|
Name |
Accession |
Description |
Interval |
E-value |
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
5-502 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 933.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 5 RYVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGITNQR 84
Cdd:COG0554 3 KYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITNQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 85 ETTVVWDRNTGRPVYNAIVWQDTRTDRLCERLAGDVGADRYKERVGLPLATYFSGPKVAWILENVDGAREAAENGDLIFG 164
Cdd:COG0554 83 ETTVVWDRKTGKPLYNAIVWQDRRTADICEELKADGLEDLIREKTGLVLDPYFSATKIKWILDNVPGARERAEAGELLFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 165 TTDSWLVWNLTGGGeggRHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVGTVSGQQLLRETPITG 244
Cdd:COG0554 163 TIDSWLIWKLTGGK---VHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDPDLFGAEIPIAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 245 ILGDQHAATFGQACFEVGQAKNTYGTGNFMLINTGEEPVHSDNGLLTTVAYRIGDqKPVYALEGSIAVTGSLIQWLRDNL 324
Cdd:COG0554 240 IAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGG-KVTYALEGSIFVAGAAVQWLRDGL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 325 GMIGSAPEVETLAAGVGDNGGVYFVPAFSGLFAPHWDAAARGAMVGMTRYVNKGHIARAALEATAFQSREVLDAMNADSG 404
Cdd:COG0554 319 GLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADSG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 405 VDLTELKVDGGMVANELLMQFQADLLRVPVVRPKVIETTALGAAYAAGLAVGFWASQDELVANWEEDKRWEPTMDEEEAE 484
Cdd:COG0554 399 IPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEELAALWKVDRRFEPQMDEEERE 478
|
490
....*....|....*...
gi 984924754 485 RALRLWKKAVERSRDWVD 502
Cdd:COG0554 479 RLYAGWKKAVERTLGWAE 496
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
6-495 |
0e+00 |
|
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466789 [Multi-domain] Cd Length: 486 Bit Score: 892.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGITNQRE 85
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 86 TTVVWDRNTGRPVYNAIVWQDTRTDRLCERLAGDVGADRYKERVGLPLATYFSGPKVAWILENVDGAREAAENGDLIFGT 165
Cdd:cd07769 81 TTVVWDKKTGKPLYNAIVWQDRRTADICEELKAKGLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAERGELLFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 166 TDSWLVWNLTGGGeggRHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVGTVSGQQLLRETPITGI 245
Cdd:cd07769 161 IDTWLIWKLTGGK---VHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTDPEGLGAGIPIAGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 246 LGDQHAATFGQACFEVGQAKNTYGTGNFMLINTGEEPVHSDNGLLTTVAYRIgDQKPVYALEGSIAVTGSLIQWLRDNLG 325
Cdd:cd07769 238 LGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQI-GGKVTYALEGSIFIAGAAIQWLRDNLG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 326 MIGSAPEVETLAAGVGDNGGVYFVPAFSGLFAPHWDAAARGAMVGMTRYVNKGHIARAALEATAFQSREVLDAMNADSGV 405
Cdd:cd07769 317 LIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDSGI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 406 DLTELKVDGGMVANELLMQFQADLLRVPVVRPKVIETTALGAAYAAGLAVGFWASQDELVANWEEDKRWEPTMDEEEAER 485
Cdd:cd07769 397 KLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDELASLWQVDKRFEPSMDEEERER 476
|
490
....*....|
gi 984924754 486 ALRLWKKAVE 495
Cdd:cd07769 477 LYRGWKKAVE 486
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
1-501 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 889.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 1 MTTPRYVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGI 80
Cdd:PRK00047 1 MMMKKYILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 81 TNQRETTVVWDRNTGRPVYNAIVWQDTRTDRLCERLAGDVGADRYKERVGLPLATYFSGPKVAWILENVDGAREAAENGD 160
Cdd:PRK00047 81 TNQRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRDGYEDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 161 LIFGTTDSWLVWNLTGGGEggrHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVG-TVSGQQLLRE 239
Cdd:PRK00047 161 LLFGTIDTWLVWKLTGGKV---HVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGkTNPYGFFGGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 240 TPITGILGDQHAATFGQACFEVGQAKNTYGTGNFMLINTGEEPVHSDNGLLTTVAYRIgDQKPVYALEGSIAVTGSLIQW 319
Cdd:PRK00047 238 VPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGI-DGKVVYALEGSIFVAGSAIQW 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 320 LRDNLGMIGSAPEVETLAAGVGDNGGVYFVPAFSGLFAPHWDAAARGAMVGMTRYVNKGHIARAALEATAFQSREVLDAM 399
Cdd:PRK00047 317 LRDGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDAM 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 400 NADSGVDLTELKVDGGMVANELLMQFQADLLRVPVVRPKVIETTALGAAYAAGLAVGFWASQDELVANWEEDKRWEPTMD 479
Cdd:PRK00047 397 QADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDELKEQWKIDRRFEPQMD 476
|
490 500
....*....|....*....|..
gi 984924754 480 EEEAERALRLWKKAVERSRDWV 501
Cdd:PRK00047 477 EEEREKLYAGWKKAVKRTLAWA 498
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
6-500 |
0e+00 |
|
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of carbohydrate kinases. [Energy metabolism, Other]
Pssm-ID: 273549 [Multi-domain] Cd Length: 493 Bit Score: 821.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGITNQRE 85
Cdd:TIGR01311 2 YILAIDQGTTSSRAIVFDKDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAGIKPDDIAAIGITNQRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 86 TTVVWDRNTGRPVYNAIVWQDTRTDRLCERLAGDVGADRYKERVGLPLATYFSGPKVAWILENVDGAREAAENGDLIFGT 165
Cdd:TIGR01311 82 TTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYGEFIREKTGLPLDPYFSATKLRWLLDNVPGVREAAERGELLFGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 166 TDSWLVWNLTGGGEggrHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVGTVSGQQLLRETPITGI 245
Cdd:TIGR01311 162 IDTWLIWNLTGGKV---HVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYTDPGLLGAEIPITGV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 246 LGDQHAATFGQACFEVGQAKNTYGTGNFMLINTGEEPVHSDNGLLTTVAYRIGDQKPVYALEGSIAVTGSLIQWLRDNLG 325
Cdd:TIGR01311 239 LGDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKKPVYALEGSVFVAGAAVQWLRDNLK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 326 MIGSAPEVETLAAGVGDNGGVYFVPAFSGLFAPHWDAAARGAMVGMTRYVNKGHIARAALEATAFQSREVLDAMNADSGV 405
Cdd:TIGR01311 319 LIKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTRDVLEAMEKDAGV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 406 DLTELKVDGGMVANELLMQFQADLLRVPVVRPKVIETTALGAAYAAGLAVGFWASQDELVANWEEDKRWEPTMDEEEAER 485
Cdd:TIGR01311 399 EITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWRVEKTFEPEMDEEEREA 478
|
490
....*....|....*
gi 984924754 486 ALRLWKKAVERSRDW 500
Cdd:TIGR01311 479 RYAGWKEAVKRSLGW 493
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
6-495 |
0e+00 |
|
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases
Pssm-ID: 198361 [Multi-domain] Cd Length: 486 Bit Score: 818.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGITNQRE 85
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 86 TTVVWDRNTGRPVYNAIVWQDTRTDRLCERLAGDVGADRYKERVGLPLATYFSGPKVAWILENVDGAREAAENGDLIFGT 165
Cdd:cd07786 81 TTVVWDRETGKPVYNAIVWQDRRTADICEELKAEGHEEMIREKTGLVLDPYFSATKIRWILDNVPGARERAERGELAFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 166 TDSWLVWNLTGGGEggrHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVGTVSGQQLLRETPITGI 245
Cdd:cd07786 161 IDSWLIWKLTGGKV---HATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDPDLLGAEIPIAGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 246 LGDQHAATFGQACFEVGQAKNTYGTGNFMLINTGEEPVHSDNGLLTTVAYRIGDqKPVYALEGSIAVTGSLIQWLRDNLG 325
Cdd:cd07786 238 AGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLGG-KVTYALEGSIFIAGAAVQWLRDGLG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 326 MIGSAPEVETLAAGVGDNGGVYFVPAFSGLFAPHWDAAARGAMVGMTRYVNKGHIARAALEATAFQSREVLDAMNADSGV 405
Cdd:cd07786 317 LIESAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEADSGI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 406 DLTELKVDGGMVANELLMQFQADLLRVPVVRPKVIETTALGAAYAAGLAVGFWASQDELVANWEEDKRWEPTMDEEEAER 485
Cdd:cd07786 397 PLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAKLWQVDRRFEPSMSEEEREA 476
|
490
....*....|
gi 984924754 486 ALRLWKKAVE 495
Cdd:cd07786 477 LYAGWKKAVK 486
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
6-497 |
0e+00 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466802 [Multi-domain] Cd Length: 499 Bit Score: 802.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIGEALARAEVTRH---DVAAVGITN 82
Cdd:cd07792 2 LVGAIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLKALGIspsDIKAIGITN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 83 QRETTVVWDRNTGRPVYNAIVWQDTRTDRLCERL--AGDVGADRYKERVGLPLATYFSGPKVAWILENVDGAREAAENGD 160
Cdd:cd07792 82 QRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELsaKTPGGKDHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDDGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 161 LIFGTTDSWLVWNLTGGGEGGRHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVGTVSGQQLLReT 240
Cdd:cd07792 162 LLFGTVDSWLIWNLTGGKNGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIASGPLAG-V 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 241 PITGILGDQHAATFGQACFEVGQAKNTYGTGNFMLINTGEEPVHSDNGLLTTVAYRIG-DQKPVYALEGSIAVTGSLIQW 319
Cdd:cd07792 241 PISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAYKLGpDAPPVYALEGSIAIAGAAVQW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 320 LRDNLGMIGSAPEVETLAAGVGDNGGVYFVPAFSGLFAPHWDAAARGAMVGMTRYVNKGHIARAALEATAFQSREVLDAM 399
Cdd:cd07792 321 LRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREILDAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 400 NADSGVDLTELKVDGGMVANELLMQFQADLLRVPVVRPKVIETTALGAAYAAGLAVGFWASQDELVA-NWEEDKRWEPTM 478
Cdd:cd07792 401 NKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSlNEGGRTVFEPQI 480
|
490
....*....|....*....
gi 984924754 479 DEEEAERALRLWKKAVERS 497
Cdd:cd07792 481 SEEERERRYKRWKKAVERS 499
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
6-504 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 734.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIGEALARAEVTRHDV----AAVGIT 81
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGHNVdsglKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 82 NQRETTVVWDRNTGRPVYNAIVWQDTRTDRLCERLAGDV--GADRYKERVGLPLATYFSGPKVAWILENVDGAREAAENG 159
Cdd:PLN02295 81 NQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKELsgGRKHFVETCGLPISTYFSATKLLWLLENVDAVKEAVKSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 160 DLIFGTTDSWLVWNLTGGGEGGRHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVGTVSGQQLLRE 239
Cdd:PLN02295 161 DALFGTIDSWLIWNLTGGASGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIAKGWPLAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 240 TPITGILGDQHAATFGQACfEVGQAKNTYGTGNFMLINTGEEPVHSDNGLLTTVAYRIGDQKPV-YALEGSIAVTGSLIQ 318
Cdd:PLN02295 241 VPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYKLGPDAPTnYALEGSVAIAGAAVQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 319 WLRDNLGMIGSAPEVETLAAGVGDNGGVYFVPAFSGLFAPHWDAAARGAMVGMTRYVNKGHIARAALEATAFQSREVLDA 398
Cdd:PLN02295 320 WLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQVKDVLDA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 399 MNAD-----SGVDLTELKVDGGMVANELLMQFQADLLRVPVVRPKVIETTALGAAYAAGLAVGFWASQDEL-VANWEEDK 472
Cdd:PLN02295 400 MRKDageekSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEEEIFaSEKWKNTT 479
|
490 500 510
....*....|....*....|....*....|..
gi 984924754 473 RWEPTMDEEEAERALRLWKKAVERSRDWVDED 504
Cdd:PLN02295 480 TFRPKLDEEERAKRYASWCKAVERSFDLADLS 511
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
6-503 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 703.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIGEAL--ARAEVTRHDVAAVGITNQ 83
Cdd:PTZ00294 3 YIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIkkLREKGPSFKIKAIGITNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 84 RETTVVWDRNTGRPVYNAIVWQDTRTDRLCERLAGDVG-ADRYKERVGLPLATYFSGPKVAWILENVDGAREAAENGDLI 162
Cdd:PTZ00294 83 RETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKYGgSNFFQKITGLPISTYFSAFKIRWMLENVPAVKDAVKEGTLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 163 FGTTDSWLVWNLTGGGEggrHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVGTVSGQQ--LLRET 240
Cdd:PTZ00294 163 FGTIDTWLIWNLTGGKS---HVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTISGEAvpLLEGV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 241 PITGILGDQHAATFGQACFEVGQAKNTYGTGNFMLINTGEEPVHSDNGLLTTVAYRIG-DQKPVYALEGSIAVTGSLIQW 319
Cdd:PTZ00294 240 PITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYQLGpNGPTVYALEGSIAVAGAGVEW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 320 LRDNLGMIGSAPEVETLAAGVGDNGGVYFVPAFSGLFAPHWDAAARGAMVGMTRYVNKGHIARAALEATAFQSREVLDAM 399
Cdd:PTZ00294 320 LRDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDVIESM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 400 NADSGVDLTELKVDGGMVANELLMQFQADLLRVPVVRPKVIETTALGAAYAAGLAVGFWASQDEL-VANWEEDKRWEPTM 478
Cdd:PTZ00294 400 EKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVkKLIRRSNSTFSPQM 479
|
490 500
....*....|....*....|....*
gi 984924754 479 DEEEAERALRLWKKAVERSRDWVDE 503
Cdd:PTZ00294 480 SAEERKAIYKEWNKAVERSLKWAKL 504
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
6-495 |
1.42e-174 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466803 [Multi-domain] Cd Length: 501 Bit Score: 500.94 E-value: 1.42e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGITNQRE 85
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 86 TTVVWDRNTGRPVYNAIVWQDTRTDRLCE-----------RLAGDV-----GADRYKERVGLPLATYFSGPKVAWILENV 149
Cdd:cd07793 81 TFLTWDKKTGKPLHNFITWQDLRAAELCEswnrslllkalRGGSKFlhfltRNKRFLAASVLKFSTAHVSIRLLWILQNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 150 DGAREAAENGDLIFGTTDSWLVWNLTGGGEggrHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVG 229
Cdd:cd07793 161 PELKEAAEKGELLFGTIDTWLLWKLTGGKV---HATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 230 TVSGQQLLRETPITGILGDQHAATFGQACFEVGQAKNTYGTGNFMLINTGEEPVHSDNGLLTTVAYRIGDqKPVYALEGS 309
Cdd:cd07793 238 STDPSIFGAEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGG-EITYLAEGN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 310 IAVTGSLIQWLRDNlGMIGSAPEVETLAAGVGDNGGVYFVPAFSGLFAPHWDAAARGAMVGMTRYVNKGHIARAALEATA 389
Cdd:cd07793 317 ASDTGTVIDWAKSI-GLFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 390 FQSREVLDAMNADSGVDLTELKVDGGMVANELLMQFQADLLRVPVVRPKVIETTALGAAYAAGLAVGFWASQDELVANWE 469
Cdd:cd07793 396 FRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEELKKLRK 475
|
490 500
....*....|....*....|....*.
gi 984924754 470 EDKRWEPTMDEEEAERALRLWKKAVE 495
Cdd:cd07793 476 IEKIFEPKMDNEKREELYKNWKKAVK 501
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
5-499 |
2.25e-115 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 349.52 E-value: 2.25e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 5 RYVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGITNQR 84
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 85 ETTVVWDRNtGRPVYNAIVWQDTRTDRLCERLAGDVGADRYKERVGLPLATYFSGPKVAWILENvdgAREAAENGDLIFG 164
Cdd:COG1070 81 HGLVLLDAD-GEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKEN---EPEIFARIAKVLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 165 TTDsWLVWNLTgggegGRHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVGTVSGQ-----QLLRE 239
Cdd:COG1070 157 PKD-YLRYRLT-----GEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEaaaetGLPAG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 240 TPITGILGDQHAATFGQACFEVGQAKNTYGTGNFMLINTgEEPVHSDNGLLTTVAYRIGDQkpvYALEGSIAVTGSLIQW 319
Cdd:COG1070 231 TPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVS-DKPLPDPEGRVHTFCHAVPGR---WLPMGATNNGGSALRW 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 320 LRDNL--GMIGSAPEVETLAAGVG-DNGGVYFVPAFSGLFAPHWDAAARGAMVGMTRYVNKGHIARAALEATAFQSREVL 396
Cdd:COG1070 307 FRDLFadGELDDYEELNALAAEVPpGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 397 DAMnADSGVDLTELKVDGGMVANELLMQFQADLLRVPVVRPKVIETTALGAAYAAGLAVGFWASQDELVANW-EEDKRWE 475
Cdd:COG1070 387 EAL-EEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMvRVGETIE 465
|
490 500
....*....|....*....|....*
gi 984924754 476 PTMDEEEA-ERALRLWKKAVERSRD 499
Cdd:COG1070 466 PDPENVAAyDELYERYRELYPALKP 490
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
6-443 |
8.46e-108 |
|
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466798 [Multi-domain] Cd Length: 433 Bit Score: 327.94 E-value: 8.46e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGITNQRE 85
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 86 TTVVWDRNtGRPVYNAIVWQDTRTDRLCerlagdvgadrykervglplatyfsgpkvawilenvdgareaaengdlifgT 165
Cdd:cd07779 81 TFVPVDED-GRPLRPAISWQDKRTAKFL---------------------------------------------------T 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 166 TDSWLVWNLTGggeggRHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVGTVSGQ-----QLLRET 240
Cdd:cd07779 109 VQDYLLYRLTG-----EFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEaaeetGLPEGT 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 241 PI--TGilGDQHAATFGQACFEVGQAKNTYGTGNFMLINTgEEPVHSDNGLLTTVAYRIGDQkpvYALEGSIAVTGSLIQ 318
Cdd:cd07779 184 PVvaGG--GDQQCAALGAGVLEPGTASLSLGTAAVVIAVS-DKPVEDPERRIPCNPSAVPGK---WVLEGSINTGGSAVR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 319 WLRDNLG-------MIGSAPE--VETLAAGV--GDNgGVYFVPAFSGLFAPHWDAAARGAMVGMTRYVNKGHIARAALEA 387
Cdd:cd07779 258 WFRDEFGqdevaekELGVSPYelLNEEAAKSppGSD-GLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEG 336
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 984924754 388 TAFQSREVLDAMnADSGVDLTELKVDGGMVANELLMQFQADLLRVPVVRPKVIETT 443
Cdd:cd07779 337 IAFELRDNLEAM-EKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEAT 391
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
6-443 |
2.75e-106 |
|
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466787 [Multi-domain] Cd Length: 392 Bit Score: 322.59 E-value: 2.75e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGITNQRE 85
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 86 TTVVWDRNtGRPVYNAIVWQDTRtdrlcerlagdvgadrYKervglplatyfsgpkvawilenvdgareaaengdliFGT 165
Cdd:cd00366 81 GVVLVDAD-GNPLRPAIIWLDRR----------------AK------------------------------------FLQ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 166 TDSWLVWNLTGggeggRHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVGTVSGQQ-----LLRET 240
Cdd:cd00366 108 PNDYIVFRLTG-----EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAaeetgLPAGT 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 241 PITGILGDQHAATFGQACFEVGQAKNTYGTGNFMLINTgEEPVHSDNGLLTTVAYRIGdqkpVYALEGSIAVTGSLIQWL 320
Cdd:cd00366 183 PVVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCT-DEPVPPDPRLLNRCHVVPG----LWLLEGAINTGGASLRWF 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 321 RDNLG----MIGSAPEVETLAAGVGDN-GGVYFVPAFSGLFAPHWDAAARGAMVGMTRYVNKGHIARAALEATAFQSREV 395
Cdd:cd00366 258 RDEFGeeedSDAEYEGLDELAAEVPPGsDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDN 337
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 984924754 396 LDAMnADSGVDLTELKVDGGMVANELLMQFQADLLRVPVVRPKVIETT 443
Cdd:cd00366 338 LEIL-EELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGA 384
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
6-443 |
1.02e-90 |
|
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466793 [Multi-domain] Cd Length: 443 Bit Score: 284.09 E-value: 1.02e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIGEALARAEvtRHDVAAVGITNQRE 85
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAG--PDPIAAISVSSQGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 86 TTVVWDRNtGRPVYNAIVWQDTRTDRLCERLAGDVGADRYKERVGLPLATYFSGPKVAWILENvdgAREAAENGDLIFGT 165
Cdd:cd07773 79 SGVPVDRD-GEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREH---EPEIFAKAAKWLSV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 166 TDsWLVWNLTgggegGRHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVGTVSGQ-----QLLRET 240
Cdd:cd07773 155 AD-YIAYRLT-----GEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEaaeelGLPAGT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 241 PItgILG--DQHAATFGQACFEVGQAKNTYGTGNFMLINTGEEPV-HSDNGLLTTVAYRIGDQKpvYALEGSIAvTGSLI 317
Cdd:cd07773 229 PV--VVGghDHLCAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLdEMLAEGGLSYGHHVPGGY--YYLAGSLP-GGALL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 318 QWLRDNLGMIGSAPEVETLAAGVGDNG--GVYFVPAFSGLFAPHWDAAARGAMVGMTRYVNKGHIARAALEATAFQSREV 395
Cdd:cd07773 304 EWFRDLFGGDESDLAAADELAEAAPPGptGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLN 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 984924754 396 LDAMnADSGVDLTELKVDGGMVANELLMQFQADLLRVPVVRPKVIETT 443
Cdd:cd07773 384 LEAL-EKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEAT 430
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
6-443 |
3.41e-89 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 281.35 E-value: 3.41e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGITNQRE 85
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 86 TTVVWDRNtGRPVYNAIVWQDTRTDRLCERLAGDVGADRYKERVGLPLATyFSGPKVAWILENvdgAREAAENGDLIFGT 165
Cdd:cd07808 81 GLVLLDKN-GRPLRPAILWNDQRSAAECEELEARLGDEILIITGNPPLPG-FTLPKLLWLKEN---EPEIFARIRKILLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 166 TDsWLVWNLTgggegGRHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVGTVSGQ-----QLLRET 240
Cdd:cd07808 156 KD-YLRYRLT-----GELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEaaeelGLPEGT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 241 P-ITGiLGDQHAATFGQACFEVGQAKNTYGT-GNFMLINtgEEPVHSDNGLLTTVAYRIGDQkpVYALeGSIAVTGSLIQ 318
Cdd:cd07808 230 PvVAG-AGDNAAAALGAGVVEPGDALISLGTsGVVFAPT--DKPVPDPKGRLHTFPHAVPGK--WYAM-GVTLSAGLSLR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 319 WLRDNLG-MIGSAPEVETLAAGVGD-NGGVYFVPAFSGLFAPHWDAAARGAMVGMTRYVNKGHIARAALEATAFQSREVL 396
Cdd:cd07808 304 WLRDLFGpDRESFDELDAEAAKVPPgSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSL 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 984924754 397 DAMnADSGVDLTELKVDGGMVANELLMQFQADLLRVPVVRPKVIETT 443
Cdd:cd07808 384 EVL-KELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGS 429
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
6-255 |
2.26e-85 |
|
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.
Pssm-ID: 395295 [Multi-domain] Cd Length: 245 Bit Score: 263.43 E-value: 2.26e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGITNQRE 85
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 86 TTVVWDRNTgRPVYNAIVWQDTRTDRLCERLAGDVGADRYKERVGLPLATYFSGPKVAWILENVDGAREAAEngdlIFGT 165
Cdd:pfam00370 81 GTVLLDKND-KPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIH----KFLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 166 TDSWLVWNLTgggegGRHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVGTV-----SGQQLLRET 240
Cdd:pfam00370 156 IHDYLRWRLT-----GVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELnpelaAMWGLDEGV 230
|
250
....*....|....*
gi 984924754 241 PITGILGDQHAATFG 255
Cdd:pfam00370 231 PVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
6-438 |
2.28e-83 |
|
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Rhodospirillum rubrum xylulose kinase (RrXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466806 [Multi-domain] Cd Length: 451 Bit Score: 265.54 E-value: 2.28e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGITNQRE 85
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 86 TTVVWDRNtGRPVYNAIVWQDTRTDRLCERLAGDVGADRYKERVGLPLATYFSGPKVAWILENvdgAREAAENGDLIFGT 165
Cdd:cd07804 81 ALVPVDEN-GKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSQSVGPKLLWIKRN---EPEVFKKTRKFLGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 166 TDsWLVWNLTgggegGRHVTDVTNASRTM-LMNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVGTVSGQQ-----LLRE 239
Cdd:cd07804 157 YD-YIVYKLT-----GEYVIDYSSAGNEGgLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEAaeetgLAEG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 240 TPITGILGDQHAATFGQACFEVGQAKNTYGTGNFMLIntgeepVHSDNGLLTTVAYRIGDQKPVYALEGSIAVTGSLIQW 319
Cdd:cd07804 231 TPVVAGTVDAAASALSAGVVEPGDLLLMLGTAGDIGV------VTDKLPTDPRLWLDYHDIPGTYVLNGGMATSGSLLRW 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 320 LRDNLGmigsAPEVETLAAGVGDN---------------GGVYFVPAFSGLFAPHWDAAARGAMVGMTRYVNKGHIARAA 384
Cdd:cd07804 305 FRDEFA----GEEVEAEKSGGDSAydlldeeaekippgsDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRAL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 984924754 385 LEATAFQSREVLDAMNaDSGVDLTELKVDGGMVANELLMQFQADLLRVPVVRPK 438
Cdd:cd07804 381 LEGVAYGLRHHLEVIR-EAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVK 433
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
6-485 |
3.56e-82 |
|
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Chromobacterium violaceum xylulose kinase (CvXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466807 [Multi-domain] Cd Length: 485 Bit Score: 263.23 E-value: 3.56e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGITNQRE 85
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 86 TTVVWDRNtGRPVYNAIVWQDTRTDRLCERLAGDVGADRYKERVGLPL--ATYfSGPKVAWILENvdgAREAAENGDLIF 163
Cdd:cd07805 81 GVVPVDKD-GNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLGGGNPpsGKD-PLAKILWLKEN---EPEIYAKTHKFL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 164 GTTDsWLVWNLTgggegGRHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVGTVSGQQ-----LLR 238
Cdd:cd07805 156 DAKD-YLNFRLT-----GRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAaaelgLPA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 239 ETPITGILGDQHAATFGQACFEVGQAkNTY-GTGNFMLINTgEEPVHSDNGLLTTVAYRIGDQkpvYALEGSIAVTGSLI 317
Cdd:cd07805 230 GTPVVGGGGDAAAAALGAGAVEEGDA-HIYlGTSGWVAAHV-PKPKTDPDHGIFTLASADPGR---YLLAAEQETAGGAL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 318 QWLRDNLGMIGSAP-----EVETLAAGVG-DNGGVYFVPAFSGLFAPHWDAAARGAMVGMTRYVNKGHIARAALEATAFQ 391
Cdd:cd07805 305 EWARDNLGGDEDLGaddyeLLDELAAEAPpGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 392 SREVLDAMNADsGVDLTELKVDGGMVANELLMQFQADLLRVPVVRPKV-IETTALGAAYAAGLAVGFWASQDELVANWEE 470
Cdd:cd07805 385 LRWLLEALEKL-TRKIDELRLVGGGARSDLWCQILADVLGRPVEVPENpQEAGALGAALLAAVGLGLLKSFDEAKALVKV 463
|
490
....*....|....*
gi 984924754 471 DKRWEPtmDEEEAER 485
Cdd:cd07805 464 EKVFEP--DPENRAR 476
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
6-443 |
4.36e-70 |
|
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466790 [Multi-domain] Cd Length: 478 Bit Score: 231.68 E-value: 4.36e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIGEALARAEvtRHDVAAVGITNQRE 85
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLG--GGEVDAIGFSSAMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 86 TTVVWDRNtGRPVYNAIVWQDTRTDRLCERLAGDVGADRYKERVGLPLATYFSGPKVAWIlenvdgareaAENGDLIFGT 165
Cdd:cd07770 79 SLLGVDED-GEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWL----------KEERPELFAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 166 TD------SWLVWNLTgggegGRHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVGTVSGQQ---- 235
Cdd:cd07770 148 AAkfvsikEYLLYRLT-----GELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFaerl 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 236 -LLRETP-ITGIlGDQHAATFGQACFEVGQAKNTYGTgnfmlinTG------EEPVHSDNGLLTTvaYRIGDQKPVYale 307
Cdd:cd07770 223 gLLAGTPvVLGA-SDGALANLGSGALDPGRAALTVGT-------SGairvvsDRPVLDPPGRLWC--YRLDENRWLV--- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 308 GSiAVT--GSLIQWLRDNLGMIGSAPEV-ETLAAGVG-DNGGVYFVPAFSGLFAPHWDAAARGAMVGMTRYVNKGHIARA 383
Cdd:cd07770 290 GG-AINngGNVLDWLRDTLLLSGDDYEElDKLAEAVPpGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRA 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 384 ALEATAFQSREVLDAMnADSGVDLTELKVDGGMVANELLMQFQADLLRVPVVRPKVIETT 443
Cdd:cd07770 369 VLEGVAFNLKSIYEAL-EELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEAS 427
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
6-443 |
2.08e-66 |
|
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466805 [Multi-domain] Cd Length: 444 Bit Score: 220.89 E-value: 2.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGITNQRE 85
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 86 TTVVWDRNtGRPVYNAIVWQDTRTDRLCERLAGDVGADRYKERVGLPLATYFSGPKVAWILENvdgAREAAENGDLIFGT 165
Cdd:cd07802 81 GLYLVDKD-GKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKEN---EPERYDRIRTVLFC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 166 TDsWLVWNLTgggegGRHVTDVTNASrTMLMNLDTLDWNEEICADMGIP--MSMLPEIVSSSAEVGTVSGQQ-----LLR 238
Cdd:cd07802 157 KD-WIRYRLT-----GEISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVTAEAaaltgLPE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 239 ETPITGILGDQHAATFGQACFEVGQAKNTYGT--GNFMLINtgeEPVHSDNGLLtTVAYRIGDQkpVYALEGSIAVTGSL 316
Cdd:cd07802 230 GTPVAAGAFDVVASALGAGAVDEGQLCVILGTwsINEVVTD---EPVVPDSVGS-NSLHADPGL--YLIVEASPTSASNL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 317 iQWLRDNLG------MIGSAPEVETLAAGVG-DNGGVYFVPaFsgLFAPHWDAAARGAMVGMTRYVNKGHIARAALEATA 389
Cdd:cd07802 304 -DWFLDTLLgeekeaGGSDYDELDELIAAVPpGSSGVIFLP-Y--LYGSGANPNARGGFFGLTAWHTRAHLLRAVYEGIA 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 984924754 390 FQSREVLDAMnaDSGVDLTELKVDGGMVANELLMQFQADLLRVPVVRPKVIETT 443
Cdd:cd07802 380 FSHRDHLERL--LVARKPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELG 431
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
6-442 |
8.55e-58 |
|
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466801 [Multi-domain] Cd Length: 429 Bit Score: 197.83 E-value: 8.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIGEALarAEVTRHDVAAVGITNQRE 85
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELP--AELRPRRVVAIAVDGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 86 TTVVWDRNtGRPVYNAIVWQDTRTDRLCERLAGdvGADRYKERVGLPLATYFSGPKVAWILENVDGAREAAEngdLIFGT 165
Cdd:cd07783 79 TLVLVDRE-GEPLRPAIMYNDARAVAEAEELAE--AAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTA---KFLHQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 166 TDsWLVWNLTgggeGGRHVTDVTNASRTMLmNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVGTVSGQ-----QLLRET 240
Cdd:cd07783 153 AD-WLAGRLT----GDRGVTDYNNALKLGY-DPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEaaeelGLPAGT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 241 PItgILG--DQHAATFGQACFEVGQAKNTYGTGN-FMLINtgEEPVHSDNGLLTTvaYRIGDqkPVYALEGSIAVTGSLI 317
Cdd:cd07783 227 PV--VAGttDSIAAFLASGAVRPGDAVTSLGTTLvLKLLS--DKRVPDPGGGVYS--HRHGD--GYWLVGGASNTGGAVL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 318 QWLrdnlgmiGSAPEVETLAAGVGDNG--GVYFVP-AFSGLFAPHWDAAARGAMVgmTRYVNKGHIARAALEATAFQSRE 394
Cdd:cd07783 299 RWF-------FSDDELAELSAQADPPGpsGLIYYPlPLRGERFPFWDPDARGFLL--PRPHDRAEFLRALLEGIAFIERL 369
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 984924754 395 VLDAMNADSGVDLTELKVDGGMVANELLMQFQADLLRVPVVRPKVIET 442
Cdd:cd07783 370 GYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEA 417
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
6-442 |
1.23e-57 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 197.77 E-value: 1.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFD-HSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGITNQR 84
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 85 ETTVVWDRNtGRPVYNAIVWQDTRTDRLCERLAGDVGADrYKERVGLPLATYFSGPKVAWILENvdgAREAAENGDLIFG 164
Cdd:cd07809 81 HGLVALDAD-GKVLRPAKLWCDTRTAPEAEELTEALGGK-KCLLVGLNIPARFTASKLLWLKEN---EPEHYARIAKILL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 165 TTDsWLVWNLTgggegGRHVTDVTNASRTMLMNLDTLDWNEEICA---DMGIPMSMLPEIVSSSAEVGTVS--GQQLL-- 237
Cdd:cd07809 156 PHD-YLNWKLT-----GEKVTGLGDASGTFPIDPRTRDYDAELLAaidPSRDLRDLLPEVLPAGEVAGRLTpeGAEELgl 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 238 -RETPITGILGDQHAATFGQACFEVGQAKNTYGT-GNFMLIntGEEPVHSDNGLLTTVAYRIGDQKPvyalegSIAVTGS 315
Cdd:cd07809 230 pAGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTsGTAYGV--SDKPVSDPHGRVATFCDSTGGMLP------LINTTNC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 316 LIQWLRDNLGMIG-SAPEVETLAAGV-GDNGGVYFVPAFSGLFAPHWdAAARGAMVGMT-RYVNKGHIARAALEATAFQS 392
Cdd:cd07809 302 LTAWTELFRELLGvSYEELDELAAQApPGAGGLLLLPFLNGERTPNL-PHGRASLVGLTlSNFTRANLARAALEGATFGL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 984924754 393 REVLDAMnADSGVDLTELKVDGGMVANELLMQFQADLLRVPVVRPKVIET 442
Cdd:cd07809 381 RYGLDIL-RELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEG 429
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
6-443 |
7.94e-50 |
|
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to Bacillus subtilis sugar kinase YoaC. It is part of the yoaDCB operon and induced by sulfate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466804 [Multi-domain] Cd Length: 448 Bit Score: 177.03 E-value: 7.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRA--GWVEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGITNQ 83
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDypDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 84 RETTVVWDRNtGRPVY---NaivwQDTRTDRLCERLAGDVGADRYKERVGLPLAtYFSGPKVAWILENvdgAREAAENGD 160
Cdd:cd07798 81 REGIVFLDKD-GRELYagpN----IDARGVEEAAEIDDEFGEEIYTTTGHWPTE-LFPAARLLWFKEN---RPEIFERIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 161 LIFGTTDsWLVWNLTGggeggRHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVGTVSGQ-----Q 235
Cdd:cd07798 152 TVLSISD-WIGYRLTG-----ELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEaarelG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 236 LLRETP-ITGiLGDQHAATFGQACFEVGQAKNTYGTgnfmlinTG------EEPVHSDNGLLTTVAYRIGDQkpvYALEG 308
Cdd:cd07798 226 LPEGTPvVVG-GADTQCALLGSGAIEPGDIGIVAGT-------TTpvqmvtDEPIIDPERRLWTGCHLVPGK---WVLES 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 309 SIAVTGSLIQWLRDNLGMIGSAP----EVETLAAGVGDNGgvyfVPAF--SGLFAPHWDAAARGAMVGMT----RYVNKG 378
Cdd:cd07798 295 NAGVTGLNYQWLKELLYGDPEDSyevlEEEASEIPPGANG----VLAFlgPQIFDARLSGLKNGGFLFPTplsaSELTRG 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 984924754 379 HIARAALEATAFQSREVLDAMNADSGVDLTELKVDGGMVANELLMQFQADLLRVPVVRPKVIETT 443
Cdd:cd07798 371 DFARAILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREAS 435
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
264-443 |
4.03e-47 |
|
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.
Pssm-ID: 426979 [Multi-domain] Cd Length: 197 Bit Score: 162.11 E-value: 4.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 264 AKNTYGTGNFMLInTGEEPVHSDNGLLTTvaYRIGDQKPVYALEGSIAVTGSLIQWLRDNLGM---IGSAPEVETLA--- 337
Cdd:pfam02782 1 LAISAGTSSFVLV-ETPEPVLSVHGVWGP--YTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLreeLRDAGNVESLAela 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 338 --AGVGDNGGVYFVPAFSGLFAPHWDAAARGAMVGMTRYVNKGHIARAALEATAFQSREVLDAMNADSGVDLTELKVDGG 415
Cdd:pfam02782 78 alAAVAPAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSGG 157
|
170 180
....*....|....*....|....*...
gi 984924754 416 MVANELLMQFQADLLRVPVVRPKVIETT 443
Cdd:pfam02782 158 GSRNPLLLQLLADALGLPVVVPGPDEAT 185
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
6-442 |
3.62e-41 |
|
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). It catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466971 [Multi-domain] Cd Length: 452 Bit Score: 153.55 E-value: 3.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGITNQRE 85
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 86 TTVVWDRNtGRPVYNAIVWQDTRTDRLCERLAGDVGADRYKERVGLPLATYFSGPKVAWILENvdgAREAAENGDLIFGT 165
Cdd:cd24121 81 GTWLVDED-GRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKEN---EPERLERARTALHC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 166 TDsWLVWNLTgggegGRHVTDVTNASRTMLmNLDTLDWNEEICADMGIP--MSMLPEIVSSSAEVGTVSGQQ-----LLR 238
Cdd:cd24121 157 KD-WLFYKLT-----GEIATDPSDASLTFL-DFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAaaatgLPA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 239 ETPITGILGDQHAATFGQACFEVGQAKNTYGTGNFMLINTgEEPVHSDNGLLTTVAYRIGDQkpvyALEGSIAVTGSL-I 317
Cdd:cd24121 230 GTPVVLGPFDVVATALGSGAIEPGDACSILGTTGVHEVVV-DEPDLEPEGVGYTICLGVPGR----WLRAMANMAGTPnL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 318 QWLRDNLGMIGSA----------PEVETLAAGV--GDNGGVYFvPAFS--GLFAPHWDAAARGAMVGMTRYVNKGHIARA 383
Cdd:cd24121 305 DWFLRELGEVLKEgaepagsdlfQDLEELAASSppGAEGVLYH-PYLSpaGERAPFVNPNARAQFTGLSLEHTRADLLRA 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 984924754 384 ALEATAFQSREVLDAMnadsGVDLTELKVDGGMVANELLMQFQADLLRVPVVRPKVIET 442
Cdd:cd24121 384 VYEGVALAMRDCYEHM----GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEF 438
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
6-443 |
1.07e-38 |
|
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466799 [Multi-domain] Cd Length: 504 Bit Score: 147.68 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFD-HSGAIVSTGQREHEQIF--PRAGWVEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGITN 82
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 83 QRETTVVWDRNtGRPVYNAIVWQDTRTDRLCERLAgdvgadRYKERVGLPLATYFSG--------PKVAWILENVDGARE 154
Cdd:cd07781 81 TSSTVVPVDED-GNPLAPAILWMDHRAQEEAAEIN------ETAHPALEYYLAYYGGvyssewmwPKALWLKRNAPEVYD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 155 AA----ENGDlifgttdsWLVWNLTGggeggRHVTDVTNAS-RTMLMNLDTLdWNEEICADMGIPMS-----MLPEIVSS 224
Cdd:cd07781 154 AAytivEACD--------WINARLTG-----RWVRSRCAAGhKWMYNEWGGG-PPREFLAALDPGLLklrekLPGEVVPV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 225 SAEVGTVSGQQ-----LLRETPITGILGDQHAATFGQACFEVGQAKNTYGTGN-FMLIntGEEPVHSDnGLLTTVayrig 298
Cdd:cd07781 220 GEPAGTLTAEAaerlgLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTcHLMV--SPKPVDIP-GICGPV----- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 299 dQKPV----YALEGSIAVTGSLIQWLRDNLG------MIGSAPEVETLAAGVGdnggvyfvPAFSGLFA---------PH 359
Cdd:cd07781 292 -PDAVvpglYGLEAGQSAVGDIFAWFVRLFVppaeerGDSIYALLSEEAAKLP--------PGESGLVAldwfngnrtPL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 360 WDAAARGAMVGMTRYVNKGHIARAALEATAFQSREVLDAMNaDSGVDLTELKVDGGMVA-NELLMQFQADLLRVPVVRPK 438
Cdd:cd07781 363 VDPRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERFE-EAGVPVNRVVACGGIAEkNPLWMQIYADVLGRPIKVPK 441
|
....*
gi 984924754 439 VIETT 443
Cdd:cd07781 442 SDQAP 446
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
6-443 |
6.43e-36 |
|
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466796 [Multi-domain] Cd Length: 436 Bit Score: 138.51 E-value: 6.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFD-HSGAIVSTGQREHEQIFP--RAGWVEHDPVEIWTNTREVIGEALARAevtRHDVAAVGITN 82
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDlESGRILESVSRPTPAPISsdDPGRSEQDPEKILEAVRNLIDELPREY---LSDVTGIGITG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 83 QRETTVVWDRNtGRPVYNAIVWQDTRTDR-LCERLAGDVGADRYKE----RVGLPLATYFsgpkvaWILENvdgaREAAE 157
Cdd:cd07777 78 QMHGIVLWDED-GNPVSPLITWQDQRCSEeFLGGLSTYGEELLPKSgmrlKPGYGLATLF------WLLRN----GPLPS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 158 NGDlIFGTTDSWLVWNLTGGGEggrHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVGTVSgQQLL 237
Cdd:cd07777 147 KAD-RAGTIGDYIVARLTGLPK---PVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLS-SALP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 238 RETPITGILGDQHAATFGQACFEVGQAKNTYGTGN--FMLINTGEEPVH------SDNGLLTTVAyrigdqkpvyALEG- 308
Cdd:cd07777 222 KGIPVYVALGDNQASVLGSGLNEENDAVLNIGTGAqlSFLTPKFELSGSveirpfFDGRYLLVAA----------SLPGg 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 309 -SIAVtgsLIQWLRDNLGMIGSAPEVETL------AAGVGDNGGVYFVPAFSGLFaphWDAAARGAMVGMTRY-VNKGHI 380
Cdd:cd07777 292 rALAV---LVDFLREWLRELGGSLSDDEIwekldeLAESEESSDLSVDPTFFGER---HDPEGRGSITNIGESnFTLGNL 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 984924754 381 ARAALEATAfqsREVLDAMnadSGVDLTELKVD------GGMVANELLMQFQADLLRVPVVRPKVIETT 443
Cdd:cd07777 366 FRALCRGIA---ENLHEML---PRLDLDLSGIErivgsgGALRKNPVLRRIIEKRFGLPVVLSEGSEEA 428
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
6-475 |
3.46e-30 |
|
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466794 [Multi-domain] Cd Length: 492 Bit Score: 123.21 E-value: 3.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIVSTGQRE--HEQIFPRAGWVEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGITNQ 83
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREwrHKEVPDVPGSMDFDTEKNWKLICECIREALKKAGIAPKSIAAISTTSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 84 RETTVVWDRNtGRPVYnAIVWQDTRTDRLCERL-AGDVGADRYKERVGLPLATYFSGPKVAWILENV-DGAREAAEngdl 161
Cdd:cd07775 81 REGIVLYDNE-GEEIW-ACANVDARAAEEVSELkELYNTLEEEVYRISGQTFALGAIPRLLWLKNNRpEIYRKAAK---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 162 iFGTTDSWLVWNLTGggeggRHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVGTVSGQ-----QL 236
Cdd:cd07775 155 -ITMLSDWIAYKLSG-----ELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEaaeetGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 237 LRETPITGILGDQHAATFGQACFEVGQAKNTYGTGNFMLINTgEEPVHSDNGLLTTVAYRIGDqkpVYALEGSIAVTGSL 316
Cdd:cd07775 229 KEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNT-AAPVTDPAMNIRVNCHVIPD---MWQAEGISFFPGLV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 317 IQWLRDNLGmigsAPEVEtLAAGVGDNG-------------GVY-FVPAFSGLF-APHWDAAARgAMVGMT----RYvNK 377
Cdd:cd07775 305 MRWFRDAFC----AEEKE-IAERLGIDAydlleemakdvppGSYgIMPIFSDVMnYKNWRHAAP-SFLNLDidpeKC-NK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 378 GHIARAALEATAFQSREVLDAMNADSGVDLTELKVDGGMVANELLMQFQADLLRVPVVRPKVIETTALGAAYAAGLAVGF 457
Cdd:cd07775 378 ATFFRAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAGI 457
|
490
....*....|....*...
gi 984924754 458 WASQDELVANWeedKRWE 475
Cdd:cd07775 458 YSSLEEAVESL---VKWE 472
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
8-429 |
1.39e-24 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 106.59 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 8 MAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIgEALARAEVTRhDVAAVGITNQRETT 87
Cdd:PRK15027 3 IGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAM-KALGDQHSLQ-DVKALGIAGQMHGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 88 VVWDRNTG--RPvynAIVWQDTRTDRLCERLAGDVGADRykERVGLPLATYFSGPKVAWIlenvdgAREAAEngdlIFGT 165
Cdd:PRK15027 81 TLLDAQQRvlRP---AILWNDGRCAQECALLEARVPQSR--VITGNLMMPGFTAPKLLWV------QRHEPE----IFRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 166 TDS------WLVWNLTGggeggRHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVGT----VSGQQ 235
Cdd:PRK15027 146 IDKvllpkdYLRLRMTG-----EFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGAllpeVAKAW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 236 LLRETPITGILGDQHAATFGQACFEVGQAKNTYGT-GNFMLINTG-----EEPVHSdngLLTTVAYRigdqkpvYALEGS 309
Cdd:PRK15027 221 GMATVPVVAGGGDNAAGAVGVGMVDANQAMLSLGTsGVYFAVSEGflskpESAVHS---FCHALPQR-------WHLMSV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 310 IAVTGSLIQWLRDNLGMiGSAPEVETLAAGVGDNGG-VYFVPAFSGLFAPHWDAAARGAMVGMTRYVNKGHIARAALEAT 388
Cdd:PRK15027 291 MLSAASCLDWAAKLTGL-SNVPALIAAAQQADESAEpVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGV 369
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 984924754 389 AFQSREVLDAMNAdSGVDLTELKVDGGMVANELLMQFQADL 429
Cdd:PRK15027 370 GYALADGMDVVHA-CGIKPQSVTLIGGGARSEYWRQMLADI 409
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
6-442 |
1.48e-21 |
|
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.
Pssm-ID: 466800 [Multi-domain] Cd Length: 540 Bit Score: 97.99 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFPRAGWVEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGITnqre 85
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 86 TT---VVWDRN--------TGRPVYNAIVWQDTRTDRLCERLAgdvgadrykeRVGLPLATYFSG--------PKVAWIL 146
Cdd:cd07782 77 ATcslVVLDAEgkpvsvspSGDDERNVILWMDHRAVEEAERIN----------ATGHEVLKYVGGkispemepPKLLWLK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 147 ENVdgaREAAENGDLIFGTTDsWLVWNLTGGGEggRHVTDVTNASRTMLMNLDTLDWNEEICADMGipmsmLPEIV---- 222
Cdd:cd07782 147 ENL---PETWAKAGHFFDLPD-FLTWKATGSLT--RSLCSLVCKWTYLAHEGSEGGWDDDFFKEIG-----LEDLVednf 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 223 ----SSSAEVGTVSGQQL---------LRE-TPI-TGILgDQHAATFGQACFEVGQAKNTY-----------GTGN-FML 275
Cdd:cd07782 216 akigSVVLPPGEPVGGGLtaeaakelgLPEgTPVgVSLI-DAHAGGLGTLGADVGGLPCEAdpltrrlalicGTSScHMA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 276 INtgEEPVHSDN-----------GLlttvayrigdqkpvYALEGSIAVTGSLIQWlrdnlgMIGS---APEVETLAAGVG 341
Cdd:cd07782 295 VS--PEPVFVPGvwgpyysamlpGL--------------WLNEGGQSATGALLDH------IIEThpaYPELKEEAKAAG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 342 DN------------------------GGVYFVPAFSGLFAPHWDAAARGAMVGMTRYVNKGHIAR---AALEATAFQSRE 394
Cdd:cd07782 353 KSiyeylnerleqlaeekglplayltRDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRH 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 984924754 395 VLDAMNAdSGVDLTELKVDGGMVANELLMQFQADLLRVPVVRPKVIET 442
Cdd:cd07782 433 IIEAMNA-AGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEA 479
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
6-442 |
2.50e-20 |
|
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466788 [Multi-domain] Cd Length: 522 Bit Score: 93.84 E-value: 2.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHS-GAIVSTGQREHEQ-IFPRAGWVEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGItNQ 83
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDLYaGLEMAQEPVPYYQdSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGV-DA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 84 RETTVVWDRN--------TGRPVYNAIVWQDTRTDRLCERLaGDVGADRYKERVGLPLATYFSGPKVAWILenvDGAREA 155
Cdd:cd07768 80 TCSLAIFDREgtplmaliPYPNEDNVIFWMDHSAVNEAQWI-NMQCPQQLLDYLGGKISPEMGVPKLKYFL---DEYSHL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 156 AENGDLIFGTTDsWLVWNLTGG------GEGGRHVTD--VTNASRTMLMNLDTLDWNEEicadmgiPMSMLPEIVSSSAE 227
Cdd:cd07768 156 RDKHFHIFDLHD-YIAYELTRLyewnicGLLGKENLDgeESGWSSSFFKNIDPRLEHLT-------TTKNLPSNVPIGTT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 228 VGTVSGQQLLRETPITGI-----LGDQHAATFGqacfeVGQAKntYGTGNFMLINTGeepvhSDNGLLTTVAYRI-GDQK 301
Cdd:cd07768 228 SGVALPEMAEKMGLHPGTavvvsCIDAHASWFA-----VASPH--LETSLFMIAGTS-----SCHMYGTTISDRIpGVWG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 302 PVYAL--------EGSIAVTGSLIQWLrdnlgmIGSAPEVETLAAGVGDNGGVYFV---------------------PAF 352
Cdd:cd07768 296 PFDTIidpdysvyEAGQSATGKLIEHL------FESHPCARKFDEALKKGADIYQVleqtirqieknnglsihiltlDMF 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 353 SGLFAPHWDAAARGAMVGM---TRYVNKGHIARAALEATAFQSREVLDAMNADsGVDLTELKVDGGMVANELLMQFQADL 429
Cdd:cd07768 370 FGNRSEFADPRLKGSFIGEsldTSMLNLTYKYIAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKNERLLQLIALV 448
|
490
....*....|...
gi 984924754 430 LRVPVVRPKVIET 442
Cdd:cd07768 449 TNVAIIKPKENMM 461
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
6-435 |
3.19e-20 |
|
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.
Pssm-ID: 466791 [Multi-domain] Cd Length: 460 Bit Score: 93.36 E-value: 3.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAIL---------------FDHsgAIVSTGQREHeqifpragWvehDPVEIWTNTREVIGEALARAEv 70
Cdd:cd07771 1 NYLAVDLGASSGRVILgsldggkleleeihrFPN--RPVEINGHLY--------W---DIDRLFDEIKEGLKKAAEQGG- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 71 trhDVAAVGITnqretTvvW-------DRNtGRPVYNAIVWQDTRTDRLCERLAGDVGADRYKERVGLPLATYFSGPKVA 143
Cdd:cd07771 67 ---DIDSIGID-----T--WgvdfgllDKN-GELLGNPVHYRDPRTEGMMEELFEKISKEELYERTGIQFQPINTLYQLY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 144 WIlenvdgareaAENGDLIFGTTDSWL------VWNLTGggeggRHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSM 217
Cdd:cd07771 136 AL----------KKEGPELLERADKLLmlpdllNYLLTG-----EKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 218 LPEIVSSSAEVGTVSGqQLLRETPITG---ILGDQH---AATFGQACFEvgqakntygtGNFMLINTG---------EEP 282
Cdd:cd07771 201 FPPIVPPGTVLGTLKP-EVAEELGLKGipvIAVASHdtaSAVAAVPAED----------EDAAFISSGtwsligvelDEP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 283 VhsdnglLTTVAYRIGdqkpvYALEGSIA--------VTG-SLIQWLRDNLGMIGSAPEVETLAAGVGDnggvyfVPAFS 353
Cdd:cd07771 270 V------ITEEAFEAG-----FTNEGGADgtirllknITGlWLLQECRREWEEEGKDYSYDELVALAEE------APPFG 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 354 GLFAP-HWDAAARGAMV----------GMTRYVNKGHIARAALEATAFQSREVLDAMNADSGVDLTELKVDGGMVANELL 422
Cdd:cd07771 333 AFIDPdDPRFLNPGDMPeairaycretGQPVPESPGEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALL 412
|
490
....*....|...
gi 984924754 423 MQFQADLLRVPVV 435
Cdd:cd07771 413 CQLTADATGLPVI 425
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
6-502 |
5.73e-20 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 92.76 E-value: 5.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIVSTGQRE--H--EQIFPraGWVEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGIT 81
Cdd:PRK10939 4 YLMALDAGTGSIRAVIFDLNGNQIAVGQAEwrHlaVPDVP--GSMEFDLEKNWQLACQCIRQALQKAGIPASDIAAVSAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 82 NQRETTVVWDRNtGRPVYnAIVWQDTRTD---RLCERLAGDVGADRYKErvglplatyfSG--------PKVAWILENV- 149
Cdd:PRK10939 82 SMREGIVLYDRN-GTEIW-ACANVDARASrevSELKELHNNFEEEVYRC----------SGqtlalgalPRLLWLAHHRp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 150 DGAREAAEngdliFGTTDSWLVWNLTgggegGRHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSMLPEIVsssaEVG 229
Cdd:PRK10939 150 DIYRQAHT-----ITMISDWIAYMLS-----GELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVK----ETG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 230 TVSGQ---------QLLRETPITGILGDQHAATFGQACFEVGQAKNTYGTGNFMLINTGEEPVHSDNGLlttvayRIGDQ 300
Cdd:PRK10939 216 TVLGHvtakaaaetGLRAGTPVVMGGGDVQLGCLGLGVVRPGQTAVLGGTFWQQVVNLPAPVTDPNMNI------RINPH 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 301 --KPVYALEGSIAVTGSLIQWLRD-----------NLGMigSAPEV-ETLAAGV--GDNGgvyFVPAFSGLF-------- 356
Cdd:PRK10939 290 viPGMVQAESISFFTGLTMRWFRDafcaeekllaeRLGI--DAYSLlEEMASRVpvGSHG---IIPIFSDVMrfkswyha 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 357 APHW-----DAAArgamvgmtryVNKGHIARAALEATAFQSREVLDAMNADSGVDLTELKVDGGMVANELLMQFQADLLR 431
Cdd:PRK10939 365 APSFinlsiDPEK----------CNKATLFRALEENAAIVSACNLQQIAAFSGVFPSSLVFAGGGSKGKLWSQILADVTG 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 984924754 432 VPVVRPKVIETTALGAAYAAGLAVGFWASQDELVANW-EEDKRWEPTMDEEEAERALR-LWKKAVERSRDWVD 502
Cdd:PRK10939 435 LPVKVPVVKEATALGCAIAAGVGAGIYSSLAETGERLvRWERTFEPNPENHELYQEAKeKWQAVYADQLGLVD 507
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
5-442 |
1.35e-18 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 88.63 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 5 RYVMAIDQGTTSTRAILFD-HSGAIVSTGQRE----HEQIF--PRAGWVEHDPVEIWTNTREVIGEALARAEVTRHDVAA 77
Cdd:COG1069 2 KYVIGVDFGTDSVRAVVVDaADGEELASAVHPyprwVIGLYlpPPPDQARQHPLDYLEALEAAVREALAQAGVDPADVVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 78 VGItnqrETT----VVWDRN----------TGRPVYNAIVWQDTR----TDRLcERLAGDVGADrYKERVGlplATYFSG 139
Cdd:COG1069 82 IGV----DATgctpVPVDADgtplallpefAENPHAMVILWKDHTaqeeAERI-NELAKARGED-YLRYVG---GIISSE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 140 ---PKVAWILENvdgAREAAENGDLIFGTTDsWLVWNLTGggeggrhvtdvtnasrTMLMNLDTL--------DWN---- 204
Cdd:COG1069 153 wfwPKILHLLRE---DPEVYEAADSFVELCD-WITWQLTG----------------SLKRSRCTAghkalwhaHEGgyps 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 205 EEICADMGIPMSMLP-----EIVSSSAEVGTVSGQQ-----LLRETPI-TGILgDQHAATFGqacfeVGQAKNTY----- 268
Cdd:COG1069 213 EEFFAALDPLLDGLAdrlgtEIYPLGEPAGTLTAEWaarlgLPPGTAVaVGAI-DAHAGAVG-----AGGVEPGTlvkvm 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 269 GTGNFMLINTGEE--------PVhsDNGLLttvayrigdqkP-VYALEGSIAVTGSLIQWLRDNLGmigSAPEVETLAAG 339
Cdd:COG1069 287 GTSTCHMLVSPEErfvpgicgQV--DGSIV-----------PgMWGYEAGQSAVGDIFAWFVRLLV---PPLEYEKEAEE 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 340 VGDN----------------GGVYFVPAFSGLFAPHWDAAARGAMVGMTRYVNKGHIARAALEATAFQSREVLDAMNAdS 403
Cdd:COG1069 351 RGISlhpllteeaaklppgeSGLHALDWFNGNRSPLADQRLKGVILGLTLGTDAEDIYRALVEATAFGTRAIIERFEE-E 429
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 984924754 404 GVDLTELKVDGG-MVANELLMQFQADLLRVPVvrpKVIET 442
Cdd:COG1069 430 GVPIDEIIACGGiATKNPLVMQIYADVTGRPI---KVAAS 466
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
6-463 |
2.81e-16 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 81.23 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIV-STGQREHEQIFPR-AGWVEHDPVEIWTNTREVIGEALAraEVTRHDVAAVGITNQ 83
Cdd:PRK10331 3 VILVLDCGATNVRAIAVDRQGKIVaRASTPNASDIAAEnSDWHQWSLDAILQRFADCCRQINS--ELTECHIRGITVTTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 84 RETTVVWDRNtGRPVYNAIVWQDTRTDRLCERLAGDVGADRYKERVGLPLATYFSGPKVAWILENVDGAREAAENGDLIf 163
Cdd:PRK10331 81 GVDGALVDKQ-GNLLYPIISWKCPRTAAVMENIERYISAQQLQQISGVGAFSFNTLYKLVWLKENHPQLLEQAHAWLFI- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 164 gttDSWLVWNLTGggeggRHVTDVTNASRTMLMNLDTLDWNEEICADMGIPMSMLPEIVSSSAEVGTVS---GQQLLRET 240
Cdd:PRK10331 159 ---SSLINHRLTG-----EFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQpsaAALLGLPV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 241 PITgILGDQHAATFgqACFEVGQAKN----TYGTGNFMLINTGE-----EPVHSdnGLLTTVAYRIGDQKPvyaleGSIA 311
Cdd:PRK10331 231 GIP-VISAGHDTQF--ALFGSGAGQNqpvlSSGTWEILMVRSAQvdtslLSQYA--GSTCELDSQSGLYNP-----GMQW 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 312 VTGSLIQWLRDNL--------GMIGSAPEVETLAAGVGdnggvyfvpafsglFAPHWDAAARGAMVGMTRYVNKGHIARA 383
Cdd:PRK10331 301 LASGVLEWVRKLFwtaetpyqTMIEEARAIPPGADGVK--------------MQCDLLACQNAGWQGVTLNTTRGHFYRA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 384 ALEATAFQSREVLDAMNADSGVDLTELKVDGGMVANELLMQFQADLLRVPVVRPKVIETTALGAAYAAGLAVGFWASQDE 463
Cdd:PRK10331 367 ALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQ 446
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
6-434 |
7.50e-07 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 51.77 E-value: 7.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFD-HSGAIVSTGQREH------EQIFPRAGWVEHDPVEIWTNTREVIGEALARAEVTRHDVAAV 78
Cdd:PRK04123 4 YVIGLDFGTDSVRALLVDcATGEELATAVVEYphwvkgRYLDLPPNQALQHPLDYIESLEAAIPAVLKEAGVDPAAVVGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 79 GITNQRETTVVWDRNtGRPVY---------NAIV--WQDTRT----DRLcERLAgdvgadryKERVGLPLATYFSG---- 139
Cdd:PRK04123 84 GVDFTGSTPAPVDAD-GTPLAllpefaenpHAMVklWKDHTAqeeaEEI-NRLA--------HERGEADLSRYIGGiyss 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 140 ----PKVAWILENVDGAREAA----ENGDlifgttdsWLVWNLTGGGEGGRHVTDVTNA--------------SRTMLMN 197
Cdd:PRK04123 154 ewfwAKILHVLREDPAVYEAAaswvEACD--------WVVALLTGTTDPQDIVRSRCAAghkalwheswgglpSADFFDA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 198 LDTLdwneeicADMGIPMSMLPEIVSSSAEVGTVSGQQ-----LLRETPITGILGDQHAATFGQACfEVGQAKNTYGTGN 272
Cdd:PRK04123 226 LDPL-------LARGLRDKLFTETWTAGEPAGTLTAEWaqrlgLPEGVAVSVGAFDAHMGAVGAGA-EPGTLVKVMGTST 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 273 -FMLINTGEEPVHS-----DNGLLttvayrigdqkP-VYALEGSIAVTGSLIQWLRDNLgmigSAPEVETLAAGVGDNGG 345
Cdd:PRK04123 298 cDILLADKQRAVPGicgqvDGSIV-----------PgLIGYEAGQSAVGDIFAWFARLL----VPPEYKDEAEARGKQLL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 346 VYF-------VPAFSGLFAPHW---------DAAARGAMVGMTRYVNKGHIARAALEATAFQSREVLDAMNaDSGVDLTE 409
Cdd:PRK04123 363 ELLteaaakqPPGEHGLVALDWfngrrtplaDQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFE-DQGVPVEE 441
|
490 500
....*....|....*....|....*.
gi 984924754 410 LKVDGGM-VANELLMQFQADLLRVPV 434
Cdd:PRK04123 442 VIAAGGIaRKNPVLMQIYADVLNRPI 467
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
5-80 |
1.65e-05 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 46.81 E-value: 1.65e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 984924754 5 RYVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQifpragwvEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGI 80
Cdd:COG1940 5 GYVIGIDIGGTKIKAALVDLDGEVLARERIPTPA--------GAGPEAVLEAIAELIEELLAEAGISRGRILGIGI 72
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
10-150 |
2.54e-04 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466797 [Multi-domain] Cd Length: 544 Bit Score: 43.55 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 10 IDQGTTSTRAILFDHSGAIVSTGQRE-HEQIFPRAGW-VEHDPVEIWTNTREVIGEALARAEVTRHDVAAVGIT------ 81
Cdd:cd07778 5 IDVGSTSVRIGIFDYHGTLLATSERPiSYKQDPKDLWfVTQSSTEIWKAIKTALKELIEELSDYIVSGIGVSATcsmvvm 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 82 NQRETTVVW-----DRNTGRPVYNAIVWQDTRTDRLCERLAGDVGADrykervglplATYFSG---------PKVAWILE 147
Cdd:cd07778 85 QRDSDTSYLvpynvIHEKSNPDQDIIFWMDHRASEETQWLNNILPDD----------ILDYLGggfipemaiPKLKYLID 154
|
...
gi 984924754 148 NVD 150
Cdd:cd07778 155 LIK 157
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
5-80 |
2.93e-04 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 42.95 E-value: 2.93e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 984924754 5 RYVMAIDQGTTSTRAILFDHSGAIVSTGQReheqifPRAGWVEHDPVEIWTNTREVIGEALARAEvTRHDVAAVGI 80
Cdd:COG2971 1 PYILGVDGGGTKTRAVLVDADGEVLGRGRA------GGANPQSVGLEEALASLREALEEALAAAG-DPADIEAVGF 69
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
6-233 |
5.11e-04 |
|
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466795 [Multi-domain] Cd Length: 514 Bit Score: 42.54 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 6 YVMAIDQGTTSTRAILFDHSGAIVSTGQREHEQIFP----RAGWVEH-DPVEIWTNTR------EVIGEALARAEVTRHD 74
Cdd:cd07776 1 LYLGLDLSTQSLKAVVIDSDLKVVAEESVNFDSDLPeygtKGGVHRDgDGGEVTSPVLmwvealDLLLEKLKAAGFDFSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 75 VAAVGITNQRETTVVWDR---------NTGRPVYNAI----------VWQDTRTDRLCERLAgdvgadrykERVGLPLAT 135
Cdd:cd07776 81 VKAISGSGQQHGSVYWSKgaesalanlDPSKSLAEQLegafsvpdspIWMDSSTTKQCRELE---------KAVGGPEAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984924754 136 Y----------FSGPKVAWILENVDGAREAAENGDLI--FGTtdSWLVwnltgggegGRHV-TDVTNASRTMLMNLDTLD 202
Cdd:cd07776 152 AkltgsrayerFTGPQIAKIAQTDPEAYENTERISLVssFLA--SLLL---------GRYApIDESDGSGMNLMDIRSRK 220
|
250 260 270
....*....|....*....|....*....|...
gi 984924754 203 WNEEICADMGIP--MSMLPEIVSSSAEVGTVSG 233
Cdd:cd07776 221 WSPELLDAATAPdlKEKLGELVPSSTVAGGISS 253
|
|
| ASKHA_NBD_eukNAGK-like |
cd24007 |
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ... |
7-80 |
4.26e-03 |
|
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) family; The eukaryotic-type NAGK-like family includes a group of proteins similar to eukaryotic N-acetyl-D-glucosamine kinases, such as Vibrio cholerae glucosamine kinase GspK, Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK), Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase (KdgK) and Clostridium acetobutylicum N-acetylmuramic acid/N-acetylglucosamine kinase (MurK). NAGK (EC 2.7.1.59), also called GlcNAc kinase, converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. It is involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. NAGK also has ManNAc kinase activity. GspK (EC 2.7.1.8), also called GlcN kinase, acts as ATP-dependent kinase, which is specific for glucosamine. StHK is a novel hexokinase that can phosphorylate not only glucose but also GlcNAc, glucosamine, and mannose. KdgK (EC 2.7.1.45), also called 2-keto-3-deoxy-D-gluconate kinase, or KDG kinase, catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). It is specific for KDG. MurK (EC 2.7.1.-/EC 2.7.1.59), also known MurNAc/GlcNAc kinase, or murein sugar kinase, catalyzes the ATP-dependent phosphorylation of both cell wall (peptidoglycan) amino sugars, N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), at the 6-hydroxyl group. The eukaryotic-type N-acetylglucosamine kinase (NAGK) family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466857 [Multi-domain] Cd Length: 295 Bit Score: 39.21 E-value: 4.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 984924754 7 VMAIDQGTTSTRAILFDHSGAIVSTGQReheqifPRAGWVEHDPVEIWTNTREVIGEALARAEvTRHDVAAVGI 80
Cdd:cd24007 1 VLGVDGGGTKTRAVLADEDGKILGRGKG------GPSNPASVGIEEAKENLKEAVREALSQAG-SLGEIDAICL 67
|
|
| |
