|
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; ... |
1-388 |
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: 797.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 1 QLNIDISNIKAIGVSNQRETTVVWDKITGEPLYNAVVWLDLRTQSTVESLSKRIPGNNNFVKSKTGLPLSTYFSAVKLRW 80
Cdd:cd07792 66 ALGISPSDIKAIGITNQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELSAKTPGGKDHFRKKTGLPISTYFSAVKLRW 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 81 LLDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGVNGGVHCTDV-----TMQVGLcfstcHSLEWDKQLCEFFGIPMEILP 155
Cdd:cd07792 146 LLDNVPEVKKAVDDGRLLFGTVDSWLIWNLTGGKNGGVHVTDVtnasrTMLMNL-----RTLQWDPELCEFFGIPMSILP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 156 NVRSSSEIYGLMKIshsvkaGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLTTVA 235
Cdd:cd07792 221 EIRSSSEVYGKIAS------GPLAGVPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 236 YKLGRDKPVYYALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQ 315
Cdd:cd07792 295 YKLGPDAPPVYALEGSIAIAGAAVQWLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQ 374
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38414 316 FTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALG 388
Cdd:cd07792 375 FTTKAHIARAALEAVCFQTREILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALG 447
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
1-388 |
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: 671.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 1 QLNIDISNIKAIGVSNQRETTVVWDKITGEPLYNAVVWLDLRTQSTVESLSKRIPGNnnFVKSKTGLPLSTYFSAVKLRW 80
Cdd:TIGR01311 63 KAGIKPDDIAAIGITNQRETTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYGE--FIREKTGLPLDPYFSATKLRW 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 81 LLDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGvngGVHCTDV-----TMQVGLcfstcHSLEWDKQLCEFFGIPMEILP 155
Cdd:TIGR01311 141 LLDNVPGVREAAERGELLFGTIDTWLIWNLTGG---KVHVTDVtnasrTMLFNI-----HTLDWDDELLELFGIPREILP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 156 NVRSSSEIYGlmkisHSVKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLTTVA 235
Cdd:TIGR01311 213 EVRSSSEVYG-----YTDPGLLGAEIPITGVLGDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 236 YKLGRDKPVYyALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQ 315
Cdd:TIGR01311 288 YQLGGKKPVY-ALEGSVFVAGAAVQWLRDNLKLIKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTR 366
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38414 316 FTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALG 388
Cdd:TIGR01311 367 GTTKAHIARAALEAIAFQTRDVLEAMEKDAGVEITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALG 439
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
1-388 |
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: 625.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 1 QLNIDISNIKAIGVSNQRETTVVWDKITGEPLYNAVVWLDLRTQSTVESLSKRipGNNNFVKSKTGLPLSTYFSAVKLRW 80
Cdd:cd07769 62 KAGISASDIAAIGITNQRETTVVWDKKTGKPLYNAIVWQDRRTADICEELKAK--GLEERIREKTGLPLDPYFSATKIKW 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 81 LLDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGvngGVHCTDV-----TMQVGLcfstcHSLEWDKQLCEFFGIPMEILP 155
Cdd:cd07769 140 ILDNVPGARERAERGELLFGTIDTWLIWKLTGG---KVHVTDVtnasrTMLFNI-----HTLEWDDELLELFGIPRSMLP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 156 NVRSSSEIYGlmkisHSVKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLTTVA 235
Cdd:cd07769 212 EVRPSSEVFG-----YTDPEGLGAGIPIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 236 YKLgrDKPVYYALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQ 315
Cdd:cd07769 287 WQI--GGKVTYALEGSIFIAGAAIQWLRDNLGLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTR 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38414 316 FTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALG 388
Cdd:cd07769 365 GTTKAHIVRAALESIAYQTRDVLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALG 437
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
3-388 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 623.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 3 NIDISNIKAIGVSNQRETTVVWDKITGEPLYNAVVWLDLRTQSTVESLSKRipGNNNFVKSKTGLPLSTYFSAVKLRWLL 82
Cdd:COG0554 67 GISAEDIAAIGITNQRETTVVWDRKTGKPLYNAIVWQDRRTADICEELKAD--GLEDLIREKTGLVLDPYFSATKIKWIL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 83 DNVRKVQKAVEEKRALFGTIDSWLIWSLTGGvngGVHCTDV-----TMQVGLcfstcHSLEWDKQLCEFFGIPMEILPNV 157
Cdd:COG0554 145 DNVPGARERAEAGELLFGTIDSWLIWKLTGG---KVHVTDVtnasrTMLFNI-----HTLDWDDELLELFGIPRSMLPEV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 158 RSSSEIYGlmkisHSVKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLTTVAYK 237
Cdd:COG0554 217 RPSSEVFG-----ETDPDLFGAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWG 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 238 LGrDKPVYyALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFT 317
Cdd:COG0554 292 LG-GKVTY-ALEGSIFVAGAAVQWLRDGLGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGT 369
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38414 318 NKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALG 388
Cdd:COG0554 370 TRAHIARAALESIAYQTRDVLDAMEADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALG 440
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
8-388 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 591.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 8 NIKAIGVSNQRETTVVWDKITGEPLYNAVVWLDLRTQSTVESLSKRIPGNNNFVKsKTGLPLSTYFSAVKLRWLLDNVRK 87
Cdd:PTZ00294 73 KIKAIGITNQRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKYGGSNFFQK-ITGLPISTYFSAFKIRWMLENVPA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 88 VQKAVEEKRALFGTIDSWLIWSLTGGvngGVHCTDVT-------MQVglcfstcHSLEWDKQLCEFFGIPMEILPNVRSS 160
Cdd:PTZ00294 152 VKDAVKEGTLLFGTIDTWLIWNLTGG---KSHVTDVTnasrtflMNI-------KTLKWDEELLNKFGIPKETLPEIKSS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 161 SEIYGLMKishSVKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLTTVAYKLGR 240
Cdd:PTZ00294 222 SENFGTIS---GEAVPLLEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYQLGP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 241 DKPVYYALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKC 320
Cdd:PTZ00294 299 NGPTVYALEGSIAVAGAGVEWLRDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRA 378
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38414 321 HIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALG 388
Cdd:PTZ00294 379 HIVRAALEAIALQTNDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALG 446
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
2-395 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 583.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 2 LNIDiSNIKAIGVSNQRETTVVWDKITGEPLYNAVVWLDLRTQSTVESLSKRIPGNNNFVKSKTGLPLSTYFSAVKLRWL 81
Cdd:PLN02295 68 HNVD-SGLKAIGITNQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKELSGGRKHFVETCGLPISTYFSATKLLWL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 82 LDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGVNGGVHCTDVTMQVGLCFSTCHSLEWDKQLCEFFGIPMEILPNVRSSS 161
Cdd:PLN02295 147 LENVDAVKEAVKSGDALFGTIDSWLIWNLTGGASGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNS 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 162 EIYGlmKISHSvkaGALEGVPISGCLGDQSAALVGQMCfQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLTTVAYKLGRD 241
Cdd:PLN02295 227 EVIG--TIAKG---WPLAGVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYKLGPD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 242 KPVYYALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCH 321
Cdd:PLN02295 301 APTNYALEGSVAIAGAAVQWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAH 380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38414 322 IAFAALEAVCFQTREILDAMNRDCGIPLSH-----LQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALGRLWRQGL 395
Cdd:PLN02295 381 IARAVLESMCFQVKDVLDAMRKDAGEEKSHkglflLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGL 459
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
3-388 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 581.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 3 NIDISNIKAIGVSNQRETTVVWDKITGEPLYNAVVWLDLRTQSTVESLSKRipGNNNFVKSKTGLPLSTYFSAVKLRWLL 82
Cdd:PRK00047 69 GISPDQIAAIGITNQRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRD--GYEDYIREKTGLVIDPYFSGTKIKWIL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 83 DNVRKVQKAVEEKRALFGTIDSWLIWSLTGGvngGVHCTDV-----TMQVGLcfstcHSLEWDKQLCEFFGIPMEILPNV 157
Cdd:PRK00047 147 DNVEGARERAEKGELLFGTIDTWLVWKLTGG---KVHVTDYtnasrTMLFNI-----HTLDWDDELLELLDIPRSMLPEV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 158 RSSSEIYGLMKISHsvkaGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLTTVAYK 237
Cdd:PRK00047 219 RPSSEVYGKTNPYG----FFGGEVPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWG 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 238 LGrDKPVYyALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFT 317
Cdd:PRK00047 295 ID-GKVVY-ALEGSIFVAGSAIQWLRDGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGT 372
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38414 318 NKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALG 388
Cdd:PRK00047 373 TKEHIIRATLESIAYQTRDVLDAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALG 443
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
1-388 |
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: 577.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 1 QLNIDISNIKAIGVSNQRETTVVWDKITGEPLYNAVVWLDLRTQSTVESLSKRipGNNNFVKSKTGLPLSTYFSAVKLRW 80
Cdd:cd07786 62 KAGIRASDIAAIGITNQRETTVVWDRETGKPVYNAIVWQDRRTADICEELKAE--GHEEMIREKTGLVLDPYFSATKIRW 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 81 LLDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGvngGVHCTDV-----TMQVGLcfstcHSLEWDKQLCEFFGIPMEILP 155
Cdd:cd07786 140 ILDNVPGARERAERGELAFGTIDSWLIWKLTGG---KVHATDVtnasrTMLFNI-----HTLEWDDELLELFGIPASMLP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 156 NVRSSSEIYGlmkisHSVKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLTTVA 235
Cdd:cd07786 212 EVKPSSEVFG-----YTDPDLLGAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 236 YKLGrdKPVYYALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQ 315
Cdd:cd07786 287 WQLG--GKVTYALEGSIFIAGAAVQWLRDGLGLIESAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTR 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38414 316 FTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALG 388
Cdd:cd07786 365 GTTRAHIARAALESIAYQTRDLLEAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALG 437
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
1-388 |
4.11e-123 |
|
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: 366.89 E-value: 4.11e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 1 QLNIDISNIKAIGVSNQRETTVVWDKITGEPLYNAVVWLDLRTQSTVESLSK---------------RIPGNNNFVKSKT 65
Cdd:cd07793 62 NAGLTPEDIAAIGISTQRNTFLTWDKKTGKPLHNFITWQDLRAAELCESWNRslllkalrggskflhFLTRNKRFLAASV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 66 gLPLSTYFSAVKLRWLLDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGvngGVHCTDVTmqvglCFSTC-----HSLEWD 140
Cdd:cd07793 142 -LKFSTAHVSIRLLWILQNNPELKEAAEKGELLFGTIDTWLLWKLTGG---KVHATDYS-----NASATglfdpFTLEWS 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 141 KQLCEFFGIPMEILPNVRSSSEIYGLMKISHSVKAgalegVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTG 220
Cdd:cd07793 213 PILLSLFGIPSSILPEVKDTSGDFGSTDPSIFGAE-----IPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 221 HKCVFSDHGLLTTVAYKLGrDKPVYyALEGSVAIAGAVIRWLRDNLGIiKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAP 300
Cdd:cd07793 288 SKPHASVKGLYPLVGWKIG-GEITY-LAEGNASDTGTVIDWAKSIGLF-DDPSETEDIAESVEDTNGVYFVPAFSGLQAP 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 301 YWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPS 380
Cdd:cd07793 365 YNDPTACAGFIGLTPSTTKAHLVRAILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPK 444
|
....*...
gi 38414 381 MPETTALG 388
Cdd:cd07793 445 NTEMSALG 452
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
1-196 |
4.29e-77 |
|
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: 239.93 E-value: 4.29e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 1 QLNIDISNIKAIGVSNQRETTVVWDKITgEPLYNAVVWLDLRTQSTVESLSKriPGNNNFVKSKTGLPLSTYFSAVKLRW 80
Cdd:pfam00370 62 QLGISLKQIKGIGISNQGHGTVLLDKND-KPLYNAILWKDRRTAEIVENLKE--EGNNQKLYEITGLPIWPGFTLSKLRW 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 81 LLDNVRKVQKAVEekraLFGTIDSWLIWSLTGgvnggVHCTDVTMQVGLCFSTCHSLEWDKQLCEFFGIPMEILPNVRSS 160
Cdd:pfam00370 139 IKENEPEVFEKIH----KFLTIHDYLRWRLTG-----VFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVES 209
|
170 180 190
....*....|....*....|....*....|....*.
gi 38414 161 SEIYGLMKISHSVKAGALEGVPISGCLGDQSAALVG 196
Cdd:pfam00370 210 SEIYGELNPELAAMWGLDEGVPVVGGGGDQQAAAFG 245
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
1-388 |
1.52e-74 |
|
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: 241.27 E-value: 1.52e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 1 QLNIDISNIKAIGVSNQRETTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRIPGNNNFvkSKTGLPLSTYFSAVKLRW 80
Cdd:COG1070 63 KAGVDPEEIAAIGVSGQMHGLVLLDA-DGEPLRPAILWNDTRAAAEAAELREELGEEALY--EITGNPLHPGFTAPKLLW 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 81 LLDNvrkvQKAVEEKRALFGTIDSWLIWSLTGgvnggVHCTDVTMQVG-LCFSTcHSLEWDKQLCEFFGIPMEILPNVRS 159
Cdd:COG1070 140 LKEN----EPEIFARIAKVLLPKDYLRYRLTG-----EFVTDYSDASGtGLLDV-RTRDWSDELLEALGIDRELLPELVP 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 160 SSEIYGlmKISHSVKA--GALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKcVFSDHGLLTTVAYK 237
Cdd:COG1070 210 PGEVAG--TLTAEAAAetGLPAGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKP-LPDPEGRVHTFCHA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 238 L-GRdkpvyYALEGSVAIAGAVIRWLRDNLGIIKTS--EEIEKLAKEVGT-SYGCYFVPAFSGLYAPYWEPSARGIICGL 313
Cdd:COG1070 287 VpGR-----WLPMGATNNGGSALRWFRDLFADGELDdyEELNALAAEVPPgADGLLFLPYLSGERTPHWDPNARGAFFGL 361
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38414 314 TQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALG 388
Cdd:COG1070 362 TLSHTRAHLARAVLEGVAFALRDGLEAL-EEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALG 435
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
1-388 |
2.24e-68 |
|
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: 222.44 E-value: 2.24e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 1 QLNIDISNIKAIGVSNQRETTVVWDKiTGEPLYNAVVWLDlrtqstveslskripgnnnfvksktglplstyfsavklrw 80
Cdd:cd00366 62 KAGIDPSDIAAIGISGQMPGVVLVDA-DGNPLRPAIIWLD---------------------------------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 81 lldnvrkvqkaveeKRALFGTIDSWLIWSLTGgvnggVHCTDVTMQVGLCFSTCHSLEWDKQLCEFFGIPMEILPNVRSS 160
Cdd:cd00366 101 --------------RRAKFLQPNDYIVFRLTG-----EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 161 SEIYGlmKISHSVKA--GALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGhKCVFSDHGLLTTVAYKL 238
Cdd:cd00366 162 GEVVG--RVTPEAAEetGLPAGTPVVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTD-EPVPPDPRLLNRCHVVP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 239 GRdkpvyYALEGSVAIAGAVIRWLRDNLGIIKTSEE----IEKLAKEVGT-SYGCYFVPAFSGLYAPYWEPSARGIICGL 313
Cdd:cd00366 239 GL-----WLLEGAINTGGASLRWFRDEFGEEEDSDAeyegLDELAAEVPPgSDGLIFLPYLSGERSPIWDPAARGVFFGL 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38414 314 TQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALG 388
Cdd:cd00366 314 TLSHTRAHLIRAVLEGVAYALRDNLEIL-EELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALG 387
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
1-388 |
7.17e-68 |
|
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: 222.39 E-value: 7.17e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 1 QLNIDISNIKAIGVSNQRETTVVWDKiTGEPLYNAVVWLDLRTqstveslskripgnnnfvksktglplstyfsavklrw 80
Cdd:cd07779 62 KAGVDPEDIAAIGLTSQRSTFVPVDE-DGRPLRPAISWQDKRT------------------------------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 81 lldnvrkvqkaveekrALFGTIDSWLIWSLTGgvnggVHCTDVTM-QVGLCFSTcHSLEWDKQLCEFFGIPMEILPNVRS 159
Cdd:cd07779 104 ----------------AKFLTVQDYLLYRLTG-----EFVTDTTSaSRTGLPDI-RTRDWSDDLLDAFGIDRDKLPELVP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 160 SSEIYGlmKISHSV--KAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTgHKCVFSDHGLLTTVAYK 237
Cdd:cd07779 162 PGTVIG--TLTKEAaeETGLPEGTPVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVS-DKPVEDPERRIPCNPSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 238 LgrdkPVYYALEGSVAIAGAVIRWLRDNLG---------IIKTSEEIEKLAKEVGT-SYGCYFVPAFSGLYAPYWEPSAR 307
Cdd:cd07779 239 V----PGKWVLEGSINTGGSAVRWFRDEFGqdevaekelGVSPYELLNEEAAKSPPgSDGLLFLPYLAGAGTPYWNPEAR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 308 GIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTAL 387
Cdd:cd07779 315 GAFIGLTLSHTRAHLARAILEGIAFELRDNLEAM-EKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATAL 393
|
.
gi 38414 388 G 388
Cdd:cd07779 394 G 394
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
1-388 |
5.59e-64 |
|
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: 213.55 E-value: 5.59e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 1 QLNIDISNIKAIGVSNQRETTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRIPgnnNFVKSKTGLPLSTYFSAVKLRW 80
Cdd:cd07808 62 KAGISPSDIAAIGLTGQMHGLVLLDK-NGRPLRPAILWNDQRSAAECEELEARLG---DEILIITGNPPLPGFTLPKLLW 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 81 LL----DNVRKVQKAVEEKralfgtiDsWLIWSLTGgvnggVHCTDVTMQVG-LCFSTcHSLEWDKQLCEFFGIPMEILP 155
Cdd:cd07808 138 LKenepEIFARIRKILLPK-------D-YLRYRLTG-----ELATDPSDASGtLLFDV-EKREWSEELLEALGLDPSILP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 156 NVRSSSEIYGlmKISHSVkAGAL---EGVP-ISGClGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTgHKCVFSDHGLL 231
Cdd:cd07808 204 PIVESTEIVG--TLTPEA-AEELglpEGTPvVAGA-GDNAAAALGAGVVEPGDALISLGTSGVVFAPT-DKPVPDPKGRL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 232 TTVAYKLGrdkPVYYALeGSVAIAGAVIRWLRDNLGIIKTS-EEIEKLAKEVG-TSYGCYFVPAFSGLYAPYWEPSARGI 309
Cdd:cd07808 279 HTFPHAVP---GKWYAM-GVTLSAGLSLRWLRDLFGPDRESfDELDAEAAKVPpGSEGLLFLPYLSGERTPYWDPNARGS 354
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38414 310 ICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALG 388
Cdd:cd07808 355 FFGLSLSHTRAHLARAVLEGVAFSLRDSLEVL-KELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYG 432
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
7-388 |
2.06e-61 |
|
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: 205.51 E-value: 2.06e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 7 SNIKAIGVSNQRETTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRIPGNNNFvkSKTGLPLSTYFSAVKLRWLLDNvr 86
Cdd:cd07773 66 DPIAAISVSSQGESGVPVDR-DGEPLGPAIVWFDPRGKEEAEELAERIGAEELY--RITGLPPSPMYSLAKLLWLREH-- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 87 kvQKAVEEKRALFGTIDSWLIWSLTGgvnggVHCTDVTMqvgLCFSTC---HSLEWDKQLCEFFGIPMEILPNVRSSSEI 163
Cdd:cd07773 141 --EPEIFAKAAKWLSVADYIAYRLTG-----EPVTDYSL---ASRTMLfdiRKRTWSEELLEAAGIDASLLPELVPSGTV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 164 YGLMKISHSVKAGALEGVPIsgCLG--DQSAALVGQMCFQIGQAKNTYGTG-CFLLC-NTGHKCVFSDHGLLTTVAYKLG 239
Cdd:cd07773 211 IGTVTPEAAEELGLPAGTPV--VVGghDHLCAALGAGVIEPGDVLDSTGTAeALLAVvDEPPLDEMLAEGGLSYGHHVPG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 240 RdkpvYYALEGSVAiAGAVIRWLRDNLGI--IKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFT 317
Cdd:cd07773 289 G----YYYLAGSLP-GGALLEWFRDLFGGdeSDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGT 363
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38414 318 NKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALG 388
Cdd:cd07773 364 TRADLLRAILEGLAFELRLNLEAL-EKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALG 433
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
1-388 |
3.69e-54 |
|
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: 186.58 E-value: 3.69e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 1 QLNIDISNIKAIGVSNQRETTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRIPGNNNFvkSKTGLPLSTYFSAVKLRW 80
Cdd:cd07804 62 KAGISPKEIAAIGVSGLVPALVPVDE-NGKPLRPAILYGDRRATEEIEWLNENIGEDRIF--EITGNPLDSQSVGPKLLW 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 81 LLDNvrkvQKAVEEKRALFGTIDSWLIWSLTGgvnggVHCTDVTmqVGLCFSTC---HSLEWDKQLCEFFGIPMEILPNV 157
Cdd:cd07804 139 IKRN----EPEVFKKTRKFLGAYDYIVYKLTG-----EYVIDYS--SAGNEGGLfdiRKRTWDEELLEALGIDPDLLPEL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 158 RSSSEIYGlmKISHSVKA--GALEGVPISGCLGDQSAALV-------GQMCFQIGqakntyGTGCFLLCntgHKCVFSDH 228
Cdd:cd07804 208 VPSTEIVG--EVTKEAAEetGLAEGTPVVAGTVDAAASALsagvvepGDLLLMLG------TAGDIGVV---TDKLPTDP 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 229 GLLTTVAyklgrDKPVYYALEGSVAIAGAVIRWLRDNLGIIKTSEE----------IEKLAKEVG-TSYGCYFVPAFSGL 297
Cdd:cd07804 277 RLWLDYH-----DIPGTYVLNGGMATSGSLLRWFRDEFAGEEVEAEksggdsaydlLDEEAEKIPpGSDGLIVLPYFMGE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 298 YAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDcGIPLSHLQVDGGMTSNKILMQLQADILYIPVV 377
Cdd:cd07804 352 RTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYGLRHHLEVIREA-GLPIKRLVAVGGGAKSPLWRQIVADVTGVPQE 430
|
410
....*....|.
gi 38414 378 KPSMPETTALG 388
Cdd:cd07804 431 YVKDTVGASLG 441
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
1-388 |
1.44e-51 |
|
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: 180.41 E-value: 1.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 1 QLNIDISNIKAIGVSNQRETTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRIPGNNnFVKSKTGLPLSTYFSAVKLRW 80
Cdd:cd07805 62 KSGIDPSDIAAIAFSGQMQGVVPVDK-DGNPLRNAIIWSDTRAAEEAEEIAGGLGGIE-GYRLGGGNPPSGKDPLAKILW 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 81 LLDN----VRKVQKaveekraLFGTIDsWLIWSLTGgvnggVHCTDVTMQVGLCFSTCHSLEWDKQLCEFFGIPMEILPN 156
Cdd:cd07805 140 LKENepeiYAKTHK-------FLDAKD-YLNFRLTG-----RAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 157 VRSSSEIYGlmKISHSVKA--GALEGVPISGCLGDQSAALVGQMCFQIGQAkNTY-GTGCFLLCNTGHKCVFSDHGLlTT 233
Cdd:cd07805 207 LVPSTEVVG--ELTPEAAAelGLPAGTPVVGGGGDAAAAALGAGAVEEGDA-HIYlGTSGWVAAHVPKPKTDPDHGI-FT 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 234 VAYKLgrdkPVYYALEGSVAIAGAVIRWLRDNLGIIKTS-----EEIEKLAKEVGT-SYGCYFVPAFSGLYAPYWEPSAR 307
Cdd:cd07805 283 LASAD----PGRYLLAAEQETAGGALEWARDNLGGDEDLgaddyELLDELAAEAPPgSNGLLFLPWLNGERSPVEDPNAR 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 308 GIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGiPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMP-ETTA 386
Cdd:cd07805 359 GAFIGLSLEHTRADLARAVLEGVAFNLRWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVPENPqEAGA 437
|
..
gi 38414 387 LG 388
Cdd:cd07805 438 LG 439
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
3-411 |
3.39e-51 |
|
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: 179.29 E-value: 3.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 3 NIDISNIKAIGVSNQRETTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRIPGNNnfVKSKTGLPLSTYFSAVKLRWLL 82
Cdd:cd07770 62 KLGGGEVDAIGFSSAMHSLLGVDE-DGEPLTPVITWADTRAAEEAERLRKEGDGSE--LYRRTGCPIHPMYPLAKLLWLK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 83 DNvrkvQKAVEEKRALFGTIDSWLIWSLTGgvnggVHCTDVTMQVGL-CFSTcHSLEWDKQLCEFFGIPMEILPNVRSSS 161
Cdd:cd07770 139 EE----RPELFAKAAKFVSIKEYLLYRLTG-----ELVTDYSTASGTgLLNI-HTLDWDEEALELLGIDEEQLPELVDPT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 162 EIYGLMKISHSVKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTgcfllcnTGHKCVFSDHGLLT----TVAYK 237
Cdd:cd07770 209 EVLPGLKPEFAERLGLLAGTPVVLGASDGALANLGSGALDPGRAALTVGT-------SGAIRVVSDRPVLDppgrLWCYR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 238 LGRDKPVyyaLEGSVAIAGAVIRWLRDNLGIIKTS-EEIEKLAKEVG-TSYGCYFVPAFSGLYAPYWEPSARGIICGLTQ 315
Cdd:cd07770 282 LDENRWL---VGGAINNGGNVLDWLRDTLLLSGDDyEELDKLAEAVPpGSHGLIFLPYLAGERAPGWNPDARGAFFGLTL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 316 FTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALG--RLWRQ 393
Cdd:cd07770 359 NHTRADILRAVLEGVAFNLKSIYEAL-EELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGaaLLALE 437
|
410 420
....*....|....*....|..
gi 38414 394 GLQK----ESAYGVSNPRICLP 411
Cdd:cd07770 438 ALGLisslEADELVKIGKVVEP 459
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
205-388 |
2.29e-50 |
|
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: 169.04 E-value: 2.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 205 AKNTYGTGCFLLCNTGHKCVFSdHGLLTTVAyklGRDKPVYYALEGSVAIAGAVIRWLRDNLGI---------IKTSEEI 275
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSV-HGVWGPYT---NEMLPGYWGLEGGQSAAGSLLAWLLQFHGLreelrdagnVESLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 276 EKLAKEVGTSyGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVD 355
Cdd:pfam02782 77 AALAAVAPAG-GLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVS 155
|
170 180 190
....*....|....*....|....*....|...
gi 38414 356 GGMTSNKILMQLQADILYIPVVKPSMPETTALG 388
Cdd:pfam02782 156 GGGSRNPLLLQLLADALGLPVVVPGPDEATALG 188
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
1-388 |
5.31e-35 |
|
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: 134.60 E-value: 5.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 1 QLNIDISNIKAIGVSNQRETTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRipGNNNFVKSKTGLPLSTYFSAVKLRW 80
Cdd:cd07802 62 KSGVDPSDIAGVGVTGHGNGLYLVDK-DGKPVRNAILSNDSRAADIVDRWEED--GTLEKVYPLTGQPLWPGQPVALLRW 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 81 LLDN----VRKVQKAVEEKralfgtiDsWLIWSLTGgvnggVHCTDVTMQvglCFSTC--HSLEWDKQLCEFFGIP--ME 152
Cdd:cd07802 139 LKENeperYDRIRTVLFCK-------D-WIRYRLTG-----EISTDYTDA---GSSLLdlDTGEYDDELLDLLGIEelKD 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 153 ILPNVRSSSEIYGlmKISHSVKA--GALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCfllCNTG--HKCVFSDH 228
Cdd:cd07802 203 KLPPLVPSTEIAG--RVTAEAAAltGLPEGTPVAAGAFDVVASALGAGAVDEGQLCVILGTWS---INEVvtDEPVVPDS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 229 GLLTTvaykLGRDKPVYYALEGSVAIAGaVIRWLRDNLG------IIKTSEEIEKLAKEVG-TSYGCYFVPaFsgLYAPY 301
Cdd:cd07802 278 VGSNS----LHADPGLYLIVEASPTSAS-NLDWFLDTLLgeekeaGGSDYDELDELIAAVPpGSSGVIFLP-Y--LYGSG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 302 WEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCgiPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSM 381
Cdd:cd07802 350 ANPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLVAR--KPETIRLTGGGARSPVWAQIFADVLGLPVEVPDG 427
|
....*..
gi 38414 382 PETTALG 388
Cdd:cd07802 428 EELGALG 434
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
4-388 |
8.85e-33 |
|
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: 128.49 E-value: 8.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 4 IDISNIKAIGVSNQRETTVVWDKiTGEPLYnAVVWLDLRTQSTVESLSKRIPgnnNFVKSKTGLPLSTYFSAVKLRWLld 83
Cdd:cd07798 67 ISPEDISAVSSTSQREGIVFLDK-DGRELY-AGPNIDARGVEEAAEIDDEFG---EEIYTTTGHWPTELFPAARLLWF-- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 84 nvRKVQKAVEEKRALFGTIDSWLIWSLTGGVnggvhCTDVTMQVGLCFSTCHSLEWDKQLCEFFGIPMEILPNVRSSSEI 163
Cdd:cd07798 140 --KENRPEIFERIATVLSISDWIGYRLTGEL-----VSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 164 YGlmKISHSVKA--GALEGVPISGCLGD-QSAALvgqmcfqigqakntyGTGCFllcNTGHKCVFSdhGllTTVAYKLGR 240
Cdd:cd07798 213 LG--TVSEEAARelGLPEGTPVVVGGADtQCALL---------------GSGAI---EPGDIGIVA--G--TTTPVQMVT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 241 DKPVY----------------YALEGSVAIAGAVIRWLRDNL--GIIKTSEEIEKLAKEVG-TSYGCYfvpAFSGLYAPY 301
Cdd:cd07798 269 DEPIIdperrlwtgchlvpgkWVLESNAGVTGLNYQWLKELLygDPEDSYEVLEEEASEIPpGANGVL---AFLGPQIFD 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 302 wePSARGIICGLTQFT--------NKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILY 373
Cdd:cd07798 346 --ARLSGLKNGGFLFPtplsaselTRGDFARAILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLG 423
|
410
....*....|....*
gi 38414 374 IPVVKPSMPETTALG 388
Cdd:cd07798 424 KPVLVPEGREASALG 438
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
3-388 |
2.10e-31 |
|
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: 124.64 E-value: 2.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 3 NIDISNIKAIGVSNQRETTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRIPgnnnFVKSKTGLPLSTYFSAVKLRWLL 82
Cdd:cd07783 62 ELRPRRVVAIAVDGTSGTLVLVDR-EGEPLRPAIMYNDARAVAEAEELAEAAG----AVAPRTGLAVSPSSSLAKLLWLK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 83 DNvrkvQKAVEEKRALFGTIDSWLIWSLTGGVNggvhCTDVTMQVGLCFStCHSLEWDKQLCEFFGIPMEILPNVRSSSE 162
Cdd:cd07783 137 RH----EPEVLAKTAKFLHQADWLAGRLTGDRG----VTDYNNALKLGYD-PETGRWPSWLLALLGIPPDLLPRVVAPGT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 163 IYGLMKISHSVKAGALEGVPIsgCLG--DQSAALVGQMCFQIGQAKNTYGTG-CF-LLCntgHKCVFSDHGLLTTvaYKL 238
Cdd:cd07783 208 VIGTLTAEAAEELGLPAGTPV--VAGttDSIAAFLASGAVRPGDAVTSLGTTlVLkLLS---DKRVPDPGGGVYS--HRH 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 239 GRDkpvYYALEGSVAIAGAVIRWL--RDNLgiiktsEEIEKLAKEVGTSyGCYFVP-AFSGLYAPYWEPSARGIICGLTq 315
Cdd:cd07783 281 GDG---YWLVGGASNTGGAVLRWFfsDDEL------AELSAQADPPGPS-GLIYYPlPLRGERFPFWDPDARGFLLPRP- 349
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38414 316 fTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSmPETTALG 388
Cdd:cd07783 350 -HDRAEFLRALLEGIAFIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAE-EEEAALG 420
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
1-388 |
6.22e-26 |
|
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: 109.18 E-value: 6.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 1 QLNIDISNIKAIGVSNQRETTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRIPGNNnfvKSKTGLPLSTYFSAVKLRW 80
Cdd:cd07809 63 DAGAELRDVAAIGISGQMHGLVALDA-DGKVLRPAKLWCDTRTAPEAEELTEALGGKK---CLLVGLNIPARFTASKLLW 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 81 LLDN----VRKVQKaveekralFGTIDSWLIWSLTGGvnggvHCTDV--TMQVGLCFSTchSLEWDKQLCEFF---GIPM 151
Cdd:cd07809 139 LKENepehYARIAK--------ILLPHDYLNWKLTGE-----KVTGLgdASGTFPIDPR--TRDYDAELLAAIdpsRDLR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 152 EILPNVRSSSEIYGlmkisHSVKAGALE-----GVPISGCLGDQSAALVGQMCFQIGQAKNTYGT-GCflLCNTGHKCVF 225
Cdd:cd07809 204 DLLPEVLPAGEVAG-----RLTPEGAEElglpaGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTsGT--AYGVSDKPVS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 226 SDHGLLTTVAyklgrDKPVYYALegSVAIAGAVIRWLRDNLGIIKTS-EEIEKLAKEV-GTSYGCYFVPAFSGLYAPYWe 303
Cdd:cd07809 277 DPHGRVATFC-----DSTGGMLP--LINTTNCLTAWTELFRELLGVSyEELDELAAQApPGAGGLLLLPFLNGERTPNL- 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 304 PSARGIICGLTQF-TNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMP 382
Cdd:cd07809 349 PHGRASLVGLTLSnFTRANLARAALEGATFGLRYGLDIL-RELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETG 427
|
....*.
gi 38414 383 ETTALG 388
Cdd:cd07809 428 EGGALG 433
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
1-388 |
1.21e-19 |
|
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: 90.85 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 1 QLNIDISNIKAIGVSNQRETTVVWDKiTGEPLYnAVVWLDLRTQSTVESLSKRIPGNNNFVKSKTGLPLStyFSAV-KLR 79
Cdd:cd07775 64 KAGIAPKSIAAISTTSMREGIVLYDN-EGEEIW-ACANVDARAAEEVSELKELYNTLEEEVYRISGQTFA--LGAIpRLL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 80 WLLDNvrkvQKAVEEKRALFGTIDSWLIWSLTGgvnggVHCTDVTMQVGLCFSTCHSLEWDKQLCEFFGIPMEILPNVRS 159
Cdd:cd07775 140 WLKNN----RPEIYRKAAKITMLSDWIAYKLSG-----ELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 160 SSEIYGLMKISHSVKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLTTVAYklg 239
Cdd:cd07775 211 SGTVIGKVTKEAAEETGLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMNIRVNCHV--- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 240 rDKPVYYAlEGSVAIAGAVIRWLRDNLGI----------IKTSEEIEKLAKEVGTsyGCY-FVPAFSGL--YApYWEPSA 306
Cdd:cd07775 288 -IPDMWQA-EGISFFPGLVMRWFRDAFCAeekeiaerlgIDAYDLLEEMAKDVPP--GSYgIMPIFSDVmnYK-NWRHAA 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 307 RGIIcGLTQFTNKCHIA--FAAL-EAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPE 383
Cdd:cd07775 363 PSFL-NLDIDPEKCNKAtfFRAImENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKE 441
|
....*
gi 38414 384 TTALG 388
Cdd:cd07775 442 ATALG 446
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
1-388 |
1.26e-19 |
|
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: 91.06 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 1 QLNIDISNIKAIGVSNQRETTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRIPGNNNFVKSKTGLPLS--TYFSavKL 78
Cdd:cd07781 65 EAGVDPEDVVGIGVDTTSSTVVPVDE-DGNPLAPAILWMDHRAQEEAAEINETAHPALEYYLAYYGGVYSseWMWP--KA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 79 RWLLDNVRKVQKA----VEEkralfgtIDsWLIWSLTGgvnggvhctdvTMQVGLCfSTCHSLEWDKQLC----EFF--- 147
Cdd:cd07781 142 LWLKRNAPEVYDAaytiVEA-------CD-WINARLTG-----------RWVRSRC-AAGHKWMYNEWGGgpprEFLaal 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 148 -----GIPMEILPNVRSSSEIYGLMKISHSVKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGT-GCFLLcnTGH 221
Cdd:cd07781 202 dpgllKLREKLPGEVVPVGEPAGTLTAEAAERLGLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTsTCHLM--VSP 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 222 KCVFSDhGLLTTVayklgrDKPV---YYALEGSVAIAGAVIRWLRDNLGI------IKTSEEIEKLAKEVGTsyGCyfvp 292
Cdd:cd07781 280 KPVDIP-GICGPV------PDAVvpgLYGLEAGQSAVGDIFAWFVRLFVPpaeergDSIYALLSEEAAKLPP--GE---- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 293 afSGLYA---------PYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTS-NK 362
Cdd:cd07781 347 --SGLVAldwfngnrtPLVDPRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERF-EEAGVPVNRVVACGGIAEkNP 423
|
410 420
....*....|....*....|....*.
gi 38414 363 ILMQLQADILYIPVVKPSMPETTALG 388
Cdd:cd07781 424 LWMQIYADVLGRPIKVPKSDQAPALG 449
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
7-388 |
1.99e-19 |
|
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: 89.97 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 7 SNIKAIGVSNQRETTVVWDKiTGEPLYNAVVWLDLRtqSTVESLSKRIPGNNNFvKSKTGLPLSTYFSAVKLRWLLdnvr 86
Cdd:cd07777 68 SDVTGIGITGQMHGIVLWDE-DGNPVSPLITWQDQR--CSEEFLGGLSTYGEEL-LPKSGMRLKPGYGLATLFWLL---- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 87 kVQKAVEEKRALFGTIDSWLIWSLTGGVNggvHCTDVTMQVGL-CFStCHSLEWDKQLCEFFGIPMEILPNVRSSSEIYG 165
Cdd:cd07777 140 -RNGPLPSKADRAGTIGDYIVARLTGLPK---PVMHPTNAASWgLFD-LETGTWNKDLLEALGLPVILLPEIVPSGEIVG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 166 lmKISHSVKAgaleGVPISGCLGDQSAALVGqmCFQIGqaKNT----YGTG---CFLLC-NTGHKCV----FSDHGLLTT 233
Cdd:cd07777 215 --TLSSALPK----GIPVYVALGDNQASVLG--SGLNE--ENDavlnIGTGaqlSFLTPkFELSGSVeirpFFDGRYLLV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 234 VAyKL--GRdkpVYYALEGSVAiagaviRWLRDnLGIIKTSEEI-EKLAKEVGTSYGC--YFVPAFSGlyaPYWEPSARG 308
Cdd:cd07777 285 AA-SLpgGR---ALAVLVDFLR------EWLRE-LGGSLSDDEIwEKLDELAESEESSdlSVDPTFFG---ERHDPEGRG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 309 IICGLTQ--FTNKcHIAFAALEAVCfqtREILDAMNRDC--GIPLSHLQVDGGM-TSNKILMQLQADILYIPVVKPSMPE 383
Cdd:cd07777 351 SITNIGEsnFTLG-NLFRALCRGIA---ENLHEMLPRLDldLSGIERIVGSGGAlRKNPVLRRIIEKRFGLPVVLSEGSE 426
|
....*
gi 38414 384 TTALG 388
Cdd:cd07777 427 EAAVG 431
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
29-388 |
2.22e-18 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 87.01 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 29 GEPLYNAVVWLDLRTQSTVESLSKRIPGNNNFVKSKTG-LPLSTYFsavKLRWLLDNvrkvqkaveeKRALFGTIDSWL- 106
Cdd:PRK10331 91 GNLLYPIISWKCPRTAAVMENIERYISAQQLQQISGVGaFSFNTLY---KLVWLKEN----------HPQLLEQAHAWLf 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 107 IWSLTGGVNGGVHCTDVTMQVGLCFSTCHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGLMKISHSVKAGALEGVPISGC 186
Cdd:PRK10331 158 ISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPSAAALLGLPVGIPVISA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 187 LGDQSAALVGQmcfqiGQAKN----TYGTGCFLLCNTGH---KCVFSDHGLLTTVAYKLGRDKPvyyaleGSVAIAGAVI 259
Cdd:PRK10331 238 GHDTQFALFGS-----GAGQNqpvlSSGTWEILMVRSAQvdtSLLSQYAGSTCELDSQSGLYNP------GMQWLASGVL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 260 RWLRDNLGiikTSEE-----IEKlAKEVGT-SYGCYFVPAFSGlyapywepSARGIICGLTQFTNKCHIAFAALEAVCFQ 333
Cdd:PRK10331 307 EWVRKLFW---TAETpyqtmIEE-ARAIPPgADGVKMQCDLLA--------CQNAGWQGVTLNTTRGHFYRAALEGLTAQ 374
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 38414 334 TREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALG 388
Cdd:PRK10331 375 LKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAG 429
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
7-388 |
9.62e-17 |
|
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: 81.90 E-value: 9.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 7 SNIKAIGVSNQRETTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRipGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVr 86
Cdd:cd24121 68 DRVAAIGVTGQGDGTWLVDE-DGRPVRDAILWLDGRAADIVERWQAD--GIAEAVFEITGTGLFPGSQAAQLAWLKENE- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 87 kvQKAVEEKRALFGTIDsWLIWSLTGgvnggVHCTDVTMQVgLCFSTCHSLEWDKQLCEFFGIP--MEILPNVRSSSEIY 164
Cdd:cd24121 144 --PERLERARTALHCKD-WLFYKLTG-----EIATDPSDAS-LTFLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 165 GLMKISHSVKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFllcntghkcvfsdHGLLTTVAYkLGRDKP- 243
Cdd:cd24121 215 GPLTPEAAAATGLPAGTPVVLGPFDVVATALGSGAIEPGDACSILGTTGV-------------HEVVVDEPD-LEPEGVg 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 244 --VYYALEGSV-----AIAG-AVIRWLRDNLGIIKTSE----------EIEKLAKEV-----GTSYGCYFVPAfsGLYAP 300
Cdd:cd24121 281 ytICLGVPGRWlramaNMAGtPNLDWFLRELGEVLKEGaepagsdlfqDLEELAASSppgaeGVLYHPYLSPA--GERAP 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 301 YWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnrdcGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPS 380
Cdd:cd24121 359 FVNPNARAQFTGLSLEHTRADLLRAVYEGVALAMRDCYEHM----GEDPGELRLSGGGARSDTWCQILADALGVPVRVPA 434
|
....*...
gi 38414 381 MPETTALG 388
Cdd:cd24121 435 GEEFGARG 442
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
273-388 |
1.85e-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: 81.43 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 273 EEIEKLAKEVGTSYGC-----YFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIA---FAALEAVCFQTREILDAMNRd 344
Cdd:cd07782 361 ERLEQLAEEKGLPLAYltrdlHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLAllyLATLQALAYGTRHIIEAMNA- 439
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 38414 345 CGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALG 388
Cdd:cd07782 440 AGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLG 483
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
1-388 |
7.34e-14 |
|
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: 73.43 E-value: 7.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 1 QLNIDISNIKAIGVSN-------QRETTVVWDKITGEPLYNAVVWLDLRTQSTVESLskripgnnNFVKSKTGLP----- 68
Cdd:cd07768 64 REGVDAYEVKGCGVDAtcslaifDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWI--------NMQCPQQLLDylggk 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 69 LSTYFSAVKLRWLLDNVRKVQKAVEEkraLFGTIDsWLIWSLTGGVNGGVhCTdvtmqvGLCFSTCHSLE--WDKQLCEF 146
Cdd:cd07768 136 ISPEMGVPKLKYFLDEYSHLRDKHFH---IFDLHD-YIAYELTRLYEWNI-CG------LLGKENLDGEEsgWSSSFFKN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 147 FGIPME------ILPNVRSSSEIYGLMKISHSVKAGALEGVPISGCLGDQSAALvgqmcfqIGQAKNTYGTGCFLLCNTG 220
Cdd:cd07768 205 IDPRLEhltttkNLPSNVPIGTTSGVALPEMAEKMGLHPGTAVVVSCIDAHASW-------FAVASPHLETSLFMIAGTS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 221 hkcvfSDHGLLTTVAYKL-GRDKPVYYAL-------EGSVAIAGAVIRWL-------RDNLGIIKTSEEI--------EK 277
Cdd:cd07768 278 -----SCHMYGTTISDRIpGVWGPFDTIIdpdysvyEAGQSATGKLIEHLfeshpcaRKFDEALKKGADIyqvleqtiRQ 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 278 LAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFT---NKCHIAFAALEAVCFQTREILDAMNRDcGIPLSHLQV 354
Cdd:cd07768 353 IEKNNGLSIHILTLDMFFGNRSEFADPRLKGSFIGESLDTsmlNLTYKYIAILEALAFGTRLIIDTFQNE-GIHIKELRA 431
|
410 420 430
....*....|....*....|....*....|....
gi 38414 355 DGGMTSNKILMQLQADILYIPVVKPSMPETTALG 388
Cdd:cd07768 432 SGGQAKNERLLQLIALVTNVAIIKPKENMMGILG 465
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
6-371 |
1.03e-12 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 69.61 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 6 ISNIKAIGVSNQRETTVVWDKiTGEPLYNAVVWLDLRTQSTVESLSKRIPGNnnfvKSKTGLPLSTYFSAVKLRWLL--- 82
Cdd:PRK15027 65 LQDVKALGIAGQMHGATLLDA-QQRVLRPAILWNDGRCAQECALLEARVPQS----RVITGNLMMPGFTAPKLLWVQrhe 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 83 -DNVRKVQKAVEEKralfgtidSWLIWSLTGgvnggVHCTDVTMQVGLCFSTCHSLEWDKQLCEFFGIPMEILPNVRSSS 161
Cdd:PRK15027 140 pEIFRQIDKVLLPK--------DYLRLRMTG-----EFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 162 EIYGLMkISHSVKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTgcfllcnTGHKCVFSDhGLLT---TVAYKL 238
Cdd:PRK15027 207 EITGAL-LPEVAKAWGMATVPVVAGGGDNAAGAVGVGMVDANQAMLSLGT-------SGVYFAVSE-GFLSkpeSAVHSF 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 239 GRDKPVYYALEGSVAIAGAVIRW------LRDNLGIIKTSEEIEKLAKEVgtsygcYFVPAFSGLYAPYWEPSARGIICG 312
Cdd:PRK15027 278 CHALPQRWHLMSVMLSAASCLDWaakltgLSNVPALIAAAQQADESAEPV------WFLPYLSGERTPHNNPQAKGVFFG 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 38414 313 LTQFTNKCHIAFAALEAVCFQTREILDAMNrDCGIPLSHLQVDGGMTSNKILMQLQADI 371
Cdd:PRK15027 352 LTHQHGPNELARAVLEGVGYALADGMDVVH-ACGIKPQSVTLIGGGARSEYWRQMLADI 409
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
243-388 |
2.27e-12 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 68.60 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 243 PVYYALEGSVAIAGAVIRWLRDNLGiikTSEEIEKLAKEVGTS----------------YGCYFVPAFSGLYAPYWEPSA 306
Cdd:COG1069 315 PGMWGYEAGQSAVGDIFAWFVRLLV---PPLEYEKEAEERGISlhpllteeaaklppgeSGLHALDWFNGNRSPLADQRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 307 RGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNrDCGIPLSHLQVDGG-MTSNKILMQLQADILYIPVVKPSMPETT 385
Cdd:COG1069 392 KGVILGLTLGTDAEDIYRALVEATAFGTRAIIERFE-EEGVPIDEIIACGGiATKNPLVMQIYADVTGRPIKVAASEQAC 470
|
...
gi 38414 386 ALG 388
Cdd:COG1069 471 ALG 473
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
29-388 |
5.10e-10 |
|
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: 61.00 E-value: 5.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 29 GEPLYNAVVWLDLRTQSTVESLSKRIPGNNNFvkSKTGLPLSTYFSAVKLRWLldnvrkvqkaVEEKRALFGTIDSWLI- 107
Cdd:cd07771 87 GELLGNPVHYRDPRTEGMMEELFEKISKEELY--ERTGIQFQPINTLYQLYAL----------KKEGPELLERADKLLMl 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 108 -----WSLTGgvnggVHCTDVTMQvglcfSTC-----HSLEWDKQLCEFFGIPMEILPNVRSSSEIYGLMKISHSvKAGA 177
Cdd:cd07771 155 pdllnYLLTG-----EKVAEYTIA-----STTqlldpRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPEVA-EELG 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 178 LEGVP-ISGCLGDQSAALVGqmcfqI-GQAKNTYgtgcFLLCNT----GhkcVFSDHGLLTTVAYKLGrdkpvyYALEGS 251
Cdd:cd07771 224 LKGIPvIAVASHDTASAVAA-----VpAEDEDAA----FISSGTwsliG---VELDEPVITEEAFEAG------FTNEGG 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 252 VA--------IAGaviRWL----RDNL---GIIKTSEEIEKLAKEVgTSYGCYFVPAFSGLYAPywePSARGIICGLTQF 316
Cdd:cd07771 286 ADgtirllknITG---LWLlqecRREWeeeGKDYSYDELVALAEEA-PPFGAFIDPDDPRFLNP---GDMPEAIRAYCRE 358
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38414 317 TN------KCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKpSMPETTALG 388
Cdd:cd07771 359 TGqpvpesPGEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIA-GPVEATAIG 435
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
307-388 |
2.72e-08 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 56.01 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 307 RGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGM-TSNKILMQLQADILYIPV-VKPSmPET 384
Cdd:PRK04123 398 KGVITGLTLGTDAPDIYRALIEATAFGTRAIMECF-EDQGVPVEEVIAAGGIaRKNPVLMQIYADVLNRPIqVVAS-DQC 475
|
....
gi 38414 385 TALG 388
Cdd:PRK04123 476 PALG 479
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
3-388 |
2.58e-06 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 49.62 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 3 NIDISNIKAIGVSNQRETTVVWDKiTGEPLYnAVVWLDLRTQSTVESLSKRIPGNNNFVKSKTGLPLStyFSAV-KLRWL 81
Cdd:PRK10939 69 GIPASDIAAVSATSMREGIVLYDR-NGTEIW-ACANVDARASREVSELKELHNNFEEEVYRCSGQTLA--LGALpRLLWL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 82 ldnvRKVQKAVEEKRALFGTIDSWLIWSLTGGV-----NGGVhctdvtmqVGLcFSTcHSLEWDKQLCEFFGIPMEILPN 156
Cdd:PRK10939 145 ----AHHRPDIYRQAHTITMISDWIAYMLSGELavdpsNAGT--------TGL-LDL-VTRDWDPALLEMAGLRADILPP 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 157 VRSSSEIYGLMKISHSVKAGALEGVPI--------SGCLG------DQSAALVGQMCFQIgqakntygtgcfllCNTGHK 222
Cdd:PRK10939 211 VKETGTVLGHVTAKAAAETGLRAGTPVvmgggdvqLGCLGlgvvrpGQTAVLGGTFWQQV--------------VNLPAP 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 223 CVFSDHGLlttvayklgRDKPvyYALEGSV---AIA---GAVIRWLRD-----------NLGiIKTSEEIEKLAKEVGT- 284
Cdd:PRK10939 277 VTDPNMNI---------RINP--HVIPGMVqaeSISfftGLTMRWFRDafcaeekllaeRLG-IDAYSLLEEMASRVPVg 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 285 SYGcyFVPAFSG-LYAPYWEPSARGIIcGLTQFTNKCHIA--FAAL-EAVCFQTREILDAMNRDCGIPLSHLQVDGGMTS 360
Cdd:PRK10939 345 SHG--IIPIFSDvMRFKSWYHAAPSFI-NLSIDPEKCNKAtlFRALeENAAIVSACNLQQIAAFSGVFPSSLVFAGGGSK 421
|
410 420
....*....|....*....|....*...
gi 38414 361 NKILMQLQADILYIPVVKPSMPETTALG 388
Cdd:PRK10939 422 GKLWSQILADVTGLPVKVPVVKEATALG 449
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
305-388 |
6.12e-04 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466792 [Multi-domain] Cd Length: 424 Bit Score: 41.86 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 305 SARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGiplsHLQVDGGMTSNKILMQLQADILY-IPVVKPSMPE 383
Cdd:cd07772 339 PGSGGRGVLSAFPSAEEAYALAILYLALMTDYALDLLGSGVG----RIIVEGGFAKNPVFLRLLAALRPdQPVYLSDDSE 414
|
....*
gi 38414 384 TTALG 388
Cdd:cd07772 415 GTALG 419
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
257-378 |
1.61e-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: 40.85 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38414 257 AVIRWLRDNLGIIKTSEE-IEKLAKEVGTS----YGCYFvpaFSGLYA----PYWEPSARGIICGLTQFTNKCHIAF--- 324
Cdd:cd07778 343 AIIELLKSDANFFETVEEkIDKYERLLGQSihylTRHMF---FYGDYLgnrtPYNDPNMSGSFIGESTDSSLTDLVLkyi 419
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 38414 325 AALEAVCFQTREILDAMNRDCgIPLSHLQVDGGMTSNKILMQLQADILYIPVVK 378
Cdd:cd07778 420 LILEFLAFQTKLIIDNFQKEK-IIIQKVVISGSQAKNARLLQLLSTVLSKIHII 472
|
|
| |
