|
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; ... |
11-510 |
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: 964.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 11 PLVGAVVQGTNSTRFLVFNSkTAELLSHHKVELTQEFPKEGWVEQDPKEILQSVYECIARTCEKLDELNIDISNIKAVGV 90
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFDS-TGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLKALGISPSDIKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 91 SNQRETTVIWDKLTGEPLYNAVVWLDLRTQTTVEDLSKKIPGNSNFVKSKTGLPLSTYFSAVKLRWMLDNVRNVQKAVEE 170
Cdd:cd07792 80 TNQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELSAKTPGGKDHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 171 GRALFGTIDSWLIWSLTGGVNGGVHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLIKTGALEG 250
Cdd:cd07792 160 GRLLFGTVDSWLIWNLTGGKNGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIASGPLAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 251 VPISGCLGDQCAALVGQMCFQEGQAKNTYGTGCFLLCNTGRKCVFSEHGLLTTVAYKLGREKPAYYALEGSVAIAGAVIR 330
Cdd:cd07792 240 VPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAYKLGPDAPPVYALEGSIAIAGAAVQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 331 WLRDNLGIIETSGDIERLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGILCGLTQFTNKCHIAFAALEAVCFQTREILEA 410
Cdd:cd07792 320 WLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREILDA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 411 MNRDCGIPLRHLQVDGGMTNNKVLMQLQADILHIPVIKPFMPETTALGAAMAAGAAEGVSVWSLEPQALSVLRMERFEPQ 490
Cdd:cd07792 400 MNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSLNEGGRTVFEPQ 479
|
490 500
....*....|....*....|
gi 41393575 491 IQATESEIRYATWKKAVMKS 510
Cdd:cd07792 480 ISEEERERRYKRWKKAVERS 499
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
11-513 |
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: 787.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 11 PLVGAVVQGTNSTRFLVFNsKTAELLSHHKVELTQEFPKEGWVEQDPKEILQSVYECIARTCEKLdelNIDISNIKAVGV 90
Cdd:TIGR01311 1 PYILAIDQGTTSSRAIVFD-KDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKA---GIKPDDIAAIGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 91 SNQRETTVIWDKLTGEPLYNAVVWLDLRTQTTVEDLSKKIPGNsnFVKSKTGLPLSTYFSAVKLRWMLDNVRNVQKAVEE 170
Cdd:TIGR01311 77 TNQRETTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYGE--FIREKTGLPLDPYFSATKLRWLLDNVPGVREAAER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 171 GRALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLIKTGAL-E 249
Cdd:TIGR01311 155 GELLFGTIDTWLIWNLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYTDPGLLgA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 250 GVPISGCLGDQCAALVGQMCFQEGQAKNTYGTGCFLLCNTGRKCVFSEHGLLTTVAYKLGREKPAYyALEGSVAIAGAVI 329
Cdd:TIGR01311 232 EIPITGVLGDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKKPVY-ALEGSVFVAGAAV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 330 RWLRDNLGIIETSGDIERLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGILCGLTQFTNKCHIAFAALEAVCFQTREILE 409
Cdd:TIGR01311 311 QWLRDNLKLIKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTRDVLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 410 AMNRDCGIPLRHLQVDGGMTNNKVLMQLQADILHIPVIKPFMPETTALGAAMAAGAAEGVSVWSLEPQALSVlRMERFEP 489
Cdd:TIGR01311 391 AMEKDAGVEITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWR-VEKTFEP 469
|
490 500
....*....|....*....|....
gi 41393575 490 QIQATESEIRYATWKKAVMKSMGW 513
Cdd:TIGR01311 470 EMDEEEREARYAGWKEAVKRSLGW 493
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
13-514 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 733.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 13 VGAVVQGTNSTRFLVFNSKtAELLSHHKVELTQEFPKEGWVEQDPKEILQSVYECIArtcEKLDELNIDISNIKAVGVSN 92
Cdd:COG0554 5 ILAIDQGTTSTRAILFDRD-GNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIR---EALAKAGISAEDIAAIGITN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 93 QRETTVIWDKLTGEPLYNAVVWLDLRTQTTVEDLSKKipGNSNFVKSKTGLPLSTYFSAVKLRWMLDNVRNVQKAVEEGR 172
Cdd:COG0554 81 QRETTVVWDRKTGKPLYNAIVWQDRRTADICEELKAD--GLEDLIREKTGLVLDPYFSATKIKWILDNVPGARERAEAGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 173 ALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLIKTGAL-EGV 251
Cdd:COG0554 159 LLFGTIDSWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDPDLFgAEI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 252 PISGCLGDQCAALVGQMCFQEGQAKNTYGTGCFLLCNTGRKCVFSEHGLLTTVAYKLGREkpAYYALEGSVAIAGAVIRW 331
Cdd:COG0554 236 PIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGGK--VTYALEGSIFVAGAAVQW 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 332 LRDNLGIIETSGDIERLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGILCGLTQFTNKCHIAFAALEAVCFQTREILEAM 411
Cdd:COG0554 314 LRDGLGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 412 NRDCGIPLRHLQVDGGMTNNKVLMQLQADILHIPVIKPFMPETTalgaamaagaaegVSVWSLEPQALSVLRMER-FEPQ 490
Cdd:COG0554 394 EADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTalgaay--laglaVGFWKSLEELAALWKVDRrFEPQ 471
|
490 500
....*....|....*....|....
gi 41393575 491 IQATESEIRYATWKKAVMKSMGWV 514
Cdd:COG0554 472 MDEEERERLYAGWKKAVERTLGWA 495
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
13-507 |
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: 729.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 13 VGAVVQGTNSTRFLVFNSKtAELLSHHKVELTQEFPKEGWVEQDPKEILQSVYECIArtcEKLDELNIDISNIKAVGVSN 92
Cdd:cd07769 2 ILAIDQGTTSTRAILFDED-GNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIR---EALAKAGISASDIAAIGITN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 93 QRETTVIWDKLTGEPLYNAVVWLDLRTQTTVEDLSKKipGNSNFVKSKTGLPLSTYFSAVKLRWMLDNVRNVQKAVEEGR 172
Cdd:cd07769 78 QRETTVVWDKKTGKPLYNAIVWQDRRTADICEELKAK--GLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAERGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 173 ALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLIKTGAL-EGV 251
Cdd:cd07769 156 LLFGTIDTWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTDPEGLgAGI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 252 PISGCLGDQCAALVGQMCFQEGQAKNTYGTGCFLLCNTGRKCVFSEHGLLTTVAYKLGreKPAYYALEGSVAIAGAVIRW 331
Cdd:cd07769 233 PIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQIG--GKVTYALEGSIFIAGAAIQW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 332 LRDNLGIIETSGDIERLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGILCGLTQFTNKCHIAFAALEAVCFQTREILEAM 411
Cdd:cd07769 311 LRDNLGLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLEAM 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 412 NRDCGIPLRHLQVDGGMTNNKVLMQLQADILHIPVIKPFMPETTalgaamaagaaeGVSVWSLEPQALSVLRMER-FEPQ 490
Cdd:cd07769 391 EKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTalgaa--ylaglAVGFWKDLDELASLWQVDKrFEPS 468
|
490
....*....|....*..
gi 41393575 491 IQATESEIRYATWKKAV 507
Cdd:cd07769 469 MDEEERERLYRGWKKAV 485
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
11-514 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 710.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 11 PLVGAVVQGTNSTRFLVFNSKtAELLSHHKVELTQEFPKEGWVEQDPKEILQSVYECIARTCEKLDELNIDISnIKAVGV 90
Cdd:PTZ00294 2 KYIGSIDQGTTSTRFIIFDEK-GNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKGPSFK-IKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 91 SNQRETTVIWDKLTGEPLYNAVVWLDLRTQTTVEDLSKKIpGNSNFVKSKTGLPLSTYFSAVKLRWMLDNVRNVQKAVEE 170
Cdd:PTZ00294 80 TNQRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKY-GGSNFFQKITGLPISTYFSAFKIRWMLENVPAVKDAVKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 171 GRALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLIK---TGA 247
Cdd:PTZ00294 159 GTLLFGTIDTWLIWNLTGG---KSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTISgeaVPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 248 LEGVPISGCLGDQCAALVGQMCFQEGQAKNTYGTGCFLLCNTGRKCVFSEHGLLTTVAYKLGREKPAYYALEGSVAIAGA 327
Cdd:PTZ00294 236 LEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYQLGPNGPTVYALEGSIAVAGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 328 VIRWLRDNLGIIETSGDIERLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGILCGLTQFTNKCHIAFAALEAVCFQTREI 407
Cdd:PTZ00294 316 GVEWLRDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 408 LEAMNRDCGIPLRHLQVDGGMTNNKVLMQLQADILHIPVIKPFMPETTalGAAMAAGAAEGVSVW-SLEP-QALSVLRME 485
Cdd:PTZ00294 396 IESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETT--ALGAALLAGLAVGVWkSLEEvKKLIRRSNS 473
|
490 500
....*....|....*....|....*....
gi 41393575 486 RFEPQIQATESEIRYATWKKAVMKSMGWV 514
Cdd:PTZ00294 474 TFSPQMSAEERKAIYKEWNKAVERSLKWA 502
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
12-514 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 687.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 12 LVGAVVQGTNSTRFLVFNsKTAELLSHHKVELTQEFPKEGWVEQDPKEILQSVYECIARTCEKLDE--LNIDiSNIKAVG 89
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYD-RDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAkgHNVD-SGLKAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 90 VSNQRETTVIWDKLTGEPLYNAVVWLDLRTQTTVEDLSKKIPGNSNFVKSKTGLPLSTYFSAVKLRWMLDNVRNVQKAVE 169
Cdd:PLN02295 79 ITNQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKELSGGRKHFVETCGLPISTYFSATKLLWLLENVDAVKEAVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 170 EGRALFGTIDSWLIWSLTGGVNGGVHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLI-KTGAL 248
Cdd:PLN02295 159 SGDALFGTIDSWLIWNLTGGASGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIaKGWPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 249 EGVPISGCLGDQCAALVGQMCfQEGQAKNTYGTGCFLLCNTGRKCVFSEHGLLTTVAYKLGREKPAYYALEGSVAIAGAV 328
Cdd:PLN02295 239 AGVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYKLGPDAPTNYALEGSVAIAGAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 329 IRWLRDNLGIIETSGDIERLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGILCGLTQFTNKCHIAFAALEAVCFQTREIL 408
Cdd:PLN02295 318 VQWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQVKDVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 409 EAMNRDCGIP-----LRHLQVDGGMTNNKVLMQLQADILHIPVIKPFMPETTalGAAMAAGAAEGVSVWSlEPQALSVLR 483
Cdd:PLN02295 398 DAMRKDAGEEkshkgLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETT--ALGAAYAAGLAVGLWT-EEEIFASEK 474
|
490 500 510
....*....|....*....|....*....|....
gi 41393575 484 ME---RFEPQIQATESEIRYATWKKAVMKSMGWV 514
Cdd:PLN02295 475 WKnttTFRPKLDEEERAKRYASWCKAVERSFDLA 508
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
13-514 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 681.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 13 VGAVVQGTNSTRFLVFNsKTAELLSHHKVELTQEFPKEGWVEQDPKEILQSVYECIArtcEKLDELNIDISNIKAVGVSN 92
Cdd:PRK00047 7 ILALDQGTTSSRAIIFD-HDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIA---EALAKAGISPDQIAAIGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 93 QRETTVIWDKLTGEPLYNAVVWLDLRTQTTVEDLSKKipGNSNFVKSKTGLPLSTYFSAVKLRWMLDNVRNVQKAVEEGR 172
Cdd:PRK00047 83 QRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRD--GYEDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 173 ALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLIKTG--ALEG 250
Cdd:PRK00047 161 LLFGTIDTWLVWKLTGG---KVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYgfFGGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 251 VPISGCLGDQCAALVGQMCFQEGQAKNTYGTGCFLLCNTGRKCVFSEHGLLTTVAYKLGrEKPaYYALEGSVAIAGAVIR 330
Cdd:PRK00047 238 VPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGID-GKV-VYALEGSIFVAGSAIQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 331 WLRDNLGIIETSGDIERLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGILCGLTQFTNKCHIAFAALEAVCFQTREILEA 410
Cdd:PRK00047 316 WLRDGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 411 MNRDCGIPLRHLQVDGGMTNNKVLMQLQADILHIPVIKPFMPETTalGAAMAAGAAEGVSVW-SL-EPQALSVLRmERFE 488
Cdd:PRK00047 396 MQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETT--ALGAAYLAGLAVGFWkDLdELKEQWKID-RRFE 472
|
490 500
....*....|....*....|....*.
gi 41393575 489 PQIQATESEIRYATWKKAVMKSMGWV 514
Cdd:PRK00047 473 PQMDEEEREKLYAGWKKAVKRTLAWA 498
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
18-507 |
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: 675.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 18 QGTNSTRFLVFNsKTAELLSHHKVELTQEFPKEGWVEQDPKEILQSVYECIArtcEKLDELNIDISNIKAVGVSNQRETT 97
Cdd:cd07786 7 QGTTSSRAILFD-HDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAR---EALAKAGIRASDIAAIGITNQRETT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 98 VIWDKLTGEPLYNAVVWLDLRTQTTVEDLSKKipGNSNFVKSKTGLPLSTYFSAVKLRWMLDNVRNVQKAVEEGRALFGT 177
Cdd:cd07786 83 VVWDRETGKPVYNAIVWQDRRTADICEELKAE--GHEEMIREKTGLVLDPYFSATKIRWILDNVPGARERAERGELAFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 178 IDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLIKTGAL-EGVPISGC 256
Cdd:cd07786 161 IDSWLIWKLTGG---KVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDPDLLgAEIPIAGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 257 LGDQCAALVGQMCFQEGQAKNTYGTGCFLLCNTGRKCVFSEHGLLTTVAYKLGREkpAYYALEGSVAIAGAVIRWLRDNL 336
Cdd:cd07786 238 AGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLGGK--VTYALEGSIFIAGAAVQWLRDGL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 337 GIIETSGDIERLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGILCGLTQFTNKCHIAFAALEAVCFQTREILEAMNRDCG 416
Cdd:cd07786 316 GLIESAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEADSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 417 IPLRHLQVDGGMTNNKVLMQLQADILHIPVIKPFMPETTalGAAMAAGAAEGVSVWSLEPQALSVLRMER-FEPQIQATE 495
Cdd:cd07786 396 IPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETT--ALGAAYLAGLAVGLWKSLDELAKLWQVDRrFEPSMSEEE 473
|
490
....*....|..
gi 41393575 496 SEIRYATWKKAV 507
Cdd:cd07786 474 REALYAGWKKAV 485
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
19-507 |
4.39e-140 |
|
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: 414.65 E-value: 4.39e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 19 GTNSTRFLVFNSKtAELLSHHKVELTQEFPKEGWVEQDPKEILQSVYECIartCEKLDELNIDISNIKAVGVSNQRETTV 98
Cdd:cd07793 8 GTTNIRCHIFDKK-GKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVI---KEALKNAGLTPEDIAAIGISTQRNTFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 99 IWDKLTGEPLYNAVVWLDLRTQTTVEDLSKK-----IPGNSNFVKSKTGLP---------LSTYFSAVKLRWMLDNVRNV 164
Cdd:cd07793 84 TWDKKTGKPLHNFITWQDLRAAELCESWNRSlllkaLRGGSKFLHFLTRNKrflaasvlkFSTAHVSIRLLWILQNNPEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 165 QKAVEEGRALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLIK 244
Cdd:cd07793 164 KEAAEKGELLFGTIDTWLLWKLTGG---KVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFGSTD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 245 ---TGAleGVPISGCLGDQCAALVGQMCFQEGQAKNTYGTGCFLLCNTGRKCVFSEHGLLTTVAYKLGREKpaYYALEGS 321
Cdd:cd07793 241 psiFGA--EIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGGEI--TYLAEGN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 322 VAIAGAVIRWLRDNLGIiETSGDIERLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGILCGLTQFTNKCHIAFAALEAVC 401
Cdd:cd07793 317 ASDTGTVIDWAKSIGLF-DDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 402 FQTREILEAMNRDCGIPLRHLQVDGGMTNNKVLMQLQADILHIPVIKPFMPETTalGAAMAAGAAEGVSVWSlEPQALSV 481
Cdd:cd07793 396 FRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMS--ALGAAFLAGLASGIWK-SKEELKK 472
|
490 500
....*....|....*....|....*...
gi 41393575 482 LR--MERFEPQIQATESEIRYATWKKAV 507
Cdd:cd07793 473 LRkiEKIFEPKMDNEKREELYKNWKKAV 500
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
12-266 |
1.58e-99 |
|
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: 301.18 E-value: 1.58e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 12 LVGAVVQGTNSTRFLVFNsKTAELLSHHKVELTQEFPKEGWVEQDPKEILQSVYECIARTCeklDELNIDISNIKAVGVS 91
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFN-EQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTL---SQLGISLKQIKGIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 92 NQRETTVIWDKLTgEPLYNAVVWLDLRTQTTVEDLSKkiPGNSNFVKSKTGLPLSTYFSAVKLRWMLDNVRNVQKAVEeg 171
Cdd:pfam00370 77 NQGHGTVLLDKND-KPLYNAILWKDRRTAEIVENLKE--EGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIH-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 172 raLFGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLIK------T 245
Cdd:pfam00370 152 --KFLTIHDYLRWRLTG-----VFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNpelaamW 224
|
250 260
....*....|....*....|.
gi 41393575 246 GALEGVPISGCLGDQCAALVG 266
Cdd:pfam00370 225 GLDEGVPVVGGGGDQQAAAFG 245
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
19-455 |
1.10e-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: 302.91 E-value: 1.10e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 19 GTNSTRFLVFNSkTAELLSHHKVELTQEFPKEGWVEQDPKEILQSVYECIARTcekLDELNIDISNIKAVGVSNQRETTV 98
Cdd:COG1070 9 GTTSVKAVLFDA-DGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIREL---LAKAGVDPEEIAAIGVSGQMHGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 99 IWDKlTGEPLYNAVVWLDLRTQTTVEDLSKKIPGNSNFvkSKTGLPLSTYFSAVKLRWMLDN----VRNVQKaveegral 174
Cdd:COG1070 85 LLDA-DGEPLRPAILWNDTRAAAEAAELREELGEEALY--EITGNPLHPGFTAPKLLWLKENepeiFARIAK-------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 175 FGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLIK------TGAL 248
Cdd:COG1070 154 VLLPKDYLRYRLTG-----EFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTaeaaaeTGLP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 249 EGVPISGCLGDQCAALVGQMCFQEGQAKNTYGTGCFLLCNTGRKcVFSEHGLLTTVAYKLgrekPAYYALEGSVAIAGAV 328
Cdd:COG1070 229 AGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKP-LPDPEGRVHTFCHAV----PGRWLPMGATNNGGSA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 329 IRWLRDNLGIIETS--GDIERLAKEVGT-SYGCYFVPAFSGLYAPYWEPSARGILCGLTQFTNKCHIAFAALEAVCFQTR 405
Cdd:COG1070 304 LRWFRDLFADGELDdyEELNALAAEVPPgADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALR 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 41393575 406 EILEAMnRDCGIPLRHLQVDGGMTNNKVLMQLQADILHIPVIKPFMPETT 455
Cdd:COG1070 384 DGLEAL-EEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGG 432
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
19-455 |
9.63e-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: 286.38 E-value: 9.63e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 19 GTNSTRFLVFNSkTAELLSHHKVELTQEFPKEGWVEQDPKEILQSVYECIArtcEKLDELNIDISNIKAVGVSNQRETTV 98
Cdd:cd00366 8 GTTSVKAALFDE-DGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIR---EVLAKAGIDPSDIAAIGISGQMPGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 99 IWDKlTGEPLYNAVVWLDlrtqttvedlskkipgnsnfvksktglplstyfsavklrwmldnvrnvqkaveeGRALFGTI 178
Cdd:cd00366 84 LVDA-DGNPLRPAIIWLD------------------------------------------------------RRAKFLQP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 179 DSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLI------KTGALEGVP 252
Cdd:cd00366 109 NDYIVFRLTG-----EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVtpeaaeETGLPAGTP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 253 ISGCLGDQCAALVGQMCFQEGQAKNTYGTGCFLLCNTGRKCVFSEHGLLTTVAYklgrekPAYYALEGSVAIAGAVIRWL 332
Cdd:cd00366 184 VVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVPPDPRLLNRCHVV------PGLWLLEGAINTGGASLRWF 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 333 RDNLGIIETS----GDIERLAKEVGT-SYGCYFVPAFSGLYAPYWEPSARGILCGLTQFTNKCHIAFAALEAVCFQTREI 407
Cdd:cd00366 258 RDEFGEEEDSdaeyEGLDELAAEVPPgSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDN 337
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 41393575 408 LEAMnRDCGIPLRHLQVDGGMTNNKVLMQLQADILHIPVIKPFMPETT 455
Cdd:cd00366 338 LEIL-EELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGA 384
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
19-455 |
2.50e-91 |
|
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: 286.72 E-value: 2.50e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 19 GTNSTRFLVFNsKTAELLSHHKVELTQEFPKEGWVEQDPKEILQSVYECIARTCEKLDelnIDISNIKAVGVSNQRETTV 98
Cdd:cd07779 8 GTTSTRAIIFD-LDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAG---VDPEDIAAIGLTSQRSTFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 99 IWDKlTGEPLYNAVVWLDLRTqttvedlskkipgnsnfvksktglplstyfsavklrwmldnvrnvqkaveegrALFGTI 178
Cdd:cd07779 84 PVDE-DGRPLRPAISWQDKRT-----------------------------------------------------AKFLTV 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 179 DSWLIWSLTggvngGVHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLI------KTGALEGVP 252
Cdd:cd07779 110 QDYLLYRLT-----GEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLtkeaaeETGLPEGTP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 253 ISGCLGDQCAALVGQMCFQEGQAKNTYGTGCFLLCNTgRKCVFSEHGLLTTVAYKLgrekPAYYALEGSVAIAGAVIRWL 332
Cdd:cd07779 185 VVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVS-DKPVEDPERRIPCNPSAV----PGKWVLEGSINTGGSAVRWF 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 333 RDNLG---------IIETSGDIERLAKEVGT-SYGCYFVPAFSGLYAPYWEPSARGILCGLTQFTNKCHIAFAALEAVCF 402
Cdd:cd07779 260 RDEFGqdevaekelGVSPYELLNEEAAKSPPgSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAF 339
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 41393575 403 QTREILEAMnRDCGIPLRHLQVDGGMTNNKVLMQLQADILHIPVIKPFMPETT 455
Cdd:cd07779 340 ELRDNLEAM-EKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEAT 391
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
19-449 |
2.48e-80 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 259.78 E-value: 2.48e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 19 GTNSTRFLVFNSKtAELLSHHKVELTQEFPKEGWVEQDPKEILQSVYECIARTcekLDELNIDISNIKAVGVSNQRETTV 98
Cdd:cd07808 8 GTSSVKAVLVDED-GRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALREL---LAKAGISPSDIAAIGLTGQMHGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 99 IWDKlTGEPLYNAVVWLDLRTQTTVEDLSKKIPgnsNFVKSKTGLPLSTYFSAVKLRWMLDNVRNVQKAVeegRALFGTI 178
Cdd:cd07808 84 LLDK-NGRPLRPAILWNDQRSAAECEELEARLG---DEILIITGNPPLPGFTLPKLLWLKENEPEIFARI---RKILLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 179 DsWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLIK------TGALEGVP 252
Cdd:cd07808 157 D-YLRYRLTG-----ELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTpeaaeeLGLPEGTP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 253 -ISGClGDQCAALVGQMCFQEGQAKNTYGTGCFLLCNTgRKCVFSEHGLLTTVAYKLGrekPAYYALeGSVAIAGAVIRW 331
Cdd:cd07808 231 vVAGA-GDNAAAALGAGVVEPGDALISLGTSGVVFAPT-DKPVPDPKGRLHTFPHAVP---GKWYAM-GVTLSAGLSLRW 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 332 LRDNLGIIETS-GDIERLAKEVG-TSYGCYFVPAFSGLYAPYWEPSARGILCGLTQFTNKCHIAFAALEAVCFQTREILE 409
Cdd:cd07808 305 LRDLFGPDRESfDELDAEAAKVPpGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLE 384
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 41393575 410 AMnRDCGIPLRHLQVDGGMTNNKVLMQLQADILHIPVIKP 449
Cdd:cd07808 385 VL-KELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVP 423
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
19-455 |
6.02e-80 |
|
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: 257.52 E-value: 6.02e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 19 GTNSTRFLVFNsKTAELLSHHKVELTQEFPKEGWVEQDPKEILQSVYECIARTCEKLDElnidiSNIKAVGVSNQRETTV 98
Cdd:cd07773 8 GTTNVKAVLFD-EDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGP-----DPIAAISVSSQGESGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 99 IWDKlTGEPLYNAVVWLDLRTQTTVEDLSKKIPGNSNFvkSKTGLPLSTYFSAVKLRWMLDNvrnvQKAVEEGRALFGTI 178
Cdd:cd07773 82 PVDR-DGEPLGPAIVWFDPRGKEEAEELAERIGAEELY--RITGLPPSPMYSLAKLLWLREH----EPEIFAKAAKWLSV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 179 DSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLIK------TGALEGVP 252
Cdd:cd07773 155 ADYIAYRLTG-----EPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTpeaaeeLGLPAGTP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 253 IsgCLG--DQCAALVGQMCFQEGQAKNTYGTG-CFLLC-NTGRKCVFSEHGLLTTVAYKLGRekpaYYALEGSVAiAGAV 328
Cdd:cd07773 230 V--VVGghDHLCAALGAGVIEPGDVLDSTGTAeALLAVvDEPPLDEMLAEGGLSYGHHVPGG----YYYLAGSLP-GGAL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 329 IRWLRDNLGI--IETSGDIERLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGILCGLTQFTNKCHIAFAALEAVCFQTRE 406
Cdd:cd07773 303 LEWFRDLFGGdeSDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRL 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 41393575 407 ILEAMnRDCGIPLRHLQVDGGMTNNKVLMQLQADILHIPVIKPFMPETT 455
Cdd:cd07773 383 NLEAL-EKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEAT 430
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
19-455 |
6.29e-70 |
|
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466790 [Multi-domain] Cd Length: 478 Bit Score: 232.45 E-value: 6.29e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 19 GTNSTRFLVFNSKtAELLSHHKVELTQEFPKEGWVEQDPKEILQSVYECIARTCEKLDelnidISNIKAVGVSNQRETTV 98
Cdd:cd07770 8 GTTSTKAVLFDED-GRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLG-----GGEVDAIGFSSAMHSLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 99 IWDKlTGEPLYNAVVWLDLRTQTTVEDLSKKipGNSNFVKSKTGLPLSTYFSAVKLRWMLDNVRNVQKAVeegrALFGTI 178
Cdd:cd07770 82 GVDE-DGEPLTPVITWADTRAAEEAERLRKE--GDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKA----AKFVSI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 179 DSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLIK------TGALEGVP 252
Cdd:cd07770 155 KEYLLYRLTG-----ELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKpefaerLGLLAGTP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 253 ISGCLGDQCAALVGQMCFQEGQAKNTYGTgcfllcnTGRKCVFSEHGLLT----TVAYKLGREKpayYALEGSVAIAGAV 328
Cdd:cd07770 230 VVLGASDGALANLGSGALDPGRAALTVGT-------SGAIRVVSDRPVLDppgrLWCYRLDENR---WLVGGAINNGGNV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 329 IRWLRDNLGIIETS-GDIERLAKEVG-TSYGCYFVPAFSGLYAPYWEPSARGILCGLTQFTNKCHIAFAALEAVCFQTRE 406
Cdd:cd07770 300 LDWLRDTLLLSGDDyEELDKLAEAVPpGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKS 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 41393575 407 ILEAMnRDCGIPLRHLQVDGGMTNNKVLMQLQADILHIPVIKPFMPETT 455
Cdd:cd07770 380 IYEAL-EELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEAS 427
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
19-449 |
3.04e-69 |
|
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: 229.72 E-value: 3.04e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 19 GTNSTRFLVFNSKtAELLSHHKVELTQEFPKEGWVEQDPKEILQSVYECIARTcekLDELNIDISNIKAVGVSNQRETTV 98
Cdd:cd07804 8 GTTGTKGVLVDED-GKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIREL---LAKAGISPKEIAAIGVSGLVPALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 99 IWDKlTGEPLYNAVVWLDLRTQTTVEDLSKKIpgNSNFVKSKTGLPLSTYFSAVKLRWMLDNVRNV-QKAveegrALFGT 177
Cdd:cd07804 84 PVDE-NGKPLRPAILYGDRRATEEIEWLNENI--GEDRIFEITGNPLDSQSVGPKLLWIKRNEPEVfKKT-----RKFLG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 178 IDSWLIWSLTGgvnggVHCTDVTNASRTM-LFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLI------KTGALEG 250
Cdd:cd07804 156 AYDYIVYKLTG-----EYVIDYSSAGNEGgLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVtkeaaeETGLAEG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 251 VPISGCLGDQCAALVGQMCFQEGQAKNTYGT-GCFLLCNtgrKCVFSEHGLLTTVAYKlgrekPAYYALEGSVAIAGAVI 329
Cdd:cd07804 231 TPVVAGTVDAAASALSAGVVEPGDLLLMLGTaGDIGVVT---DKLPTDPRLWLDYHDI-----PGTYVLNGGMATSGSLL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 330 RWLRDNLG-----IIETSGD-----IERLAKEVG-TSYGCYFVPAFSGLYAPYWEPSARGILCGLTQFTNKCHIAFAALE 398
Cdd:cd07804 303 RWFRDEFAgeeveAEKSGGDsaydlLDEEAEKIPpGSDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRALLE 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 41393575 399 AVCFQTREILEAMNRDcGIPLRHLQVDGGMTNNKVLMQLQADILHIPVIKP 449
Cdd:cd07804 383 GVAYGLRHHLEVIREA-GLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYV 432
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
34-449 |
8.91e-66 |
|
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: 221.62 E-value: 8.91e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 34 ELLSHHKVELTQEFPKEGWVEQDPKEILQSVYECiarTCEKLDELNIDISNIKAVGVSNQRETTVIWDKlTGEPLYNAVV 113
Cdd:cd07805 22 ELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRA---TRALLEKSGIDPSDIAAIAFSGQMQGVVPVDK-DGNPLRNAII 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 114 WLDLRTQTTVEDLSKKIPGNSnFVKSKTGLPLSTYFSAVKLRWMLDNVRNVQKAVeegRALFGTIDsWLIWSLTGgvngg 193
Cdd:cd07805 98 WSDTRAAEEAEEIAGGLGGIE-GYRLGGGNPPSGKDPLAKILWLKENEPEIYAKT---HKFLDAKD-YLNFRLTG----- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 194 VHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLI------KTGALEGVPISGCLGDQCAALVGQ 267
Cdd:cd07805 168 RAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELtpeaaaELGLPAGTPVVGGGGDAAAAALGA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 268 MCFQEGQAkNTY-GTGCFLLCNTGRKCVFSEHGLLTTVAyklgrEKPAYYALEGSVAIAGAVIRWLRDNLGIIETSGD-- 344
Cdd:cd07805 248 GAVEEGDA-HIYlGTSGWVAAHVPKPKTDPDHGIFTLAS-----ADPGRYLLAAEQETAGGALEWARDNLGGDEDLGAdd 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 345 ---IERLAKEVGT-SYGCYFVPAFSGLYAPYWEPSARGILCGLTQFTNKCHIAFAALEAVCFQTREILEAMNRDCGiPLR 420
Cdd:cd07805 322 yelLDELAAEAPPgSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWLLEALEKLTR-KID 400
|
410 420
....*....|....*....|....*....
gi 41393575 421 HLQVDGGMTNNKVLMQLQADILHIPVIKP 449
Cdd:cd07805 401 ELRLVGGGARSDLWCQILADVLGRPVEVP 429
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
19-458 |
5.58e-51 |
|
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: 180.82 E-value: 5.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 19 GTNSTRFLVFNSKTAELLSHHkVELTQEFPKEGWVEQDPKEILQSVYECIARTCEKLdelNIDISNIKAVGVSNQRETTV 98
Cdd:cd07802 8 GTTNVKAVLFDLDGREIAVAS-RPTPVISPRPGWAERDMDELWQATAEAIRELLEKS---GVDPSDIAGVGVTGHGNGLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 99 IWDKlTGEPLYNAVVWLDLRTQTTVEDLSKKipGNSNFVKSKTGLPLSTYFSAVKLRWMLDNVRNVQKAVeegRALFGTI 178
Cdd:cd07802 84 LVDK-DGKPVRNAILSNDSRAADIVDRWEED--GTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRI---RTVLFCK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 179 DsWLIWSLTGgvnggVHCTDVTNASrTMLFNIHSLEWDKELCDFFEIP--MDLLPNVFSSSEIYGLI------KTGALEG 250
Cdd:cd07802 158 D-WIRYRLTG-----EISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVtaeaaaLTGLPEG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 251 VPISGCLGDQCAALVGQMCFQEGQAKNTYGTGCfllCNTG--RKCVFSEHGLLTTVAYKLGRekpaYYALEGSVAIAGaV 328
Cdd:cd07802 231 TPVAAGAFDVVASALGAGAVDEGQLCVILGTWS---INEVvtDEPVVPDSVGSNSLHADPGL----YLIVEASPTSAS-N 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 329 IRWLRDNLGIIETSGD------IERLAKEVG-TSYGCYFVPaFsgLYAPYWEPSARGILCGLTQFTNKCHIAFAALEAVC 401
Cdd:cd07802 303 LDWFLDTLLGEEKEAGgsdydeLDELIAAVPpGSSGVIFLP-Y--LYGSGANPNARGGFFGLTAWHTRAHLLRAVYEGIA 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 41393575 402 FQTREILEAMNRDCgiPLRHLQVDGGMTNNKVLMQLQADILHIPVIKPFMPETTALG 458
Cdd:cd07802 380 FSHRDHLERLLVAR--KPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALG 434
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
19-449 |
1.92e-46 |
|
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466801 [Multi-domain] Cd Length: 429 Bit Score: 168.17 E-value: 1.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 19 GTNSTRFLVFNSKtAELLSHHKVELTQEFPKEGWVEQDPKEILQSVYECIARTCEKLdelniDISNIKAVGVSNQRETTV 98
Cdd:cd07783 8 GTSGVRAVVVDED-GTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAEL-----RPRRVVAIAVDGTSGTLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 99 IWDKlTGEPLYNAVVWLDLRtqttVEDLSKKIPGNSNFVKSKTGLPLSTYFSAVKLRWMLDNVRNVQKAVeegrALFGTI 178
Cdd:cd07783 82 LVDR-EGEPLRPAIMYNDAR----AVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKT----AKFLHQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 179 DSWLIWSLTGGVNggvhCTDVTNASRTmLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLI------KTGALEGVP 252
Cdd:cd07783 153 ADWLAGRLTGDRG----VTDYNNALKL-GYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLtaeaaeELGLPAGTP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 253 IsgCLG--DQCAALVGQMCFQEGQAKNTYGTG-CF-LLCntgRKCVFSEHGLLTTvaYKLGREkpaYYALEGSVAIAGAV 328
Cdd:cd07783 228 V--VAGttDSIAAFLASGAVRPGDAVTSLGTTlVLkLLS---DKRVPDPGGGVYS--HRHGDG---YWLVGGASNTGGAV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 329 IRWLRDNlgiietsGDIERLAKEVGTSY--GCYFVP-AFSGLYAPYWEPSARGILCGLTqfTNKCHIAFAALEAVCFQTR 405
Cdd:cd07783 298 LRWFFSD-------DELAELSAQADPPGpsGLIYYPlPLRGERFPFWDPDARGFLLPRP--HDRAEFLRALLEGIAFIER 368
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 41393575 406 EILEAMNRDCGIPLRHLQVDGGMTNNKVLMQLQADILHIPVIKP 449
Cdd:cd07783 369 LGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIA 412
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
275-458 |
2.08e-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: 158.64 E-value: 2.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 275 AKNTYGTGCFLLCnTGRKCVFSEHGLLTTVAyklGREKPAYYALEGSVAIAGAVIRWLRDNLGI---IETSGDIERLAKE 351
Cdd:pfam02782 1 LAISAGTSSFVLV-ETPEPVLSVHGVWGPYT---NEMLPGYWGLEGGQSAAGSLLAWLLQFHGLreeLRDAGNVESLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 352 VGTS-----YGCYFVPAFSGLYAPYWEPSARGILCGLTQFTNKCHIAFAALEAVCFQTREILEAMNRDCGIPLRHLQVDG 426
Cdd:pfam02782 77 AALAavapaGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSG 156
|
170 180 190
....*....|....*....|....*....|..
gi 41393575 427 GMTNNKVLMQLQADILHIPVIKPFMPETTALG 458
Cdd:pfam02782 157 GGSRNPLLLQLLADALGLPVVVPGPDEATALG 188
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
19-458 |
1.63e-40 |
|
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: 152.38 E-value: 1.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 19 GTNSTRFLVFNSKTAELLSHHKvELTQEFPK--EGWVEQDPKEILQSVYECIARTcekLDELNIDISNIKAVGVSNQRET 96
Cdd:cd07798 8 GTGGGRCALVDSEGKIVAIAYR-EWEYYTDDdyPDAKEFDPEELWEKICEAIREA---LKKAGISPEDISAVSSTSQREG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 97 TVIWDKlTGEPLYnAVVWLDLRTQTTVEDLSKKIPgnsNFVKSKTGLPLSTYFSAVKLRWMLDNvrnvQKAVEEGRALFG 176
Cdd:cd07798 84 IVFLDK-DGRELY-AGPNIDARGVEEAAEIDDEFG---EEIYTTTGHWPTELFPAARLLWFKEN----RPEIFERIATVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 177 TIDSWLIWSLTGGVnggvhCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLIK------TGALEG 250
Cdd:cd07798 155 SISDWIGYRLTGEL-----VSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSeeaareLGLPEG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 251 VPISGCLGD-QCAALvGQMCFQEGQAKNTYGTGCFLLCNTGRkCVFSEHGLLTTVAYkLGREKpayYALEGSVAIAGAVI 329
Cdd:cd07798 230 TPVVVGGADtQCALL-GSGAIEPGDIGIVAGTTTPVQMVTDE-PIIDPERRLWTGCH-LVPGK---WVLESNAGVTGLNY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 330 RWLRDNL-GIIETS-GDIERLAKEVG-TSYGCYfvpAFSGLYAPYwePSARGILCGLTQFT--------NKCHIAFAALE 398
Cdd:cd07798 304 QWLKELLyGDPEDSyEVLEEEASEIPpGANGVL---AFLGPQIFD--ARLSGLKNGGFLFPtplsaselTRGDFARAILE 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 399 AVCFQTREILEAMNRDCGIPLRHLQVDGGMTNNKVLMQLQADILHIPVIKPFMPETTALG 458
Cdd:cd07798 379 NIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALG 438
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
19-458 |
1.81e-32 |
|
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: 129.59 E-value: 1.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 19 GTNSTRFLVFNSKTAELLSHHKVELTQEFPKEGWVEQDPKEILQSVYECIArtcEKLDELNIDISNIKAVGVSNQRETTV 98
Cdd:cd07809 8 GTQSIKAVLIDAETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFA---QLLKDAGAELRDVAAIGISGQMHGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 99 IWDKlTGEPLYNAVVWLDLRTQTTVEDLSKKIPGNsnfVKSKTGLPLSTYFSAVKLRWMLDNvrnvqkavEEGraLFGTI 178
Cdd:cd07809 85 ALDA-DGKVLRPAKLWCDTRTAPEAEELTEALGGK---KCLLVGLNIPARFTASKLLWLKEN--------EPE--HYARI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 179 DS------WLIWSLTGGvnggvHCTDVTNASRTMLFNIHSLEWDKELCDFFE---IPMDLLPNVFSSSEIYGLI-KTGAL 248
Cdd:cd07809 151 AKillphdYLNWKLTGE-----KVTGLGDASGTFPIDPRTRDYDAELLAAIDpsrDLRDLLPEVLPAGEVAGRLtPEGAE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 249 E-----GVPISGCLGDQCAALVGQMCFQEGQAKNTYGT-GCflLCNTGRKCVFSEHGLLTTVAYKLGREKPayyalegSV 322
Cdd:cd07809 226 ElglpaGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTsGT--AYGVSDKPVSDPHGRVATFCDSTGGMLP-------LI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 323 AIAGAVIRWLRDNLGIIETS-GDIERLAKEV-GTSYGCYFVPAFSGLYAPYWePSARGILCGLTQF-TNKCHIAFAALEA 399
Cdd:cd07809 297 NTTNCLTAWTELFRELLGVSyEELDELAAQApPGAGGLLLLPFLNGERTPNL-PHGRASLVGLTLSnFTRANLARAALEG 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 41393575 400 VCFQTREILEAMnRDCGIPLRHLQVDGGMTNNKVLMQLQADILHIPVIKPFMPETTALG 458
Cdd:cd07809 376 ATFGLRYGLDIL-RELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALG 433
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
19-447 |
2.07e-29 |
|
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: 121.49 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 19 GTNSTRFLVFNSKTAELLSHHKVE--LTQEFPKEGWVEQDPKEILQSVYECIaRTCekLDELNIDISNIKAVGV---SNq 93
Cdd:cd07781 8 GTQSVRAGLVDLADGEELASAVVPypTGYIPPRPGWAEQNPADYWEALEEAV-RGA--LAEAGVDPEDVVGIGVdttSS- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 94 retTVIWDKLTGEPLYNAVVWLDLRTQ---TTVEDLSKKIPGNSnfvKSKTGLPLS--TYFSavKLRWMLDNVRNVQKA- 167
Cdd:cd07781 84 ---TVVPVDEDGNPLAPAILWMDHRAQeeaAEINETAHPALEYY---LAYYGGVYSseWMWP--KALWLKRNAPEVYDAa 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 168 ---VEEGralfgtidSWLIWSLTGGVNGGVhCtdvtNASRTMLFNIHSLEWDKELC-----DFFEIPMDLLPNVFSSSEI 239
Cdd:cd07781 156 ytiVEAC--------DWINARLTGRWVRSR-C----AAGHKWMYNEWGGGPPREFLaaldpGLLKLREKLPGEVVPVGEP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 240 YGLI------KTGALEGVPISGCLGDQCAALVGQMCFQEGQAKNTYGT-GCFLLcnTGRKCVFSEhGLLTTVAyklGREK 312
Cdd:cd07781 223 AGTLtaeaaeRLGLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTsTCHLM--VSPKPVDIP-GICGPVP---DAVV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 313 PAYYALEGSVAIAGAVIRWLRDNLG--IIETSGDI----ERLAKEVGTsyGCyfvpafSGLYA---------PYWEPSAR 377
Cdd:cd07781 297 PGLYGLEAGQSAVGDIFAWFVRLFVppAEERGDSIyallSEEAAKLPP--GE------SGLVAldwfngnrtPLVDPRLR 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41393575 378 GILCGLTQFTNKCHIAFAALEAVCFQTREILEAMnRDCGIPLRHLQVDGGMT-NNKVLMQLQADILHIPVI 447
Cdd:cd07781 369 GAIVGLTLGTTPAHIYRALLEATAFGTRAIIERF-EEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPIK 438
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
19-447 |
3.95e-29 |
|
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: 119.63 E-value: 3.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 19 GTNSTRFLVFNSKTAELLS----HHKVELTQEFPkeGWVEQDPKEILQSVYECIARTCEKLDelnidiSNIKAVGVSNQR 94
Cdd:cd07777 8 GTTSIKAALLDLESGRILEsvsrPTPAPISSDDP--GRSEQDPEKILEAVRNLIDELPREYL------SDVTGIGITGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 95 ETTVIWDKlTGEPLYNAVVWLDLRTqtTVEDLSKKIPGNSNFvKSKTGLPLSTYFSAVKLRWMLdnvrnVQKAVEEGRAL 174
Cdd:cd07777 80 HGIVLWDE-DGNPVSPLITWQDQRC--SEEFLGGLSTYGEEL-LPKSGMRLKPGYGLATLFWLL-----RNGPLPSKADR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 175 FGTIDSWLIWSLTGGVNggvHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLIKTGALEGVPIS 254
Cdd:cd07777 151 AGTIGDYIVARLTGLPK---PVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLSSALPKGIPVY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 255 GCLGDQCAALVGQMCFQEGQAKNTYGTG---CFLLCNTGRKCV-----FSEHGLLTTVAyKLgrekPAYYALEgsvAIAG 326
Cdd:cd07777 228 VALGDNQASVLGSGLNEENDAVLNIGTGaqlSFLTPKFELSGSveirpFFDGRYLLVAA-SL----PGGRALA---VLVD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 327 AVIRWLRDnLGIIETSGDI-ERLAKEVGTSYGC--YFVPAFSGlyaPYWEPSARGILCGLTQ--FTNKcHIAFAALEAVC 401
Cdd:cd07777 300 FLREWLRE-LGGSLSDDEIwEKLDELAESEESSdlSVDPTFFG---ERHDPEGRGSITNIGEsnFTLG-NLFRALCRGIA 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 41393575 402 fqtREILEAMNRDC--GIPLRHLQVDGGM-TNNKVLMQLQADILHIPVI 447
Cdd:cd07777 375 ---ENLHEMLPRLDldLSGIERIVGSGGAlRKNPVLRRIIEKRFGLPVV 420
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
19-461 |
1.71e-26 |
|
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: 112.33 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 19 GTNSTRFLVFNSKTAELlSHHKVELTQEFPKEGWVEQDPKEILQSVYECIARTCEKLDELNidiSNIKAVGVSNQRETTV 98
Cdd:cd24121 8 GTSVVKAVAFDLDGREL-AVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLP---DRVAAIGVTGQGDGTW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 99 IWDKLtGEPLYNAVVWLDLRTQTTVEDLSKKipGNSNFVKSKTGLPLSTYFSAVKLRWMLDNVrnvQKAVEEGRALFGTI 178
Cdd:cd24121 84 LVDED-GRPVRDAILWLDGRAADIVERWQAD--GIAEAVFEITGTGLFPGSQAAQLAWLKENE---PERLERARTALHCK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 179 DsWLIWSLTGgvnggVHCTDVTNASRTMlFNIHSLEWDKELCDFFEIP--MDLLPNVFSSSEIYGLI------KTGALEG 250
Cdd:cd24121 158 D-WLFYKLTG-----EIATDPSDASLTF-LDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLtpeaaaATGLPAG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 251 VPISGCLGDQCAALVGQMCFQEGQAKNTYGTGCFllcntgrkcvfseHGLLTTVAYkLGREKPAY---YALEGSV----- 322
Cdd:cd24121 231 TPVVLGPFDVVATALGSGAIEPGDACSILGTTGV-------------HEVVVDEPD-LEPEGVGYticLGVPGRWlrama 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 323 AIAG-AVIRWLRDNLGIIETSG----------DIERLAKEV-----GTSYGCYFVPAfsGLYAPYWEPSARGILCGLTQF 386
Cdd:cd24121 297 NMAGtPNLDWFLRELGEVLKEGaepagsdlfqDLEELAASSppgaeGVLYHPYLSPA--GERAPFVNPNARAQFTGLSLE 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41393575 387 TNKCHIAFAALEAVCFQTREILEAMnrdcGIPLRHLQVDGGMTNNKVLMQLQADILHIPVIKPFMPETTALGAAM 461
Cdd:cd24121 375 HTRADLLRAVYEGVALAMRDCYEHM----GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAM 445
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
15-455 |
6.59e-24 |
|
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: 105.11 E-value: 6.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 15 AVVQGTNSTRFLVFNSKTAELLSHHKVELTQEFPK-EGWVEQDPKEILQSVYECIARTCEKLDelnIDISNIKAVGVSNQ 93
Cdd:cd07775 4 ALDAGTGSGRAVIFDLEGNQIAVAQREWRHKEVPDvPGSMDFDTEKNWKLICECIREALKKAG---IAPKSIAAISTTSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 94 RETTVIWDKlTGEPLYnAVVWLDLRTQTTVEDLSKKIPGNSNFVKSKTGLPLStyFSAV-KLRWmldnVRNVQKAVEEGR 172
Cdd:cd07775 81 REGIVLYDN-EGEEIW-ACANVDARAAEEVSELKELYNTLEEEVYRISGQTFA--LGAIpRLLW----LKNNRPEIYRKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 173 ALFGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLIK------TG 246
Cdd:cd07775 153 AKITMLSDWIAYKLSG-----ELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTkeaaeeTG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 247 ALEGVPISGCLGDQCAALVGQMCFQEGQAKNTYGTGCFLLCNTGRKcVFSEHGLLTTVAYKLgrekPAYYALEGSVAIAG 326
Cdd:cd07775 228 LKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAP-VTDPAMNIRVNCHVI----PDMWQAEGISFFPG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 327 AVIRWLRDNLGIIETSGD----------IERLAKEVGTsyGCY-FVPAFSGL--YApYWEPSARGILcGLTQFTNKCHIA 393
Cdd:cd07775 303 LVMRWFRDAFCAEEKEIAerlgidaydlLEEMAKDVPP--GSYgIMPIFSDVmnYK-NWRHAAPSFL-NLDIDPEKCNKA 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41393575 394 --FAAL-EAVCFQTREILEAMNRDCGIPLRHLQVDGGMTNNKVLMQLQADILHIPVIKPFMPETT 455
Cdd:cd07775 379 tfFRAImENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEAT 443
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
19-441 |
3.59e-21 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 96.57 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 19 GTNSTRFLVFNSKtAELLSHHKVELTQEFPKEGWVEQDPKEILQSVyeciARTCEKLDELNiDISNIKAVGVSNQRETTV 98
Cdd:PRK15027 8 GTSGVKVILLNEQ-GEVVASQTEKLTVSRPHPLWSEQDPEQWWQAT----DRAMKALGDQH-SLQDVKALGIAGQMHGAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 99 IWDKlTGEPLYNAVVWLDLRTQTTVEDLSKKIPGNsnfvKSKTGLPLSTYFSAVKLRWmldnvrnVQKAVEEgraLFGTI 178
Cdd:PRK15027 82 LLDA-QQRVLRPAILWNDGRCAQECALLEARVPQS----RVITGNLMMPGFTAPKLLW-------VQRHEPE---IFRQI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 179 DS------WLIWSLTggvngGVHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYG-----LIKTGA 247
Cdd:PRK15027 147 DKvllpkdYLRLRMT-----GEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGallpeVAKAWG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 248 LEGVPISGCLGDQCAALVGQMCFQEGQAKNTYGTgcfllcnTGRKCVFSEhGLLT---TVAYKLGREKPAYYALEGSVAI 324
Cdd:PRK15027 222 MATVPVVAGGGDNAAGAVGVGMVDANQAMLSLGT-------SGVYFAVSE-GFLSkpeSAVHSFCHALPQRWHLMSVMLS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 325 AGAVIRWLRDNLGIIETSGDIERLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGILCGLTQFTNKCHIAFAALEAVCFQT 404
Cdd:PRK15027 294 AASCLDWAAKLTGLSNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYAL 373
|
410 420 430
....*....|....*....|....*....|....*..
gi 41393575 405 REILEAMNrDCGIPLRHLQVDGGMTNNKVLMQLQADI 441
Cdd:PRK15027 374 ADGMDVVH-ACGIKPQSVTLIGGGARSEYWRQMLADI 409
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
52-455 |
1.65e-20 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 94.32 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 52 WVEQDPKEILQSVYECIARTCEKLDElnidiSNIKAVGVsnqreTT-----VIWDKlTGEPLYNAVVWLDLRTQTTVEDL 126
Cdd:PRK10331 44 WHQWSLDAILQRFADCCRQINSELTE-----CHIRGITV-----TTfgvdgALVDK-QGNLLYPIISWKCPRTAAVMENI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 127 SKKIPGNSNFVKSKTG-LPLSTYFsavKLRWMLDNVRNvqkaveegraLFGTIDSWL-IWSLTGGVNGGVHCTDVTNASR 204
Cdd:PRK10331 113 ERYISAQQLQQISGVGaFSFNTLY---KLVWLKENHPQ----------LLEQAHAWLfISSLINHRLTGEFTTDITMAGT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 205 TMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLIKTGALE------GVPISGCLGDQCAALVGQMCfQEGQAKNT 278
Cdd:PRK10331 180 SQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPSAAAllglpvGIPVISAGHDTQFALFGSGA-GQNQPVLS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 279 YGTGCFLLCNTGR---KCVFSEHGLLTTVAYKLGREKPAYYALegsvaiAGAVIRWLRDNLGIIETSGD--IERlAKEVG 353
Cdd:PRK10331 259 SGTWEILMVRSAQvdtSLLSQYAGSTCELDSQSGLYNPGMQWL------ASGVLEWVRKLFWTAETPYQtmIEE-ARAIP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 354 T-SYGCYFVPAFSGlyapywepSARGILCGLTQFTNKCHIAFAALEAVCFQTREILEAMNRDCGIPLRHLQVDGGMTNNK 432
Cdd:PRK10331 332 PgADGVKMQCDLLA--------CQNAGWQGVTLNTTRGHFYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNA 403
|
410 420
....*....|....*....|...
gi 41393575 433 VLMQLQADILHIPVIKPFMPETT 455
Cdd:PRK10331 404 LWNQIKANMLDIPIKVLDDAETT 426
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
19-449 |
9.51e-18 |
|
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: 86.14 E-value: 9.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 19 GTNSTRFLVFNSKTAELLSHHKVELTQ-EFPKEGWVEQDPKEILQSVYECIARTcekLDELNIDISNIKAVGVSN----- 92
Cdd:cd07768 8 GTSSARAGVYDLYAGLEMAQEPVPYYQdSSKKSWKFWQKSTEIIKALQKCVQKL---NIREGVDAYEVKGCGVDAtcsla 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 93 --QRETTVIWDKLTGEPLYNAVVWLDLRTQTTVEDLskkipgnsNFVKSKTGLP-----LSTYFSAVKLRWMLDNVRNVQ 165
Cdd:cd07768 85 ifDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWI--------NMQCPQQLLDylggkISPEMGVPKLKYFLDEYSHLR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 166 KAVEEgraLFGTIDsWLIWSLTGgvnggvhctDVTNASRTMLF--NIHSLE--WDKElcdFFEIpMDLLPNVFSSSEIYG 241
Cdd:cd07768 157 DKHFH---IFDLHD-YIAYELTR---------LYEWNICGLLGkeNLDGEEsgWSSS---FFKN-IDPRLEHLTTTKNLP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 242 LIKTgalegvpisgcLGDQCAALVGQMCFQEGQAKNTY----------GTGCFLLCNTGRKCVFSEHgllTTVAYKLGRE 311
Cdd:cd07768 220 SNVP-----------IGTTSGVALPEMAEKMGLHPGTAvvvscidahaSWFAVASPHLETSLFMIAG---TSSCHMYGTT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 312 K----------------PAYYALEGSVAIAGAVIRWL-------RDNLGIIETSGDI--------ERLAKEVGTSYGCYF 360
Cdd:cd07768 286 IsdripgvwgpfdtiidPDYSVYEAGQSATGKLIEHLfeshpcaRKFDEALKKGADIyqvleqtiRQIEKNNGLSIHILT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 361 VPAFSGLYAPYWEPSARGILCGLTQFT---NKCHIAFAALEAVCFQTREILEAMNRDcGIPLRHLQVDGGMTNNKVLMQL 437
Cdd:cd07768 366 LDMFFGNRSEFADPRLKGSFIGESLDTsmlNLTYKYIAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKNERLLQL 444
|
490
....*....|..
gi 41393575 438 QADILHIPVIKP 449
Cdd:cd07768 445 IALVTNVAIIKP 456
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
105-447 |
2.03e-16 |
|
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: 81.81 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 105 GEPLYNAVVWLDLRTQTTVEDLSKKIPGNSNFvkSKTGLPLSTYFSAVKLRWMldnvrnvqkaVEEGRALFGTIDSWLI- 183
Cdd:cd07771 87 GELLGNPVHYRDPRTEGMMEELFEKISKEELY--ERTGIQFQPINTLYQLYAL----------KKEGPELLERADKLLMl 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 184 -----WSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLIKT-----GALEGVP- 252
Cdd:cd07771 155 pdllnYLLTG-----EKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPevaeeLGLKGIPv 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 253 ISGCLGDQCAALVGQMCFQEGQAkntygtgcFLLCNT----GrkcVFSEHGLLTTVAYKLGrekpayYALEGSVA----- 323
Cdd:cd07771 230 IAVASHDTASAVAAVPAEDEDAA--------FISSGTwsliG---VELDEPVITEEAFEAG------FTNEGGADgtirl 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 324 ---IAGaviRWL----RDNL---GIIETSGDIERLAKEVgTSYGCYFVPAFSGLYAPYWEPSArgI--LCGLTQFT---N 388
Cdd:cd07771 293 lknITG---LWLlqecRREWeeeGKDYSYDELVALAEEA-PPFGAFIDPDDPRFLNPGDMPEA--IraYCRETGQPvpeS 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 41393575 389 KCHIAFAALEAVCFQTREILEAMNRDCGIPLRHLQVDGGMTNNKVLMQLQADILHIPVI 447
Cdd:cd07771 367 PGEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPVI 425
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
19-449 |
8.85e-16 |
|
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: 80.27 E-value: 8.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 19 GTNSTRFLVFNSkTAELLSHHKVELTQEFPKEGWVEQDPKEILQSVYECIaRTCekLDELNIDISNIKAVGVsnqrETT- 97
Cdd:cd07782 8 GTGSARAGLFDL-DGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAV-KEV--LEGAGVDPEQVKGIGF----DATc 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 98 --VIWDK--------LTGEPLYNAVVWLDLRTQTTVEdlskKIpgNSnfvkskTGLPLSTYFSAV--------KLRWMLd 159
Cdd:cd07782 80 slVVLDAegkpvsvsPSGDDERNVILWMDHRAVEEAE----RI--NA------TGHEVLKYVGGKispemeppKLLWLK- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 160 nvRNVQKAVEEGRALFGTIDsWLIWSLTGGVNGGVhCTDVtnASRTMLFNIHSLE-WDKelcDFFE-IPMDLLpnvfsSS 237
Cdd:cd07782 147 --ENLPETWAKAGHFFDLPD-FLTWKATGSLTRSL-CSLV--CKWTYLAHEGSEGgWDD---DFFKeIGLEDL-----VE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 238 EIYGLIKTGALE-GVPISGCLGDQCAAlvgQMCFQEGQAKNT-----Y----GT-GCFLLCNTGRKCVFSEHglLTTVA- 305
Cdd:cd07782 213 DNFAKIGSVVLPpGEPVGGGLTAEAAK---ELGLPEGTPVGVslidaHagglGTlGADVGGLPCEADPLTRR--LALICg 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 306 -----YKLGREK---------------PAYYALEGSVAIAGAVIRWlrdnlgIIET---SGDIERLAKEVGTSY------ 356
Cdd:cd07782 288 tsschMAVSPEPvfvpgvwgpyysamlPGLWLNEGGQSATGALLDH------IIEThpaYPELKEEAKAAGKSIyeylne 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 357 ------------------GCYFVPAFSGLYAPYWEPSARGILCGLTQFTNKCHIA---FAALEAVCFQTREILEAMNRdC 415
Cdd:cd07782 362 rleqlaeekglplayltrDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLAllyLATLQALAYGTRHIIEAMNA-A 440
|
490 500 510
....*....|....*....|....*....|....
gi 41393575 416 GIPLRHLQVDGGMTNNKVLMQLQADILHIPVIKP 449
Cdd:cd07782 441 GHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLP 474
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
19-458 |
6.47e-11 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 64.75 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 19 GTNSTRFLVFNSKTAELLSHHKVELTQ------EFPKEGWVEQDPKEILQSVYECIartCEKLDELNIDISNIKAVGVSN 92
Cdd:COG1069 10 GTDSVRAVVVDAADGEELASAVHPYPRwviglyLPPPPDQARQHPLDYLEALEAAV---REALAQAGVDPADVVGIGVDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 93 QRETTVIWDKlTGEPL-----------YNAVVWLDLRTQTTVEDLskkipgnsNFVKSKTGLPLSTY---------FSAv 152
Cdd:COG1069 87 TGCTPVPVDA-DGTPLallpefaenphAMVILWKDHTAQEEAERI--------NELAKARGEDYLRYvggiissewFWP- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 153 KLRWMLdnvrnvqkavEEGRALFGTIDS------WLIWSLTGGVNGGVhCTdvtnASRTMLFNIHSLEWDKElcDFFEIp 226
Cdd:COG1069 157 KILHLL----------REDPEVYEAADSfvelcdWITWQLTGSLKRSR-CT----AGHKALWHAHEGGYPSE--EFFAA- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 227 MDLLPNVFS---SSEIYGL------------IKTGALEGVPISGCLGDQCAALVGQMCFQEGQ-AKNtYGT-GCFLLCNT 289
Cdd:COG1069 219 LDPLLDGLAdrlGTEIYPLgepagtltaewaARLGLPPGTAVAVGAIDAHAGAVGAGGVEPGTlVKV-MGTsTCHMLVSP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 290 GRKC-------VFSehGLLttvayklgrekPAYYALEGSVAIAGAVIRWLRDNLG-------IIETSGD--IERLAKE-- 351
Cdd:COG1069 298 EERFvpgicgqVDG--SIV-----------PGMWGYEAGQSAVGDIFAWFVRLLVppleyekEAEERGIslHPLLTEEaa 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 352 ---VGTSyGCYFVPAFSGLYAPYWEPSARGILCGLTQFTNKCHIAFAALEAVCFQTREILEAMNrDCGIPLRHLQVDGG- 427
Cdd:COG1069 365 klpPGES-GLHALDWFNGNRSPLADQRLKGVILGLTLGTDAEDIYRALVEATAFGTRAIIERFE-EEGVPIDEIIACGGi 442
|
490 500 510
....*....|....*....|....*....|.
gi 41393575 428 MTNNKVLMQLQADILHIPVIKPFMPETTALG 458
Cdd:COG1069 443 ATKNPLVMQIYADVTGRPIKVAASEQACALG 473
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
15-266 |
6.39e-08 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 55.40 E-value: 6.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 15 AVVQGTNSTRFLVFNSKTAELLSHHKVELTQEFPK-EGWVEQDPKEILQSVYECIArtcEKLDELNIDISNIKAVGVSNQ 93
Cdd:PRK10939 7 ALDAGTGSIRAVIFDLNGNQIAVGQAEWRHLAVPDvPGSMEFDLEKNWQLACQCIR---QALQKAGIPASDIAAVSATSM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 94 RETTVIWDKlTGEPLYnAVVWLDLRTQTTVEDLSKKIPGNSNFVKSKTGLPLStyFSAV-KLRWmldnVRNVQKAVEEGR 172
Cdd:PRK10939 84 REGIVLYDR-NGTEIW-ACANVDARASREVSELKELHNNFEEEVYRCSGQTLA--LGALpRLLW----LAHHRPDIYRQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 173 ALFGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLI------KTG 246
Cdd:PRK10939 156 HTITMISDWIAYMLSG-----ELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVtakaaaETG 230
|
250 260 270
....*....|....*....|....*....|....
gi 41393575 247 ALEGVPI--------SGCLG------DQCAALVG 266
Cdd:PRK10939 231 LRAGTPVvmgggdvqLGCLGlgvvrpGQTAVLGG 264
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
377-446 |
1.69e-07 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 54.08 E-value: 1.69e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41393575 377 RGILCGLTQFTNKCHIAFAALEAVCFQTREILEAMnRDCGIPLRHLQVDGGM-TNNKVLMQLQADILHIPV 446
Cdd:PRK04123 398 KGVITGLTLGTDAPDIYRALIEATAFGTRAIMECF-EDQGVPVEEVIAAGGIaRKNPVLMQIYADVLNRPI 467
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
19-453 |
2.67e-03 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466797 [Multi-domain] Cd Length: 544 Bit Score: 40.47 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 19 GTNSTRFLVFNSKTaELLSHHKVELT-QEFPKEGW-VEQDPKEILQSVYECIARTCEKLDELNIDISNIKA---VGVSNQ 93
Cdd:cd07778 8 GSTSVRIGIFDYHG-TLLATSERPISyKQDPKDLWfVTQSSTEIWKAIKTALKELIEELSDYIVSGIGVSAtcsMVVMQR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 94 RETT-------VIWDKltGEPLYNAVVWLDLRTQTTVEDLSKKIPGNS-NFVKSK----TGLPlstyfsavKLRWMLDNV 161
Cdd:cd07778 87 DSDTsylvpynVIHEK--SNPDQDIIFWMDHRASEETQWLNNILPDDIlDYLGGGfipeMAIP--------KLKYLIDLI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 162 RNVQ-KAVE--------EGRALFGTIDSWLIWSLTGGVNGGVHCTDVTNASRTMLfniHSLEWDKELCDFFEIPMDLLPN 232
Cdd:cd07778 157 KEDTfKKLEvfdlhdwiSYMLATNLGHSNIVPVNAPPSIGIGIDGSLKGWSKDFY---SKLKISTKVCNVGNTFKEAPPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 233 VFSSSEI-YGLIKTGALEGVPISGCLGDQC----AALVGQMC---FQEGQAKNTYGTG-CFLLcntGRKCV--------- 294
Cdd:cd07778 234 PYAGIPIgKVNVILASYLGIDKSTVVGHGCidcyAGWFSTFAaakTLDTTLFMVAGTStCFLY---ATSSSqvgpipgiw 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 295 ----------------FSEHGLLTTvayKLGREKPAYYALEGSVAIAGAVIRwlrdnlgiiETSGDIERLAKEVGTS-YG 357
Cdd:cd07778 311 gpfdqllknysvyeggQSATGKLIE---KLFNSHPAIIELLKSDANFFETVE---------EKIDKYERLLGQSIHYlTR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393575 358 CYFvpaFSGLYA----PYWEPSARGILCGLTQFTNKCHIAF---AALEAVCFQTREILEAMNRDCgIPLRHLQVDGGMTN 430
Cdd:cd07778 379 HMF---FYGDYLgnrtPYNDPNMSGSFIGESTDSSLTDLVLkyiLILEFLAFQTKLIIDNFQKEK-IIIQKVVISGSQAK 454
|
490 500
....*....|....*....|...
gi 41393575 431 NKVLMQLQADILHIPVIKPFMPE 453
Cdd:cd07778 455 NARLLQLLSTVLSKIHIIVPLSD 477
|
|
| |
