|
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; ... |
11-516 |
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: 990.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 11 PLVGAVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGQLNIDISNIKAIGV 90
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFDS-TGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLKALGISPSDIKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 91 SNQRETTVVWDKITGEPLYNAVVWLDLRTQSTVESLSKRIPGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVRKVQKAVEE 170
Cdd:cd07792 80 TNQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELSAKTPGGKDHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 171 KRALFGTIDSWLIWSLTGGVNGGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGLMKIshsvk 250
Cdd:cd07792 160 GRLLFGTVDSWLIWNLTGGKNGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIAS----- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 251 aGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLTTVAYKLGRDKPVYYALEGSVAI 330
Cdd:cd07792 235 -GPLAGVPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAYKLGPDAPPVYALEGSIAI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 331 AGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQT 410
Cdd:cd07792 314 AGAAVQWLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 411 REILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALGAAMAAGAAEGVGVWSLEPEDLSAVTM 490
Cdd:cd07792 394 REILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSLNEGGR 473
|
490 500
....*....|....*....|....*.
gi 42794763 491 ERFEPQINAEESEIRYSTWKKAVMKS 516
Cdd:cd07792 474 TVFEPQISEEERERRYKRWKKAVERS 499
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
11-519 |
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: 829.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 11 PLVGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGV 90
Cdd:TIGR01311 1 PYILAIDQGTTSSRAIVFD-KDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAG---IKPDDIAAIGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 91 SNQRETTVVWDKITGEPLYNAVVWLDLRTQSTVESLSKRIPGNnnFVKSKTGLPLSTYFSAVKLRWLLDNVRKVQKAVEE 170
Cdd:TIGR01311 77 TNQRETTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYGE--FIREKTGLPLDPYFSATKLRWLLDNVPGVREAAER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 171 KRALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGlmkisHSVK 250
Cdd:TIGR01311 155 GELLFGTIDTWLIWNLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYG-----YTDP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 251 AGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLTTVAYKLGRDKPVYyALEGSVAI 330
Cdd:TIGR01311 227 GLLGAEIPITGVLGDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKKPVY-ALEGSVFV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 331 AGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQT 410
Cdd:TIGR01311 306 AGAAVQWLRDNLKLIKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 411 REILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALGAAMAAGAAEGVGVWSLEPEDLSAVTm 490
Cdd:TIGR01311 386 RDVLEAMEKDAGVEITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWRVE- 464
|
490 500
....*....|....*....|....*....
gi 42794763 491 ERFEPQINAEESEIRYSTWKKAVMKSMGW 519
Cdd:TIGR01311 465 KTFEPEMDEEEREARYAGWKEAVKRSLGW 493
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
13-513 |
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: 753.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 13 VGAVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVSN 92
Cdd:cd07769 2 ILAIDQGTTSTRAILFDED-GNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAG---ISASDIAAIGITN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 93 QRETTVVWDKITGEPLYNAVVWLDLRTQSTVESLSKRipGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVRKVQKAVEEKR 172
Cdd:cd07769 78 QRETTVVWDKKTGKPLYNAIVWQDRRTADICEELKAK--GLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAERGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 173 ALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGlmkisHSVKAG 252
Cdd:cd07769 156 LLFGTIDTWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFG-----YTDPEG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 253 ALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLTTVAYKLgrDKPVYYALEGSVAIAG 332
Cdd:cd07769 228 LGAGIPIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQI--GGKVTYALEGSIFIAG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 333 AVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTRE 412
Cdd:cd07769 306 AAIQWLRDNLGLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 413 ILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalgaamaagaaegvgVWSLEPEDLSAVTMER 492
Cdd:cd07769 386 VLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTalgaayl--aglavgFWKDLDELASLWQVDK 463
|
490 500
....*....|....*....|..
gi 42794763 493 -FEPQINAEESEIRYSTWKKAV 513
Cdd:cd07769 464 rFEPSMDEEERERLYRGWKKAV 485
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
13-520 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 749.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 13 VGAVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVSN 92
Cdd:COG0554 5 ILAIDQGTTSTRAILFDRD-GNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAG---ISAEDIAAIGITN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 93 QRETTVVWDKITGEPLYNAVVWLDLRTQSTVESLSKRipGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVRKVQKAVEEKR 172
Cdd:COG0554 81 QRETTVVWDRKTGKPLYNAIVWQDRRTADICEELKAD--GLEDLIREKTGLVLDPYFSATKIKWILDNVPGARERAEAGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 173 ALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGlmkisHSVKAG 252
Cdd:COG0554 159 LLFGTIDSWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFG-----ETDPDL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 253 ALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLTTVAYKLGrDKPVYyALEGSVAIAG 332
Cdd:COG0554 231 FGAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLG-GKVTY-ALEGSIFVAG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 333 AVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTRE 412
Cdd:COG0554 309 AAVQWLRDGLGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 413 ILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalgaamaagaaegvgVWSlEPEDLSAV--TM 490
Cdd:COG0554 389 VLDAMEADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTalgaayl--aglavgFWK-SLEELAALwkVD 465
|
490 500 510
....*....|....*....|....*....|
gi 42794763 491 ERFEPQINAEESEIRYSTWKKAVMKSMGWV 520
Cdd:COG0554 466 RRFEPQMDEEERERLYAGWKKAVERTLGWA 495
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
11-520 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 719.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 11 PLVGAVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGQLNIDISnIKAIGV 90
Cdd:PTZ00294 2 KYIGSIDQGTTSTRFIIFDEK-GNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKGPSFK-IKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 91 SNQRETTVVWDKITGEPLYNAVVWLDLRTQSTVESLSKRIPGNNNFVKsKTGLPLSTYFSAVKLRWLLDNVRKVQKAVEE 170
Cdd:PTZ00294 80 TNQRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKYGGSNFFQK-ITGLPISTYFSAFKIRWMLENVPAVKDAVKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 171 KRALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGLMKishSVK 250
Cdd:PTZ00294 159 GTLLFGTIDTWLIWNLTGG---KSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTIS---GEA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 251 AGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLTTVAYKLGRDKPVYYALEGSVAI 330
Cdd:PTZ00294 233 VPLLEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYQLGPNGPTVYALEGSIAV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 331 AGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQT 410
Cdd:PTZ00294 313 AGAGVEWLRDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 411 REILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalGAAMAAGAAEGVGVW-SLEP-EDLSAV 488
Cdd:PTZ00294 393 NDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETT--ALGAALLAGLAVGVWkSLEEvKKLIRR 470
|
490 500 510
....*....|....*....|....*....|..
gi 42794763 489 TMERFEPQINAEESEIRYSTWKKAVMKSMGWV 520
Cdd:PTZ00294 471 SNSTFSPQMSAEERKAIYKEWNKAVERSLKWA 502
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
12-520 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 708.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 12 LVGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGQ--LNIDiSNIKAIG 89
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYD-RDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAkgHNVD-SGLKAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 90 VSNQRETTVVWDKITGEPLYNAVVWLDLRTQSTVESLSKRIPGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVRKVQKAVE 169
Cdd:PLN02295 79 ITNQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKELSGGRKHFVETCGLPISTYFSATKLLWLLENVDAVKEAVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 170 EKRALFGTIDSWLIWSLTGGVNGGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGlmKISHSv 249
Cdd:PLN02295 159 SGDALFGTIDSWLIWNLTGGASGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIG--TIAKG- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 250 kaGALEGVPISGCLGDQSAALVGQMCfQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLTTVAYKLGRDKPVYYALEGSVA 329
Cdd:PLN02295 236 --WPLAGVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYKLGPDAPTNYALEGSVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 330 IAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQ 409
Cdd:PLN02295 313 IAGAAVQWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 410 TREILDAMNRDCGIPLSH-----LQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalGAAMAAGAAEGVGVWSlePED 484
Cdd:PLN02295 393 VKDVLDAMRKDAGEEKSHkglflLRVDGGATANNLLMQIQADLLGSPVVRPADIETT--ALGAAYAAGLAVGLWT--EEE 468
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 42794763 485 LSAVTMER----FEPQINAEESEIRYSTWKKAVMKSMGWV 520
Cdd:PLN02295 469 IFASEKWKntttFRPKLDEEERAKRYASWCKAVERSFDLA 508
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
13-520 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 695.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 13 VGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEktcEKLGQLNIDISNIKAIGVSN 92
Cdd:PRK00047 7 ILALDQGTTSSRAIIFD-HDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIA---EALAKAGISPDQIAAIGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 93 QRETTVVWDKITGEPLYNAVVWLDLRTQSTVESLSKRipGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVRKVQKAVEEKR 172
Cdd:PRK00047 83 QRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRD--GYEDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 173 ALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGLMKISHsvkaG 252
Cdd:PRK00047 161 LLFGTIDTWLVWKLTGG---KVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYG----F 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 253 ALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLTTVAYKLGrDKPVYyALEGSVAIAG 332
Cdd:PRK00047 234 FGGEVPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGID-GKVVY-ALEGSIFVAG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 333 AVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTRE 412
Cdd:PRK00047 312 SAIQWLRDGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 413 ILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalgaamaagaaegvgvwSL------------ 480
Cdd:PRK00047 392 VLDAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETT-----------------ALgaaylaglavgf 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 42794763 481 --EPEDLSAVTME--RFEPQINAEESEIRYSTWKKAVMKSMGWV 520
Cdd:PRK00047 455 wkDLDELKEQWKIdrRFEPQMDEEEREKLYAGWKKAVKRTLAWA 498
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
15-513 |
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: 688.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 15 AVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEktcEKLGQLNIDISNIKAIGVSNQR 94
Cdd:cd07786 4 AIDQGTTSSRAILFD-HDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAR---EALAKAGIRASDIAAIGITNQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 95 ETTVVWDKITGEPLYNAVVWLDLRTQSTVESLSKRipGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVRKVQKAVEEKRAL 174
Cdd:cd07786 80 ETTVVWDRETGKPVYNAIVWQDRRTADICEELKAE--GHEEMIREKTGLVLDPYFSATKIRWILDNVPGARERAERGELA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 175 FGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGlmkisHSVKAGAL 254
Cdd:cd07786 158 FGTIDSWLIWKLTGG---KVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFG-----YTDPDLLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 255 EGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLTTVAYKLGrdKPVYYALEGSVAIAGAV 334
Cdd:cd07786 230 AEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLG--GKVTYALEGSIFIAGAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 335 IRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREIL 414
Cdd:cd07786 308 VQWLRDGLGLIESAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 415 DAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTAL--------GAAMAAGAAEGVGVWSLEpedls 486
Cdd:cd07786 388 EAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALgaaylaglAVGLWKSLDELAKLWQVD----- 462
|
490 500
....*....|....*....|....*..
gi 42794763 487 avtmERFEPQINAEESEIRYSTWKKAV 513
Cdd:cd07786 463 ----RRFEPSMSEEEREALYAGWKKAV 485
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
15-513 |
7.51e-151 |
|
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: 441.23 E-value: 7.51e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 15 AVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVSNQR 94
Cdd:cd07793 4 AVDVGTTNIRCHIFDKK-GKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAG---LTPEDIAAIGISTQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 95 ETTVVWDKITGEPLYNAVVWLDLRTQSTVESLSK---------------RIPGNNNFVKSKTgLPLSTYFSAVKLRWLLD 159
Cdd:cd07793 80 NTFLTWDKKTGKPLHNFITWQDLRAAELCESWNRslllkalrggskflhFLTRNKRFLAASV-LKFSTAHVSIRLLWILQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 160 NVRKVQKAVEEKRALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEI 239
Cdd:cd07793 159 NNPELKEAAEKGELLFGTIDTWLLWKLTGG---KVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 240 YGLMKISHSVKAgalegVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLTTVAYKLGrDKP 319
Cdd:cd07793 236 FGSTDPSIFGAE-----IPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIG-GEI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 320 VYyALEGSVAIAGAVIRWLRDNLGIiKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIA 399
Cdd:cd07793 310 TY-LAEGNASDTGTVIDWAKSIGLF-DDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 400 FAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalGAAMAAGAAEGVGVWS 479
Cdd:cd07793 388 RAILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMS--ALGAAFLAGLASGIWK 465
|
490 500 510
....*....|....*....|....*....|....*.
gi 42794763 480 lEPEDLSAV--TMERFEPQINAEESEIRYSTWKKAV 513
Cdd:cd07793 466 -SKEELKKLrkIEKIFEPKMDNEKREELYKNWKKAV 500
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
12-272 |
8.02e-114 |
|
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: 337.00 E-value: 8.02e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 12 LVGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEklgQLNIDISNIKAIGVS 91
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFN-EQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLS---QLGISLKQIKGIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 92 NQRETTVVWDKITgEPLYNAVVWLDLRTQSTVESLSKriPGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVRKVQKAVEek 171
Cdd:pfam00370 77 NQGHGTVLLDKND-KPLYNAILWKDRRTAEIVENLKE--EGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIH-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 172 raLFGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGLMKISHSVKA 251
Cdd:pfam00370 152 --KFLTIHDYLRWRLTG-----VFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMW 224
|
250 260
....*....|....*....|.
gi 42794763 252 GALEGVPISGCLGDQSAALVG 272
Cdd:pfam00370 225 GLDEGVPVVGGGGDQQAAAFG 245
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
6-461 |
9.20e-96 |
|
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: 299.44 E-value: 9.20e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 6 KAVLGplvgaVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNI 85
Cdd:COG1070 1 KYVLG-----IDIGTTSVKAVLFDA-DGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAG---VDPEEI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 86 KAIGVSNQRETTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRIPGNNNFvkSKTGLPLSTYFSAVKLRWLLDNvrkvQ 165
Cdd:COG1070 72 AAIGVSGQMHGLVLLDA-DGEPLRPAILWNDTRAAAEAAELREELGEEALY--EITGNPLHPGFTAPKLLWLKEN----E 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 166 KAVEEKRALFGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGlmKI 245
Cdd:COG1070 145 PEIFARIAKVLLPKDYLRYRLTG-----EFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAG--TL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 246 SHSVKA--GALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKcVFSDHGLLTTVAYKL-GRdkpvyY 322
Cdd:COG1070 218 TAEAAAetGLPAGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKP-LPDPEGRVHTFCHAVpGR-----W 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 323 ALEGSVAIAGAVIRWLRDNLGIIKTS--EEIEKLAKEVGT-SYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIA 399
Cdd:COG1070 292 LPMGATNNGGSALRWFRDLFADGELDdyEELNALAAEVPPgADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLA 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42794763 400 FAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 461
Cdd:COG1070 372 RAVLEGVAFALRDGLEAL-EEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGG 432
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
15-461 |
1.19e-92 |
|
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: 289.42 E-value: 1.19e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 15 AVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVSNQR 94
Cdd:cd07779 4 GIDVGTTSTRAIIFD-LDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAG---VDPEDIAAIGLTSQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 95 ETTVVWDKiTGEPLYNAVVWLDLRTqstveslskripgnnnfvksktglplstyfsavklrwlldnvrkvqkaveekrAL 174
Cdd:cd07779 80 STFVPVDE-DGRPLRPAISWQDKRT-----------------------------------------------------AK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 175 FGTIDSWLIWSLTggvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGlmKISHSV--KAG 252
Cdd:cd07779 106 FLTVQDYLLYRLT-----GEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIG--TLTKEAaeETG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 253 ALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTgHKCVFSDHGLLTTVAYKLgrdkPVYYALEGSVAIAG 332
Cdd:cd07779 179 LPEGTPVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVS-DKPVEDPERRIPCNPSAV----PGKWVLEGSINTGG 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 333 AVIRWLRDNLG---------IIKTSEEIEKLAKEVGT-SYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAA 402
Cdd:cd07779 254 SAVRWFRDEFGqdevaekelGVSPYELLNEEAAKSPPgSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAI 333
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 42794763 403 LEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 461
Cdd:cd07779 334 LEGIAFELRDNLEAM-EKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEAT 391
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
15-461 |
2.84e-92 |
|
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: 287.15 E-value: 2.84e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 15 AVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVSNQR 94
Cdd:cd00366 4 GIDIGTTSVKAALFDE-DGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAG---IDPSDIAAIGISGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 95 ETTVVWDKiTGEPLYNAVVWLDlrtqstveslskripgnnnfvksktglplstyfsavklrwlldnvrkvqkaveeKRAL 174
Cdd:cd00366 80 PGVVLVDA-DGNPLRPAIIWLD------------------------------------------------------RRAK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 175 FGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGlmKISHSVKA--G 252
Cdd:cd00366 105 FLQPNDYIVFRLTG-----EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVG--RVTPEAAEetG 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 253 ALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGhKCVFSDHGLLTTVAYKLGRdkpvyYALEGSVAIAG 332
Cdd:cd00366 178 LPAGTPVVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTD-EPVPPDPRLLNRCHVVPGL-----WLLEGAINTGG 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 333 AVIRWLRDNLGIIKTSEE----IEKLAKEVGT-SYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVC 407
Cdd:cd00366 252 ASLRWFRDEFGEEEDSDAeyegLDELAAEVPPgSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVA 331
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 42794763 408 FQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 461
Cdd:cd00366 332 YALRDNLEIL-EELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGA 384
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
12-461 |
5.47e-84 |
|
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: 267.53 E-value: 5.47e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 12 LVGaVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGQlnidiSNIKAIGVS 91
Cdd:cd07773 2 LLG-IDIGTTNVKAVLFD-EDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGP-----DPIAAISVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 92 NQRETTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRIPGNNNFvkSKTGLPLSTYFSAVKLRWLLDNvrkvQKAVEEK 171
Cdd:cd07773 75 SQGESGVPVDR-DGEPLGPAIVWFDPRGKEEAEELAERIGAEELY--RITGLPPSPMYSLAKLLWLREH----EPEIFAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 172 RALFGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGLMKISHSVKA 251
Cdd:cd07773 148 AAKWLSVADYIAYRLTG-----EPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 252 GALEGVPIsgCLG--DQSAALVGQMCFQIGQAKNTYGTG-CFLLC-NTGHKCVFSDHGLLTTVAYKLGRdkpvYYALEGS 327
Cdd:cd07773 223 GLPAGTPV--VVGghDHLCAALGAGVIEPGDVLDSTGTAeALLAVvDEPPLDEMLAEGGLSYGHHVPGG----YYYLAGS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 328 VAiAGAVIRWLRDNLGI--IKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEA 405
Cdd:cd07773 297 LP-GGALLEWFRDLFGGdeSDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEG 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 42794763 406 VCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 461
Cdd:cd07773 376 LAFELRLNLEAL-EKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEAT 430
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
8-461 |
5.73e-81 |
|
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: 260.93 E-value: 5.73e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 8 VLGplvgaVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTcekLGQLNIDISNIKA 87
Cdd:cd07808 2 LLG-----IDLGTSSVKAVLVDED-GRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALREL---LAKAGISPSDIAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 88 IGVSNQRETTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRIPgnnNFVKSKTGLPLSTYFSAVKLRWLL----DNVRK 163
Cdd:cd07808 73 IGLTGQMHGLVLLDK-NGRPLRPAILWNDQRSAAECEELEARLG---DEILIITGNPPLPGFTLPKLLWLKenepEIFAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 164 VQKAVEEKralfgtiDsWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGlm 243
Cdd:cd07808 149 IRKILLPK-------D-YLRYRLTG-----ELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVG-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 244 KISHSVkAGAL---EGVP-ISGClGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTgHKCVFSDHGLLTTVAYKLGrdkP 319
Cdd:cd07808 214 TLTPEA-AEELglpEGTPvVAGA-GDNAAAALGAGVVEPGDALISLGTSGVVFAPT-DKPVPDPKGRLHTFPHAVP---G 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 320 VYYALeGSVAIAGAVIRWLRDNLGIIKTS-EEIEKLAKEVG-TSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCH 397
Cdd:cd07808 288 KWYAM-GVTLSAGLSLRWLRDLFGPDRESfDELDAEAAKVPpGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAH 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794763 398 IAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 461
Cdd:cd07808 367 LARAVLEGVAFSLRDSLEVL-KELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGS 429
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
15-461 |
6.85e-75 |
|
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: 244.77 E-value: 6.85e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 15 AVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGQLNIDisnikAIGVSNQR 94
Cdd:cd07770 4 GIDIGTTSTKAVLFDED-GRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVD-----AIGFSSAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 95 ETTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRIPGNNnfVKSKTGLPLSTYFSAVKLRWLLDNvrkvQKAVEEKRAL 174
Cdd:cd07770 78 HSLLGVDE-DGEPLTPVITWADTRAAEEAERLRKEGDGSE--LYRRTGCPIHPMYPLAKLLWLKEE----RPELFAKAAK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 175 FGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGLMKISHSVKAGAL 254
Cdd:cd07770 151 FVSIKEYLLYRLTG-----ELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAERLGLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 255 EGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTgcfllcnTGHKCVFSDHGLLT----TVAYKLGRDKPVyyaLEGSVAI 330
Cdd:cd07770 226 AGTPVVLGASDGALANLGSGALDPGRAALTVGT-------SGAIRVVSDRPVLDppgrLWCYRLDENRWL---VGGAINN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 331 AGAVIRWLRDNLGIIKTS-EEIEKLAKEVG-TSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCF 408
Cdd:cd07770 296 GGNVLDWLRDTLLLSGDDyEELDKLAEAVPpGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAF 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 42794763 409 QTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 461
Cdd:cd07770 376 NLKSIYEAL-EELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEAS 427
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
12-456 |
1.27e-71 |
|
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: 235.50 E-value: 1.27e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 12 LVGaVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVS 91
Cdd:cd07804 2 LLG-IDIGTTGTKGVLVDED-GKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAG---ISPKEIAAIGVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 92 NQRETTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRIPGNNNFvkSKTGLPLSTYFSAVKLRWLLDNvrkvQKAVEEK 171
Cdd:cd07804 77 GLVPALVPVDE-NGKPLRPAILYGDRRATEEIEWLNENIGEDRIF--EITGNPLDSQSVGPKLLWIKRN----EPEVFKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 172 RALFGTIDSWLIWSLTGgvnggVHCTDVTNASRTM-LFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGlmKISHSVK 250
Cdd:cd07804 150 TRKFLGAYDYIVYKLTG-----EYVIDYSSAGNEGgLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVG--EVTKEAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 251 A--GALEGVPISGCLGDQSAALV-------GQMCFQIGqakntyGTGCFLLCntgHKCVFSDHGLLTTVAyklgrDKPVY 321
Cdd:cd07804 223 EetGLAEGTPVVAGTVDAAASALsagvvepGDLLLMLG------TAGDIGVV---TDKLPTDPRLWLDYH-----DIPGT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 322 YALEGSVAIAGAVIRWLRDNLGIIKTSEE----------IEKLAKEVG-TSYGCYFVPAFSGLYAPYWEPSARGIICGLT 390
Cdd:cd07804 289 YVLNGGMATSGSLLRWFRDEFAGEEVEAEksggdsaydlLDEEAEKIPpGSDGLIVLPYFMGERTPIWDPDARGVIFGLT 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42794763 391 QFTNKCHIAFAALEAVCFQTREILDAMNRDcGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPS 456
Cdd:cd07804 369 LSHTRAHLYRALLEGVAYGLRHHLEVIREA-GLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVK 433
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
15-459 |
2.19e-65 |
|
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: 220.08 E-value: 2.19e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 15 AVDQGTSSTrflvfnsKTA------ELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECiekTCEKLGQLNIDISNIKAI 88
Cdd:cd07805 4 AIDLGTSGV-------KAAlvdldgELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRA---TRALLEKSGIDPSDIAAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 89 GVSNQRETTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRIPGNNnFVKSKTGLPLSTYFSAVKLRWLLDN----VRKV 164
Cdd:cd07805 74 AFSGQMQGVVPVDK-DGNPLRNAIIWSDTRAAEEAEEIAGGLGGIE-GYRLGGGNPPSGKDPLAKILWLKENepeiYAKT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 165 QKaveekraLFGTIDsWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGlmK 244
Cdd:cd07805 152 HK-------FLDAKD-YLNFRLTG-----RAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVG--E 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 245 ISHSVKA--GALEGVPISGCLGDQSAALVGQMCFQIGQAkNTY-GTGCFLLCNTGHKCVFSDHGlLTTVAYKLgrdkPVY 321
Cdd:cd07805 217 LTPEAAAelGLPAGTPVVGGGGDAAAAALGAGAVEEGDA-HIYlGTSGWVAAHVPKPKTDPDHG-IFTLASAD----PGR 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 322 YALEGSVAIAGAVIRWLRDNLGIIKTS-----EEIEKLAKEVGT-SYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNK 395
Cdd:cd07805 291 YLLAAEQETAGGALEWARDNLGGDEDLgaddyELLDELAAEAPPgSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTR 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794763 396 CHIAFAALEAVCFQTREILDAMNRDCGiPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPE 459
Cdd:cd07805 371 ADLARAVLEGVAFNLRWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVPENPQ 433
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
15-460 |
2.09e-48 |
|
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: 173.18 E-value: 2.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 15 AVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLgqlniDISNIKAIGVSNQR 94
Cdd:cd07783 4 GIDLGTSGVRAVVVDED-GTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAEL-----RPRRVVAIAVDGTS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 95 ETTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRIPgnnnFVKSKTGLPLSTYFSAVKLRWLLDNvrkvQKAVEEKRAL 174
Cdd:cd07783 78 GTLVLVDR-EGEPLRPAIMYNDARAVAEAEELAEAAG----AVAPRTGLAVSPSSSLAKLLWLKRH----EPEVLAKTAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 175 FGTIDSWLIWSLTGGVNggvhCTDVTNASRTmLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGLMKISHSVKAGAL 254
Cdd:cd07783 149 FLHQADWLAGRLTGDRG----VTDYNNALKL-GYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 255 EGVPIsgCLG--DQSAALVGQMCFQIGQAKNTYGTG-CF-LLCntgHKCVFSDHGLLTTvaYKLGRDkpvYYALEGSVAI 330
Cdd:cd07783 224 AGTPV--VAGttDSIAAFLASGAVRPGDAVTSLGTTlVLkLLS---DKRVPDPGGGVYS--HRHGDG---YWLVGGASNT 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 331 AGAVIRWL--RDNLgiiktsEEIEKLAKEVGTSyGCYFVP-AFSGLYAPYWEPSARGIICGLTqfTNKCHIAFAALEAVC 407
Cdd:cd07783 294 GGAVLRWFfsDDEL------AELSAQADPPGPS-GLIYYPlPLRGERFPFWDPDARGFLLPRP--HDRAEFLRALLEGIA 364
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 42794763 408 FQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPET 460
Cdd:cd07783 365 FIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEA 417
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
12-464 |
2.45e-48 |
|
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: 173.12 E-value: 2.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 12 LVGaVDQGTSSTRFLVFNSKTAELLSHHqVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVS 91
Cdd:cd07802 2 LLG-IDNGTTNVKAVLFDLDGREIAVAS-RPTPVISPRPGWAERDMDELWQATAEAIRELLEKSG---VDPSDIAGVGVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 92 NQRETTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRipGNNNFVKSKTGLPLSTYFSAVKLRWLLDN----VRKVQKA 167
Cdd:cd07802 77 GHGNGLYLVDK-DGKPVRNAILSNDSRAADIVDRWEED--GTLEKVYPLTGQPLWPGQPVALLRWLKENeperYDRIRTV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 168 VEEKralfgtiDsWLIWSLTGgvnggVHCTDVTNASrTMLFNIHSLEWDKQLCEFFGIP--MEILPNVRSSSEIYGlmKI 245
Cdd:cd07802 154 LFCK-------D-WIRYRLTG-----EISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAG--RV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 246 SHSVKA--GALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCfllCNTG--HKCVFSDHGLLTTvaykLGRDKPVY 321
Cdd:cd07802 218 TAEAAAltGLPEGTPVAAGAFDVVASALGAGAVDEGQLCVILGTWS---INEVvtDEPVVPDSVGSNS----LHADPGLY 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 322 YALEGSVAIAGaVIRWLRDNLG------IIKTSEEIEKLAKEVG-TSYGCYFVPaFsgLYAPYWEPSARGIICGLTQFTN 394
Cdd:cd07802 291 LIVEASPTSAS-NLDWFLDTLLgeekeaGGSDYDELDELIAAVPpGSSGVIFLP-Y--LYGSGANPNARGGFFGLTAWHT 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 395 KCHIAFAALEAVCFQTREILDAMNRDCgiPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALG 464
Cdd:cd07802 367 RAHLLRAVYEGIAFSHRDHLERLLVAR--KPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALG 434
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
281-464 |
1.02e-45 |
|
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: 159.03 E-value: 1.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 281 AKNTYGTGCFLLCNTGHKCVFSdHGLLTTVAyklGRDKPVYYALEGSVAIAGAVIRWLRDNLGI---------IKTSEEI 351
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSV-HGVWGPYT---NEMLPGYWGLEGGQSAAGSLLAWLLQFHGLreelrdagnVESLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 352 EKLAKEVGTSyGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVD 431
Cdd:pfam02782 77 AALAAVAPAG-GLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVS 155
|
170 180 190
....*....|....*....|....*....|...
gi 42794763 432 GGMTSNKILMQLQADILYIPVVKPSMPETTALG 464
Cdd:pfam02782 156 GGGSRNPLLLQLLADALGLPVVVPGPDEATALG 188
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
15-464 |
5.30e-43 |
|
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: 158.93 E-value: 5.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 15 AVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPREGW-VEQDPKEILHSVYECIEKTcekLGQLNIDISNIKAIGVSNQ 93
Cdd:cd07798 4 VIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYPDaKEFDPEELWEKICEAIREA---LKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 94 RETTVVWDKiTGEPLYnAVVWLDLRTQSTVESLSKRIPgnnNFVKSKTGLPLSTYFSAVKLRWLldnvRKVQKAVEEKRA 173
Cdd:cd07798 81 REGIVFLDK-DGRELY-AGPNIDARGVEEAAEIDDEFG---EEIYTTTGHWPTELFPAARLLWF----KENRPEIFERIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 174 LFGTIDSWLIWSLTGGVnggvhCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGlmKISHSVKA-- 251
Cdd:cd07798 152 TVLSISDWIGYRLTGEL-----VSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLG--TVSEEAARel 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 252 GALEGVPISGCLGD-QSAALvgqmcfqigqakntyGTGCFllcNTGHKCVFSdhGllTTVAYKLGRDKPVY--------- 321
Cdd:cd07798 225 GLPEGTPVVVGGADtQCALL---------------GSGAI---EPGDIGIVA--G--TTTPVQMVTDEPIIdperrlwtg 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 322 -------YALEGSVAIAGAVIRWLRDNL--GIIKTSEEIEKLAKEVG-TSYGCYfvpAFSGLYAPYwePSARGIICGLTQ 391
Cdd:cd07798 283 chlvpgkWVLESNAGVTGLNYQWLKELLygDPEDSYEVLEEEASEIPpGANGVL---AFLGPQIFD--ARLSGLKNGGFL 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 392 FT--------NKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTAL 463
Cdd:cd07798 358 FPtplsaselTRGDFARAILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASAL 437
|
.
gi 42794763 464 G 464
Cdd:cd07798 438 G 438
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
8-464 |
3.44e-36 |
|
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: 139.99 E-value: 3.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 8 VLGplvgaVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTcekLGQLNIDISNIKA 87
Cdd:cd07809 2 VLG-----IDLGTQSIKAVLIDAETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQL---LKDAGAELRDVAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 88 IGVSNQRETTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRIPGNNnfvKSKTGLPLSTYFSAVKLRWLLDN----VRK 163
Cdd:cd07809 74 IGISGQMHGLVALDA-DGKVLRPAKLWCDTRTAPEAEELTEALGGKK---CLLVGLNIPARFTASKLLWLKENepehYAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 164 VQKaveekralFGTIDSWLIWSLTGGvnggvHCTDVTNASRTMLFNIHSLEWDKQLCEFF---GIPMEILPNVRSSSEIY 240
Cdd:cd07809 150 IAK--------ILLPHDYLNWKLTGE-----KVTGLGDASGTFPIDPRTRDYDAELLAAIdpsRDLRDLLPEVLPAGEVA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 241 GlmkisHSVKAGALE-----GVPISGCLGDQSAALVGQMCFQIGQAKNTYGT-GCflLCNTGHKCVFSDHGLLTTVAykl 314
Cdd:cd07809 217 G-----RLTPEGAEElglpaGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTsGT--AYGVSDKPVSDPHGRVATFC--- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 315 grDKPVYYALegSVAIAGAVIRWLRDNLGIIKTS-EEIEKLAKEV-GTSYGCYFVPAFSGLYAPYWePSARGIICGLTQF 392
Cdd:cd07809 287 --DSTGGMLP--LINTTNCLTAWTELFRELLGVSyEELDELAAQApPGAGGLLLLPFLNGERTPNL-PHGRASLVGLTLS 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42794763 393 -TNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALG 464
Cdd:cd07809 362 nFTRANLARAALEGATFGLRYGLDIL-RELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALG 433
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
15-461 |
1.45e-30 |
|
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: 123.87 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 15 AVDQGTSSTRFLVFNSKTAELLS----HHQVEIKQEFPreGWVEQDPKEILHSVYECIEKTCEKLGqlnidiSNIKAIGV 90
Cdd:cd07777 4 GIDIGTTSIKAALLDLESGRILEsvsrPTPAPISSDDP--GRSEQDPEKILEAVRNLIDELPREYL------SDVTGIGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 91 SNQRETTVVWDKiTGEPLYNAVVWLDLRtqSTVESLSKRIPGNNNFvKSKTGLPLSTYFSAVKLRWLLdnvrkVQKAVEE 170
Cdd:cd07777 76 TGQMHGIVLWDE-DGNPVSPLITWQDQR--CSEEFLGGLSTYGEEL-LPKSGMRLKPGYGLATLFWLL-----RNGPLPS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 171 KRALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGlmKISHSVK 250
Cdd:cd07777 147 KADRAGTIGDYIVARLTGL---PKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVG--TLSSALP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 251 AgaleGVPISGCLGDQSAALVGqmCFQIGqaKNT----YGTG---CFLLC-NTGHKCV----FSDHGLLTTVAyKL--GR 316
Cdd:cd07777 222 K----GIPVYVALGDNQASVLG--SGLNE--ENDavlnIGTGaqlSFLTPkFELSGSVeirpFFDGRYLLVAA-SLpgGR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 317 dkpVYYALEGSVAiagaviRWLRDnLGIIKTSEEI-EKLAKEVGTSYGC--YFVPAFSGlyaPYWEPSARGIICGLTQ-- 391
Cdd:cd07777 293 ---ALAVLVDFLR------EWLRE-LGGSLSDDEIwEKLDELAESEESSdlSVDPTFFG---ERHDPEGRGSITNIGEsn 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42794763 392 FTNKcHIAFAALEAVCfqtREILDAMNRDC--GIPLSHLQVDGGM-TSNKILMQLQADILYIPVVKPSMPETT 461
Cdd:cd07777 360 FTLG-NLFRALCRGIA---ENLHEMLPRLDldLSGIERIVGSGGAlRKNPVLRRIIEKRFGLPVVLSEGSEEA 428
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
15-461 |
1.66e-27 |
|
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: 115.51 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 15 AVDQGTSSTRFLVFNsKTAELLSHHQVE-IKQEFPR-EGWVEQDPKEILHSVYECIEKTCEklgQLNIDISNIKAIGVSN 92
Cdd:cd07775 4 ALDAGTGSGRAVIFD-LEGNQIAVAQREwRHKEVPDvPGSMDFDTEKNWKLICECIREALK---KAGIAPKSIAAISTTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 93 QRETTVVWDKiTGEPLYnAVVWLDLRTQSTVESLSKRIPGNNNFVKSKTGLPLStyFSAV-KLRWLLDNvrkvQKAVEEK 171
Cdd:cd07775 80 MREGIVLYDN-EGEEIW-ACANVDARAAEEVSELKELYNTLEEEVYRISGQTFA--LGAIpRLLWLKNN----RPEIYRK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 172 RALFGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGLMKISHSVKA 251
Cdd:cd07775 152 AAKITMLSDWIAYKLSG-----ELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEAAEET 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 252 GALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLTTVAYklgrDKPVYYAlEGSVAIA 331
Cdd:cd07775 227 GLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMNIRVNCHV----IPDMWQA-EGISFFP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 332 GAVIRWLRDNLGI----------IKTSEEIEKLAKEVGTsyGCY-FVPAFSGL--YApYWEPSARGIIcGLTQFTNKCHI 398
Cdd:cd07775 302 GLVMRWFRDAFCAeekeiaerlgIDAYDLLEEMAKDVPP--GSYgIMPIFSDVmnYK-NWRHAAPSFL-NLDIDPEKCNK 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42794763 399 A--FAAL-EAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 461
Cdd:cd07775 378 AtfFRAImENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEAT 443
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
12-467 |
2.09e-27 |
|
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: 114.64 E-value: 2.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 12 LVGaVDQGTSSTRFLVFNSKTAELlSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGQLNidiSNIKAIGVS 91
Cdd:cd24121 2 LIG-IDAGTSVVKAVAFDLDGREL-AVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLP---DRVAAIGVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 92 NQRETTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRipGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVrkvQKAVEEK 171
Cdd:cd24121 77 GQGDGTWLVDE-DGRPVRDAILWLDGRAADIVERWQAD--GIAEAVFEITGTGLFPGSQAAQLAWLKENE---PERLERA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 172 RALFGTIDsWLIWSLTGgvnggVHCTDVTNASRTMlFNIHSLEWDKQLCEFFGIP--MEILPNVRSSSEIYGLMKISHSV 249
Cdd:cd24121 151 RTALHCKD-WLFYKLTG-----EIATDPSDASLTF-LDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 250 KAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFllcntghkcvfsdHGLLTTVAYkLGRDKP---VYYALEG 326
Cdd:cd24121 224 ATGLPAGTPVVLGPFDVVATALGSGAIEPGDACSILGTTGV-------------HEVVVDEPD-LEPEGVgytICLGVPG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 327 SV-----AIAG-AVIRWLRDNLGIIKTSE----------EIEKLAKEV-----GTSYGCYFVPAfsGLYAPYWEPSARGI 385
Cdd:cd24121 290 RWlramaNMAGtPNLDWFLRELGEVLKEGaepagsdlfqDLEELAASSppgaeGVLYHPYLSPA--GERAPFVNPNARAQ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 386 ICGLTQFTNKCHIAFAALEAVCFQTREILDAMnrdcGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALGA 465
Cdd:cd24121 368 FTGLSLEHTRADLLRAVYEGVALAMRDCYEHM----GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGA 443
|
..
gi 42794763 466 AM 467
Cdd:cd24121 444 AM 445
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
8-461 |
7.28e-27 |
|
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: 113.79 E-value: 7.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 8 VLGplvgaVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEF--PREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNI 85
Cdd:cd07781 2 VIG-----IDFGTQSVRAGLVDLADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAEAG---VDPEDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 86 KAIGVSNQRETTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRIPGNNNFVKSKTGLPLS--TYFSavKLRWLLDNVRK 163
Cdd:cd07781 74 VGIGVDTTSSTVVPVDE-DGNPLAPAILWMDHRAQEEAAEINETAHPALEYYLAYYGGVYSseWMWP--KALWLKRNAPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 164 VQKA----VEEkralfgtIDsWLIWSLTGGVNGGVhCtdvtNASRTMLFNIHSLEWDKQLCEFFGIPM----EILP-NVR 234
Cdd:cd07781 151 VYDAaytiVEA-------CD-WINARLTGRWVRSR-C----AAGHKWMYNEWGGGPPREFLAALDPGLlklrEKLPgEVV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 235 SSSEIYGLMKISHSVKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGT-GCFLLcnTGHKCVFSDhGLLTTVayk 313
Cdd:cd07781 218 PVGEPAGTLTAEAAERLGLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTsTCHLM--VSPKPVDIP-GICGPV--- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 314 lgrDKPV---YYALEGSVAIAGAVIRWLRDNLGI------IKTSEEIEKLAKEVGTsyGCyfvpafSGLYA--------- 375
Cdd:cd07781 292 ---PDAVvpgLYGLEAGQSAVGDIFAWFVRLFVPpaeergDSIYALLSEEAAKLPP--GE------SGLVAldwfngnrt 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 376 PYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTS-NKILMQLQADILYIPVVK 454
Cdd:cd07781 361 PLVDPRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERF-EEAGVPVNRVVACGGIAEkNPLWMQIYADVLGRPIKV 439
|
....*..
gi 42794763 455 PSMPETT 461
Cdd:cd07781 440 PKSDQAP 446
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
17-461 |
1.65e-24 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 106.27 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 17 DQGTSSTRFLVFNSKTAELLSHHQ---VEIKQEFPRegWVEQDPKEILHSVYECIEKTCEKLGQlnidiSNIKAIGVsnq 93
Cdd:PRK10331 8 DCGATNVRAIAVDRQGKIVARASTpnaSDIAAENSD--WHQWSLDAILQRFADCCRQINSELTE-----CHIRGITV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 94 reTT-----VVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRIPGNNNFVKSKTG-LPLSTYFsavKLRWLLDNvrkvqka 167
Cdd:PRK10331 78 --TTfgvdgALVDK-QGNLLYPIISWKCPRTAAVMENIERYISAQQLQQISGVGaFSFNTLY---KLVWLKEN------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 168 veeKRALFGTIDSWL-IWSLTGGVNGGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGLMKIS 246
Cdd:PRK10331 145 ---HPQLLEQAHAWLfISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 247 HSVKAGALEGVPISGCLGDQSAALVGQmcfqiGQAKN----TYGTGCFLLCNTGH---KCVFSDHGLLTTVAYKLGRDKP 319
Cdd:PRK10331 222 AAALLGLPVGIPVISAGHDTQFALFGS-----GAGQNqpvlSSGTWEILMVRSAQvdtSLLSQYAGSTCELDSQSGLYNP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 320 vyyaleGSVAIAGAVIRWLRDNLGiikTSEE-----IEKlAKEVGT-SYGCYFVPAFSGlyapywepSARGIICGLTQFT 393
Cdd:PRK10331 297 ------GMQWLASGVLEWVRKLFW---TAETpyqtmIEE-ARAIPPgADGVKMQCDLLA--------CQNAGWQGVTLNT 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42794763 394 NKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 461
Cdd:PRK10331 359 TRGHFYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETT 426
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
16-447 |
2.57e-22 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 100.04 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 16 VDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEIlhsvYECIEKTCEKLGQLNiDISNIKAIGVSNQRE 95
Cdd:PRK15027 5 IDLGTSGVKVILLNEQ-GEVVASQTEKLTVSRPHPLWSEQDPEQW----WQATDRAMKALGDQH-SLQDVKALGIAGQMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 96 TTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRIPGNnnfvKSKTGLPLSTYFSAVKLRWLL----DNVRKVQKAVEEK 171
Cdd:PRK15027 79 GATLLDA-QQRVLRPAILWNDGRCAQECALLEARVPQS----RVITGNLMMPGFTAPKLLWVQrhepEIFRQIDKVLLPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 172 ralfgtidSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGLMkISHSVKA 251
Cdd:PRK15027 154 --------DYLRLRMTG-----EFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGAL-LPEVAKA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 252 GALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTgcfllcnTGHKCVFSDhGLLT---TVAYKLGRDKPVYYALEGSV 328
Cdd:PRK15027 220 WGMATVPVVAGGGDNAAGAVGVGMVDANQAMLSLGT-------SGVYFAVSE-GFLSkpeSAVHSFCHALPQRWHLMSVM 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 329 AIAGAVIRW------LRDNLGIIKTSEEIEKLAKEVgtsygcYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAA 402
Cdd:PRK15027 292 LSAASCLDWaakltgLSNVPALIAAAQQADESAEPV------WFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAV 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 42794763 403 LEAVCFQTREILDAMNrDCGIPLSHLQVDGGMTSNKILMQLQADI 447
Cdd:PRK15027 366 LEGVGYALADGMDVVH-ACGIKPQSVTLIGGGARSEYWRQMLADI 409
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
15-460 |
5.47e-21 |
|
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.
Pssm-ID: 466800 [Multi-domain] Cd Length: 540 Bit Score: 96.06 E-value: 5.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 15 AVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVsnqr 94
Cdd:cd07782 4 GVDVGTGSARAGLFDL-DGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAG---VDPEQVKGIGF---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 95 ETT---VVWDK--------ITGEPLYNAVVWLDLRTQSTVEslskRIpgnnnfvkSKTGLPLSTYFSAV--------KLR 155
Cdd:cd07782 76 DATcslVVLDAegkpvsvsPSGDDERNVILWMDHRAVEEAE----RI--------NATGHEVLKYVGGKispemeppKLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 156 WLLDNvrkvQKAVEEKRALFGTIDSWLIWSLTGGVNGGVhCTDVtnASRTMLFNIHSLE-WDKQLCEFFGIPmEILPNVR 234
Cdd:cd07782 144 WLKEN----LPETWAKAGHFFDLPDFLTWKATGSLTRSL-CSLV--CKWTYLAHEGSEGgWDDDFFKEIGLE-DLVEDNF 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 235 SsseiyglmKISHSVKAGaleGVPISGCLGDQSAAlvgqmcfQIGQAKNT---------Y--GTGCflLCNTGHKCVFSD 303
Cdd:cd07782 216 A--------KIGSVVLPP---GEPVGGGLTAEAAK-------ELGLPEGTpvgvslidaHagGLGT--LGADVGGLPCEA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 304 HGLLTTVAYKLG--------RDKPV--------YY-AL-------EGSVAIAGAVIRWlrdnlgIIKT---SEEIEKLAK 356
Cdd:cd07782 276 DPLTRRLALICGtsschmavSPEPVfvpgvwgpYYsAMlpglwlnEGGQSATGALLDH------IIEThpaYPELKEEAK 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 357 EVGTSY------------------------GCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIA---FAALEAVCFQ 409
Cdd:cd07782 350 AAGKSIyeylnerleqlaeekglplayltrDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLAllyLATLQALAYG 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 42794763 410 TREILDAMNRdCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPET 460
Cdd:cd07782 430 TRHIIEAMNA-AGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEA 479
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
16-460 |
8.38e-21 |
|
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466788 [Multi-domain] Cd Length: 522 Bit Score: 95.77 E-value: 8.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 16 VDQGTSSTRFLVFNSKTAELLSHHQVEIKQ-EFPREGWVEQDPKEILHSVYECIEKTcekLGQLNIDISNIKAIGVSN-- 92
Cdd:cd07768 5 VDVGTSSARAGVYDLYAGLEMAQEPVPYYQdSSKKSWKFWQKSTEIIKALQKCVQKL---NIREGVDAYEVKGCGVDAtc 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 93 -----QRETTVVWDKITGEPLYNAVVWLDLRTQSTVESLskripgnnNFVKSKTGLP-----LSTYFSAVKLRWLLDNVR 162
Cdd:cd07768 82 slaifDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWI--------NMQCPQQLLDylggkISPEMGVPKLKYFLDEYS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 163 KVQKAVEEkraLFGTIDsWLIWSLTGgvnggvhctDVTNASRTMLF--NIHSLE--WDKQLCEFFGIPME------ILPN 232
Cdd:cd07768 154 HLRDKHFH---IFDLHD-YIAYELTR---------LYEWNICGLLGkeNLDGEEsgWSSSFFKNIDPRLEhltttkNLPS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 233 VRSSSEIYGLMKISHSVKAGALEGVPISGCLGDQSAALvgqmcfqIGQAKNTYGTGCFLLCNTGhkcvfSDHGLLTTVAY 312
Cdd:cd07768 221 NVPIGTTSGVALPEMAEKMGLHPGTAVVVSCIDAHASW-------FAVASPHLETSLFMIAGTS-----SCHMYGTTISD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 313 KL-GRDKPVYYAL-------EGSVAIAGAVIRWL-------RDNLGIIKTSEEI--------EKLAKEVGTSYGCYFVPA 369
Cdd:cd07768 289 RIpGVWGPFDTIIdpdysvyEAGQSATGKLIEHLfeshpcaRKFDEALKKGADIyqvleqtiRQIEKNNGLSIHILTLDM 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 370 FSGLYAPYWEPSARGIICGLTQFT---NKCHIAFAALEAVCFQTREILDAMNRDcGIPLSHLQVDGGMTSNKILMQLQAD 446
Cdd:cd07768 369 FFGNRSEFADPRLKGSFIGESLDTsmlNLTYKYIAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKNERLLQLIAL 447
|
490
....*....|....
gi 42794763 447 ILYIPVVKPSMPET 460
Cdd:cd07768 448 VTNVAIIKPKENMM 461
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
105-453 |
2.18e-15 |
|
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: 78.34 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 105 GEPLYNAVVWLDLRTQSTVESLSKRIPGNNNFvkSKTGLPLSTYFSAVKLRWLldnvrkvqkaVEEKRALFGTIDSWLI- 183
Cdd:cd07771 87 GELLGNPVHYRDPRTEGMMEELFEKISKEELY--ERTGIQFQPINTLYQLYAL----------KKEGPELLERADKLLMl 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 184 -----WSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGLMKISHSvKAGALEGVP 258
Cdd:cd07771 155 pdllnYLLTG-----EKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPEVA-EELGLKGIP 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 259 -ISGCLGDQSAALVGqmcfqI-GQAKNTYgtgcFLLCNT----GhkcVFSDHGLLTTVAYKLGrdkpvyYALEGSVA--- 329
Cdd:cd07771 229 vIAVASHDTASAVAA-----VpAEDEDAA----FISSGTwsliG---VELDEPVITEEAFEAG------FTNEGGADgti 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 330 -----IAGaviRWL----RDNL---GIIKTSEEIEKLAKEVgTSYGCYFVPAFSGLYAPywePSARGIICGLTQFTN--- 394
Cdd:cd07771 291 rllknITG---LWLlqecRREWeeeGKDYSYDELVALAEEA-PPFGAFIDPDDPRFLNP---GDMPEAIRAYCRETGqpv 363
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42794763 395 ---KCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVV 453
Cdd:cd07771 364 pesPGEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPVI 425
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
5-464 |
1.41e-14 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 76.31 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 5 KKAVLGplvgaVDQGTSSTRFLVFNSKTAELLSHHQVEIKQ------EFPREGWVEQDPKEILHSVYECIektCEKLGQL 78
Cdd:COG1069 1 EKYVIG-----VDFGTDSVRAVVVDAADGEELASAVHPYPRwviglyLPPPPDQARQHPLDYLEALEAAV---REALAQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 79 NIDISNIKAIGVSNQRETTVVWDKiTGEPL-----------YNAVVWLDLRTQSTVEslskRIpgnnNFVKSKTGLPLST 147
Cdd:COG1069 73 GVDPADVVGIGVDATGCTPVPVDA-DGTPLallpefaenphAMVILWKDHTAQEEAE----RI----NELAKARGEDYLR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 148 Y---------FSAvKLRWLLdnvrkvqkavEEKRALFGTIDS------WLIWSLTGGVNGGVhCTdvtnASRTMLFNIHS 212
Cdd:COG1069 144 YvggiissewFWP-KILHLL----------REDPEVYEAADSfvelcdWITWQLTGSLKRSR-CT----AGHKALWHAHE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 213 LEW-DKqlcEFF---GIPMEILPNvRSSSEIYGLmkishSVKAGAL-----------EGVPISGCLGDQSAALVGqmcfq 277
Cdd:COG1069 208 GGYpSE---EFFaalDPLLDGLAD-RLGTEIYPL-----GEPAGTLtaewaarlglpPGTAVAVGAIDAHAGAVG----- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 278 IGQAKNTY-----GT-GCFLLCNTGHKCVFS-----DHGLLttvayklgrdkPVYYALEGSVAIAGAVIRWLRDNLGiik 346
Cdd:COG1069 274 AGGVEPGTlvkvmGTsTCHMLVSPEERFVPGicgqvDGSIV-----------PGMWGYEAGQSAVGDIFAWFVRLLV--- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 347 TSEEIEKLAKEVGTS----------------YGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQT 410
Cdd:COG1069 340 PPLEYEKEAEERGISlhpllteeaaklppgeSGLHALDWFNGNRSPLADQRLKGVILGLTLGTDAEDIYRALVEATAFGT 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 42794763 411 REILDAMNrDCGIPLSHLQVDGG-MTSNKILMQLQADILYIPVVKPSMPETTALG 464
Cdd:COG1069 420 RAIIERFE-EEGVPIDEIIACGGiATKNPLVMQIYADVTGRPIKVAASEQACALG 473
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
15-461 |
6.91e-12 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 67.72 E-value: 6.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 15 AVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPR-EGWVEQDPKEILHSVYECIEktcEKLGQLNIDISNIKAIGVSNQ 93
Cdd:PRK10939 7 ALDAGTGSIRAVIFDLNGNQIAVGQAEWRHLAVPDvPGSMEFDLEKNWQLACQCIR---QALQKAGIPASDIAAVSATSM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 94 RETTVVWDKiTGEPLYnAVVWLDLRTQSTVESLSKRIPGNNNFVKSKTGLPLStyFSAV-KLRWLldnvRKVQKAVEEKR 172
Cdd:PRK10939 84 REGIVLYDR-NGTEIW-ACANVDARASREVSELKELHNNFEEEVYRCSGQTLA--LGALpRLLWL----AHHRPDIYRQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 173 ALFGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGLMKISHSVKAG 252
Cdd:PRK10939 156 HTITMISDWIAYMLSG-----ELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAKAAAETG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 253 ALEGVPI--------SGCLG------DQSAALVGQMCFQIgqakntygtgcfllCNTGHKCVFSDHGLlttvayklgRDK 318
Cdd:PRK10939 231 LRAGTPVvmgggdvqLGCLGlgvvrpGQTAVLGGTFWQQV--------------VNLPAPVTDPNMNI---------RIN 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 319 PvyYALEGSV---AIA---GAVIRWLRD-----------NLGiIKTSEEIEKLAKEVGT-SYGcyFVPAFSG-LYAPYWE 379
Cdd:PRK10939 288 P--HVIPGMVqaeSISfftGLTMRWFRDafcaeekllaeRLG-IDAYSLLEEMASRVPVgSHG--IIPIFSDvMRFKSWY 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 380 PSARGIIcGLTQFTNKCHIA--FAAL-EAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPS 456
Cdd:PRK10939 363 HAAPSFI-NLSIDPEKCNKAtlFRALeENAAIVSACNLQQIAAFSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPV 441
|
....*
gi 42794763 457 MPETT 461
Cdd:PRK10939 442 VKEAT 446
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
16-454 |
3.90e-08 |
|
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: 55.87 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 16 VDQGTSSTRFLVFNSKTaELLSHHQVEI-KQEFPREGW-VEQDPKEILHSVYECIEKTCEKLGQLNIDISNIKA---IGV 90
Cdd:cd07778 5 IDVGSTSVRIGIFDYHG-TLLATSERPIsYKQDPKDLWfVTQSSTEIWKAIKTALKELIEELSDYIVSGIGVSAtcsMVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 91 SNQRETTVVWDKITGEPLY-----NAVVWLDLRTQSTVESLskripgNNNFVKSKTGLPLSTYF---SAVKLRWLLDNVr 162
Cdd:cd07778 84 MQRDSDTSYLVPYNVIHEKsnpdqDIIFWMDHRASEETQWL------NNILPDDILDYLGGGFIpemAIPKLKYLIDLI- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 163 kvqKAVEEKRALFGTIDSWLIWSLTGGVNGG--VHCTDVTNASRTM---LFNihsleWDKQLCEFFGIPMEILPNVRSSS 237
Cdd:cd07778 157 ---KEDTFKKLEVFDLHDWISYMLATNLGHSniVPVNAPPSIGIGIdgsLKG-----WSKDFYSKLKISTKVCNVGNTFK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 238 EIYGLM----KISH-SVKAGALEGVPIS-----GCLgDQSAALVGQMCfQIGQAKNTY----GTG-CFLLcntGHKCVFS 302
Cdd:cd07778 229 EAPPLPyagiPIGKvNVILASYLGIDKStvvghGCI-DCYAGWFSTFA-AAKTLDTTLfmvaGTStCFLY---ATSSSQV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 303 DH-----GLLTTvaykLGRDKPVYyalEGSVAIAG-----------AVIRWLRDNLGIIKTSEE-IEKLAKEVGTS---- 361
Cdd:cd07778 304 GPipgiwGPFDQ----LLKNYSVY---EGGQSATGklieklfnshpAIIELLKSDANFFETVEEkIDKYERLLGQSihyl 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 362 YGCYFvpaFSGLYA----PYWEPSARGIICGLTQFTNKCHIAF---AALEAVCFQTREILDAMNRDCgIPLSHLQVDGGM 434
Cdd:cd07778 377 TRHMF---FYGDYLgnrtPYNDPNMSGSFIGESTDSSLTDLVLkyiLILEFLAFQTKLIIDNFQKEK-IIIQKVVISGSQ 452
|
490 500
....*....|....*....|
gi 42794763 435 TSNKILMQLQADILYIPVVK 454
Cdd:cd07778 453 AKNARLLQLLSTVLSKIHII 472
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
383-464 |
1.76e-04 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 44.07 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794763 383 RGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGM-TSNKILMQLQADILYIPV-VKPSmPET 460
Cdd:PRK04123 398 KGVITGLTLGTDAPDIYRALIEATAFGTRAIMECF-EDQGVPVEEVIAAGGIaRKNPVLMQIYADVLNRPIqVVAS-DQC 475
|
....
gi 42794763 461 TALG 464
Cdd:PRK04123 476 PALG 479
|
|
| |
