|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
10-474 |
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: 891.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 10 PLVGAVDQGTSSTRFLVFNSkTAELLSHHQVELEQKFPKEGWVEQDPKEILQSVYECIERTCEKLTELNIDISSIKAIGV 89
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFDS-TGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLKALGISPSDIKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 90 SNQRETTIIWDKYTGEPLYNAVVWLDLRTQATVETLSKRIPGNNNFVKSKTGLPLSTYFSAVKLHWILGNVRKVKKAVEE 169
Cdd:cd07792 80 TNQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELSAKTPGGKDHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 170 ERALFGTVDSWLIWSLTGGPNGGVHCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYGLMKIshslk 249
Cdd:cd07792 160 GRLLFGTVDSWLIWNLTGGKNGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIAS----- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 250 aGALEGVPLSGCLGDQSAALVGQMCFQDGQAKNT-----------------------------------------GSVAI 288
Cdd:cd07792 235 -GPLAGVPISGCLGDQQAALVGQGCFKPGEAKNTygtgcfllyntgeepvfskhgllttvayklgpdappvyaleGSIAI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 289 AGAVIRWLRDNLGILKTSEEIEKLAKEAGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTSKQHIAFAALEAVCFQT 368
Cdd:cd07792 314 AGAAVQWLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 369 KEILDAMNKDCGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAGSAEGVGVWSLEPEDLSAVTM 448
Cdd:cd07792 394 REILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSLNEGGR 473
|
490 500
....*....|....*....|....*.
gi 2119497851 449 ERFEPQINPEESEIRFAIWKKAVQKS 474
Cdd:cd07792 474 TVFEPQISEEERERRYKRWKKAVERS 499
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
10-477 |
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: 724.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 10 PLVGAVDQGTSSTRFLVFNsKTAELLSHHQVELEQKFPKEGWVEQDPKEILQSVYECIERTCEKLtelNIDISSIKAIGV 89
Cdd:TIGR01311 1 PYILAIDQGTTSSRAIVFD-KDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKA---GIKPDDIAAIGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 90 SNQRETTIIWDKYTGEPLYNAVVWLDLRTQATVETLSKRIPGnnNFVKSKTGLPLSTYFSAVKLHWILGNVRKVKKAVEE 169
Cdd:TIGR01311 77 TNQRETTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYG--EFIREKTGLPLDPYFSATKLRWLLDNVPGVREAAER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 170 ERALFGTVDSWLIWSLTGgpnGGVHCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYGLMKISHSlk 249
Cdd:TIGR01311 155 GELLFGTIDTWLIWNLTG---GKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYTDPGLL-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 250 agaLEGVPLSGCLGDQSAALVGQMCFQDGQAKNT----------------------------------------GSVAIA 289
Cdd:TIGR01311 230 ---GAEIPITGVLGDQQAALFGQACFKPGQAKNTygtgcfllmntgekpviskhgllttvayqlggkkpvyaleGSVFVA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 290 GAVIRWLRDNLGILKTSEEIEKLAKEAGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTSKQHIAFAALEAVCFQTK 369
Cdd:TIGR01311 307 GAAVQWLRDNLKLIKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 370 EILDAMNKDCGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAGSAEGVGVWSLEPEDLSAVTmE 449
Cdd:TIGR01311 387 DVLEAMEKDAGVEITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWRVE-K 465
|
490 500
....*....|....*....|....*...
gi 2119497851 450 RFEPQINPEESEIRFAIWKKAVQKSMGW 477
Cdd:TIGR01311 466 TFEPEMDEEEREARYAGWKEAVKRSLGW 493
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
12-472 |
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: 679.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 12 VGAVDQGTSSTRFLVFNSKtAELLSHHQVELEQKFPKEGWVEQDPKEILQSVYECIErtcEKLTELNIDISSIKAIGVSN 91
Cdd:cd07769 2 ILAIDQGTTSTRAILFDED-GNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIR---EALAKAGISASDIAAIGITN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 92 QRETTIIWDKYTGEPLYNAVVWLDLRTQATVETLSKRipGNNNFVKSKTGLPLSTYFSAVKLHWILGNVRKVKKAVEEER 171
Cdd:cd07769 78 QRETTVVWDKKTGKPLYNAIVWQDRRTADICEELKAK--GLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAERGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 172 ALFGTVDSWLIWSLTGGpngGVHCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYGlmkisHSLKAG 251
Cdd:cd07769 156 LLFGTIDTWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFG-----YTDPEG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 252 ALEGVPLSGCLGDQSAALVGQMCFQDGQAKNT---------------------------------------GSVAIAGAV 292
Cdd:cd07769 228 LGAGIPIAGILGDQQAALFGQGCFEPGMAKNTygtgcfllmntgekpvpskngllttiawqiggkvtyaleGSIFIAGAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 293 IRWLRDNLGILKTSEEIEKLAKEAGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTSKQHIAFAALEAVCFQTKEIL 372
Cdd:cd07769 308 IQWLRDNLGLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 373 DAMNKDCGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAGSAegVGVWSLEPEDLSAVTMER-F 451
Cdd:cd07769 388 EAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLA--VGFWKDLDELASLWQVDKrF 465
|
490 500
....*....|....*....|.
gi 2119497851 452 EPQINPEESEIRFAIWKKAVQ 472
Cdd:cd07769 466 EPSMDEEERERLYRGWKKAVE 486
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
12-478 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 677.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 12 VGAVDQGTSSTRFLVFNSKtAELLSHHQVELEQKFPKEGWVEQDPKEILQSVYECIErtcEKLTELNIDISSIKAIGVSN 91
Cdd:COG0554 5 ILAIDQGTTSTRAILFDRD-GNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIR---EALAKAGISAEDIAAIGITN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 92 QRETTIIWDKYTGEPLYNAVVWLDLRTQATVETLSKRipGNNNFVKSKTGLPLSTYFSAVKLHWILGNVRKVKKAVEEER 171
Cdd:COG0554 81 QRETTVVWDRKTGKPLYNAIVWQDRRTADICEELKAD--GLEDLIREKTGLVLDPYFSATKIKWILDNVPGARERAEAGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 172 ALFGTVDSWLIWSLTGGpngGVHCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYGlmkisHSLKAG 251
Cdd:COG0554 159 LLFGTIDSWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFG-----ETDPDL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 252 ALEGVPLSGCLGDQSAALVGQMCFQDGQAKNT---------------------------------------GSVAIAGAV 292
Cdd:COG0554 231 FGAEIPIAGIAGDQQAALFGQACFEPGMAKNTygtgcfllmntgdepvrskngllttiawglggkvtyaleGSIFVAGAA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 293 IRWLRDNLGILKTSEEIEKLAKEAGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTSKQHIAFAALEAVCFQTKEIL 372
Cdd:COG0554 311 VQWLRDGLGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 373 DAMNKDCGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAGSAegVGVWSlEPEDLSAV--TMER 450
Cdd:COG0554 391 DAMEADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLA--VGFWK-SLEELAALwkVDRR 467
|
490 500
....*....|....*....|....*...
gi 2119497851 451 FEPQINPEESEIRFAIWKKAVQKSMGWA 478
Cdd:COG0554 468 FEPQMDEEERERLYAGWKKAVERTLGWA 495
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
10-478 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 635.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 10 PLVGAVDQGTSSTRFLVFNSKtAELLSHHQVELEQKFPKEGWVEQDPKEILQSVYECIERTCEKLTELNIDISsIKAIGV 89
Cdd:PTZ00294 2 KYIGSIDQGTTSTRFIIFDEK-GNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKGPSFK-IKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 90 SNQRETTIIWDKYTGEPLYNAVVWLDLRTQATVETLSKRIPGNNNFVKsKTGLPLSTYFSAVKLHWILGNVRKVKKAVEE 169
Cdd:PTZ00294 80 TNQRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKYGGSNFFQK-ITGLPISTYFSAFKIRWMLENVPAVKDAVKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 170 ERALFGTVDSWLIWSLTGgpnGGVHCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYGLMKishSLK 249
Cdd:PTZ00294 159 GTLLFGTIDTWLIWNLTG---GKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTIS---GEA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 250 AGALEGVPLSGCLGDQSAALVGQMCFQDGQAKNT-----------------------------------------GSVAI 288
Cdd:PTZ00294 233 VPLLEGVPITGCIGDQQAALIGHGCFEKGDAKNTygtgcfllmntgteivfskhgllttvcyqlgpngptvyaleGSIAV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 289 AGAVIRWLRDNLGILKTSEEIEKLAKEAGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTSKQHIAFAALEAVCFQT 368
Cdd:PTZ00294 313 AGAGVEWLRDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 369 KEILDAMNKDCGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAGSAegVGVW-SLEP-EDLSAV 446
Cdd:PTZ00294 393 NDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLA--VGVWkSLEEvKKLIRR 470
|
490 500 510
....*....|....*....|....*....|..
gi 2119497851 447 TMERFEPQINPEESEIRFAIWKKAVQKSMGWA 478
Cdd:PTZ00294 471 SNSTFSPQMSAEERKAIYKEWNKAVERSLKWA 502
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
12-478 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 625.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 12 VGAVDQGTSSTRFLVFNsKTAELLSHHQVELEQKFPKEGWVEQDPKEILQSVYECIErtcEKLTELNIDISSIKAIGVSN 91
Cdd:PRK00047 7 ILALDQGTTSSRAIIFD-HDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIA---EALAKAGISPDQIAAIGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 92 QRETTIIWDKYTGEPLYNAVVWLDLRTQATVETLSKRipGNNNFVKSKTGLPLSTYFSAVKLHWILGNVRKVKKAVEEER 171
Cdd:PRK00047 83 QRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRD--GYEDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 172 ALFGTVDSWLIWSLTGGpngGVHCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYGLMKISHSLKAg 251
Cdd:PRK00047 161 LLFGTIDTWLVWKLTGG---KVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYGFFGG- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 252 aleGVPLSGCLGDQSAALVGQMCFQDGQAKNT---------------------------------------GSVAIAGAV 292
Cdd:PRK00047 237 ---EVPIAGIAGDQQAALFGQLCFEPGMAKNTygtgcfmlmntgekavksengllttiawgidgkvvyaleGSIFVAGSA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 293 IRWLRDNLGILKTSEEIEKLAKEAGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTSKQHIAFAALEAVCFQTKEIL 372
Cdd:PRK00047 314 IQWLRDGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 373 DAMNKDCGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAGSAegVGVWSlEPEDLSAVTME--R 450
Cdd:PRK00047 394 DAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLA--VGFWK-DLDELKEQWKIdrR 470
|
490 500
....*....|....*....|....*...
gi 2119497851 451 FEPQINPEESEIRFAIWKKAVQKSMGWA 478
Cdd:PRK00047 471 FEPQMDEEEREKLYAGWKKAVKRTLAWA 498
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
11-478 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 621.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 11 LVGAVDQGTSSTRFLVFNsKTAELLSHHQVELEQKFPKEGWVEQDPKEILQSVYECIERTCEKLTELNIDISS-IKAIGV 89
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYD-RDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGHNVDSgLKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 90 SNQRETTIIWDKYTGEPLYNAVVWLDLRTQATVETLSKRIPGNNNFVKSKTGLPLSTYFSAVKLHWILGNVRKVKKAVEE 169
Cdd:PLN02295 80 TNQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKELSGGRKHFVETCGLPISTYFSATKLLWLLENVDAVKEAVKS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 170 ERALFGTVDSWLIWSLTGGPNGGVHCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYGlmKISHSlk 249
Cdd:PLN02295 160 GDALFGTIDSWLIWNLTGGASGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIG--TIAKG-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 250 aGALEGVPLSGCLGDQSAALVGQMCfQDGQAKNT-----------------------------------------GSVAI 288
Cdd:PLN02295 236 -WPLAGVPIAGCLGDQHAAMLGQRC-RPGEAKSTygtgcfillntgeevvpskhgllttvayklgpdaptnyaleGSVAI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 289 AGAVIRWLRDNLGILKTSEEIEKLAKEAGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTSKQHIAFAALEAVCFQT 368
Cdd:PLN02295 314 AGAAVQWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 369 KEILDAMNKDCGIPLTH-----LQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAGSAegVGVWSlePEDL 443
Cdd:PLN02295 394 KDVLDAMRKDAGEEKSHkglflLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLA--VGLWT--EEEI 469
|
490 500 510
....*....|....*....|....*....|....*....
gi 2119497851 444 SAVTMER----FEPQINPEESEIRFAIWKKAVQKSMGWA 478
Cdd:PLN02295 470 FASEKWKntttFRPKLDEEERAKRYASWCKAVERSFDLA 508
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
14-472 |
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: 617.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 14 AVDQGTSSTRFLVFNsKTAELLSHHQVELEQKFPKEGWVEQDPKEILQSVYECIErtcEKLTELNIDISSIKAIGVSNQR 93
Cdd:cd07786 4 AIDQGTTSSRAILFD-HDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAR---EALAKAGIRASDIAAIGITNQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 94 ETTIIWDKYTGEPLYNAVVWLDLRTQATVETLSKRipGNNNFVKSKTGLPLSTYFSAVKLHWILGNVRKVKKAVEEERAL 173
Cdd:cd07786 80 ETTVVWDRETGKPVYNAIVWQDRRTADICEELKAE--GHEEMIREKTGLVLDPYFSATKIRWILDNVPGARERAERGELA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 174 FGTVDSWLIWSLTGGpngGVHCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYGlmkisHSLKAGAL 253
Cdd:cd07786 158 FGTIDSWLIWKLTGG---KVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFG-----YTDPDLLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 254 EGVPLSGCLGDQSAALVGQMCFQDGQAKNT---------------------------------------GSVAIAGAVIR 294
Cdd:cd07786 230 AEIPIAGIAGDQQAALFGQACFEPGMAKNTygtgcfmlmntgekpvrskngllttiawqlggkvtyaleGSIFIAGAAVQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 295 WLRDNLGILKTSEEIEKLAKEAGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTSKQHIAFAALEAVCFQTKEILDA 374
Cdd:cd07786 310 WLRDGLGLIESAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 375 MNKDCGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAGSAegVGVWSLEPEDLSAVTMER-FEP 453
Cdd:cd07786 390 MEADSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLA--VGLWKSLDELAKLWQVDRrFEP 467
|
490
....*....|....*....
gi 2119497851 454 QINPEESEIRFAIWKKAVQ 472
Cdd:cd07786 468 SMSEEEREALYAGWKKAVK 486
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
14-472 |
5.00e-138 |
|
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: 408.10 E-value: 5.00e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 14 AVDQGTSSTRFLVFNSKtAELLSHHQVELEQKFPKEGWVEQDPKEILQSVYECIERTcekLTELNIDISSIKAIGVSNQR 93
Cdd:cd07793 4 AVDVGTTNIRCHIFDKK-GKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEA---LKNAGLTPEDIAAIGISTQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 94 ETTIIWDKYTGEPLYNAVVWLDLRTQATVETLSK---------------RIPGNNNFVKSKTgLPLSTYFSAVKLHWILG 158
Cdd:cd07793 80 NTFLTWDKKTGKPLHNFITWQDLRAAELCESWNRslllkalrggskflhFLTRNKRFLAASV-LKFSTAHVSIRLLWILQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 159 NVRKVKKAVEEERALFGTVDSWLIWSLTGGPnggVHCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEI 238
Cdd:cd07793 159 NNPELKEAAEKGELLFGTIDTWLLWKLTGGK---VHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 239 YGLMKISHSLKAgalegVPLSGCLGDQSAALVGQMCFQDGQAK-----------NTGSVAIA------------------ 289
Cdd:cd07793 236 FGSTDPSIFGAE-----IPITAVVADQQAALFGECCFDKGDVKitmgtgtfidiNTGSKPHAsvkglyplvgwkiggeit 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 290 ----------GAVIRWLRDNLGIlKTSEEIEKLAKEAGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTSKQHIAFA 359
Cdd:cd07793 311 ylaegnasdtGTVIDWAKSIGLF-DDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 360 ALEAVCFQTKEILDAMNKDCGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAGSAegVGVWSlE 439
Cdd:cd07793 390 ILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLA--SGIWK-S 466
|
490 500 510
....*....|....*....|....*....|....*
gi 2119497851 440 PEDLSAV--TMERFEPQINPEESEIRFAIWKKAVQ 472
Cdd:cd07793 467 KEELKKLrkIEKIFEPKMDNEKREELYKNWKKAVK 501
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
11-271 |
1.40e-104 |
|
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: 313.12 E-value: 1.40e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 11 LVGAVDQGTSSTRFLVFNsKTAELLSHHQVELEQKFPKEGWVEQDPKEILQSVYECIERTCeklTELNIDISSIKAIGVS 90
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFN-EQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTL---SQLGISLKQIKGIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 91 NQRETTIIWDKYTgEPLYNAVVWLDLRTQATVETLSKriPGNNNFVKSKTGLPLSTYFSAVKLHWILGNVRKVKKAVEee 170
Cdd:pfam00370 77 NQGHGTVLLDKND-KPLYNAILWKDRRTAEIVENLKE--EGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIH-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 171 raLFGTVDSWLIWSLTGgpnggVHCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYGLMKISHSLKA 250
Cdd:pfam00370 152 --KFLTIHDYLRWRLTG-----VFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMW 224
|
250 260
....*....|....*....|.
gi 2119497851 251 GALEGVPLSGCLGDQSAALVG 271
Cdd:pfam00370 225 GLDEGVPVVGGGGDQQAAAFG 245
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
14-473 |
3.44e-95 |
|
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: 297.51 E-value: 3.44e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 14 AVDQGTSSTRFLVFNSkTAELLSHHQVELEQKFPKEGWVEQDPKEILQSVYECIERTcekLTELNIDISSIKAIGVSNQR 93
Cdd:COG1070 5 GIDIGTTSVKAVLFDA-DGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIREL---LAKAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 94 ETTIIWDKyTGEPLYNAVVWLDLRTQATVETLSKRIPGNNNFvkSKTGLPLSTYFSAVKLHWIL----GNVRKVKKavee 169
Cdd:COG1070 81 HGLVLLDA-DGEPLRPAILWNDTRAAAEAAELREELGEEALY--EITGNPLHPGFTAPKLLWLKenepEIFARIAK---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 170 eralFGTVDSWLIWSLTGgpnggVHCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYGLMKISHSLK 249
Cdd:COG1070 154 ----VLLPKDYLRYRLTG-----EFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 250 AGALEGVPLSGCLGDQSAALVGQMCFQDGQAKNT------------------------------------GSVAIAGAVI 293
Cdd:COG1070 225 TGLPAGTPVVAGAGDNAAAALGAGAVEPGDAAVSlgtsgvvfvvsdkplpdpegrvhtfchavpgrwlpmGATNNGGSAL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 294 RWLRDNLGILKTS--EEIEKLAKEAGT-SYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTSKQHIAFAALEAVCFQTKE 370
Cdd:COG1070 305 RWFRDLFADGELDdyEELNALAAEVPPgADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 371 ILDAMnKDCGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAgsAEGVGVWSLEPEDLSAVT--M 448
Cdd:COG1070 385 GLEAL-EEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLA--AVGLGLYDDLEEAAAAMVrvG 461
|
490 500
....*....|....*....|....*...
gi 2119497851 449 ERFEPqiNPEESEI---RFAIWKKAVQK 473
Cdd:COG1070 462 ETIEP--DPENVAAydeLYERYRELYPA 487
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
14-462 |
1.53e-89 |
|
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: 280.94 E-value: 1.53e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 14 AVDQGTSSTRFLVFNsKTAELLSHHQVELEQKFPKEGWVEQDPKEILQSVYECIERTCEKLtelNIDISSIKAIGVSNQR 93
Cdd:cd07779 4 GIDVGTTSTRAIIFD-LDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKA---GVDPEDIAAIGLTSQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 94 ETTIIWDKyTGEPLYNAVVWLDLRTqatvetlskripgnnnfvksktglplstyfsavklHWILgnvrkvkkaveeeral 173
Cdd:cd07779 80 STFVPVDE-DGRPLRPAISWQDKRT-----------------------------------AKFL---------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 174 fgTVDSWLIWSLTGgpnggVHCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYGlmKISH--SLKAG 251
Cdd:cd07779 108 --TVQDYLLYRLTG-----EFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIG--TLTKeaAEETG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 252 ALEGVPLSGCLGDQSAALVGQMCFQDGQAKN---TGSVAIA---------------------------------GAVIRW 295
Cdd:cd07779 179 LPEGTPVVAGGGDQQCAALGAGVLEPGTASLslgTAAVVIAvsdkpvedperripcnpsavpgkwvlegsintgGSAVRW 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 296 LRDNLG------ILKTSEEIEKLAKEAGT----SYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTSKQHIAFAALEAVC 365
Cdd:cd07779 259 FRDEFGqdevaeKELGVSPYELLNEEAAKsppgSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIA 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 366 FQTKEILDAMnKDCGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAgsAEGVGVWSLEPEDLSA 445
Cdd:cd07779 339 FELRDNLEAM-EKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILA--AVGAGIYPDFEEAVKA 415
|
490
....*....|....*....
gi 2119497851 446 VTM--ERFEPqiNPEESEI 462
Cdd:cd07779 416 MVRvtDTFEP--DPENVAI 432
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
14-427 |
2.51e-85 |
|
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: 268.66 E-value: 2.51e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 14 AVDQGTSSTRFLVFNSkTAELLSHHQVELEQKFPKEGWVEQDPKEILQSVYECIErtcEKLTELNIDISSIKAIGVSNQR 93
Cdd:cd00366 4 GIDIGTTSVKAALFDE-DGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIR---EVLAKAGIDPSDIAAIGISGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 94 ETTIIWDKYtGEPLYNAVVWLDlrtqatvetlskripgnnnfvksktglplstyfsavklhwilgnvrkvkkaveeERAL 173
Cdd:cd00366 80 PGVVLVDAD-GNPLRPAIIWLD------------------------------------------------------RRAK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 174 FGTVDSWLIWSLTGgpnggVHCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYGlmKISH--SLKAG 251
Cdd:cd00366 105 FLQPNDYIVFRLTG-----EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVG--RVTPeaAEETG 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 252 ALEGVPLSGCLGDQSAALVGQMCFQDGQAKN-TGSVAI----------------------------------AGAVIRWL 296
Cdd:cd00366 178 LPAGTPVVAGGGDTAAAALGAGVVEPGDAVDsTGTSSVlsvctdepvppdprllnrchvvpglwllegaintGGASLRWF 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 297 RDNLGILKTSE-EIEKLAKEAGT----SYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTSKQHIAFAALEAVCFQTKEI 371
Cdd:cd00366 258 RDEFGEEEDSDaEYEGLDELAAEvppgSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDN 337
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2119497851 372 LDAMnKDCGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAA 427
Cdd:cd00366 338 LEIL-EELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
11-432 |
6.95e-83 |
|
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: 264.06 E-value: 6.95e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 11 LVGaVDQGTSSTRFLVFNsKTAELLSHHQVELEQKFPKEGWVEQDPKEILQSVYECIERTCEKLtelniDISSIKAIGVS 90
Cdd:cd07773 2 LLG-IDIGTTNVKAVLFD-EDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQA-----GPDPIAAISVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 91 NQRETTIIWDKyTGEPLYNAVVWLDLRTQATVETLSKRIPGNNNFvkSKTGLPLSTYFSAVKLHWIlgnvRKVKKAVEEE 170
Cdd:cd07773 75 SQGESGVPVDR-DGEPLGPAIVWFDPRGKEEAEELAERIGAEELY--RITGLPPSPMYSLAKLLWL----REHEPEIFAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 171 RALFGTVDSWLIWSLTGGPnggvhCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYGLMKISHSLKA 250
Cdd:cd07773 148 AAKWLSVADYIAYRLTGEP-----VTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 251 GALEGVPLsgCLG--DQSAALVGQMCFQDGQAKN-TGSV-AI------------------------------------AG 290
Cdd:cd07773 223 GLPAGTPV--VVGghDHLCAALGAGVIEPGDVLDsTGTAeALlavvdeppldemlaegglsyghhvpggyyylagslpGG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 291 AVIRWLRDNLGI--LKTSEEIEKLAKEAGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTSKQHIAFAALEAVCFQT 368
Cdd:cd07773 301 ALLEWFRDLFGGdeSDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFEL 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119497851 369 KEILDAMNKdCGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAGSAEG 432
Cdd:cd07773 381 RLNLEALEK-AGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
15-470 |
1.62e-80 |
|
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: 259.01 E-value: 1.62e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 15 VDQGTSSTRFLVFNSKtAELLSHHQVELEQKFPKEGWVEQDPKEILQSVYECIERTcekLTELNIDISSIKAIGVSNQRE 94
Cdd:cd07808 5 IDLGTSSVKAVLVDED-GRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALREL---LAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 95 TTIIWDKyTGEPLYNAVVWLDLRTQATVETLSKRIPgnnNFVKSKTGLPLSTYFSAVKLHWILGN----VRKVKKAveee 170
Cdd:cd07808 81 GLVLLDK-NGRPLRPAILWNDQRSAAECEELEARLG---DEILIITGNPPLPGFTLPKLLWLKENepeiFARIRKI---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 171 raLFgTVDsWLIWSLTGgpnggVHCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYGlmKISHSLkA 250
Cdd:cd07808 153 --LL-PKD-YLRYRLTG-----ELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVG--TLTPEA-A 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 251 GAL---EGVPLSGCLGDQSAALVGQMCFQDGQAKNT------------------------------------GSVAIAGA 291
Cdd:cd07808 221 EELglpEGTPVVAGAGDNAAAALGAGVVEPGDALISlgtsgvvfaptdkpvpdpkgrlhtfphavpgkwyamGVTLSAGL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 292 VIRWLRDNLGILKTS-EEIEKLAKEAG-TSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTSKQHIAFAALEAVCFQTK 369
Cdd:cd07808 301 SLRWLRDLFGPDRESfDELDAEAAKVPpGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 370 EILDAMnKDCGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAGSaeGVGVWSLEPEDLSAV--T 447
Cdd:cd07808 381 DSLEVL-KELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAV--GAGVFDDLEEAAAACikI 457
|
490 500
....*....|....*....|....*.
gi 2119497851 448 MERFEPqiNPEESEI---RFAIWKKA 470
Cdd:cd07808 458 EKTIEP--DPERHEAydeLYARYREL 481
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
14-469 |
4.83e-76 |
|
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: 247.47 E-value: 4.83e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 14 AVDQGTSSTRFLVFNSKtAELLSHHQVELEQKFPKEGWVEQDPKEILQSVYECIERTCEKLtelniDISSIKAIGVSNQR 93
Cdd:cd07770 4 GIDIGTTSTKAVLFDED-GRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKL-----GGGEVDAIGFSSAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 94 ETTIIWDKyTGEPLYNAVVWLDLRTQATVETLSKRIPGNNnfVKSKTGLPLSTYFSAVKLHWIlgnvRKVKKAVEEERAL 173
Cdd:cd07770 78 HSLLGVDE-DGEPLTPVITWADTRAAEEAERLRKEGDGSE--LYRRTGCPIHPMYPLAKLLWL----KEERPELFAKAAK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 174 FGTVDSWLIWSLTGgpnggVHCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYGLMKISHSLKAGAL 253
Cdd:cd07770 151 FVSIKEYLLYRLTG-----ELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAERLGLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 254 EGVPLSGCLGDQSAALVGQMCFQDGQAK-NTG-SVAI---------------------------------AGAVIRWLRD 298
Cdd:cd07770 226 AGTPVVLGASDGALANLGSGALDPGRAAlTVGtSGAIrvvsdrpvldppgrlwcyrldenrwlvggainnGGNVLDWLRD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 299 NLGILKTS-EEIEKLAKEAG-TSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTSKQHIAFAALEAVCFQTKEILDAMn 376
Cdd:cd07770 306 TLLLSGDDyEELDKLAEAVPpGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEAL- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 377 KDCGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAGSAEGVGVwSLEPEDLSAVTmERFEPqiN 456
Cdd:cd07770 385 EELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLIS-SLEADELVKIG-KVVEP--D 460
|
490
....*....|....*.
gi 2119497851 457 PEESEI---RFAIWKK 469
Cdd:cd07770 461 PENHAIyaeLYERFKK 476
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
14-468 |
3.36e-71 |
|
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: 234.72 E-value: 3.36e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 14 AVDQGTSSTrflvfnsKTA------ELLSHHQVELEQKFPKEGWVEQDPKEILQSVYECierTCEKLTELNIDISSIKAI 87
Cdd:cd07805 4 AIDLGTSGV-------KAAlvdldgELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRA---TRALLEKSGIDPSDIAAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 88 GVSNQRETTIIWDKyTGEPLYNAVVWLDLRTQATVETLSKRIPGNNnFVKSKTGLPLSTYFSAVKLHWIlgnvrkvKK-- 165
Cdd:cd07805 74 AFSGQMQGVVPVDK-DGNPLRNAIIWSDTRAAEEAEEIAGGLGGIE-GYRLGGGNPPSGKDPLAKILWL-------KEne 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 166 --AVEEERALFGTVDsWLIWSLTGgpnggVHCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYG--L 241
Cdd:cd07805 145 peIYAKTHKFLDAKD-YLNFRLTG-----RAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGelT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 242 MKISHSLkaGALEGVPLSGCLGDQSAALVGQMCFQDGQA----------------------KNTGSVA------------ 287
Cdd:cd07805 219 PEAAAEL--GLPAGTPVVGGGGDAAAAALGAGAVEEGDAhiylgtsgwvaahvpkpktdpdHGIFTLAsadpgryllaae 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 288 --IAGAVIRWLRDNLGILKTS-----EEIEKLAKEAGT-SYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTSKQHIAFA 359
Cdd:cd07805 297 qeTAGGALEWARDNLGGDEDLgaddyELLDELAAEAPPgSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 360 ALEAVCFQTKEILDAMNKDCGiPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMP-ETTALGAAMAAGSaeGVGVW-S 437
Cdd:cd07805 377 VLEGVAFNLRWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVPENPqEAGALGAALLAAV--GLGLLkS 453
|
490 500 510
....*....|....*....|....*....|....
gi 2119497851 438 LEPEDLSAVTMERFEPqiNPEESEI---RFAIWK 468
Cdd:cd07805 454 FDEAKALVKVEKVFEP--DPENRARydrLYEVFK 485
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
11-432 |
7.21e-63 |
|
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: 212.00 E-value: 7.21e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 11 LVGaVDQGTSSTRFLVFNSKtAELLSHHQVELEQKFPKEGWVEQDPKEILQSVYECIERTCEKLtelNIDISSIKAIGVS 90
Cdd:cd07804 2 LLG-IDIGTTGTKGVLVDED-GKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKA---GISPKEIAAIGVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 91 NQRETTIIWDKYtGEPLYNAVVWLDLRTQATVETLSKRIPGNNNFvkSKTGLPLSTYFSAVKLHWILGN----VRKVKKa 166
Cdd:cd07804 77 GLVPALVPVDEN-GKPLRPAILYGDRRATEEIEWLNENIGEDRIF--EITGNPLDSQSVGPKLLWIKRNepevFKKTRK- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 167 veeeralFGTVDSWLIWSLTGgpnggVHCTDVTNASRTM-LFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYGlmKIS 245
Cdd:cd07804 153 -------FLGAYDYIVYKLTG-----EYVIDYSSAGNEGgLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVG--EVT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 246 H--SLKAGALEGVPLSGCLGDQSAALV-------GQMCFQDGQA-----------------------KNT----GSVAIA 289
Cdd:cd07804 219 KeaAEETGLAEGTPVVAGTVDAAASALsagvvepGDLLLMLGTAgdigvvtdklptdprlwldyhdiPGTyvlnGGMATS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 290 GAVIRWLRDNLGILKTSEE-------IEKLAKEAGT----SYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTSKQHIAF 358
Cdd:cd07804 299 GSLLRWFRDEFAGEEVEAEksggdsaYDLLDEEAEKippgSDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYR 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119497851 359 AALEAVCFQTKEILDAMNKDcGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAGSAEG 432
Cdd:cd07804 379 ALLEGVAYGLRHHLEVIREA-GLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
11-432 |
1.56e-46 |
|
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: 168.11 E-value: 1.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 11 LVGaVDQGTSSTRFLVFNSKTAELLSHHqVELEQKFPKEGWVEQDPKEILQSVYECIERTCEKlteLNIDISSIKAIGVS 90
Cdd:cd07802 2 LLG-IDNGTTNVKAVLFDLDGREIAVAS-RPTPVISPRPGWAERDMDELWQATAEAIRELLEK---SGVDPSDIAGVGVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 91 NQRETTIIWDKyTGEPLYNAVVWLDLRTQATVETLSKRipGNNNFVKSKTGLPLSTYFSAVKLHWILgnvrkvkkavEEE 170
Cdd:cd07802 77 GHGNGLYLVDK-DGKPVRNAILSNDSRAADIVDRWEED--GTLEKVYPLTGQPLWPGQPVALLRWLK----------ENE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 171 RALF---GTV----DsWLIWSLTggpngGVHCTDVTNASrTMLFNIHSLEWDVELCEFFEIP--MTILPNIRSSSEIYGL 241
Cdd:cd07802 144 PERYdriRTVlfckD-WIRYRLT-----GEISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 242 MKISHSLKAGALEGVPLSGCLGDQSAALVGQMCFQDGQAkntgsVAIAG------------------------------- 290
Cdd:cd07802 217 VTAEAAALTGLPEGTPVAAGAFDVVASALGAGAVDEGQL-----CVILGtwsinevvtdepvvpdsvgsnslhadpglyl 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 291 ---------AVIRWLRDNLG----ILKTS--EEIEKLAK--EAGTSyGCYFVPaFsgLYAPYWEPSARGIICGLTQFTSK 353
Cdd:cd07802 292 iveasptsaSNLDWFLDTLLgeekEAGGSdyDELDELIAavPPGSS-GVIFLP-Y--LYGSGANPNARGGFFGLTAWHTR 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119497851 354 QHIAFAALEAVCFQTKEILDAMNKDCgiPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAGSAEG 432
Cdd:cd07802 368 AHLLRAVYEGIAFSHRDHLERLLVAR--KPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
14-430 |
4.44e-46 |
|
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: 166.63 E-value: 4.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 14 AVDQGTSSTRFLVFNSKtAELLSHHQVELEQKFPKEGWVEQDPKEILQSVYECIERTCEKLtelniDISSIKAIGVSNQR 93
Cdd:cd07783 4 GIDLGTSGVRAVVVDED-GTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAEL-----RPRRVVAIAVDGTS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 94 ETTIIWDKYtGEPLYNAVVWLDLRTQATVETLSKRIPgnnnFVKSKTGLPLSTYFSAVKLHWIlgnvRKVKKAVEEERAL 173
Cdd:cd07783 78 GTLVLVDRE-GEPLRPAIMYNDARAVAEAEELAEAAG----AVAPRTGLAVSPSSSLAKLLWL----KRHEPEVLAKTAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 174 FGTVDSWLIWSLTGGPNggvhCTDVTNASRTmLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYG--LMKISHSLkaG 251
Cdd:cd07783 149 FLHQADWLAGRLTGDRG----VTDYNNALKL-GYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGtlTAEAAEEL--G 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 252 ALEGVPLsgCLG--DQSAALVGQMCFQDGQAKNT-GS-----------VAIA-----------------------GAVIR 294
Cdd:cd07783 222 LPAGTPV--VAGttDSIAAFLASGAVRPGDAVTSlGTtlvlkllsdkrVPDPgggvyshrhgdgywlvggasntgGAVLR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 295 WL--RDNLgilktsEEIEKLAKEAGTSyGCYFVP-AFSGLYAPYWEPSARGIICGLTqfTSKQHIAFAALEAVCFQTKEI 371
Cdd:cd07783 300 WFfsDDEL------AELSAQADPPGPS-GLIYYPlPLRGERFPFWDPDARGFLLPRP--HDRAEFLRALLEGIAFIERLG 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2119497851 372 LDAMNKDCGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSmPETTALGAAMAAGSA 430
Cdd:cd07783 371 YERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAE-EEEAALGAALLAAAG 428
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
14-432 |
2.58e-44 |
|
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: 162.01 E-value: 2.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 14 AVDQGTSSTRFLVFNSKTAELLSHHQvELEQKFPK--EGWVEQDPKEILQSVYECIERTcekLTELNIDISSIKAIGVSN 91
Cdd:cd07798 4 VIDIGTGGGRCALVDSEGKIVAIAYR-EWEYYTDDdyPDAKEFDPEELWEKICEAIREA---LKKAGISPEDISAVSSTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 92 QRETTIIWDKyTGEPLYnAVVWLDLRTQATVETLSKRIPgnnNFVKSKTGLPLSTYFSAVKLHWIlgnvRKVKKAVEEER 171
Cdd:cd07798 80 QREGIVFLDK-DGRELY-AGPNIDARGVEEAAEIDDEFG---EEIYTTTGHWPTELFPAARLLWF----KENRPEIFERI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 172 ALFGTVDSWLIWSLTGGPnggvhCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYGLMKISHSLKAG 251
Cdd:cd07798 151 ATVLSISDWIGYRLTGEL-----VSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAARELG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 252 ALEGVPLSGCLGDQSAALVGQMCFQDGQaknTGSVA---------------------------------------IAGAV 292
Cdd:cd07798 226 LPEGTPVVVGGADTQCALLGSGAIEPGD---IGIVAgtttpvqmvtdepiidperrlwtgchlvpgkwvlesnagVTGLN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 293 IRWLRDNL--GILKTSEEIEKLAKEAG-TSYGCYfvpAFSGLYAPYwePSARGIICGLTQFT--------SKQHIAFAAL 361
Cdd:cd07798 303 YQWLKELLygDPEDSYEVLEEEASEIPpGANGVL---AFLGPQIFD--ARLSGLKNGGFLFPtplsaselTRGDFARAIL 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119497851 362 EAVCFQTKEILDAMNKDCGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAGSAEG 432
Cdd:cd07798 378 ENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
284-430 |
2.56e-42 |
|
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: 149.78 E-value: 2.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 284 GSVAIAGAVIRWLRDNLGIL---------KTSEEIEKLAKEAGTSyGCYFVPAFSGLYAPYWEPSARGIICGLTQFTSKQ 354
Cdd:pfam02782 42 GGQSAAGSLLAWLLQFHGLReelrdagnvESLAELAALAAVAPAG-GLLFYPDFSGNRAPGADPGARGSITGLSSPTTLA 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119497851 355 HIAFAALEAVCFQTKEILDAMNKDCGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAGSA 430
Cdd:pfam02782 121 HLYRAILESLALQLRQILEALTKQEGHPIDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
11-430 |
2.34e-39 |
|
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: 148.47 E-value: 2.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 11 LVGAVDQGTSSTRFLVFNSKTAELLSHHQVELEQKFPKEGWVEQDPKEILQSVYECIErtcEKLTELNIDISSIKAIGVS 90
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDAETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFA---QLLKDAGAELRDVAAIGIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 91 NQRETTIIWDKyTGEPLYNAVVWLDLRTQATVETLSKRIPGNNnfvKSKTGLPLSTYFSAVKLHWIL----GNVRKVKKa 166
Cdd:cd07809 78 GQMHGLVALDA-DGKVLRPAKLWCDTRTAPEAEELTEALGGKK---CLLVGLNIPARFTASKLLWLKenepEHYARIAK- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 167 veeeralFGTVDSWLIWSLTGGpnggvHCTDVTNASRTMLFNIHSLEWDVELCEFFE---IPMTILPNIRSSSEIYGLMK 243
Cdd:cd07809 153 -------ILLPHDYLNWKLTGE-----KVTGLGDASGTFPIDPRTRDYDAELLAAIDpsrDLRDLLPEVLPAGEVAGRLT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 244 ISHSLKAGALEGVPLSGCLGDQSAALVGQMCFQDGQ-------------------AKNTGSVA------------IAGAV 292
Cdd:cd07809 221 PEGAEELGLPAGIPVAPGEGDNMTGALGTGVVNPGTvavslgtsgtaygvsdkpvSDPHGRVAtfcdstggmlplINTTN 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 293 I--RWLRDNLGILKTS-EEIEKLA-KEAGTSYGCYFVPAFSGLYAPYWePSARGIICGLT--QFTsKQHIAFAALEAVCF 366
Cdd:cd07809 301 CltAWTELFRELLGVSyEELDELAaQAPPGAGGLLLLPFLNGERTPNL-PHGRASLVGLTlsNFT-RANLARAALEGATF 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119497851 367 QTKEILDAMNKDcGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAGSA 430
Cdd:cd07809 379 GLRYGLDILREL-GVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWG 441
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
14-427 |
1.90e-33 |
|
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: 131.58 E-value: 1.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 14 AVDQGTSSTRFLVFNSKTAELLshHQVELEQKFPK----EGWVEQDPKEILQSVYECIERTCEKLTelnidiSSIKAIGV 89
Cdd:cd07777 4 GIDIGTTSIKAALLDLESGRIL--ESVSRPTPAPIssddPGRSEQDPEKILEAVRNLIDELPREYL------SDVTGIGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 90 SNQRETTIIWDKyTGEPLYNAVVWLDLRtqATVETLSKRIPGNNNFvKSKTGLPLSTYFSAVKLHWILGNvrkvkKAVEE 169
Cdd:cd07777 76 TGQMHGIVLWDE-DGNPVSPLITWQDQR--CSEEFLGGLSTYGEEL-LPKSGMRLKPGYGLATLFWLLRN-----GPLPS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 170 ERALFGTVDSWLIWSLTGGPNggvHCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYGlmkishSLK 249
Cdd:cd07777 147 KADRAGTIGDYIVARLTGLPK---PVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVG------TLS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 250 AGALEGVPLSGCLGDQSAALVG-----------------QMCFQDGQAKNTGSVAI----------------AGAVIRWL 296
Cdd:cd07777 218 SALPKGIPVYVALGDNQASVLGsglneendavlnigtgaQLSFLTPKFELSGSVEIrpffdgryllvaaslpGGRALAVL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 297 RD-------NLGILKTSEEI-EKLAKEAGTSYGC--YFVPAFSGlyaPYWEPSARGIICGLTQ--FTSKqHIAFAALEAV 364
Cdd:cd07777 298 VDflrewlrELGGSLSDDEIwEKLDELAESEESSdlSVDPTFFG---ERHDPEGRGSITNIGEsnFTLG-NLFRALCRGI 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119497851 365 CFQTKEILDAMNKDcGIPLTHLQVDGGM-TNNKILMQLQADILYIPVVKPSMPETTALGAAMAA 427
Cdd:cd07777 374 AENLHEMLPRLDLD-LSGIERIVGSGGAlRKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
11-432 |
4.92e-33 |
|
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: 130.82 E-value: 4.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 11 LVGaVDQGTSSTRFLVFNSKTAELlSHHQVELEQKFPKEGWVEQDPKEILQSVYECIERTCEKLTELNidiSSIKAIGVS 90
Cdd:cd24121 2 LIG-IDAGTSVVKAVAFDLDGREL-AVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLP---DRVAAIGVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 91 NQRETTIIWDKyTGEPLYNAVVWLDLRTQATVETLSKRipGNNNFVKSKTGLPLSTYFSAVKLHWILGNvrkVKKAVEEE 170
Cdd:cd24121 77 GQGDGTWLVDE-DGRPVRDAILWLDGRAADIVERWQAD--GIAEAVFEITGTGLFPGSQAAQLAWLKEN---EPERLERA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 171 RALFGTVDsWLIWSLTggpngGVHCTDVTNASRTMlFNIHSLEWDVELCEFFEIP--MTILPNIRSSSEIYGLMKISHSL 248
Cdd:cd24121 151 RTALHCKD-WLFYKLT-----GEIATDPSDASLTF-LDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 249 KAGALEGVPLSGCLGDQSAALVGQMCFQDGQA---------------------KNTGSV---AIAGAVIR---------- 294
Cdd:cd24121 224 ATGLPAGTPVVLGPFDVVATALGSGAIEPGDAcsilgttgvhevvvdepdlepEGVGYTiclGVPGRWLRamanmagtpn 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 295 --WLRDNLGILKTSE----------EIEKLAKEA-----GTSYGCYFVPAfsGLYAPYWEPSARGIICGLTQFTSKQHIA 357
Cdd:cd24121 304 ldWFLRELGEVLKEGaepagsdlfqDLEELAASSppgaeGVLYHPYLSPA--GERAPFVNPNARAQFTGLSLEHTRADLL 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119497851 358 FAALEAVCFQTKEILDAMnkdcGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAGSAEG 432
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; ... |
15-433 |
1.96e-32 |
|
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: 129.96 E-value: 1.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 15 VDQGTSSTRFLVFNSKTAELLSHHQVELEQKF--PKEGWVEQDPKEILQSVYECIERTCEkltELNIDISSIKAIGV--- 89
Cdd:cd07781 5 IDFGTQSVRAGLVDLADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALA---EAGVDPEDVVGIGVdtt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 90 SNqretTIIWDKYTGEPLYNAVVWLDLRTQATVETLSKRIPGNNNFVKSKTGLPLS--TYFSavKLHWILGNVRKVKKA- 166
Cdd:cd07781 82 SS----TVVPVDEDGNPLAPAILWMDHRAQEEAAEINETAHPALEYYLAYYGGVYSseWMWP--KALWLKRNAPEVYDAa 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 167 ---VEEeralfgtVDsWLIWSLTGGPNGGVhCTDVTNA---------SRTMLFNIHSLewDVELCEFFEipmtilPNIRS 234
Cdd:cd07781 156 ytiVEA-------CD-WINARLTGRWVRSR-CAAGHKWmynewgggpPREFLAALDPG--LLKLREKLP------GEVVP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 235 SSEIYGLMKISHSLKAGALEGVPLSGCLGDQSAALVGQMCFQDGQ-AKNTGS-----------VAI-------------- 288
Cdd:cd07781 219 VGEPAGTLTAEAAERLGLPAGIPVAQGGIDAHMGAIGAGVVEPGTlALIMGTstchlmvspkpVDIpgicgpvpdavvpg 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 289 ----------AGAVIRWLRDNLGILKTSEE-------IEKLAKEAGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFT 351
Cdd:cd07781 299 lygleagqsaVGDIFAWFVRLFVPPAEERGdsiyallSEEAAKLPPGESGLVALDWFNGNRTPLVDPRLRGAIVGLTLGT 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 352 SKQHIAFAALEAVCFQTKEILDAMnKDCGIPLTHLQVDGGMT-NNKILMQLQADILYIPVVKPSMPETTALGAAMAAGSA 430
Cdd:cd07781 379 TPAHIYRALLEATAFGTRAIIERF-EEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVA 457
|
...
gi 2119497851 431 EGV 433
Cdd:cd07781 458 AGV 460
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
14-462 |
5.79e-30 |
|
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466794 [Multi-domain] Cd Length: 492 Bit Score: 122.83 E-value: 5.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 14 AVDQGTSSTRFLVFNsktaelLSHHQVELEQK------FPK-EGWVEQDPKEILQSVYECIERTCEKLtelNIDISSIKA 86
Cdd:cd07775 4 ALDAGTGSGRAVIFD------LEGNQIAVAQRewrhkeVPDvPGSMDFDTEKNWKLICECIREALKKA---GIAPKSIAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 87 IGVSNQRETTIIWDKyTGEPLYnAVVWLDLRTQATVETLSKRIPGNNNFVKSKTGLPLStyFSAV-KLHWilgnVRKVKK 165
Cdd:cd07775 75 ISTTSMREGIVLYDN-EGEEIW-ACANVDARAAEEVSELKELYNTLEEEVYRISGQTFA--LGAIpRLLW----LKNNRP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 166 AVEEERALFGTVDSWLIWSLTGgpnggVHCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYGLMKIS 245
Cdd:cd07775 147 EIYRKAAKITMLSDWIAYKLSG-----ELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 246 HSLKAGALEGVPL--------SGCLG------DQSAALVG---QMCFQ------DGQAK---NTGSV-------AIA--- 289
Cdd:cd07775 222 AAEETGLKEGTPVvvgggdvqLGCLGlgvvrpGQTAVLGGsfwQQEVNtaapvtDPAMNirvNCHVIpdmwqaeGISffp 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 290 GAVIRWLRDNLGilktsEEIEKLAKEAGTS-Y------------GCY-FVPAFSGL--YApYWEPSARGIIcGLT---QF 350
Cdd:cd07775 302 GLVMRWFRDAFC-----AEEKEIAERLGIDaYdlleemakdvppGSYgIMPIFSDVmnYK-NWRHAAPSFL-NLDidpEK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 351 TSKQHIAFAALEAVCFQTKEILDAMNKDCGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAGSa 430
Cdd:cd07775 375 CNKATFFRAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGV- 453
|
490 500 510
....*....|....*....|....*....|....
gi 2119497851 431 eGVGVW-SLEPEDLSAVTMER-FEPqiNPEESEI 462
Cdd:cd07775 454 -GAGIYsSLEEAVESLVKWEReYLP--NPENHEV 484
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
16-458 |
1.68e-29 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 120.90 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 16 DQGTSSTRFLVFNSKTAELLSHHQV-ELEQKFPKEGWVEQDPKEILQSVYECIERTCEKLTELNIDISSIKAIGVSNQre 94
Cdd:PRK10331 8 DCGATNVRAIAVDRQGKIVARASTPnASDIAAENSDWHQWSLDAILQRFADCCRQINSELTECHIRGITVTTFGVDGA-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 95 ttiIWDKyTGEPLYNAVVWLDLRTQATVETLSKRIPGNNNFVKSKTG-LPLSTYFsavKLHWIlgnvrkvkkaVEEERAL 173
Cdd:PRK10331 86 ---LVDK-QGNLLYPIISWKCPRTAAVMENIERYISAQQLQQISGVGaFSFNTLY---KLVWL----------KENHPQL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 174 FGTVDSWL-IWSLTGGPNGGVHCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYGLMKISHSLKAGA 252
Cdd:PRK10331 149 LEQAHAWLfISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPSAAALLGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 253 LEGVPLSGCLGDQSAALVGQ-----------------M------------------CFQDGQAK--NTGSVAIAGAVIRW 295
Cdd:PRK10331 229 PVGIPVISAGHDTQFALFGSgagqnqpvlssgtweilMvrsaqvdtsllsqyagstCELDSQSGlyNPGMQWLASGVLEW 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 296 LRDNLgiLKTSEEIEKLAKEAGT----SYGCYFVPAFSGlyapywepSARGIICGLTQFTSKQHIAFAALEAVCFQTKEI 371
Cdd:PRK10331 309 VRKLF--WTAETPYQTMIEEARAippgADGVKMQCDLLA--------CQNAGWQGVTLNTTRGHFYRAALEGLTAQLKRN 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 372 LDAMNKDCGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAGSaeGVGVWSlEPEDLSA---VTM 448
Cdd:PRK10331 379 LQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWY--GVGEFS-SPEQARAqmkYQY 455
|
490
....*....|
gi 2119497851 449 ERFEPQINPE 458
Cdd:PRK10331 456 RYFYPQTEPE 465
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
15-456 |
7.49e-23 |
|
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: 101.93 E-value: 7.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 15 VDQGTSSTRFLVFNSKTAELLSHHQVELEQ-KFPKEGWVEQDPKEILQSVYECIERTcekLTELNIDISSIKAIGVSN-- 91
Cdd:cd07768 5 VDVGTSSARAGVYDLYAGLEMAQEPVPYYQdSSKKSWKFWQKSTEIIKALQKCVQKL---NIREGVDAYEVKGCGVDAtc 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 92 -----QRETTIIWDKYTGEPLYNAVVWLDLRTQATVETLskripgnnNFVKSKTGLP-----LSTYFSAVKLHWILGNVR 161
Cdd:cd07768 82 slaifDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWI--------NMQCPQQLLDylggkISPEMGVPKLKYFLDEYS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 162 KVKKAVEEeraLFGTVDsWLIWSLTGgpnggvhctDVTNASRTMLF--NIHSLE--WD------VELCEFFEIPMTILPN 231
Cdd:cd07768 154 HLRDKHFH---IFDLHD-YIAYELTR---------LYEWNICGLLGkeNLDGEEsgWSssffknIDPRLEHLTTTKNLPS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 232 IRSSSEIYGLMKISHSLKAGALEGVPLS-GC------------------------------LGDQSAALVGQMC--FQDG 278
Cdd:cd07768 221 NVPIGTTSGVALPEMAEKMGLHPGTAVVvSCidahaswfavasphletslfmiagtsschmYGTTISDRIPGVWgpFDTI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 279 ----QAKNTGSVAIAGAVIRWL-------RDNLGILKTSEEI--------EKLAKEAGTSYGCYFVPAFSGLYAPYWEPS 339
Cdd:cd07768 301 idpdYSVYEAGQSATGKLIEHLfeshpcaRKFDEALKKGADIyqvleqtiRQIEKNNGLSIHILTLDMFFGNRSEFADPR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 340 ARGIICGLTQFTSKQHIAF---AALEAVCFQTKEILDAMNKDcGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMP 416
Cdd:cd07768 381 LKGSFIGESLDTSMLNLTYkyiAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKEN 459
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2119497851 417 ETTALGAAMAAGSAEG--VGVWSLEPEDLS-AVTMERFEPQIN 456
Cdd:cd07768 460 MMGILGAAVLAKVAAGkkQLADSITEADISnDRKSETFEPLAY 502
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
307-433 |
9.86e-22 |
|
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: 98.38 E-value: 9.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 307 EEIEKLAKEAGTSYGC-----YFVPAFSGLYAPYWEPSARGIICGLTQFTSKQHIA---FAALEAVCFQTKEILDAMNKd 378
Cdd:cd07782 361 ERLEQLAEEKGLPLAYltrdlHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLAllyLATLQALAYGTRHIIEAMNA- 439
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2119497851 379 CGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAGSAEGV 433
Cdd:cd07782 440 AGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGD 494
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
15-405 |
1.74e-19 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 91.18 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 15 VDQGTSSTRFLVFNSKtAELLSHHQVELEQKFPKEGWVEQDPKEILQSVyeciERTCEKLTELNiDISSIKAIGVSNQRE 94
Cdd:PRK15027 5 IDLGTSGVKVILLNEQ-GEVVASQTEKLTVSRPHPLWSEQDPEQWWQAT----DRAMKALGDQH-SLQDVKALGIAGQMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 95 TTIIWDKYTgEPLYNAVVWLDLRTQATVETLSKRIPGNnnfvKSKTGLPLSTYFSAVKLHWILgnvrkvkkavEEERALF 174
Cdd:PRK15027 79 GATLLDAQQ-RVLRPAILWNDGRCAQECALLEARVPQS----RVITGNLMMPGFTAPKLLWVQ----------RHEPEIF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 175 GTVDS------WLIWSLTggpngGVHCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYGLMkISHSL 248
Cdd:PRK15027 144 RQIDKvllpkdYLRLRMT-----GEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGAL-LPEVA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 249 KAGALEGVPLSGCLGDQSAALVGQMCFQDGQAK-NTGSVAIAGAVI--------------------RW-----------L 296
Cdd:PRK15027 218 KAWGMATVPVVAGGGDNAAGAVGVGMVDANQAMlSLGTSGVYFAVSegflskpesavhsfchalpqRWhlmsvmlsaasC 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 297 RDNLGILKTSEEIEKL---AKEAGTSYG-CYFVPAFSGLYAPYWEPSARGIICGLTQFTSKQHIAFAALEAVCFQTKEIL 372
Cdd:PRK15027 298 LDWAAKLTGLSNVPALiaaAQQADESAEpVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGM 377
|
410 420 430
....*....|....*....|....*....|...
gi 2119497851 373 DAMNkDCGIPLTHLQVDGGMTNNKILMQLQADI 405
Cdd:PRK15027 378 DVVH-ACGIKPQSVTLIGGGARSEYWRQMLADI 409
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
15-433 |
1.14e-18 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 89.02 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 15 VDQGTSSTRFLVFNSKTAELLSH------HQVELEQKFPKEGWVEQDPKEILQSVYECIertCEKLTELNIDISSIKAIG 88
Cdd:COG1069 7 VDFGTDSVRAVVVDAADGEELASavhpypRWVIGLYLPPPPDQARQHPLDYLEALEAAV---REALAQAGVDPADVVGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 89 VsnqrETTI--------------IWDKYTGEPLYNAVVWLDLRTQATVEtlskRIpgnnNFVKSKTGLPLSTY------- 147
Cdd:COG1069 84 V----DATGctpvpvdadgtplaLLPEFAENPHAMVILWKDHTAQEEAE----RI----NELAKARGEDYLRYvggiiss 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 148 --FSAvKLHWILgnvrkvkkavEEERALFGTVDS------WLIWSLTGGPNGGVhCTdvtnASRTMLFNIHSLEWDVElc 219
Cdd:COG1069 152 ewFWP-KILHLL----------REDPEVYEAADSfvelcdWITWQLTGSLKRSR-CT----AGHKALWHAHEGGYPSE-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 220 EFFEipmTILPNI-----RSSSEIYGLmkishSLKAGAL-----------EGVPLS-----------GCLGDQSAALV-- 270
Cdd:COG1069 214 EFFA---ALDPLLdgladRLGTEIYPL-----GEPAGTLtaewaarlglpPGTAVAvgaidahagavGAGGVEPGTLVkv 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 271 ------------------GqMCfqdGQAKntGSV-----------AIAGAVIRWLRDNLGilkTSEEIEKLAKEAGTS-- 319
Cdd:COG1069 286 mgtstchmlvspeerfvpG-IC---GQVD--GSIvpgmwgyeagqSAVGDIFAWFVRLLV---PPLEYEKEAEERGISlh 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 320 --------------YGCYFVPAFSGLYAPYWEPSARGIICGLTQFTSKQHIAFAALEAVCFQTKEILDAMNkDCGIPLTH 385
Cdd:COG1069 357 pllteeaaklppgeSGLHALDWFNGNRSPLADQRLKGVILGLTLGTDAEDIYRALVEATAFGTRAIIERFE-EEGVPIDE 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2119497851 386 LQVDGG-MTNNKILMQLQADILYIPVVKPSMPETTALGAAMAAGSAEGV 433
Cdd:COG1069 436 IIACGGiATKNPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGA 484
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
14-426 |
7.58e-17 |
|
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: 82.96 E-value: 7.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 14 AVDQGTSSTRFLV--FNSKTAELL-----SHHQVELEQKFpkeGWveqDpkeiLQSVYECIERTCEKLTELNIDISSIka 86
Cdd:cd07771 4 AVDLGASSGRVILgsLDGGKLELEeihrfPNRPVEINGHL---YW---D----IDRLFDEIKEGLKKAAEQGGDIDSI-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 87 iGVsnqreTTiiW-------DKYtGEPLYNAVVWLDLRTQATVETLSKRIPGNNNFvkSKTGLPLSTYFSAVKLHWIlgn 159
Cdd:cd07771 72 -GI-----DT--WgvdfgllDKN-GELLGNPVHYRDPRTEGMMEELFEKISKEELY--ERTGIQFQPINTLYQLYAL--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 160 vrkvkkaVEEERALFGTVDSWLI------WSLTGGPnggvhCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIR 233
Cdd:cd07771 138 -------KKEGPELLERADKLLMlpdllnYLLTGEK-----VAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 234 SSSEIYGLMKISHSLKAG----------------ALEGVPLsgcLGDQSA-------ALVGQMC---------FQDGqAK 281
Cdd:cd07771 206 PPGTVLGTLKPEVAEELGlkgipviavashdtasAVAAVPA---EDEDAAfissgtwSLIGVELdepviteeaFEAG-FT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 282 NTGSVA--------IAGaviRWL----RDNLGILKTS---EEIEKLAKEAgTSYGCYFVPAFSGLYAPywePSARGIICG 346
Cdd:cd07771 282 NEGGADgtirllknITG---LWLlqecRREWEEEGKDysyDELVALAEEA-PPFGAFIDPDDPRFLNP---GDMPEAIRA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 347 LTQFT------SKQHIAFAALEAVCFQTKEILDAMNKDCGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKpSMPETTA 420
Cdd:cd07771 355 YCRETgqpvpeSPGEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIA-GPVEATA 433
|
....*.
gi 2119497851 421 LGAAMA 426
Cdd:cd07771 434 IGNLLV 439
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
14-476 |
1.39e-16 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 82.36 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 14 AVDQGTSSTRFLVFNsktaelLSHHQVELEQK---------FPkeGWVEQDPKEILQSVYECIErtcEKLTELNIDISSI 84
Cdd:PRK10939 7 ALDAGTGSIRAVIFD------LNGNQIAVGQAewrhlavpdVP--GSMEFDLEKNWQLACQCIR---QALQKAGIPASDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 85 KAIGVSNQRETTIIWDKyTGEPLYnAVVWLDLRTQATVETLSKRIPGNNNFVKSKTGLPLStyFSAV-KLHWIlgnvRKV 163
Cdd:PRK10939 76 AAVSATSMREGIVLYDR-NGTEIW-ACANVDARASREVSELKELHNNFEEEVYRCSGQTLA--LGALpRLLWL----AHH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 164 KKAVEEERALFGTVDSWLIWSLTGgpnggVHCTDVTNASRTMLFNIHSLEWDVELCEFFEIPMTILPNIRSSSEIYGLMK 243
Cdd:PRK10939 148 RPDIYRQAHTITMISDWIAYMLSG-----ELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 244 ISHSLKAGALEGVPL--------SGCLG------DQSAALVGQMCFQ----------------------DGQAKNTGSVA 287
Cdd:PRK10939 223 AKAAAETGLRAGTPVvmgggdvqLGCLGlgvvrpGQTAVLGGTFWQQvvnlpapvtdpnmnirinphviPGMVQAESISF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 288 IAGAVIRWLRD-----------NLGIlKTSEEIEKLAKE--AGtSYGcyFVPAFSGLY--------AP-YWEPSARGIIC 345
Cdd:PRK10939 303 FTGLTMRWFRDafcaeekllaeRLGI-DAYSLLEEMASRvpVG-SHG--IIPIFSDVMrfkswyhaAPsFINLSIDPEKC 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 346 GltqftsKQHIAFAALEAVCFQTKEILDAMNKDCGIPLTHLQVDGGMTNNKILMQLQADILYIPVVKPSMPETTALGAAM 425
Cdd:PRK10939 379 N------KATLFRALEENAAIVSACNLQQIAAFSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATALGCAI 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2119497851 426 AAGSaeGVGVW-SLEPEDLSAVTMER-FEPqiNPEESEIRFAI---WKKAVQKSMG 476
Cdd:PRK10939 453 AAGV--GAGIYsSLAETGERLVRWERtFEP--NPENHELYQEAkekWQAVYADQLG 504
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
341-433 |
2.94e-12 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 68.72 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 341 RGIICGLTQFTSKQHIAFAALEAVCFQTKEILDAMnKDCGIPLTHLQVDGGM-TNNKILMQLQADILYIPV-VKPSmPET 418
Cdd:PRK04123 398 KGVITGLTLGTDAPDIYRALIEATAFGTRAIMECF-EDQGVPVEEVIAAGGIaRKNPVLMQIYADVLNRPIqVVAS-DQC 475
|
90
....*....|....*
gi 2119497851 419 TALGAAMAAGSAEGV 433
Cdd:PRK04123 476 PALGAAIFAAVAAGA 490
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
339-427 |
6.48e-08 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. 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: 466792 [Multi-domain] Cd Length: 424 Bit Score: 54.96 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 339 SARGIICGLTQFTSKQHIAFAALEAVCFQTKEILDAMNKDCGipltHLQVDGGMTNNKILMQLQADILY-IPVVKPSMPE 417
Cdd:cd07772 339 PGSGGRGVLSAFPSAEEAYALAILYLALMTDYALDLLGSGVG----RIIVEGGFAKNPVFLRLLAALRPdQPVYLSDDSE 414
|
90
....*....|
gi 2119497851 418 TTALGAAMAA 427
Cdd:cd07772 415 GTALGAALLA 424
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
291-412 |
6.94e-04 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466797 [Multi-domain] Cd Length: 544 Bit Score: 42.39 E-value: 6.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119497851 291 AVIRWLRDNLGILKTSEE-IEKLAKEAGTS----YGCYFvpaFSGLYA----PYWEPSARGIICGLTQFTSKQHIAF--- 358
Cdd:cd07778 343 AIIELLKSDANFFETVEEkIDKYERLLGQSihylTRHMF---FYGDYLgnrtPYNDPNMSGSFIGESTDSSLTDLVLkyi 419
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2119497851 359 AALEAVCFQTKEILDAMNKDCgIPLTHLQVDGGMTNNKILMQLQADILYIPVVK 412
Cdd:cd07778 420 LILEFLAFQTKLIIDNFQKEK-IIIQKVVISGSQAKNARLLQLLSTVLSKIHII 472
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