|
Name |
Accession |
Description |
Interval |
E-value |
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
4-502 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 977.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 4 EKFVLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAEINRHNLAAVGITNQ 83
Cdd:COG0554 2 KKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITNQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 84 RETTVVWDKNTGEPVYNAIVWQDMRTSDIVKELEGDEGPDRFRQICGLGLSPYFSGSKIKWILDNVEGARERAEAGDLYF 163
Cdd:COG0554 82 RETTVVWDRKTGKPLYNAIVWQDRRTADICEELKADGLEDLIREKTGLVLDPYFSATKIKWILDNVPGARERAEAGELLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 164 GNTDSWVLWNLTGGvngGVHCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYGYGRKNGLLIDTPIA 243
Cdd:COG0554 162 GTIDSWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDPDLFGAEIPIA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 244 GILGDQQAATFGQACFEKGMAKNTYGTGCFMLMNTGTEPVFSDNGLLTTVAYKIGEQPaVYALEGSIAVAGSLVQWLRDN 323
Cdd:COG0554 239 GIAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGGKV-TYALEGSIFVAGAAVQWLRDG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 324 LGMIVKSSDIGELASTVEDNGGVYFVPAFSGLFAPYWRSDARGAIVGLTRYVNKGHIARAVEESTAFQSAEVLDAMNADA 403
Cdd:COG0554 318 LGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 404 GVPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAAGMAVGYWSGTDDVVANWQEGKRWTPSMEPAER 483
Cdd:COG0554 398 GIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEELAALWKVDRRFEPQMDEEER 477
|
490
....*....|....*....
gi 512630313 484 DRTYRLWKKAVTRTLDWVD 502
Cdd:COG0554 478 ERLYAGWKKAVERTLGWAE 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: 931.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 6 FVLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAEINRHNLAAVGITNQRE 85
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 86 TTVVWDKNTGEPVYNAIVWQDMRTSDIVKELEGDEGPDRFRQICGLGLSPYFSGSKIKWILDNVEGARERAEAGDLYFGN 165
Cdd:cd07769 81 TTVVWDKKTGKPLYNAIVWQDRRTADICEELKAKGLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAERGELLFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 166 TDSWVLWNLTGGvngGVHCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYGYGRKNGLLIDTPIAGI 245
Cdd:cd07769 161 IDTWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTDPEGLGAGIPIAGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 246 LGDQQAATFGQACFEKGMAKNTYGTGCFMLMNTGTEPVFSDNGLLTTVAYKIGEQPaVYALEGSIAVAGSLVQWLRDNLG 325
Cdd:cd07769 238 LGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQIGGKV-TYALEGSIFIAGAAIQWLRDNLG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 326 MIVKSSDIGELASTVEDNGGVYFVPAFSGLFAPYWRSDARGAIVGLTRYVNKGHIARAVEESTAFQSAEVLDAMNADAGV 405
Cdd:cd07769 317 LIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDSGI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 406 PLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAAGMAVGYWSGTDDVVANWQEGKRWTPSMEPAERDR 485
Cdd:cd07769 397 KLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDELASLWQVDKRFEPSMDEEERER 476
|
490
....*....|
gi 512630313 486 TYRLWKKAVT 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: 930.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 1 MTTEKFVLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAEINRHNLAAVGI 80
Cdd:PRK00047 1 MMMKKYILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 81 TNQRETTVVWDKNTGEPVYNAIVWQDMRTSDIVKELEGDEGPDRFRQICGLGLSPYFSGSKIKWILDNVEGARERAEAGD 160
Cdd:PRK00047 81 TNQRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRDGYEDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 161 LYFGNTDSWVLWNLTGGvngGVHCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYGYGRKNG-LLID 239
Cdd:PRK00047 161 LLFGTIDTWLVWKLTGG---KVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYGfFGGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 240 TPIAGILGDQQAATFGQACFEKGMAKNTYGTGCFMLMNTGTEPVFSDNGLLTTVAYKIGEQPaVYALEGSIAVAGSLVQW 319
Cdd:PRK00047 238 VPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGIDGKV-VYALEGSIFVAGSAIQW 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 320 LRDNLGMIVKSSDIGELASTVEDNGGVYFVPAFSGLFAPYWRSDARGAIVGLTRYVNKGHIARAVEESTAFQSAEVLDAM 399
Cdd:PRK00047 317 LRDGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDAM 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 400 NADAGVPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAAGMAVGYWSGTDDVVANWQEGKRWTPSME 479
Cdd:PRK00047 397 QADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDELKEQWKIDRRFEPQMD 476
|
490 500
....*....|....*....|..
gi 512630313 480 PAERDRTYRLWKKAVTRTLDWV 501
Cdd:PRK00047 477 EEEREKLYAGWKKAVKRTLAWA 498
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
5-497 |
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: 867.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 5 KFVLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAE---INRHNLAAVGIT 81
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLKalgISPSDIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 82 NQRETTVVWDKNTGEPVYNAIVWQDMRTSDIVKELEGDE--GPDRFRQICGLGLSPYFSGSKIKWILDNVEGARERAEAG 159
Cdd:cd07792 81 NQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELSAKTpgGKDHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 160 DLYFGNTDSWVLWNLTGGVNGGVHCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYGYgRKNGLLID 239
Cdd:cd07792 161 RLLFGTVDSWLIWNLTGGKNGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGK-IASGPLAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 240 TPIAGILGDQQAATFGQACFEKGMAKNTYGTGCFMLMNTGTEPVFSDNGLLTTVAYKIG-EQPAVYALEGSIAVAGSLVQ 318
Cdd:cd07792 240 VPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAYKLGpDAPPVYALEGSIAIAGAAVQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 319 WLRDNLGMIVKSSDIGELASTVEDNGGVYFVPAFSGLFAPYWRSDARGAIVGLTRYVNKGHIARAVEESTAFQSAEVLDA 398
Cdd:cd07792 320 WLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREILDA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 399 MNADAGVPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAAGMAVGYWSGTDDVVA-NWQEGKRWTPS 477
Cdd:cd07792 400 MNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSlNEGGRTVFEPQ 479
|
490 500
....*....|....*....|
gi 512630313 478 MEPAERDRTYRLWKKAVTRT 497
Cdd:cd07792 480 ISEEERERRYKRWKKAVERS 499
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
5-500 |
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: 861.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 5 KFVLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAEINRHNLAAVGITNQR 84
Cdd:TIGR01311 1 PYILAIDQGTTSSRAIVFDKDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAGIKPDDIAAIGITNQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 85 ETTVVWDKNTGEPVYNAIVWQDMRTSDIVKELEGDEGPDRFRQICGLGLSPYFSGSKIKWILDNVEGARERAEAGDLYFG 164
Cdd:TIGR01311 81 ETTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYGEFIREKTGLPLDPYFSATKLRWLLDNVPGVREAAERGELLFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 165 NTDSWVLWNLTGGvngGVHCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYGYGRKNGLLIDTPIAG 244
Cdd:TIGR01311 161 TIDTWLIWNLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYTDPGLLGAEIPITG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 245 ILGDQQAATFGQACFEKGMAKNTYGTGCFMLMNTGTEPVFSDNGLLTTVAYKIGEQPAVYALEGSIAVAGSLVQWLRDNL 324
Cdd:TIGR01311 238 VLGDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKKPVYALEGSVFVAGAAVQWLRDNL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 325 GMIVKSSDIGELASTVEDNGGVYFVPAFSGLFAPYWRSDARGAIVGLTRYVNKGHIARAVEESTAFQSAEVLDAMNADAG 404
Cdd:TIGR01311 318 KLIKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTRDVLEAMEKDAG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 405 VPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAAGMAVGYWSGTDDVVANWQEGKRWTPSMEPAERD 484
Cdd:TIGR01311 398 VEITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWRVEKTFEPEMDEEERE 477
|
490
....*....|....*.
gi 512630313 485 RTYRLWKKAVTRTLDW 500
Cdd:TIGR01311 478 ARYAGWKEAVKRSLGW 493
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
6-494 |
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: 858.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 6 FVLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAEINRHNLAAVGITNQRE 85
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 86 TTVVWDKNTGEPVYNAIVWQDMRTSDIVKEL--EGDEgpDRFRQICGLGLSPYFSGSKIKWILDNVEGARERAEAGDLYF 163
Cdd:cd07786 81 TTVVWDRETGKPVYNAIVWQDRRTADICEELkaEGHE--EMIREKTGLVLDPYFSATKIRWILDNVPGARERAERGELAF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 164 GNTDSWVLWNLTGGvngGVHCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYGYGRKNGLLIDTPIA 243
Cdd:cd07786 159 GTIDSWLIWKLTGG---KVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDPDLLGAEIPIA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 244 GILGDQQAATFGQACFEKGMAKNTYGTGCFMLMNTGTEPVFSDNGLLTTVAYKIGEQPaVYALEGSIAVAGSLVQWLRDN 323
Cdd:cd07786 236 GIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLGGKV-TYALEGSIFIAGAAVQWLRDG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 324 LGMIVKSSDIGELASTVEDNGGVYFVPAFSGLFAPYWRSDARGAIVGLTRYVNKGHIARAVEESTAFQSAEVLDAMNADA 403
Cdd:cd07786 315 LGLIESAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEADS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 404 GVPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAAGMAVGYWSGTDDVVANWQEGKRWTPSMEPAER 483
Cdd:cd07786 395 GIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAKLWQVDRRFEPSMSEEER 474
|
490
....*....|.
gi 512630313 484 DRTYRLWKKAV 494
Cdd:cd07786 475 EALYAGWKKAV 485
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
6-504 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 756.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 6 FVLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAEINRHN----LAAVGIT 81
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGHNvdsgLKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 82 NQRETTVVWDKNTGEPVYNAIVWQDMRTSDIVKELEGD--EGPDRFRQICGLGLSPYFSGSKIKWILDNVEGARERAEAG 159
Cdd:PLN02295 81 NQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKElsGGRKHFVETCGLPISTYFSATKLLWLLENVDAVKEAVKSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 160 DLYFGNTDSWVLWNLTGGVNGGVHCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYGYGRKNGLLID 239
Cdd:PLN02295 161 DALFGTIDSWLIWNLTGGASGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIAKGWPLAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 240 TPIAGILGDQQAATFGQACfEKGMAKNTYGTGCFMLMNTGTEPVFSDNGLLTTVAYKIGEQ-PAVYALEGSIAVAGSLVQ 318
Cdd:PLN02295 241 VPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYKLGPDaPTNYALEGSVAIAGAAVQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 319 WLRDNLGMIVKSSDIGELASTVEDNGGVYFVPAFSGLFAPYWRSDARGAIVGLTRYVNKGHIARAVEESTAFQSAEVLDA 398
Cdd:PLN02295 320 WLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQVKDVLDA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 399 MNADAG-----VPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAAGMAVGYWSgTDDVVAN--WQEG 471
Cdd:PLN02295 400 MRKDAGeekshKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWT-EEEIFASekWKNT 478
|
490 500 510
....*....|....*....|....*....|...
gi 512630313 472 KRWTPSMEPAERDRTYRLWKKAVTRTLDWVDDD 504
Cdd:PLN02295 479 TTFRPKLDEEERAKRYASWCKAVERSFDLADLS 511
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
5-502 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 742.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 5 KFVLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAEIN--RHNLAAVGITN 82
Cdd:PTZ00294 2 KYIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKgpSFKIKAIGITN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 83 QRETTVVWDKNTGEPVYNAIVWQDMRTSDIVKELEGD-EGPDRFRQICGLGLSPYFSGSKIKWILDNVEGARERAEAGDL 161
Cdd:PTZ00294 82 QRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKyGGSNFFQKITGLPISTYFSAFKIRWMLENVPAVKDAVKEGTL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 162 YFGNTDSWVLWNLTGGvngGVHCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYGY--GRKNGLLID 239
Cdd:PTZ00294 162 LFGTIDTWLIWNLTGG---KSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTisGEAVPLLEG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 240 TPIAGILGDQQAATFGQACFEKGMAKNTYGTGCFMLMNTGTEPVFSDNGLLTTVAYKIGEQ-PAVYALEGSIAVAGSLVQ 318
Cdd:PTZ00294 239 VPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYQLGPNgPTVYALEGSIAVAGAGVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 319 WLRDNLGMIVKSSDIGELASTVEDNGGVYFVPAFSGLFAPYWRSDARGAIVGLTRYVNKGHIARAVEESTAFQSAEVLDA 398
Cdd:PTZ00294 319 WLRDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDVIES 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 399 MNADAGVPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAAGMAVGYWSGTDDV-VANWQEGKRWTPS 477
Cdd:PTZ00294 399 MEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVkKLIRRSNSTFSPQ 478
|
490 500
....*....|....*....|....*
gi 512630313 478 MEPAERDRTYRLWKKAVTRTLDWVD 502
Cdd:PTZ00294 479 MSAEERKAIYKEWNKAVERSLKWAK 503
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
6-494 |
0e+00 |
|
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: 521.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 6 FVLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAEINRHNLAAVGITNQRE 85
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 86 TTVVWDKNTGEPVYNAIVWQDMRTSDIVKE---------LEGD-------EGPDRFRQICGLGLSPYFSGSKIKWILDNV 149
Cdd:cd07793 81 TFLTWDKKTGKPLHNFITWQDLRAAELCESwnrslllkaLRGGskflhflTRNKRFLAASVLKFSTAHVSIRLLWILQNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 150 EGARERAEAGDLYFGNTDSWVLWNLTGGvngGVHCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYG 229
Cdd:cd07793 161 PELKEAAEKGELLFGTIDTWLLWKLTGG---KVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 230 YGRKNGLLIDTPIAGILGDQQAATFGQACFEKGMAKNTYGTGCFMLMNTGTEPVFSDNGLLTTVAYKIGEQPaVYALEGS 309
Cdd:cd07793 238 STDPSIFGAEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGGEI-TYLAEGN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 310 IAVAGSLVQWLRDNlGMIVKSSDIGELASTVEDNGGVYFVPAFSGLFAPYWRSDARGAIVGLTRYVNKGHIARAVEESTA 389
Cdd:cd07793 317 ASDTGTVIDWAKSI-GLFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 390 FQSAEVLDAMNADAGVPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAAGMAVGYWSGTDDVVANWQ 469
Cdd:cd07793 396 FRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEELKKLRK 475
|
490 500
....*....|....*....|....*
gi 512630313 470 EGKRWTPSMEPAERDRTYRLWKKAV 494
Cdd:cd07793 476 IEKIFEPKMDNEKREELYKNWKKAV 500
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
5-497 |
3.18e-124 |
|
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: 371.86 E-value: 3.18e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 5 KFVLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAEINRHNLAAVGITNQR 84
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 85 ETTVVWDKNtGEPVYNAIVWQDMRTSDIVKELEGDEGPDRFRQICGLGLSPYFSGSKIKWILDNVEGARERAEagdlYFG 164
Cdd:COG1070 81 HGLVLLDAD-GEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIA----KVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 165 NTDSWVLWNLTggvngGVHCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYGYGRKN-----GLLID 239
Cdd:COG1070 156 LPKDYLRYRLT-----GEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEaaaetGLPAG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 240 TPIAGILGDQQAATFGQACFEKGMAKNTYGTGCFMLMNTgTEPVFSDNGLLTTVAYKIgeqPAVYALEGSIAVAGSLVQW 319
Cdd:COG1070 231 TPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVS-DKPLPDPEGRVHTFCHAV---PGRWLPMGATNNGGSALRW 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 320 LRDNLGMIVKSS--DIGELASTVE-DNGGVYFVPAFSGLFAPYWRSDARGAIVGLTRYVNKGHIARAVEESTAFQSAEVL 396
Cdd:COG1070 307 FRDLFADGELDDyeELNALAAEVPpGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 397 DAMnADAGVPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAAGMAVGYWSGTDDVVANW-QEGKRWT 475
Cdd:COG1070 387 EAL-EEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMvRVGETIE 465
|
490 500
....*....|....*....|...
gi 512630313 476 PSMEPAER-DRTYRLWKKAVTRT 497
Cdd:COG1070 466 PDPENVAAyDELYERYRELYPAL 488
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
6-479 |
1.33e-118 |
|
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: 355.29 E-value: 1.33e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 6 FVLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAEINRHNLAAVGITNQRE 85
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 86 TTVVWDKNtGEPVYNAIVWQDMRTSdivkelegdegpdrfrqicglglspyfsgskikwildnvegareraeagdlYFGN 165
Cdd:cd07779 81 TFVPVDED-GRPLRPAISWQDKRTA---------------------------------------------------KFLT 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 166 TDSWVLWNLTGgvnggVHCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYGYGRKN-----GLLIDT 240
Cdd:cd07779 109 VQDYLLYRLTG-----EFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEaaeetGLPEGT 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 241 PI--AGilGDQQAATFGQACFEKGMAKNTYGTGCFMLMNTGtEPVFSDNGLLTTVAYKIgeqPAVYALEGSIAVAGSLVQ 318
Cdd:cd07779 184 PVvaGG--GDQQCAALGAGVLEPGTASLSLGTAAVVIAVSD-KPVEDPERRIPCNPSAV---PGKWVLEGSINTGGSAVR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 319 WLRDNLG---MIVKSSDIG------ELASTVE-DNGGVYFVPAFSGLFAPYWRSDARGAIVGLTRYVNKGHIARAVEEST 388
Cdd:cd07779 258 WFRDEFGqdeVAEKELGVSpyellnEEAAKSPpGSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGI 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 389 AFQSAEVLDAMnADAGVPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAAGMAVGYWSGTDDVVANW 468
Cdd:cd07779 338 AFELRDNLEAM-EKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAM 416
|
490
....*....|..
gi 512630313 469 -QEGKRWTPSME 479
Cdd:cd07779 417 vRVTDTFEPDPE 428
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
7-451 |
5.96e-108 |
|
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: 326.83 E-value: 5.96e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 7 VLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAEINRHNLAAVGITNQRET 86
Cdd:cd00366 2 LLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 87 TVVWDKNtGEPVYNAIVWQDMRTsdivkelegdegpdrfrqicglglspyfsgskikwildnvegareraeagdlYFGNT 166
Cdd:cd00366 82 VVLVDAD-GNPLRPAIIWLDRRA----------------------------------------------------KFLQP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 167 DSWVLWNLTGgvnggVHCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYG-----YGRKNGLLIDTP 241
Cdd:cd00366 109 NDYIVFRLTG-----EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGrvtpeAAEETGLPAGTP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 242 IAGILGDQQAATFGQACFEKGMAKNTYGTGCFMLMNTGtEPVFSDNGLLTTVAYkigeQPAVYALEGSIAVAGSLVQWLR 321
Cdd:cd00366 184 VVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTD-EPVPPDPRLLNRCHV----VPGLWLLEGAINTGGASLRWFR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 322 DNLG----MIVKSSDIGELASTVEDN-GGVYFVPAFSGLFAPYWRSDARGAIVGLTRYVNKGHIARAVEESTAFQSAEVL 396
Cdd:cd00366 259 DEFGeeedSDAEYEGLDELAAEVPPGsDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNL 338
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 512630313 397 DAMnADAGVPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAA 451
Cdd:cd00366 339 EIL-EELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
7-456 |
2.57e-100 |
|
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: 308.75 E-value: 2.57e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 7 VLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAEinRHNLAAVGITNQRET 86
Cdd:cd07773 2 LLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAG--PDPIAAISVSSQGES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 87 TVVWDKNtGEPVYNAIVWQDMRTSDIVKELEGDEGPDRFRQICGLGLSPYFSGSKIKWILDNvegARERAEAGDLYFGNT 166
Cdd:cd07773 80 GVPVDRD-GEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREH---EPEIFAKAAKWLSVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 167 DsWVLWNLTggvngGVHCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYGY-----GRKNGLLIDTP 241
Cdd:cd07773 156 D-YIAYRLT-----GEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTvtpeaAEELGLPAGTP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 242 IagILG--DQQAATFGQACFEKGMAKNTYGT--GCFMLMNTGTEPVFSDNGLLTTVAYKIGEQpavYALEGSIAvAGSLV 317
Cdd:cd07773 230 V--VVGghDHLCAALGAGVIEPGDVLDSTGTaeALLAVVDEPPLDEMLAEGGLSYGHHVPGGY---YYLAGSLP-GGALL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 318 QWLRDNLGM--IVKSSDIGELASTVEDNGGVYFVPAFSGLFAPYWRSDARGAIVGLTRYVNKGHIARAVEESTAFQSAEV 395
Cdd:cd07773 304 EWFRDLFGGdeSDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLN 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512630313 396 LDAMnADAGVPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAAGMAVG 456
Cdd:cd07773 384 LEAL-EKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
6-493 |
1.64e-97 |
|
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: 302.92 E-value: 1.64e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 6 FVLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAEINRHNLAAVGITNQRE 85
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 86 TTVVWDKNtGEPVYNAIVWQDMRTSDIVKELEGDEGPDRFRQICGLgLSPYFSGSKIKWIldnvegARERAEAgdlyFGN 165
Cdd:cd07808 81 GLVLLDKN-GRPLRPAILWNDQRSAAECEELEARLGDEILIITGNP-PLPGFTLPKLLWL------KENEPEI----FAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 166 TDSWVL------WNLTggvngGVHCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYGYGRKN----- 234
Cdd:cd07808 149 IRKILLpkdylrYRLT-----GELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEaaeel 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 235 GLLIDTPIAGILGDQQAATFGQACFEKGMAKNTYGTGCFMLMNTGtEPVFSDNGLLTTVAYKIGEQpaVYALeGSIAVAG 314
Cdd:cd07808 224 GLPEGTPVVAGAGDNAAAALGAGVVEPGDALISLGTSGVVFAPTD-KPVPDPKGRLHTFPHAVPGK--WYAM-GVTLSAG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 315 SLVQWLRDNLGMIVKS-SDIGELASTVED-NGGVYFVPAFSGLFAPYWRSDARGAIVGLTRYVNKGHIARAVEESTAFQS 392
Cdd:cd07808 300 LSLRWLRDLFGPDRESfDELDAEAAKVPPgSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 393 AEVLDAMnADAGVPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAAGMAVGYWSGTDDVVANW-QEG 471
Cdd:cd07808 380 RDSLEVL-KELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACiKIE 458
|
490 500
....*....|....*....|...
gi 512630313 472 KRWTPSMEPAER-DRTYRLWKKA 493
Cdd:cd07808 459 KTIEPDPERHEAyDELYARYREL 481
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
6-255 |
6.78e-96 |
|
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: 290.39 E-value: 6.78e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 6 FVLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAEINRHNLAAVGITNQRE 85
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 86 TTVVWDKNTgEPVYNAIVWQDMRTSDIVKELEGDEGPDRFRQICGLGLSPYFSGSKIKWILDNVEGARERAEAgdlyFGN 165
Cdd:pfam00370 81 GTVLLDKND-KPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHK----FLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 166 TDSWVLWNLTggvngGVHCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYGYGR-----KNGLLIDT 240
Cdd:pfam00370 156 IHDYLRWRLT-----GVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNpelaaMWGLDEGV 230
|
250
....*....|....*
gi 512630313 241 PIAGILGDQQAATFG 255
Cdd:pfam00370 231 PVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
6-491 |
2.57e-86 |
|
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: 274.01 E-value: 2.57e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 6 FVLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAEINRHNLAAVGITNQRE 85
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 86 TTVVWDKNtGEPVYNAIVWQDMRTSDIVKELEGDEGPDRFRQICGLG-LSPYFSGSKIKWILDNvegARERAEAGDLYFG 164
Cdd:cd07805 81 GVVPVDKD-GNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLGGGNpPSGKDPLAKILWLKEN---EPEIYAKTHKFLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 165 NTDsWVLWNLTggvngGVHCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYGYGRKN-----GLLID 239
Cdd:cd07805 157 AKD-YLNFRLT-----GRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEaaaelGLPAG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 240 TPIAGILGDQQAATFGQACFEKGMAkNTY-GTGCFMLMNTgTEPVFSDNGLLTTVAYKIgeqPAVYALEGSIAVAGSLVQ 318
Cdd:cd07805 231 TPVVGGGGDAAAAALGAGAVEEGDA-HIYlGTSGWVAAHV-PKPKTDPDHGIFTLASAD---PGRYLLAAEQETAGGALE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 319 WLRDNLGMIVKSSD-----IGELASTVE-DNGGVYFVPAFSGLFAPYWRSDARGAIVGLTRYVNKGHIARAVEESTAFQS 392
Cdd:cd07805 306 WARDNLGGDEDLGAddyelLDELAAEAPpGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 393 AEVLDAMNADAGvPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKV-IETTALGAAYAAGMAVGYWSGTDDVVANWQEG 471
Cdd:cd07805 386 RWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVPENpQEAGALGAALLAAVGLGLLKSFDEAKALVKVE 464
|
490 500
....*....|....*....|.
gi 512630313 472 KRWTPSMEPAER-DRTYRLWK 491
Cdd:cd07805 465 KVFEPDPENRARyDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
6-456 |
4.79e-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: 264.39 E-value: 4.79e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 6 FVLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAEINRHNLAAVGITNQRE 85
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 86 TTVVWDKNtGEPVYNAIVWQDMRTSDIVKELEGDEGPDRFRQICGLGLSPYFSGSKIKWILDN----VEGAReraeagdl 161
Cdd:cd07804 81 ALVPVDEN-GKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSQSVGPKLLWIKRNepevFKKTR-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 162 YFGNTDSWVLWNLTggvngGVHCTDVTNASRTM-LMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYGY-----GRKNG 235
Cdd:cd07804 152 KFLGAYDYIVYKLT-----GEYVIDYSSAGNEGgLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEvtkeaAEETG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 236 LLIDTPIAGILGDQQAATFGQACFEKG--MAKntYGT-GCFMLMntgTEPVFSDNGLLTTVAYkigeQPAVYALEGSIAV 312
Cdd:cd07804 227 LAEGTPVVAGTVDAAASALSAGVVEPGdlLLM--LGTaGDIGVV---TDKLPTDPRLWLDYHD----IPGTYVLNGGMAT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 313 AGSLVQWLRDNLG----MIVKSSDIG------ELASTVE---DngGVYFVPAFSGLFAPYWRSDARGAIVGLTRYVNKGH 379
Cdd:cd07804 298 SGSLLRWFRDEFAgeevEAEKSGGDSaydlldEEAEKIPpgsD--GLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAH 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512630313 380 IARAVEESTAFQSAEVLDAMNaDAGVPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAAGMAVG 456
Cdd:cd07804 376 LYRALLEGVAYGLRHHLEVIR-EAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
6-492 |
4.81e-79 |
|
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: 254.79 E-value: 4.81e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 6 FVLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAEinRHNLAAVGITNQRE 85
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLG--GGEVDAIGFSSAMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 86 TTVVWDKNtGEPVYNAIVWQDMRTSDIVKELEGDEGPDRFRQICGLGLSPYFSGSKIKWILDNVEGARERAEagdlYFGN 165
Cdd:cd07770 79 SLLGVDED-GEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAA----KFVS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 166 TDSWVLWNLTggvngGVHCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYGYGRKN-----GLLIDT 240
Cdd:cd07770 154 IKEYLLYRLT-----GELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEfaerlGLLAGT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 241 P-IAGIlGDQQAATFGQACFEKGMAKNTYGTGCFMLMNTgTEPVFSDNGLLTTvaYKIGEQpaVYALEGSIAVAGSLVQW 319
Cdd:cd07770 229 PvVLGA-SDGALANLGSGALDPGRAALTVGTSGAIRVVS-DRPVLDPPGRLWC--YRLDEN--RWLVGGAINNGGNVLDW 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 320 LRDNLGMIVKS-SDIGELASTVE-DNGGVYFVPAFSGLFAPYWRSDARGAIVGLTRYVNKGHIARAVEESTAFQSAEVLD 397
Cdd:cd07770 303 LRDTLLLSGDDyEELDKLAEAVPpGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 398 AMnADAGVPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAAGMAVGYWSGtDDVVANWQEGKRWTPS 477
Cdd:cd07770 383 AL-EELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISS-LEADELVKIGKVVEPD 460
|
490
....*....|....*.
gi 512630313 478 MEPAER-DRTYRLWKK 492
Cdd:cd07770 461 PENHAIyAELYERFKK 476
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
6-456 |
5.03e-70 |
|
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: 230.13 E-value: 5.03e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 6 FVLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAEINRHNLAAVGITNQRE 85
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 86 TTVVWDKNtGEPVYNAIVWQDMRTSDIVKELEGDEGPDRFRQICGLGLSPYFSGSKIKWILDNvegARERAEAGDLYFGN 165
Cdd:cd07802 81 GLYLVDKD-GKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKEN---EPERYDRIRTVLFC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 166 TDsWVLWNLTggvngGVHCTDVTNASrTMLMDIRTLSWREDVCEIFGIP--MSMLPEIKSSSEIYGY-----GRKNGLLI 238
Cdd:cd07802 157 KD-WIRYRLT-----GEISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRvtaeaAALTGLPE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 239 DTPIAGILGDQQAATFGQACFEKGMAKNTYGTGCfmlMNTG--TEPVFSDNGLLTTVAYKIGEqpaVYALEGSIAVAGSL 316
Cdd:cd07802 230 GTPVAAGAFDVVASALGAGAVDEGQLCVILGTWS---INEVvtDEPVVPDSVGSNSLHADPGL---YLIVEASPTSASNL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 317 vQWLRDNLGMIVKSSDIG-------ELASTVEDNGGVYFVPaFsgLFAPYWRSDARGAIVGLTRYVNKGHIARAVEESTA 389
Cdd:cd07802 304 -DWFLDTLLGEEKEAGGSdydeldeLIAAVPPGSSGVIFLP-Y--LYGSGANPNARGGFFGLTAWHTRAHLLRAVYEGIA 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512630313 390 FQSAEVLDAMnaDAGVPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAAGMAVG 456
Cdd:cd07802 380 FSHRDHLERL--LVARKPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
6-456 |
5.86e-59 |
|
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: 201.30 E-value: 5.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 6 FVLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFP--NPGWVEHNPIEIWDTTRTVVAEALQKAEINRHNLAAVGITNQ 83
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDddYPDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 84 RETTVVWDKNtGEPVY---NaivwQDMRTSDIVKELEGDEGpDRFRQICGLGLSPYFSGSKIKWILDNVEGARERAEAgd 160
Cdd:cd07798 81 REGIVFLDKD-GRELYagpN----IDARGVEEAAEIDDEFG-EEIYTTTGHWPTELFPAARLLWFKENRPEIFERIAT-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 161 lyFGNTDSWVLWNLTGGVnggvhCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYG-----YGRKNG 235
Cdd:cd07798 153 --VLSISDWIGYRLTGEL-----VSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGtvseeAARELG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 236 LLIDTPIAGILGDQQAATFGQACFEKGMAKNTYGTGCFMLMNTGtEPVFSDNGLLTTVAYKIGEQpavYALEGSIAVAGS 315
Cdd:cd07798 226 LPEGTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTD-EPIIDPERRLWTGCHLVPGK---WVLESNAGVTGL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 316 LVQWLRDNLGMIVKSS--DIGELASTVEDN-GGVYfvpAF--SGLFAPYWRSDARGAIV----GLTRYVNKGHIARAVEE 386
Cdd:cd07798 302 NYQWLKELLYGDPEDSyeVLEEEASEIPPGaNGVL---AFlgPQIFDARLSGLKNGGFLfptpLSASELTRGDFARAILE 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 387 STAFQSAEVLDAMNADAGVPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAAGMAVG 456
Cdd:cd07798 379 NIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
6-455 |
6.45e-55 |
|
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: 190.13 E-value: 6.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 6 FVLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAEINRhnLAAVGITNQRE 85
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPRR--VVAIAVDGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 86 TTVVWDKNtGEPVYNAIVWQDMRTSDIVKELEGDEGPDRFRqiCGLGLSPYFSGSKIKWILDNVEGARERAEagdlYFGN 165
Cdd:cd07783 79 TLVLVDRE-GEPLRPAIMYNDARAVAEAEELAEAAGAVAPR--TGLAVSPSSSLAKLLWLKRHEPEVLAKTA----KFLH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 166 TDSWVLWNLTGGVNggvhCTDVTNASRTMLmDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYG-----YGRKNGLLIDT 240
Cdd:cd07783 152 QADWLAGRLTGDRG----VTDYNNALKLGY-DPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGtltaeAAEELGLPAGT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 241 PIagILG--DQQAATFGQACFEKGMAKNTYGTG-CFMLmnTGTEPVFSDNGLLTTvaYKIGEQpaVYALEGSIAVAGSLV 317
Cdd:cd07783 227 PV--VAGttDSIAAFLASGAVRPGDAVTSLGTTlVLKL--LSDKRVPDPGGGVYS--HRHGDG--YWLVGGASNTGGAVL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 318 QWLrdnlgmiVKSSDIGELASTVEDNG--GVYFVP-AFSGLFAPYWRSDARGAIvgLTRYVNKGHIARAVEESTAFQSAE 394
Cdd:cd07783 299 RWF-------FSDDELAELSAQADPPGpsGLIYYPlPLRGERFPFWDPDARGFL--LPRPHDRAEFLRALLEGIAFIERL 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512630313 395 VLDAMNADAGVPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKvIETTALGAAYAAGMAV 455
Cdd:cd07783 370 GYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAE-EEEAALGAALLAAAGL 429
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
264-454 |
1.84e-54 |
|
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: 181.37 E-value: 1.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 264 AKNTYGTGCFMLMnTGTEPVFSDNGLLTTVAYKIGeqPAVYALEGSIAVAGSLVQWLRDNLGM---IVKSSDIGELA--- 337
Cdd:pfam02782 1 LAISAGTSSFVLV-ETPEPVLSVHGVWGPYTNEML--PGYWGLEGGQSAAGSLLAWLLQFHGLreeLRDAGNVESLAela 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 338 --STVEDNGGVYFVPAFSGLFAPYWRSDARGAIVGLTRYVNKGHIARAVEESTAFQSAEVLDAMNADAGVPLKELKVDGG 415
Cdd:pfam02782 78 alAAVAPAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSGG 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 512630313 416 MTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAAGMA 454
Cdd:pfam02782 158 GSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
6-456 |
5.87e-54 |
|
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: 187.76 E-value: 5.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 6 FVLAIDQGTTSTRAIIFN-HAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAEINRHNLAAVGITNQR 84
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 85 ETTVVWDKNtGEPVYNAIVWQDMRTSDIVKELEGDEGPDRFRQIcGLGLSPYFSGSKIKWILDNVEGARERAEA----GD 160
Cdd:cd07809 81 HGLVALDAD-GKVLRPAKLWCDTRTAPEAEELTEALGGKKCLLV-GLNIPARFTASKLLWLKENEPEHYARIAKillpHD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 161 lyfgntdsWVLWNLTGGvnggvHCTDVTNASRTMLMDIRTLSWREDVCEIF---GIPMSMLPEIKSSSEIYGYGRKN--- 234
Cdd:cd07809 159 --------YLNWKLTGE-----KVTGLGDASGTFPIDPRTRDYDAELLAAIdpsRDLRDLLPEVLPAGEVAGRLTPEgae 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 235 --GLLIDTPIAGILGDQQAATFGQACFEKGMAKNTYGT-GCfmLMNTGTEPVFSDNGLLTTVAYkigeqpAVYALEGSIA 311
Cdd:cd07809 226 elGLPAGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTsGT--AYGVSDKPVSDPHGRVATFCD------STGGMLPLIN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 312 VAGSLVQWLRDNLGMI-VKSSDIGELASTVE-DNGGVYFVPAFSGLFAPYWRsDARGAIVGLT-RYVNKGHIARAVEEST 388
Cdd:cd07809 298 TTNCLTAWTELFRELLgVSYEELDELAAQAPpGAGGLLLLPFLNGERTPNLP-HGRASLVGLTlSNFTRANLARAALEGA 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512630313 389 AFQSAEVLDAMnADAGVPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAAGMAVG 456
Cdd:cd07809 377 TFGLRYGLDIL-RELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
6-456 |
5.96e-50 |
|
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: 177.43 E-value: 5.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 6 FVLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAEINRHNLAAVGITNQRE 85
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 86 TTVVWDKNtGEPVYNAIVWQDMRTSDIVKELEGDEGPDRFRQICGLGLSPYFSGSKIKWILDNvegARERAEAGDLYFGN 165
Cdd:cd24121 81 GTWLVDED-GRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKEN---EPERLERARTALHC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 166 TDsWVLWNLTggvngGVHCTDVTNASRTMLmDIRTLSWREDVCEIFGIP--MSMLPEIKSSSEIYGYGRKN-----GLLI 238
Cdd:cd24121 157 KD-WLFYKLT-----GEIATDPSDASLTFL-DFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEaaaatGLPA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 239 DTPIAGILGDQQAATFGQACFEKGMAKNTYGTGCF--MLMNtgtEPVFSDNGLLTTVAYKIGEQPA-VYAlegsiAVAGS 315
Cdd:cd24121 230 GTPVVLGPFDVVATALGSGAIEPGDACSILGTTGVheVVVD---EPDLEPEGVGYTICLGVPGRWLrAMA-----NMAGT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 316 L-VQWLRDNLGMIVKSS----------DIGELASTVE-DNGGVYFVPAFS--GLFAPYWRSDARGAIVGLTRYVNKGHIA 381
Cdd:cd24121 302 PnLDWFLRELGEVLKEGaepagsdlfqDLEELAASSPpGAEGVLYHPYLSpaGERAPFVNPNARAQFTGLSLEHTRADLL 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512630313 382 RAVEESTAFQSAEVLDAMnadaGVPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAAGMAVG 456
Cdd:cd24121 382 RAVYEGVALAMRDCYEHM----GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
6-493 |
1.76e-46 |
|
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: 168.87 E-value: 1.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 6 FVLAIDQGTTSTRAIIFN-HAGEIVSVGQKEFTQIF--PNPGWVEHNPIEIWDTTRTVVAEALQKAEINRHNLAAVGITN 82
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 83 QRETTVVWDKNtGEPVYNAIVWQDMRTSDIVKELE--GDEGPDRFRQICGLGLSPYFSGSKIKWILDNVEGARERA---- 156
Cdd:cd07781 81 TSSTVVPVDED-GNPLAPAILWMDHRAQEEAAEINetAHPALEYYLAYYGGVYSSEWMWPKALWLKRNAPEVYDAAytiv 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 157 EAGDlyfgntdsWVLWNLTGGVNGGVhCtdvtNASRTMLMDIRTLSWREDVCEIFGIPMS-----MLPEIKSSSEIYGY- 230
Cdd:cd07781 160 EACD--------WINARLTGRWVRSR-C----AAGHKWMYNEWGGGPPREFLAALDPGLLklrekLPGEVVPVGEPAGTl 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 231 ----GRKNGLLIDTPIAGILGDQQAATFGQACFEKG-MAKNTyGT-GCFMLMntGTEPVFS-------DNGLLttvayki 297
Cdd:cd07781 227 taeaAERLGLPAGIPVAQGGIDAHMGAIGAGVVEPGtLALIM-GTsTCHLMV--SPKPVDIpgicgpvPDAVV------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 298 geqPAVYALEGSIAVAGSLVQWLRDNLGMIVKSSDI------GELASTVEdnggvyfvPAFSGLFA---------PYWRS 362
Cdd:cd07781 297 ---PGLYGLEAGQSAVGDIFAWFVRLFVPPAEERGDsiyallSEEAAKLP--------PGESGLVAldwfngnrtPLVDP 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 363 DARGAIVGLTRYVNKGHIARAVEESTAFQSAEVLDAMNaDAGVPLKELKVDGGMT-HDDLVMQFQADLCGVDVVRPKVIE 441
Cdd:cd07781 366 RLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERFE-EAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQ 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 512630313 442 TTALGAAYAAGMAVGYWSGTDDVVANW-QEGKRWTPSMEPAER-DRTYRLWKKA 493
Cdd:cd07781 445 APALGAAILAAVAAGVYADIEEAADAMvRVDRVYEPDPENHAVyEELYALYKEL 498
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
6-490 |
1.93e-43 |
|
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: 160.58 E-value: 1.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 6 FVLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQI-FPN-PGWVEHNPIEIWDTTRTVVAEALQKAEINRHNLAAVGITNQ 83
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREWRHKeVPDvPGSMDFDTEKNWKLICECIREALKKAGIAPKSIAAISTTSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 84 RETTVVWDKNtGEPVYnAIVWQDMRTSDIVKEL-EGDEGPDR--FR---QICGLGLSPyfsgsKIKWILDNVEGARERAE 157
Cdd:cd07775 81 REGIVLYDNE-GEEIW-ACANVDARAAEEVSELkELYNTLEEevYRisgQTFALGAIP-----RLLWLKNNRPEIYRKAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 158 agdlYFGNTDSWVLWNLTggvngGVHCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYGYGRKN--- 234
Cdd:cd07775 154 ----KITMLSDWIAYKLS-----GELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEaae 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 235 --GLLIDTPIAGILGDQQAATFGQACFEKGMAKNTYGTGCFMLMNTgTEPVFSDNGLLTTVAYKIgeqPAVYALEGSIAV 312
Cdd:cd07775 225 etGLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNT-AAPVTDPAMNIRVNCHVI---PDMWQAEGISFF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 313 AGSLVQWLRDNLG----MIVKSSDIG------ELASTVEdnGGVY-FVPAFSGLF-APYWRSDARgAIVGLT----RYvN 376
Cdd:cd07775 301 PGLVMRWFRDAFCaeekEIAERLGIDaydlleEMAKDVP--PGSYgIMPIFSDVMnYKNWRHAAP-SFLNLDidpeKC-N 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 377 KGHIARAVEESTAFQSAEVLDAMNADAGVPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAAGMAVG 456
Cdd:cd07775 377 KATFFRAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAG 456
|
490 500 510
....*....|....*....|....*....|....*.
gi 512630313 457 YWSGTDDVVANWQEGKR-WTPSMEPAER-DRTYRLW 490
Cdd:cd07775 457 IYSSLEEAVESLVKWEReYLPNPENHEVyQDLYEKW 492
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
6-451 |
5.14e-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: 138.89 E-value: 5.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 6 FVLAIDQGTTSTRAIIFN-HAGEIVSVGQKEFTQIFP--NPGWVEHNPIEIWDTTRTVVAEALQKAeinRHNLAAVGITN 82
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDlESGRILESVSRPTPAPISsdDPGRSEQDPEKILEAVRNLIDELPREY---LSDVTGIGITG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 83 QRETTVVWDKNtGEPVYNAIVWQDMRTSDIVKELEGDEGPDrFRQICGLGLSPYFSGSKIKWILDNvegarERAEAGDLY 162
Cdd:cd07777 78 QMHGIVLWDED-GNPVSPLITWQDQRCSEEFLGGLSTYGEE-LLPKSGMRLKPGYGLATLFWLLRN-----GPLPSKADR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 163 FGNTDSWVLWNLTGGvngGVHCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYGYGRkNGLLIDTPI 242
Cdd:cd07777 151 AGTIGDYIVARLTGL---PKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLS-SALPKGIPV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 243 AGILGDQQAATFGQACFEKGMAKNTYGTGC--FMLMNTGTEPV------FSDNGLLTTVAykigeqpavyALEG--SIAV 312
Cdd:cd07777 227 YVALGDNQASVLGSGLNEENDAVLNIGTGAqlSFLTPKFELSGsveirpFFDGRYLLVAA----------SLPGgrALAV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 313 agsLVQWLRDNLGMIVKSSDIGEL------ASTVEDNGGVYFVPAFSGLFapyWRSDARGAIVGLTRY-VNKGHIARAve 385
Cdd:cd07777 297 ---LVDFLREWLRELGGSLSDDEIwekldeLAESEESSDLSVDPTFFGER---HDPEGRGSITNIGESnFTLGNLFRA-- 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512630313 386 estAFQS-AEVLDAMnADaGVPLKELKVD------GGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAA 451
Cdd:cd07777 369 ---LCRGiAENLHEM-LP-RLDLDLSGIErivgsgGALRKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
5-505 |
3.72e-30 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 123.19 E-value: 3.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 5 KFVLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQI-FPN-PGWVEHNPIEIWDTTRTVVAEALQKAEINRHNLAAVGITN 82
Cdd:PRK10939 3 SYLMALDAGTGSIRAVIFDLNGNQIAVGQAEWRHLaVPDvPGSMEFDLEKNWQLACQCIRQALQKAGIPASDIAAVSATS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 83 QRETTVVWDKNtGEPVYnAIVWQDMRTSDIVKELEGDEG--PDRFRQICG----LGLSPyfsgsKIKWILDNVEGARERA 156
Cdd:PRK10939 83 MREGIVLYDRN-GTEIW-ACANVDARASREVSELKELHNnfEEEVYRCSGqtlaLGALP-----RLLWLAHHRPDIYRQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 157 EAgdlyFGNTDSWVLWNLTggvngGVHCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYGY-----G 231
Cdd:PRK10939 156 HT----ITMISDWIAYMLS-----GELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHvtakaA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 232 RKNGLLIDTPIAGILGDQQAATFGQACFEKGMAKNTYGTGCFMLMNTgTEPVFSDNGLLTTVAYKIgeqPAVYALEGSIA 311
Cdd:PRK10939 227 AETGLRAGTPVVMGGGDVQLGCLGLGVVRPGQTAVLGGTFWQQVVNL-PAPVTDPNMNIRINPHVI---PGMVQAESISF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 312 VAGSLVQWLRDNLGMIVKS----------SDIGELASTVEdnGGVYFV-PAFSGLFApY--WRSdARGAIVGLT---RYV 375
Cdd:PRK10939 303 FTGLTMRWFRDAFCAEEKLlaerlgidaySLLEEMASRVP--VGSHGIiPIFSDVMR-FksWYH-AAPSFINLSidpEKC 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 376 NKGHIARAVEESTAFQSAEVLDAMNADAGVPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAAYAAGMAV 455
Cdd:PRK10939 379 NKATLFRALEENAAIVSACNLQQIAAFSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGA 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 512630313 456 GYWSGTDDVVANW-QEGKRWTPSMEPAE-RDRTYRLWKKAVTRTLDWVDDDV 505
Cdd:PRK10939 459 GIYSSLAETGERLvRWERTFEPNPENHElYQEAKEKWQAVYADQLGLVDHGL 510
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
8-456 |
7.85e-26 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 110.44 E-value: 7.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 8 LAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAEINrhNLAAVGITNQRETT 87
Cdd:PRK15027 3 IGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQ--DVKALGIAGQMHGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 88 VVWDKNTgEPVYNAIVWQDMRTSDIVKELEgdEGPDRFRQICGLGLSPYFSGSKIKWIldnvegarERAEAGdlYFGNTD 167
Cdd:PRK15027 81 TLLDAQQ-RVLRPAILWNDGRCAQECALLE--ARVPQSRVITGNLMMPGFTAPKLLWV--------QRHEPE--IFRQID 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 168 SWVL------WNLTggvngGVHCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYGYGR----KNGLL 237
Cdd:PRK15027 148 KVLLpkdylrLRMT-----GEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLpevaKAWGM 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 238 IDTPIAGILGDQQAATFGQACFEKGMAKNTYGT-GCFMLMNTG--TEPVFSDNGLLTTVaykigeqPAVYALEGSIAVAG 314
Cdd:PRK15027 223 ATVPVVAGGGDNAAGAVGVGMVDANQAMLSLGTsGVYFAVSEGflSKPESAVHSFCHAL-------PQRWHLMSVMLSAA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 315 SLVQWLRDNLGMIVKSSDIGELASTVEDNGGVYFVPAFSGLFAPYWRSDARGAIVGLTRYVNKGHIARAVEESTAFQSAE 394
Cdd:PRK15027 296 SCLDWAAKLTGLSNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALAD 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512630313 395 VLDAMNAdAGVPLKELKVDGGMTHDDLVMQFQADLCGVDV-------VRPkviettALGAAYAAGMAVG 456
Cdd:PRK15027 376 GMDVVHA-CGIKPQSVTLIGGGARSEYWRQMLADISGQQLdyrtggdVGP------ALGAARLAQIAAN 437
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
7-481 |
2.03e-22 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 100.10 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 7 VLAIDQGTTSTRAIIFNHAGEIV-SVGQKEFTQIFP-NPGWveHnpieIWDttrtvVAEALQK---------AEINRHNL 75
Cdd:PRK10331 4 ILVLDCGATNVRAIAVDRQGKIVaRASTPNASDIAAeNSDW--H----QWS-----LDAILQRfadccrqinSELTECHI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 76 AAVGITNQRETTVVWDKNtGEPVYNAIVWQDMRTSDIVKELEGDEGPDRFRQICGLGLSPYFSGSKIKWILDNVEGARER 155
Cdd:PRK10331 73 RGITVTTFGVDGALVDKQ-GNLLYPIISWKCPRTAAVMENIERYISAQQLQQISGVGAFSFNTLYKLVWLKENHPQLLEQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 156 AEAgdlyFGNTDSWVLWNLTGgvnggVHCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSSSEIYGY----- 230
Cdd:PRK10331 152 AHA----WLFISSLINHRLTG-----EFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTlqpsa 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 231 GRKNGLLIDTPIAGILGDQQAATFGQacfekGMAKNtygtgcfmlmntgtEPVFSDNGLLTTVAYKIGEQPAVYALE-GS 309
Cdd:PRK10331 223 AALLGLPVGIPVISAGHDTQFALFGS-----GAGQN--------------QPVLSSGTWEILMVRSAQVDTSLLSQYaGS 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 310 I----AVAGSL---VQWLRDN----LGMIVKSSD------IGELASTVEDNGGVYFVPAFSGLfapywrsdARGAIVGLT 372
Cdd:PRK10331 284 TceldSQSGLYnpgMQWLASGvlewVRKLFWTAEtpyqtmIEEARAIPPGADGVKMQCDLLAC--------QNAGWQGVT 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 373 RYVNKGHIARAVEESTAFQSAEVLDAMNADAGVPLKELKVDGGMTHDDLVMQFQADL--CGVDVVrpKVIETTALGAAYA 450
Cdd:PRK10331 356 LNTTRGHFYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMldIPIKVL--DDAETTVAGAAMF 433
|
490 500 510
....*....|....*....|....*....|..
gi 512630313 451 AGMAVGYWSGTDDVVANWQ-EGKRWTPSMEPA 481
Cdd:PRK10331 434 GWYGVGEFSSPEQARAQMKyQYRYFYPQTEPE 465
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
7-474 |
9.02e-22 |
|
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: 97.98 E-value: 9.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 7 VLAIDQGTTSTRAIIFNHAGeivsvGQKEFTQI--FPNPgwvehnPIEI-----WDTTRTV--VAEALQKAEINRHNLAA 77
Cdd:cd07771 2 YLAVDLGASSGRVILGSLDG-----GKLELEEIhrFPNR------PVEInghlyWDIDRLFdeIKEGLKKAAEQGGDIDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 78 VGITnqretTvvW-------DKNtGEPVYNAIVWQDMRTSDIVKELEGDEGPDRFRQICGLGLSPYFSGSKIKWILDNVE 150
Cdd:cd07771 71 IGID-----T--WgvdfgllDKN-GELLGNPVHYRDPRTEGMMEELFEKISKEELYERTGIQFQPINTLYQLYALKKEGP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 151 GARERAEA----GDL--YFgntdswvlwnLTggvngGVHCTDVTNASRTMLMDIRTLSWREDVCEIFGIPMSMLPEIKSS 224
Cdd:cd07771 143 ELLERADKllmlPDLlnYL----------LT-----GEKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 225 SEIYGY----GRKNGLLIDTPIAGILG-DQQAATFGQACFEKGMAkntY---GTGCFMlmntGTEpvfSDNGLLTTVAYK 296
Cdd:cd07771 208 GTVLGTlkpeVAEELGLKGIPVIAVAShDTASAVAAVPAEDEDAA---FissGTWSLI----GVE---LDEPVITEEAFE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 297 IG---EQpavyALEGSIA----VAG-SLVQWLRDNL---GMIVKSSDIGELASTVEDNGGVYFV--PAFsglFAPywrSD 363
Cdd:cd07771 278 AGftnEG----GADGTIRllknITGlWLLQECRREWeeeGKDYSYDELVALAEEAPPFGAFIDPddPRF---LNP---GD 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 364 ARGAIV------GLTRYVNKGHIARAVEESTAFQSAEVLDAMNADAGVPLKELKVDGGMTHDDLVMQFQADLCGVDVVR- 436
Cdd:cd07771 348 MPEAIRaycretGQPVPESPGEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAg 427
|
490 500 510
....*....|....*....|....*....|....*...
gi 512630313 437 PkvIETTALGAAYAAGMAVGywsgtddVVANWQEGKRW 474
Cdd:cd07771 428 P--VEATAIGNLLVQLIALG-------EIKSLEEGREL 456
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
8-490 |
1.76e-21 |
|
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: 97.31 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 8 LAIDQGTTSTRAIIFN-HAGEIVSVGQKEFTQ-IFPNPGWVEHNPIEIWDTTRTVVAEALQKAEINRHNLAAVGItNQRE 85
Cdd:cd07768 3 IGVDVGTSSARAGVYDlYAGLEMAQEPVPYYQdSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGV-DATC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 86 TTVVWDK----NTGEPVY----NAIVWQDMRTSDIVKELEgDEGPDRFRQICGLGLSPYFSGSKIKWILDNVEGARERAe 157
Cdd:cd07768 82 SLAIFDRegtpLMALIPYpnedNVIFWMDHSAVNEAQWIN-MQCPQQLLDYLGGKISPEMGVPKLKYFLDEYSHLRDKH- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 158 agDLYFGNTDsWVLWNLTGGVNGGVhCTDVTNASrtmlMDIRTLSWREDVCEIFGIPMS------MLPEIKSSSEIYGYG 231
Cdd:cd07768 160 --FHIFDLHD-YIAYELTRLYEWNI-CGLLGKEN----LDGEESGWSSSFFKNIDPRLEhltttkNLPSNVPIGTTSGVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 232 -----RKNGLLIDTPIAGILGDQQAATFG--QACFEKGMAKNTYGTGCFMLMNTGTEPVFSDNGllttvAYKIGEQPAVY 304
Cdd:cd07768 232 lpemaEKMGLHPGTAVVVSCIDAHASWFAvaSPHLETSLFMIAGTSSCHMYGTTISDRIPGVWG-----PFDTIIDPDYS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 305 ALEGSIAVAGSLVQWL-------RDNLGMIVKSSDIGEL----ASTVEDNGG----VYFVPAFSGLFAPYWRSDARGAIV 369
Cdd:cd07768 307 VYEAGQSATGKLIEHLfeshpcaRKFDEALKKGADIYQVleqtIRQIEKNNGlsihILTLDMFFGNRSEFADPRLKGSFI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 370 GL---TRYVNKGHIARAVEESTAFQSAEVLDAMNADaGVPLKELKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALG 446
Cdd:cd07768 387 GEsldTSMLNLTYKYIAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILG 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 512630313 447 AAY----AAGMAVGYWSGTDDVVANWQEGKRWTPSMEP--AERDRTYRLW 490
Cdd:cd07768 466 AAVlakvAAGKKQLADSITEADISNDRKSETFEPLAYRlgADYILLYKLL 515
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
6-492 |
6.91e-20 |
|
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: 92.60 E-value: 6.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 6 FVLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTQIFPNPGWVEHNPIEIWDTTRTVVAEALQKAEINRHNLAAVGITnqre 85
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 86 TT---VVWDKN--------TGEPVYNAIVWQDMRTsdiVKELE--GDEGPDRFRQICGlGLSPYFSGSKIKWILDNVEGA 152
Cdd:cd07782 77 ATcslVVLDAEgkpvsvspSGDDERNVILWMDHRA---VEEAEriNATGHEVLKYVGG-KISPEMEPPKLLWLKENLPET 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 153 RERA-EAGDLyfgnTDsWVLWNLTGGVNGGVhCTdVTNASRTMLMDIRTLSWREDVCEIFGIP-MSMLPEIKSSSEIY-- 228
Cdd:cd07782 153 WAKAgHFFDL----PD-FLTWKATGSLTRSL-CS-LVCKWTYLAHEGSEGGWDDDFFKEIGLEdLVEDNFAKIGSVVLpp 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 229 GYGRKN----------GLLIDTPIAGILGDQQAATFGQ-ACFEKGMAKNTY----------GTG-CFMLMNTgtEPVFSD 286
Cdd:cd07782 226 GEPVGGgltaeaakelGLPEGTPVGVSLIDAHAGGLGTlGADVGGLPCEADpltrrlalicGTSsCHMAVSP--EPVFVP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 287 -------NGLLttvaykigeqPAVYALEGSIAVAGSLVQWlrdnlgMIVKSSDIGELASTVEDNG--------------- 344
Cdd:cd07782 304 gvwgpyySAML----------PGLWLNEGGQSATGALLDH------IIETHPAYPELKEEAKAAGksiyeylnerleqla 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 345 ------------GVYFVPAFSGLFAPYWRSDARGAIVGLTRYVNKGHIAR---AVEESTAFQSAEVLDAMNAdAGVPLKE 409
Cdd:cd07782 368 eekglplayltrDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHIIEAMNA-AGHKIDT 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 410 LKVDGGMTHDDLVMQFQADLCGVDVVRPKVIETTALGAA----YAAGmavGYWSGTDDVVANWQEGKRWTPSMEPAER-D 484
Cdd:cd07782 447 IFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAilgaVASG---DFPSLWDAMAAMSGPGKVVEPNEELKKYhD 523
|
....*...
gi 512630313 485 RTYRLWKK 492
Cdd:cd07782 524 RKYEVFLK 531
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
4-451 |
6.82e-18 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 86.32 E-value: 6.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 4 EKFVLAIDQGTTSTRAIIFN-HAGEIVSVGQKEFTQ------IFPNPGWVEHNPIEIWDTTRTVVAEALQKAEINRHNLA 76
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDaADGEELASAVHPYPRwviglyLPPPPDQARQHPLDYLEALEAAVREALAQAGVDPADVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 77 AVGItnqrETT----VVWDKN----------TGEPVYNAIVWQDMRTSD----IVkELEGDEGPDrFRQICGLGLSP--Y 136
Cdd:COG1069 81 GIGV----DATgctpVPVDADgtplallpefAENPHAMVILWKDHTAQEeaerIN-ELAKARGED-YLRYVGGIISSewF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 137 FSgsKIKWILDNvegARERAEAGDLYFGNTDsWVLWNLTGGVNGGVhCTdVT-----NASRTMLMDirtlswrEDVCEIF 211
Cdd:COG1069 155 WP--KILHLLRE---DPEVYEAADSFVELCD-WITWQLTGSLKRSR-CT-AGhkalwHAHEGGYPS-------EEFFAAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 212 GIPMSMLPEiKSSSEIYGYG-----------RKNGLLIDTPIAGILGDQQAATFG-QACFEKGMAKNtYGT-GCFMLmnT 278
Cdd:COG1069 220 DPLLDGLAD-RLGTEIYPLGepagtltaewaARLGLPPGTAVAVGAIDAHAGAVGaGGVEPGTLVKV-MGTsTCHML--V 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 279 GTEPVF-------SDNGLLttvaykigeqPAVYALEGSIAVAGSLVQWLRDNLgmiVKSSDIGELASTVEDNggVY---- 347
Cdd:COG1069 296 SPEERFvpgicgqVDGSIV----------PGMWGYEAGQSAVGDIFAWFVRLL---VPPLEYEKEAEERGIS--LHpllt 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 348 -----FVPAFSGLFA-PYW---RS-----DARGAIVGLTRYVNKGHIARAVEESTAFQSAEVLDAMNAdAGVPLKELKVD 413
Cdd:COG1069 361 eeaakLPPGESGLHAlDWFngnRSpladqRLKGVILGLTLGTDAEDIYRALVEATAFGTRAIIERFEE-EGVPIDEIIAC 439
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 512630313 414 GG-MTHDDLVMQFQADLCGVDVVRPKVIETTALGAA-YAA 451
Cdd:COG1069 440 GGiATKNPLVMQIYADVTGRPIKVAASEQACALGAAmFAA 479
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
352-456 |
9.61e-07 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 51.39 E-value: 9.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 352 FSGLFAPYWRSDARGAIVGLTRYVNKGHIARAVEESTAFQSAEVLDAMNaDAGVPLKELKVDGGM-THDDLVMQFQADLC 430
Cdd:PRK04123 385 FNGRRTPLADQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFE-DQGVPVEEVIAAGGIaRKNPVLMQIYADVL 463
|
90 100
....*....|....*....|....*....
gi 512630313 431 GVDVvrpKVI---ETTALGAAYAAGMAVG 456
Cdd:PRK04123 464 NRPI---QVVasdQCPALGAAIFAAVAAG 489
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
5-80 |
1.11e-04 |
|
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: 44.12 E-value: 1.11e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512630313 5 KFVLAIDQGTTSTRAIIFNHAGEIVsvgqkeFTQIFPNPgwVEHNPIEIWDTTRTVVAEALQKAEINRHNLAAVGI 80
Cdd:COG1940 5 GYVIGIDIGGTKIKAALVDLDGEVL------ARERIPTP--AGAGPEAVLEAIAELIEELLAEAGISRGRILGIGI 72
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
8-149 |
1.44e-03 |
|
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: 41.24 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 8 LAIDQGTTSTRAIIFNHAGEIVSVGQKE--FTQIFPNPGWVEHNPIEIWDTtrtvVAEALQKA--EINRHNLAAVGIT-- 81
Cdd:cd07778 3 IGIDVGSTSVRIGIFDYHGTLLATSERPisYKQDPKDLWFVTQSSTEIWKA----IKTALKELieELSDYIVSGIGVSat 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 82 ------NQRETTVVW-----DKNTGEPVYNAIVWQDMRTSdivKELEGDEGPDRFRQICGLGLS--PYFSGSKIKWILDN 148
Cdd:cd07778 79 csmvvmQRDSDTSYLvpynvIHEKSNPDQDIIFWMDHRAS---EETQWLNNILPDDILDYLGGGfiPEMAIPKLKYLIDL 155
|
.
gi 512630313 149 V 149
Cdd:cd07778 156 I 156
|
|
| ASKHA_NBD_eukNAGK-like |
cd24007 |
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ... |
7-91 |
8.87e-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: 38.05 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512630313 7 VLAIDQGTTSTRAIIFNHAGEIVSVGQKEFTqifpNPGWVEHNpiEIWDTTRTVVAEALQKA----EINRHNLAAVGITN 82
Cdd:cd24007 1 VLGVDGGGTKTRAVLADEDGKILGRGKGGPS----NPASVGIE--EAKENLKEAVREALSQAgslgEIDAICLGLAGIDS 74
|
....*....
gi 512630313 83 QRETTVVWD 91
Cdd:cd24007 75 EEDRERLRS 83
|
|
| |
