALPDNPVGHAFHQFLKQSGVD---MSLTAWQghrvglyylengfgcRASQVY--YDRCGS-S 110
Cdd:PRK09434 36 VGIAR-LGG---ESGFIGRVGDDPFGRFMQQTLQDEGVDttyLRLDPAH---------------RTSTVVvdLDDQGErS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 111 FSALDKDSLDLAAIFEGISHF------HFSGISLALGKKTQDLIEILAReAKKRDICISFDLNFRSSMIA-VADAKRLFS 183
Cdd:PRK09434 97 FTFMVRPSADLFLQPQDLPPFrqgewlHLCSIALSAEPSRSTTFEAMRR-IKAAGGFVSFDPNLREDLWQdEAELRECLR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 184 HFAQYADII-FGMEPLLLDSDdfdmfdrkkadTTMIRERLAGLYQRYQLQ----------AIYHTERsndaqGSNHFKAY 252
Cdd:PRK09434 176 QALALADVVkLSEEELCFLSG-----------TSQLEDAIYALADRYPIAlllvtlgaegVLVHTRG-----QVQHFPAP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1731567761 253 AYDgqfyesCEVTTpvlqrvGSGDAFVAGLLYQLLEGNEKQRNLDFAVATA 303
Cdd:PRK09434 240 SVD------PVDTT------GAGDAFVAGLLAGLSQAGLWTDEAELAEIIA 278
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
3-312 |
8.30e-90 |
|
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: 270.60 E-value: 8.30e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 3 KLLLVGEPLIRVSPNQFQPLTNACEAQLFFGGSEVNIARTLGGFGLEARLFTALPDNPVGHAFHQFLKQSGVDMSL-TAW 81
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHvRVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 82 QGHRVGLYYLENGFGcRASQVYYDRCGSSFSALDKDSLDLAAiFEGISHFHFSGISLALGKKTQDLIEILAREAKKRDIC 161
Cdd:cd01166 81 PGRPTGLYFLEIGAG-GERRVLYYRAGSAASRLTPEDLDEAA-LAGADHLHLSGITLALSESAREALLEALEAAKARGVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 162 ISFDLNFRSSMIAVADAKRLFSHFAQYADIIFGMEpllldsDDFDMFDRKKADTTMIRErlaglYQRYQLQAIYHTERsN 241
Cdd:cd01166 159 VSFDLNYRPKLWSAEEAREALEELLPYVDIVLPSE------EEAEALLGDEDPTDAAER-----ALALALGVKAVVVK-L 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1731567761 242 DAQGsnhfkAYAYD-GQFYESCEVTTPVLQRVGSGDAFVAGLLYQLLEGNEKQRNLDFAVATASLKCTVVED 312
Cdd:cd01166 227 GAEG-----ALVYTgGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGD 293
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
3-313 |
2.01e-40 |
|
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: 143.49 E-value: 2.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 3 KLLLVGEPLIRVSPN-----QFQPLTNACEAQLFFGGSEVNIARTLGGFGLEARLFTALPDNPVGHAFHQFLKQSGVDMS 77
Cdd:COG0524 1 DVLVIGEALVDLVARvdrlpKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 78 LTAW-QGHRVGLYYLENGFGCRASQVYYdrcGSSFSALDKDSLDlAAIFEGISHFHFSGISLAlGKKTQDLIEILAREAK 156
Cdd:COG0524 81 GVRRdPGAPTGLAFILVDPDGERTIVFY---RGANAELTPEDLD-EALLAGADILHLGGITLA-SEPPREALLAALEAAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 157 KRDICISFDLNFRSSMIavADAKRLFSHFAQYADIIFGMEP---LLLDSDDFdmfdrkkadttmirERLAGLYQRYQLQA 233
Cdd:COG0524 156 AAGVPVSLDPNYRPALW--EPARELLRELLALVDILFPNEEeaeLLTGETDP--------------EEAAAALLARGVKL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 234 IYHTERsndAQGSnhfkAYAYDGQFYESCEVTTPVLQRVGSGDAFVAGLLYQLLEGNEKQRNLDFAVATASLKCTVVEDQ 313
Cdd:COG0524 220 VVVTLG---AEGA----LLYTGGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQ 292
|
|
| KDG_KDGal_kin_Halo |
NF041332 |
bifunctional 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase; |
1-333 |
3.88e-40 |
|
bifunctional 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase;
Pssm-ID: 469229 [Multi-domain] Cd Length: 318 Bit Score: 143.13 E-value: 3.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 1 MSKLLLVGEPLIRVSPNQFQPLTNACEAQLFFGGSEVNIARTLGGFGLEARLFTALPDNPVGHAFHQFLKQSGVDMSLTA 80
Cdd:NF041332 1 MTDLVTFGETMLRLSPPGGERLETADELDVRAGGAESNVAVAAARLGADATWLSKLPDSPLGRRVVGELRSHGVDTDVVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 81 WQGHRVGLYYLENGFGCRASQVYYDRCGSSFSALDKDSLDLAAIfEGISHFHFSGISLALGKKTQDLIEILAREAKKRDI 160
Cdd:NF041332 81 DDEGRQGTYYLEHGGEPRGTNVIYDRADAAVTTATPEELPLDRI-RDAEVFYTSGITPALSETLAETTAALLEAAQEAGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 161 CISFDLNFRSSMIAVADAKRLFSHFAQYADIIFGMEpllldSDDFDMFDRkKADTTMIRERLAglyQRYQLQAIYHTers 240
Cdd:NF041332 160 TTAFDLNYRSKLWSPEEARETLESLFPAVDVLVVAE-----RDARTVLGR-DGDAEEIAHGLA---SEYDFETVVVT--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 241 ndaQGSNHFKAYAyDGQFYESCEVTTPVLQRVGSGDAFVAGLLYQLLEGNEKQRNLDFAVATASLKCTVVEDQLYHSVQQ 320
Cdd:NF041332 228 ---RGEEGALALH-DGEVHEQPAYEADTVDPIGTGDAFVGGFLARRLAGGDVPTALEYGAATAALKRTIPGDVAVVTPEE 303
|
330
....*....|....*
gi 1731567761 321 VEAVLANQR--DIQR 333
Cdd:NF041332 304 VEAVVEDGGgdGISR 318
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
3-310 |
5.65e-28 |
|
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: 110.42 E-value: 5.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 3 KLLLVGEPLI-RVSPNQFQPLTNACEAqlffGGSEVNIARTLGGFGLEARLFTALPDNPVGHAFHQFLKQSGVDMSLTAW 81
Cdd:cd01167 1 KVVCFGEALIdFIPEGSGAPETFTKAP----GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 82 QGH-RVGLYYLENGFGCRASQVYYDRCGSSFSALDKDSLDLaaiFEGISHFHFSGISLAlGKKTQDLIEILAREAKKRDI 160
Cdd:cd01167 77 DPAaPTTLAFVTLDADGERSFEFYRGPAADLLLDTELNPDL---LSEADILHFGSIALA-SEPSRSALLELLEAAKKAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 161 CISFDLNFRSSMIAVAD-AKRLFSHFAQYADIIfgmepllldsddfdmfdrKKADttmirERLAGLYQRYQLQAIYHTER 239
Cdd:cd01167 153 LISFDPNLRPPLWRDEEeARERIAELLELADIV------------------KLSD-----EELELLFGEEDPEEIAALLL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 240 SNDAQ------GSNhfKAYAYDGQFYESCE-VTTPVLQRVGSGDAFVAGLLYQLLEGNEKQRN-------LDFAVATASL 305
Cdd:cd01167 210 LFGLKlvlvtrGAD--GALLYTKGGVGEVPgIPVEVVDTTGAGDAFVAGLLAQLLSRGLLALDedelaeaLRFANAVGAL 287
|
....*
gi 1731567761 306 KCTVV 310
Cdd:cd01167 288 TCTKA 292
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
3-314 |
9.54e-22 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 93.18 E-value: 9.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 3 KLLLVGEPLIRVSPNQFQPLTNACEAQ---LFFGGSEVNIARTLGGFGLEARLFTALPDNPVGHAFHQFLKQSGVDMSLT 79
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPGELVRVStveKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 80 AWQGH-RVGLYYLENGFGCRASQVYYDrcGSSFSALDKDSLDLAAIFEGISHFHFSGI-SLALGKKTQDLIEILAREAKK 157
Cdd:pfam00294 81 VIDEDtRTGTALIEVDGDGERTIVFNR--GAAADLTPEELEENEDLLENADLLYISGSlPLGLPEATLEELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 158 rdicisFDLNFRSSMIAVADAkrlFSHFAQYADIIFGMEpllldsDDFD-MFDRKKADTTMIRERLAGLYQRYQLQAIYh 236
Cdd:pfam00294 159 ------FDPNLLDPLGAAREA---LLELLPLADLLKPNE------EELEaLTGAKLDDIEEALAALHKLLAKGIKTVIV- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 237 terSNDAQGsnhfkAYAYDGQFyESCEVTTP---VLQRVGSGDAFVAGLLYQLLEGNEKQRNLDFAVATASLKCTVVEDQ 313
Cdd:pfam00294 223 ---TLGADG-----ALVVEGDG-EVHVPAVPkvkVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
|
.
gi 1731567761 314 L 314
Cdd:pfam00294 294 T 294
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
32-306 |
7.81e-13 |
|
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: 67.72 E-value: 7.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 32 FGGSEVNIARTLGGFGLEARLFTALPDNPVGHAFHQFLKQSGVDMSL--TAWQGHRVGLYYLENGFGcraSQVYYDRCGS 109
Cdd:cd01942 35 FGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSHvrVVDEDSTGVAFILTDGDD---NQIAYFYPGA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 110 SFSALDKDSLDLAAIFEGIshfHFSGISlalgkktqDLIEiLAREAKKRDICISFDLNFRSSMIAVADAKRLFSHfaqyA 189
Cdd:cd01942 112 MDELEPNDEADPDGLADIV---HLSSGP--------GLIE-LARELAAGGITVSFDPGQELPRLSGEELEEILER----A 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 190 DIIFgmepllLDSDDFDMFDRKKADTTMIRERLAGlyqryqlqAIYHTersndaQGSNHFKAYAYDGQFYESCEVTTPVL 269
Cdd:cd01942 176 DILF------VNDYEAELLKERTGLSEAELASGVR--------VVVVT------LGPKGAIVFEDGEEVEVPAVPAVKVV 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 1731567761 270 QRVGSGDAFVAGLLYQLLEGNEKQRNLDFAVATASLK 306
Cdd:cd01942 236 DTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLK 272
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
31-305 |
2.01e-12 |
|
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: 66.85 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 31 FFGGSEVNIARTLGGFGLEARLFTALPDNPVGHAFHQFLKQSGVDMS-LTAWQGHRVGLYYLENGFGCRASQVYYdRCGS 109
Cdd:TIGR04382 32 YLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTShVVTDPGRRTSLVFLEIKPPDEFPLLFY-RENA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 110 SFSALDKDSLDLAAIFEGiSHFHFSGISLAlGKKTQDLIEILAREAKKRDICISFDLNFRS-SMIAVADAKRLFSHFAQY 188
Cdd:TIGR04382 111 ADLALTPDDVDEDYIASA-RALLVSGTALS-QEPSREAVLKALEYARAAGVRVVLDIDYRPyLWKSPEEAGIYLRLVLPL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 189 ADIIFGMEpllldsDDFDMFDRKKADttmirERLAGLYQRY--QLQAIYHTERsndaqGSNhfkAYAYDGQFYESCEVTT 266
Cdd:TIGR04382 189 VDVIIGTR------EEFDIAGGEGDD-----EAAARALLDAgvEILVVKRGPE-----GSL---VYTGDGEGVEVPGFPV 249
|
250 260 270
....*....|....*....|....*....|....*....
gi 1731567761 267 PVLQRVGSGDAFVAGLLYQLLEGNEKQRNLDFAVATASL 305
Cdd:TIGR04382 250 EVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAI 288
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
31-308 |
4.38e-08 |
|
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: 53.45 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 31 FFGGSEVNIARTLGGFGLEARLFTALPDNPVGHAFHQFLKQSGVDMS-LTAWQGHRVGLYYLENGFGCRASQVYYDRcgs 109
Cdd:cd01945 34 IGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSfIVVAPGARSPISSITDITGDRATISITAI--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 110 sFSALDKDSLDLAAIFeGISHFHFSG--ISLALgkktqdlieILAREAKKRDICISFDLNfrssmiavADAKRLFSHFAQ 187
Cdd:cd01945 111 -DTQAAPDSLPDAILG-GADAVLVDGrqPEAAL---------HLAQEARARGIPIPLDLD--------GGGLRVLEELLP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 188 YADIIFGMEPLLLDSDDfdmfdrkkADTTMIRERLAGLYQRyqlqAIYHTersndaQGSNHFKAYAYDGqfyESCEVTTP 267
Cdd:cd01945 172 LADHAICSENFLRPNTG--------SADDEALELLASLGIP----FVAVT------LGEAGCLWLERDG---ELFHVPAF 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1731567761 268 ---VLQRVGSGDAFVAGLLYQLLEGNEKQRNLDFAVATASLKCT 308
Cdd:cd01945 231 pveVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCR 274
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
272-326 |
4.73e-06 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 47.44 E-value: 4.73e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1731567761 272 VGSGDAFVAGLLYQLLEGNEKQRNLDFAVATASLKCTVVEDQLYhSVQQVEAVLA 326
Cdd:COG1105 248 VGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTGLP-DREDVEELLA 301
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
10-310 |
4.03e-05 |
|
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: 44.53 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 10 PLIRVSPNQFQPLTNACEAQLFFGGSEVNIARTLGGFGLEARLFTALPDNPVGHAFHQFLKQSGVDMSLtawqghrvglY 89
Cdd:cd01168 32 DMILADMEEQEELLAKLPVKYIAGGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRY----------Q 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 90 YLENGF-GCRASQVYYD----RC---GSS--FSA--LDKDSLDLAAIFeGISHFHFSGislalgkkTQDLIEILAREAKK 157
Cdd:cd01168 102 VQPDGPtGTCAVLVTPDaertMCtylGAAneLSPddLDWSLLAKAKYL-YLEGYLLTV--------PPEAILLAAEHAKE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 158 RDICISFDLnfrSSMIAVADAKRLFSHFAQYADIIFGMEpllldsDDFDMFdrKKADTTMIRERLAGLYQRYQLQAIYhT 237
Cdd:cd01168 173 NGVKIALNL---SAPFIVQRFKEALLELLPYVDILFGNE------EEAEAL--AEAETTDDLEAALKLLALRCRIVVI-T 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1731567761 238 ERSNDAQgsnhfkaYAYDGQfyescEVTTPVLQRV------GSGDAFVAGLLYQLLEGNEKQRNLDFAVATASLKCTVV 310
Cdd:cd01168 241 QGAKGAV-------VVEGGE-----VYPVPAIPVEkivdtnGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQL 307
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
265-306 |
6.24e-05 |
|
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: 44.06 E-value: 6.24e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1731567761 265 TTPVLQRVGSGDAFVAGLLYQLLEGNEKQRNLDFAVATASLK 306
Cdd:cd01164 241 KVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSAT 282
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
272-333 |
1.08e-04 |
|
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: 43.33 E-value: 1.08e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1731567761 272 VGSGDAFVAGLLYQLLEGNEKQRNLDFAVATASlkctvvedqlyHSVQQVEAVLANQRDIQR 333
Cdd:TIGR03168 247 VGAGDSMVAGFLAGLARGLSLEEALRFAVAAGS-----------AAAFSPGTGLPDPEDVEE 297
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
37-303 |
1.57e-04 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 43.00 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 37 VNIARtLGGfglEARLFTALPDNPVGHAFHQFLKQSGVD---MSLTAWQghrvglyylengfgcRASQVY--YDRCGS-S 110
Cdd:PRK09434 36 VGIAR-LGG---ESGFIGRVGDDPFGRFMQQTLQDEGVDttyLRLDPAH---------------RTSTVVvdLDDQGErS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 111 FSALDKDSLDLAAIFEGISHF------HFSGISLALGKKTQDLIEILAReAKKRDICISFDLNFRSSMIA-VADAKRLFS 183
Cdd:PRK09434 97 FTFMVRPSADLFLQPQDLPPFrqgewlHLCSIALSAEPSRSTTFEAMRR-IKAAGGFVSFDPNLREDLWQdEAELRECLR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 184 HFAQYADII-FGMEPLLLDSDdfdmfdrkkadTTMIRERLAGLYQRYQLQ----------AIYHTERsndaqGSNHFKAY 252
Cdd:PRK09434 176 QALALADVVkLSEEELCFLSG-----------TSQLEDAIYALADRYPIAlllvtlgaegVLVHTRG-----QVQHFPAP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1731567761 253 AYDgqfyesCEVTTpvlqrvGSGDAFVAGLLYQLLEGNEKQRNLDFAVATA 303
Cdd:PRK09434 240 SVD------PVDTT------GAGDAFVAGLLAGLSQAGLWTDEAELAEIIA 278
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
3-304 |
2.24e-04 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 42.03 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 3 KLLLVGEPLIRVSPNqfqpLTNAceaqlFFGGSEVNIARTLGGFGLEARLFTALPDNPVGHAFHQFLKQSGVDMSLTAWQ 82
Cdd:PRK09813 2 KLATIGDNCVDIYPQ----LGKA-----FSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 83 GHRVGLYYLENGFGCRASQVYYDRCGSSFsALDKDSLDLAAIFEgISHfhfSGIslaLGKKTQDLIEIlaREAKKRdicI 162
Cdd:PRK09813 73 HGVTAQTQVELHDNDRVFGDYTEGVMADF-ALSEEDYAWLAQYD-IVH---AAI---WGHAEDAFPQL--HAAGKL---T 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 163 SFDLnfrssmiavadAKRLFSHFAQyadiifgmepLLLDSDDFdMFDRKKADTTMIRERLAGLYQRYQLQAIYhterSND 242
Cdd:PRK09813 140 AFDF-----------SDKWDSPLWQ----------TLVPHLDY-AFASAPQEDEFLRLKMKAIVARGAGVVIV----TLG 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1731567761 243 AQGSnhfkaYAYDG-QFYESCEVTTPVLQRVGSGDAFVAGLLYQLLEGNEKQRNLDFAVATAS 304
Cdd:PRK09813 194 ENGS-----IAWDGaQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAA 251
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
261-305 |
3.65e-04 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 41.60 E-value: 3.65e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1731567761 261 SCEVTTPVlqrvGSGDAFVAGLLYQLLEGNEKQRNLDFAVATASL 305
Cdd:PRK09513 244 ACDVVSTV----GAGDSMVGGLIYGLLMRESSEHTLRLATAVSAL 284
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
255-310 |
3.90e-04 |
|
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.
Pssm-ID: 238914 [Multi-domain] Cd Length: 290 Bit Score: 41.62 E-value: 3.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1731567761 255 DGQFYEsCEVTTP--VLQRVGSGDAFVAGLLYQLLEGNEK-QRNLDFAVATASLKCTVV 310
Cdd:cd01939 230 DGEYVH-SPAHKPirVVDTLGAGDTFNAAVIYALNKGPDDlSEALDFGNRVASQKCTGV 287
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
272-306 |
6.18e-04 |
|
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: 41.04 E-value: 6.18e-04
10 20 30
....*....|....*....|....*....|....*
gi 1731567761 272 VGSGDAFVAGLLYQLLEGNEKQRNLDFAVATASLK 306
Cdd:TIGR03828 247 VGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAA 281
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
23-305 |
8.47e-04 |
|
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: 40.37 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 23 TNACEAQLFFGGSEVNIARTLGGFGLEARLFTALPDNPVGHAFHQFLKQSGVDMSLTAWQGHRVGLYylengfgcrasqv 102
Cdd:cd01941 25 SNPGHVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRGIVFEGRSTASY------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 103 yydrcgssfSA-LDKDSLDLAAIFEGISHFHFSgiSLALGKKTQDLieilaREAKkrdiCISFDLNfrssmIAVADAKRL 181
Cdd:cd01941 92 ---------TAiLDKDGDLVVALADMDIYELLT--PDFLRKIREAL-----KEAK----PIVVDAN-----LPEEALEYL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 182 FShFAQYADIIFGMEPllldsddFDMFDRKKadttmIRERLAGLY----QRYQLQAIY-----HTERSNDAQ-------- 244
Cdd:cd01941 147 LA-LAAKHGVPVAFEP-------TSAPKLKK-----LFYLLHAIDlltpNRAELEALAgalieNNEDENKAAkilllpgi 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731567761 245 -------GSNHfkAYAYDGQfYESCEVTTPVLQRV------GSGDAFVAGLLYQLLEGNEKQRNLDFAVATASL 305
Cdd:cd01941 214 knvivtlGAKG--VLLSSRE-GGVETKLFPAPQPEtvvnvtGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAAL 284
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
264-305 |
1.60e-03 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 39.91 E-value: 1.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1731567761 264 VTTPVLQRV---GSGDAFVAGLLYQLLEGNEKQRNLDFAVATASL 305
Cdd:PRK09954 294 LTAPAHTTVdsfGADDGFMAGLVYSFLEGYSFRDSARFAMACAAI 338
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
12-173 |
3.65e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 38.62 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 12 IRVSPNQFQPLTNACeaqlffGGSEVNIARTL-GGFGLEARLFTALPDNPVGHAFHQFLKQSGVDMS-LTAWQGHRVGLY 89
Cdd:PLN02379 71 ILPSPDDLSPIKTMA------GGSVANTIRGLsAGFGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSrLRAKKGPTAQCV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 90 YLENGFGCRASQvyydRCGSSFSALDKDSLdlaaifegiSHFHFSGIS---LALGKKTQDLIEILAREAKKRDICISFDL 166
Cdd:PLN02379 145 CLVDALGNRTMR----PCLSSAVKLQADEL---------TKEDFKGSKwlvLRYGFYNLEVIEAAIRLAKQEGLSVSLDL 211
|
170
....*....|....
gi 1731567761 167 -------NFRSSMI 173
Cdd:PLN02379 212 asfemvrNFRSPLL 225
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
118-287 |
8.19e-03 |
|
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: 37.07 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 118 SLDLAAIFEGISHFHFSGISLALgkktqDLIEILAREAKKRDICISFDLNFRssmiAVADAKRLFSHFAQYADIIFgmep 197
Cdd:cd00287 48 RLGVSVTLVGADAVVISGLSPAP-----EAVLDALEEARRRGVPVVLDPGPR----AVRLDGEELEKLLPGVDILT---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731567761 198 llLDSDDFDMFDRKKADTTMIRERLAGLYQRYQLQAIYHTErsnDAQGSnhfkaYAYDGQFYESC--EVTTPVLQRVGSG 275
Cdd:cd00287 115 --PNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTL---GEKGA-----IVATRGGTEVHvpAFPVKVVDTTGAG 184
|
170
....*....|..
gi 1731567761 276 DAFVAGLLYQLL 287
Cdd:cd00287 185 DAFLAALAAGLA 196
|
|
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