|
Name |
Accession |
Description |
Interval |
E-value |
| glpK |
PRK00047 |
glycerol kinase GlpK; |
1-498 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 1070.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 1 MTDKKYIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEALAKADINSDQIAAIGI 80
Cdd:PRK00047 1 MMMKKYILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 81 TNQRETVVVWERETGKPIYNAIVWQCRRTAEICEQLKRDGMEEYIRKATGLVVDPYFSGTKVKWILDHVEGSRERAKRGE 160
Cdd:PRK00047 81 TNQRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRDGYEDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 161 LLFGTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYGQTNIGGKGGTRIPI 240
Cdd:PRK00047 161 LLFGTIDTWLVWKLTGGKVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYGFFGGEVPI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 241 AGIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVTSTHGLLTTIACGPRGEVNYALEGAVFMAGASIQWLRDE 320
Cdd:PRK00047 241 AGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGIDGKVVYALEGSIFVAGSAIQWLRDG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 321 MKLISDAFDSEYFATKVKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLEAMQADS 400
Cdd:PRK00047 321 LKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 401 GIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAVIEREFRPGIETTER 480
Cdd:PRK00047 401 GIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDELKEQWKIDRRFEPQMDEEER 480
|
490
....*....|....*...
gi 496082303 481 NYRYSGWKKAVKRALAWE 498
Cdd:PRK00047 481 EKLYAGWKKAVKRTLAWA 498
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
4-499 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 1024.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 4 KKYIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEALAKADINSDQIAAIGITNQ 83
Cdd:COG0554 2 KKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITNQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 84 RETVVVWERETGKPIYNAIVWQCRRTAEICEQLKRDGMEEYIRKATGLVVDPYFSGTKVKWILDHVEGSRERAKRGELLF 163
Cdd:COG0554 82 RETTVVWDRKTGKPLYNAIVWQDRRTADICEELKADGLEDLIREKTGLVLDPYFSATKIKWILDNVPGARERAEAGELLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 164 GTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYGQTNIGGKGGtRIPIAGI 243
Cdd:COG0554 162 GTIDSWLIWKLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDPDLFGA-EIPIAGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 244 AGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVTSTHGLLTTIACGPRGEVNYALEGAVFMAGASIQWLRDEMKL 323
Cdd:COG0554 241 AGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGGKVTYALEGSIFVAGAAVQWLRDGLGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 324 ISDAFDSEYFATKVKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLEAMQADSGIR 403
Cdd:COG0554 321 IDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADSGIP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 404 LHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAVIEREFRPGIETTERNYR 483
Cdd:COG0554 401 LKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEELAALWKVDRRFEPQMDEEERERL 480
|
490
....*....|....*.
gi 496082303 484 YSGWKKAVKRALAWEE 499
Cdd:COG0554 481 YAGWKKAVERTLGWAE 496
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
6-492 |
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: 971.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEALAKADINSDQIAAIGITNQRE 85
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 86 TVVVWERETGKPIYNAIVWQCRRTAEICEQLKRDGMEEYIRKATGLVVDPYFSGTKVKWILDHVEGSRERAKRGELLFGT 165
Cdd:cd07769 81 TTVVWDKKTGKPLYNAIVWQDRRTADICEELKAKGLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAERGELLFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 166 VDTWLIWKMTQGRVHVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYGQTNIGGkGGTRIPIAGIAG 245
Cdd:cd07769 161 IDTWLIWKLTGGKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTDPEG-LGAGIPIAGILG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 246 DQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVTSTHGLLTTIACGPRGEVNYALEGAVFMAGASIQWLRDEMKLIS 325
Cdd:cd07769 240 DQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQIGGKVTYALEGSIFIAGAAIQWLRDNLGLIE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 326 DAFDSEYFATKVKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLEAMQADSGIRLH 405
Cdd:cd07769 320 DAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDSGIKLK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 406 ALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAVIEREFRPGIETTERNYRYS 485
Cdd:cd07769 400 ELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDELASLWQVDKRFEPSMDEEERERLYR 479
|
....*..
gi 496082303 486 GWKKAVK 492
Cdd:cd07769 480 GWKKAVE 486
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
6-492 |
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: 971.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEALAKADINSDQIAAIGITNQRE 85
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 86 TVVVWERETGKPIYNAIVWQCRRTAEICEQLKRDGMEEYIRKATGLVVDPYFSGTKVKWILDHVEGSRERAKRGELLFGT 165
Cdd:cd07786 81 TTVVWDRETGKPVYNAIVWQDRRTADICEELKAEGHEEMIREKTGLVLDPYFSATKIRWILDNVPGARERAERGELAFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 166 VDTWLIWKMTQGRVHVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYGQTNIGGkGGTRIPIAGIAG 245
Cdd:cd07786 161 IDSWLIWKLTGGKVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDPDL-LGAEIPIAGIAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 246 DQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVTSTHGLLTTIACGPRGEVNYALEGAVFMAGASIQWLRDEMKLIS 325
Cdd:cd07786 240 DQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLGGKVTYALEGSIFIAGAAVQWLRDGLGLIE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 326 DAFDSEYFATKVKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLEAMQADSGIRLH 405
Cdd:cd07786 320 SAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEADSGIPLK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 406 ALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAVIEREFRPGIETTERNYRYS 485
Cdd:cd07786 400 ELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAKLWQVDRRFEPSMSEEEREALYA 479
|
....*..
gi 496082303 486 GWKKAVK 492
Cdd:cd07786 480 GWKKAVK 486
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
5-497 |
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: 876.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 5 KYIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEALAKADINSDQIAAIGITNQR 84
Cdd:TIGR01311 1 PYILAIDQGTTSSRAIVFDKDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAGIKPDDIAAIGITNQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 85 ETVVVWERETGKPIYNAIVWQCRRTAEICEQLKRDGMEEYIRKATGLVVDPYFSGTKVKWILDHVEGSRERAKRGELLFG 164
Cdd:TIGR01311 81 ETTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYGEFIREKTGLPLDPYFSATKLRWLLDNVPGVREAAERGELLFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 165 TVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYGQTNiGGKGGTRIPIAGIA 244
Cdd:TIGR01311 161 TIDTWLIWNLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYTD-PGLLGAEIPITGVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 245 GDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVTSTHGLLTTIACGPRGEVN-YALEGAVFMAGASIQWLRDEMKL 323
Cdd:TIGR01311 240 GDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKKPvYALEGSVFVAGAAVQWLRDNLKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 324 ISDAFDSEYFATKVKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLEAMQADSGIR 403
Cdd:TIGR01311 320 IKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTRDVLEAMEKDAGVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 404 LHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAVIEREFRPGIETTERNYR 483
Cdd:TIGR01311 400 ITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWRVEKTFEPEMDEEEREAR 479
|
490
....*....|....
gi 496082303 484 YSGWKKAVKRALAW 497
Cdd:TIGR01311 480 YAGWKEAVKRSLGW 493
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
5-494 |
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: 759.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 5 KYIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEALAKA---DINSDQIAAIGIT 81
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLkalGISPSDIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 82 NQRETVVVWERETGKPIYNAIVWQCRRTAEICEQL--KRDGMEEYIRKATGLVVDPYFSGTKVKWILDHVEGSRERAKRG 159
Cdd:cd07792 81 NQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELsaKTPGGKDHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 160 ELLFGTVDTWLIWKMT---QGRVHVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYGQTNIGGKGGt 236
Cdd:cd07792 161 RLLFGTVDSWLIWNLTggkNGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIASGPLAG- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 237 rIPIAGIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVTSTHGLLTTIA--CGPRGEVNYALEGAVFMAGASI 314
Cdd:cd07792 240 -VPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAykLGPDAPPVYALEGSIAIAGAAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 315 QWLRDEMKLISDAFDSEYFATKVKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLE 394
Cdd:cd07792 319 QWLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREILD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 395 AMQADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAVIERE-FRP 473
Cdd:cd07792 399 AMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSLNEGGRTvFEP 478
|
490 500
....*....|....*....|.
gi 496082303 474 GIETTERNYRYSGWKKAVKRA 494
Cdd:cd07792 479 QISEEERERRYKRWKKAVERS 499
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
4-499 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 690.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 4 KKYIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEALAKADIN--SDQIAAIGIT 81
Cdd:PTZ00294 1 MKYIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKgpSFKIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 82 NQRETVVVWERETGKPIYNAIVWQCRRTAEICEQLKRD-GMEEYIRKATGLVVDPYFSGTKVKWILDHVEGSRERAKRGE 160
Cdd:PTZ00294 81 NQRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKyGGSNFFQKITGLPISTYFSAFKIRWMLENVPAVKDAVKEGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 161 LLFGTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYG----QTNIGGKGgt 236
Cdd:PTZ00294 161 LLFGTIDTWLIWNLTGGKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGtisgEAVPLLEG-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 237 rIPIAGIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVTSTHGLLTTIA--CGPRGEVNYALEGAVFMAGASI 314
Cdd:PTZ00294 239 -VPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCyqLGPNGPTVYALEGSIAVAGAGV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 315 QWLRDEMKLISDAFDSEYFATKVKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLE 394
Cdd:PTZ00294 318 EWLRDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDVIE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 395 AMQADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAVIE-REFRP 473
Cdd:PTZ00294 398 SMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVKKLIRRSnSTFSP 477
|
490 500
....*....|....*....|....*.
gi 496082303 474 GIETTERNYRYSGWKKAVKRALAWEE 499
Cdd:PTZ00294 478 QMSAEERKAIYKEWNKAVERSLKWAK 503
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
6-497 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 669.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEALAKADINS----DQIAAIGIT 81
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGhnvdSGLKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 82 NQRETVVVWERETGKPIYNAIVWQCRRTAEICEQLKRD--GMEEYIRKATGLVVDPYFSGTKVKWILDHVEGSRERAKRG 159
Cdd:PLN02295 81 NQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKElsGGRKHFVETCGLPISTYFSATKLLWLLENVDAVKEAVKSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 160 ELLFGTVDTWLIWKMT---QGRVHVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYGQTNIGGKGGt 236
Cdd:PLN02295 161 DALFGTIDSWLIWNLTggaSGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIAKGWPLA- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 237 RIPIAGIAGDQQAALFGQLCvKEGMAKNTYGTGCFMLMNTGEKAVTSTHGLLTTIA--CGPRGEVNYALEGAVFMAGASI 314
Cdd:PLN02295 240 GVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAykLGPDAPTNYALEGSVAIAGAAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 315 QWLRDEMKLISDAFDSEYFATKVKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLE 394
Cdd:PLN02295 319 QWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQVKDVLD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 395 AMQAD-----SGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDEL-QEKAVIE 468
Cdd:PLN02295 399 AMRKDageekSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEEEIFaSEKWKNT 478
|
490 500
....*....|....*....|....*....
gi 496082303 469 REFRPGIETTERNYRYSGWKKAVKRALAW 497
Cdd:PLN02295 479 TTFRPKLDEEERAKRYASWCKAVERSFDL 507
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
6-492 |
0e+00 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466803 [Multi-domain] Cd Length: 501 Bit Score: 575.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEALAKADINSDQIAAIGITNQRE 85
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 86 TVVVWERETGKPIYNAIVWQCRRTAEICEQLKRDGMEEYIRKATGLV----------------VDPYFSGTKVKWILDHV 149
Cdd:cd07793 81 TFLTWDKKTGKPLHNFITWQDLRAAELCESWNRSLLLKALRGGSKFLhfltrnkrflaasvlkFSTAHVSIRLLWILQNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 150 EGSRERAKRGELLFGTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYGQTN 229
Cdd:cd07793 161 PELKEAAEKGELLFGTIDTWLLWKLTGGKVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFGSTD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 230 IGGkGGTRIPIAGIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVTSTHGLLTTIACGPRGEVNYALEGAVFM 309
Cdd:cd07793 241 PSI-FGAEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGGEITYLAEGNASD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 310 AGASIQWLRDEMkLISDAFDSEYFATKVKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQT 389
Cdd:cd07793 320 TGTVIDWAKSIG-LFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIAFRV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 390 RDVLEAMQADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAVIER 469
Cdd:cd07793 399 KQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEELKKLRKIEK 478
|
490 500
....*....|....*....|...
gi 496082303 470 EFRPGIETTERNYRYSGWKKAVK 492
Cdd:cd07793 479 IFEPKMDNEKREELYKNWKKAVK 501
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
6-480 |
1.12e-117 |
|
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: 352.98 E-value: 1.12e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEALAKADINSDQIAAIGITNQRE 85
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 86 TVV-VweRETGKPIYNAIVWQCRRTAEICeqlkrdgmeeyirkatglvvdpyfsgtkvkwildhvegsrerakrgellfg 164
Cdd:cd07779 81 TFVpV--DEDGRPLRPAISWQDKRTAKFL--------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 165 TVDTWLIWKMTqGRvHVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYGQTN------IGGKGGTRI 238
Cdd:cd07779 108 TVQDYLLYRLT-GE-FVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTkeaaeeTGLPEGTPV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 239 pIAGiAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVTSTHGLLTTIACGPRgevNYALEGAVFMAGASIQWLR 318
Cdd:cd07779 186 -VAG-GGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPG---KWVLEGSINTGGSAVRWFR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 319 DE------MKLISDAFDSEYFATKVKDT----NGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQ 388
Cdd:cd07779 261 DEfgqdevAEKELGVSPYELLNEEAAKSppgsDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFE 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 389 TRDVLEAMQaDSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAV-I 467
Cdd:cd07779 341 LRDNLEAME-KAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAMVrV 419
|
490
....*....|...
gi 496082303 468 EREFRPGIETTER 480
Cdd:cd07779 420 TDTFEPDPENVAI 432
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
5-493 |
1.33e-116 |
|
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: 352.21 E-value: 1.33e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 5 KYIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEALAKADINSDQIAAIGITNQR 84
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 85 ETVVVWEREtGKPIYNAIVWQCRRTAEICEQLKRDGMEEYIRKATGLVVDPYFSGTKVKWILDHVEGSRERAKRgellFG 164
Cdd:COG1070 81 HGLVLLDAD-GEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAK----VL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 165 TVDTWLIWKMTqGRvHVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYGQTN------IGGKGGTRI 238
Cdd:COG1070 156 LPKDYLRYRLT-GE-FVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTaeaaaeTGLPAGTPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 239 pIAGiAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTgEKAVTSTHGLLTTIACGPRGevNYALEGAVFMAGASIQWLR 318
Cdd:COG1070 234 -VAG-AGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVS-DKPLPDPEGRVHTFCHAVPG--RWLPMGATNNGGSALRWFR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 319 DEmkLISDAFDS-EYFATKVKDT----NGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVL 393
Cdd:COG1070 309 DL--FADGELDDyEELNALAAEVppgaDGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 394 EAMQAdSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAV-IEREFR 472
Cdd:COG1070 387 EALEE-AGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMVrVGETIE 465
|
490 500
....*....|....*....|...
gi 496082303 473 PGIETTERnYR--YSGWKKAVKR 493
Cdd:COG1070 466 PDPENVAA-YDelYERYRELYPA 487
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
6-253 |
2.17e-115 |
|
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: 340.08 E-value: 2.17e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEALAKADINSDQIAAIGITNQRE 85
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 86 TVVVWERETgKPIYNAIVWQCRRTAEICEQLKRDGMEEYIRKATGLVVDPYFSGTKVKWILDHVEGSRERAKrgelLFGT 165
Cdd:pfam00370 81 GTVLLDKND-KPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIH----KFLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 166 VDTWLIWKMTQgrVHVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYGQTNIGGKGGT----RIPIA 241
Cdd:pfam00370 156 IHDYLRWRLTG--VFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMWgldeGVPVV 233
|
250
....*....|..
gi 496082303 242 GIAGDQQAALFG 253
Cdd:pfam00370 234 GGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
6-448 |
1.80e-114 |
|
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: 343.39 E-value: 1.80e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEALAKADINSDQIAAIGITNQRE 85
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 86 TVVVWEREtGKPIYNAIVWQCRRtaeiceqlkrdgmeeyirkatglvvdpyfsgtkvkwildhvegsrerAKrgellFGT 165
Cdd:cd00366 81 GVVLVDAD-GNPLRPAIIWLDRR-----------------------------------------------AK-----FLQ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 166 VDTWLIWKMTQgrVHVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYGQTN------IGGKGGTriP 239
Cdd:cd00366 108 PNDYIVFRLTG--EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTpeaaeeTGLPAGT--P 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 240 IAGIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVTstHGLLTTIACGPRGevNYALEGAVFMAGASIQWLRD 319
Cdd:cd00366 184 VVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVPP--DPRLLNRCHVVPG--LWLLEGAINTGGASLRWFRD 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 320 EMKLISDAFDSEYF----ATKVKD-TNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLE 394
Cdd:cd00366 260 EFGEEEDSDAEYEGldelAAEVPPgSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLE 339
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 496082303 395 AMQADsGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLA 448
Cdd:cd00366 340 ILEEL-GVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
6-453 |
1.03e-103 |
|
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: 317.61 E-value: 1.03e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEALAKADInsDQIAAIGITNQRE 85
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGP--DPIAAISVSSQGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 86 TVVVWEREtGKPIYNAIVWQCRRTAEICEQLKRDGMEEYIRKATGLVVDPYFSGTKVKWILDHVEGSRERAKRgellFGT 165
Cdd:cd07773 79 SGVPVDRD-GEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAK----WLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 166 VDTWLIWKMTqGRvHVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYGQTN------IGGKGGTRIP 239
Cdd:cd07773 154 VADYIAYRLT-GE-PVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTpeaaeeLGLPAGTPVV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 240 IAGIagDQQAALFGQLCVKEGMAKNTYGTG-CFMLMNTGEKAVTSTHGLLTTIACGPRGEVnYALEGAVFmAGASIQWLR 318
Cdd:cd07773 232 VGGH--DHLCAALGAGVIEPGDVLDSTGTAeALLAVVDEPPLDEMLAEGGLSYGHHVPGGY-YYLAGSLP-GGALLEWFR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 319 DEM--KLISDAFDSEYFATKVKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLEAM 396
Cdd:cd07773 308 DLFggDESDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEAL 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 496082303 397 QAdSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVG 453
Cdd:cd07773 388 EK-AGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
6-490 |
1.28e-100 |
|
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: 311.01 E-value: 1.28e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEALAKADINSDQIAAIGITNQRE 85
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 86 TVVVWErETGKPIYNAIVWQCRRTAEICEQLKRDGMEEyIRKATGLVVDPYFSGTKVKWILDHVEGSRERAKRgeLLFgT 165
Cdd:cd07808 81 GLVLLD-KNGRPLRPAILWNDQRSAAECEELEARLGDE-ILIITGNPPLPGFTLPKLLWLKENEPEIFARIRK--ILL-P 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 166 VDtWLIWKMTqGRvHVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYGQTN------IGGKGGTRIp 239
Cdd:cd07808 156 KD-YLRYRLT-GE-LATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTpeaaeeLGLPEGTPV- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 240 IAGiAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTgEKAVTSTHGLLTTIaCGPRGEVNYALeGAVFMAGASIQWLRD 319
Cdd:cd07808 232 VAG-AGDNAAAALGAGVVEPGDALISLGTSGVVFAPT-DKPVPDPKGRLHTF-PHAVPGKWYAM-GVTLSAGLSLRWLRD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 320 EMKLISDAFDSeyFATKVKDT----NGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLEA 395
Cdd:cd07808 308 LFGPDRESFDE--LDAEAAKVppgsEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 396 MQaDSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAV-IEREFRPG 474
Cdd:cd07808 386 LK-ELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACIkIEKTIEPD 464
|
490
....*....|....*..
gi 496082303 475 IETTER-NYRYSGWKKA 490
Cdd:cd07808 465 PERHEAyDELYARYREL 481
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
6-480 |
1.53e-89 |
|
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: 282.10 E-value: 1.53e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEALAKADINSDQIAAIGITNQRE 85
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 86 TVV-VweRETGKPIYNAIVWQCRRTAEICEQL-KRDGMEEYIRKATGLVVDPYFSGTKVKWILDHvegSRERAKRGELLF 163
Cdd:cd07805 81 GVVpV--DKDGNPLRNAIIWSDTRAAEEAEEIaGGLGGIEGYRLGGGNPPSGKDPLAKILWLKEN---EPEIYAKTHKFL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 164 GTVDtWLIWKMTqGRVhVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYG--------QTNIggKGG 235
Cdd:cd07805 156 DAKD-YLNFRLT-GRA-ATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGeltpeaaaELGL--PAG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 236 TRIpIAGiAGDQQAALFGQLCVKEGMAkNTY-GTGCFMLMNTGEKAVTSTHGlLTTIACGPRGEVNYAleGAVFMAGASI 314
Cdd:cd07805 231 TPV-VGG-GGDAAAAALGAGAVEEGDA-HIYlGTSGWVAAHVPKPKTDPDHG-IFTLASADPGRYLLA--AEQETAGGAL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 315 QWLRDEMKLISDAFDSEY-FATK-VKDT----NGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQ 388
Cdd:cd07805 305 EWARDNLGGDEDLGADDYeLLDElAAEAppgsNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 389 TRDVLEAMQADSGiRLHALRVDGGAVANNFLMQFQSDILGTRVERPEV-REVTALGAAYLAGLAVGFWQNLDELQEKAVI 467
Cdd:cd07805 385 LRWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVPENpQEAGALGAALLAAVGLGLLKSFDEAKALVKV 463
|
490
....*....|...
gi 496082303 468 EREFRPGIETTER 480
Cdd:cd07805 464 EKVFEPDPENRAR 476
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
6-453 |
3.93e-86 |
|
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: 272.48 E-value: 3.93e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEALAKADINSDQIAAIGITNQRE 85
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 86 TVVVWEREtGKPIYNAIVWQCRRTAEICEQLKRDGMEEYIRKATGLVVDPYFSGTKVKWILDHVEGSRERAKRgellFGT 165
Cdd:cd07804 81 ALVPVDEN-GKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRK----FLG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 166 VDTWLIWKMTqGRVhVTDYTNASRTM-LFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYG--------QTniGGKGGT 236
Cdd:cd07804 156 AYDYIVYKLT-GEY-VIDYSSAGNEGgLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGevtkeaaeET--GLAEGT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 237 RIpIAGiAGDQQAALFGQLCVKEG--MAKntYGT-GCFMLMNtgEKAVTStHGLLTTIACGPRGevnYALEGAVFMAGAS 313
Cdd:cd07804 232 PV-VAG-TVDAAASALSAGVVEPGdlLLM--LGTaGDIGVVT--DKLPTD-PRLWLDYHDIPGT---YVLNGGMATSGSL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 314 IQWLRDEM------------KLISDAFDSEyfATKVKDT-NGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRA 380
Cdd:cd07804 302 LRWFRDEFageeveaeksggDSAYDLLDEE--AEKIPPGsDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRA 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496082303 381 TLESIAYQTRDVLEAMqADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVG 453
Cdd:cd07804 380 LLEGVAYGLRHHLEVI-REAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
6-480 |
4.82e-79 |
|
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466790 [Multi-domain] Cd Length: 478 Bit Score: 254.79 E-value: 4.82e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWasqsSTLVEALAK--ADINSDQIAAIGITNQ 83
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEIL----EAVLEALKEvlAKLGGGEVDAIGFSSA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 84 RETVVVWEREtGKPIYNAIVWQCRRTAEICEQLKRDGMEEYIRKATGLVVDPYFSGTKVKWILDHVEGSRERAKRgellF 163
Cdd:cd07770 77 MHSLLGVDED-GEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAAK----F 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 164 GTVDTWLIWKMTqGRvHVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYGQ------TNIGGKGGTR 237
Cdd:cd07770 152 VSIKEYLLYRLT-GE-LVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGlkpefaERLGLLAGTP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 238 IpIAGiAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTgEKAVTSTHGLLTTIACGPRgevNYALEGAVFMAGASIQWL 317
Cdd:cd07770 230 V-VLG-ASDGALANLGSGALDPGRAALTVGTSGAIRVVS-DRPVLDPPGRLWCYRLDEN---RWLVGGAINNGGNVLDWL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 318 RDEMKLISDAFD--SEYFATKVKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLEA 395
Cdd:cd07770 304 RDTLLLSGDDYEelDKLAEAVPPGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 396 MQaDSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLdELQEKAVIEREFRPGI 475
Cdd:cd07770 384 LE-ELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSL-EADELVKIGKVVEPDP 461
|
....*
gi 496082303 476 ETTER 480
Cdd:cd07770 462 ENHAI 466
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
6-453 |
5.87e-70 |
|
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466805 [Multi-domain] Cd Length: 444 Bit Score: 230.13 E-value: 5.87e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEALAKADINSDQIAAIGITNQRE 85
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 86 TVVVWEREtGKPIYNAIVWQCRRTAEICEQLKRDGMEEYIRKATGLVVDPYFSGTKVKWILDHvegSRERAKRGELLFGT 165
Cdd:cd07802 81 GLYLVDKD-GKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKEN---EPERYDRIRTVLFC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 166 VDtWLIWKMTqGRVHvTDYTNASrTMLFNIHELDWDDKMLDALDIP--RAMLPEVRKSSEVYG--------QTNIggKGG 235
Cdd:cd07802 157 KD-WIRYRLT-GEIS-TDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGrvtaeaaaLTGL--PEG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 236 TriPIAGIAGDQQAALFGQLCVKEGMAKNTYGTGCfmlMNTG--EKAVTSTHGLLTTIACGPrgevNYALEGAVFMAGAS 313
Cdd:cd07802 231 T--PVAAGAFDVVASALGAGAVDEGQLCVILGTWS---INEVvtDEPVVPDSVGSNSLHADP----GLYLIVEASPTSAS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 314 -IQWLRDEM--------KLISDAFDsEYFATKVKDTNGVYVVPAFTGLGApywDPYARGAIFGLTRGVNSNHIIRATLES 384
Cdd:cd07802 302 nLDWFLDTLlgeekeagGSDYDELD-ELIAAVPPGSSGVIFLPYLYGSGA---NPNARGGFFGLTAWHTRAHLLRAVYEG 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496082303 385 IAYQTRDVLEAMQADSGIRlhALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVG 453
Cdd:cd07802 378 IAFSHRDHLERLLVARKPE--TIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
6-452 |
2.36e-61 |
|
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: 207.07 E-value: 2.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWasqsSTLVEALAK--ADINSDQIAAIGITNQ 83
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWW----EALRSLLRElpAELRPRRVVAIAVDGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 84 RETVVVWEREtGKPIYNAIVWQCRRTAEICEQLKRdgMEEYIRKATGLVVDPYFSGTKVKWILDHVEGSRERAKRgeLLF 163
Cdd:cd07783 77 SGTLVLVDRE-GEPLRPAIMYNDARAVAEAEELAE--AAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAK--FLH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 164 GTvdTWLIWKMTqGRVHVTDYTNASRTmLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYGQT------NIGGKGGTR 237
Cdd:cd07783 152 QA--DWLAGRLT-GDRGVTDYNNALKL-GYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLtaeaaeELGLPAGTP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 238 IpIAGIAgDQQAALFGQLCVKEGMAKNTYGTG-CFMLMnTGEKAVTSTHGllttIACGPRGEVNYALEGAVFMAGASIQW 316
Cdd:cd07783 228 V-VAGTT-DSIAAFLASGAVRPGDAVTSLGTTlVLKLL-SDKRVPDPGGG----VYSHRHGDGYWLVGGASNTGGAVLRW 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 317 L--RDEMKLISDAFDSEYfatkvkdTNGVYVVP-AFTGLGAPYWDPYARGAIfgLTRGVNSNHIIRATLESIAYQTRDVL 393
Cdd:cd07783 301 FfsDDELAELSAQADPPG-------PSGLIYYPlPLRGERFPFWDPDARGFL--LPRPHDRAEFLRALLEGIAFIERLGY 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 496082303 394 EAMQADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREvTALGAAYLAGLAV 452
Cdd:cd07783 372 ERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEE-AALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
6-453 |
2.27e-59 |
|
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to Bacillus subtilis sugar kinase YoaC. It is part of the yoaDCB operon and induced by sulfate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466804 [Multi-domain] Cd Length: 448 Bit Score: 202.45 E-value: 2.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPK--PGWVEHDPMEIWASQSSTLVEALAKADINSDQIAAIGITNQ 83
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDdyPDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 84 RETVVVWEREtGKPIY---N----AIVWQcrrtAEICEQLkrdgmEEYIRKATGLVVDPYFSGTKVKWILDHVEGSRERA 156
Cdd:cd07798 81 REGIVFLDKD-GRELYagpNidarGVEEA----AEIDDEF-----GEEIYTTTGHWPTELFPAARLLWFKENRPEIFERI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 157 KRgellFGTVDTWLIWKMTqGRVhVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYG------QTNI 230
Cdd:cd07798 151 AT----VLSISDWIGYRLT-GEL-VSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGtvseeaAREL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 231 GGKGGTRIPIAGiaGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVTSTHGLLTTIACGPRGevnYALEGAVFMA 310
Cdd:cd07798 225 GLPEGTPVVVGG--ADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTGCHLVPGK---WVLESNAGVT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 311 GASIQWLRDEM-KLISDAFD--SEYFATKVKDTNGVYvvpAFTGLGAPYWD--PYARGAIF----GLTRGVNSNHIIRAT 381
Cdd:cd07798 300 GLNYQWLKELLyGDPEDSYEvlEEEASEIPPGANGVL---AFLGPQIFDARlsGLKNGGFLfptpLSASELTRGDFARAI 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082303 382 LESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVG 453
Cdd:cd07798 377 LENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
6-453 |
1.86e-52 |
|
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: 183.98 E-value: 1.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEALAKADINSDQIAAIGITNQRE 85
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 86 -TVVVweRETGKPIYNAIVWQCRRTAEICEQLKRDGMEEYIRKATGLVVDPYFSGTKVKWILDHvegSRERAKRGELLFG 164
Cdd:cd24121 81 gTWLV--DEDGRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKEN---EPERLERARTALH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 165 TVDtWLIWKMTQGRvhVTDYTNASRTMlFNIHELDWDDKMLDALDIP--RAMLPEVRKSSEVYGQTN------IGGKGGT 236
Cdd:cd24121 156 CKD-WLFYKLTGEI--ATDPSDASLTF-LDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTpeaaaaTGLPAGT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 237 riPIAGIAGDQQAALFGQLCVKEGMAKNTYGTGCF--MLMNtgeKAVTSTHGLLTTIACGPRGEVNYALegAVFMAGASI 314
Cdd:cd24121 232 --PVVLGPFDVVATALGSGAIEPGDACSILGTTGVheVVVD---EPDLEPEGVGYTICLGVPGRWLRAM--ANMAGTPNL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 315 QWLRDEM-------KLISDAFDSEYFATKVKD----TNGVYVVP--AFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRAT 381
Cdd:cd24121 305 DWFLRELgevlkegAEPAGSDLFQDLEELAASsppgAEGVLYHPylSPAGERAPFVNPNARAQFTGLSLEHTRADLLRAV 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082303 382 LESIAYQTRDVLEAMQADSGirlhALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVG 453
Cdd:cd24121 385 YEGVALAMRDCYEHMGEDPG----ELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
6-453 |
1.61e-49 |
|
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: 175.82 E-value: 1.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMD-HDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEALAKADINSDQIAAIGITNQR 84
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 85 ETVVVWEREtGKPIYNAIVWQCRRTAEICEQLkrdgMEEYIRKA---TGLVVDPYFSGTKVKWILDHVEGSRERAKRGEL 161
Cdd:cd07809 81 HGLVALDAD-GKVLRPAKLWCDTRTAPEAEEL----TEALGGKKcllVGLNIPARFTASKLLWLKENEPEHYARIAKILL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 162 LFGtvdtWLIWKMTqGRvHVTDYTNASRTMLFNIHELDWDDKMLDALD---IPRAMLPEVRKSSEVYGQ-TNIGGKGG-- 235
Cdd:cd07809 156 PHD----YLNWKLT-GE-KVTGLGDASGTFPIDPRTRDYDAELLAAIDpsrDLRDLLPEVLPAGEVAGRlTPEGAEELgl 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 236 -TRIPIAGIAGDQQAALFGQLCVKEGMAKNTYGT-GCfmLMNTGEKAVTSTHGLLTTIAcgprgEVNYALEGAVFMAGAS 313
Cdd:cd07809 230 pAGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTsGT--AYGVSDKPVSDPHGRVATFC-----DSTGGMLPLINTTNCL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 314 IQWLRDEMKLIS---DAFDSEYFATKVkDTNGVYVVPAFTGLGAPYWdPYARGAIFGLTrgvNSN----HIIRATLESIA 386
Cdd:cd07809 303 TAWTELFRELLGvsyEELDELAAQAPP-GAGGLLLLPFLNGERTPNL-PHGRASLVGLT---LSNftraNLARAALEGAT 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082303 387 YQTRDVLEAMQADsGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVG 453
Cdd:cd07809 378 FGLRYGLDILREL-GVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
262-451 |
3.41e-47 |
|
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: 162.49 E-value: 3.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 262 AKNTYGTGCFMLMnTGEKAVTSTHGLLTTIAcGPRGEVNYALEGAVFMAGASIQWLRDEM----KLISDAFDSEYFATK- 336
Cdd:pfam02782 1 LAISAGTSSFVLV-ETPEPVLSVHGVWGPYT-NEMLPGYWGLEGGQSAAGSLLAWLLQFHglreELRDAGNVESLAELAa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 337 ---VKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGA 413
Cdd:pfam02782 79 laaVAPAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSGGG 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 496082303 414 VANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLA 451
Cdd:pfam02782 159 SRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
6-476 |
8.59e-46 |
|
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: 166.74 E-value: 8.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFeqIYPK----PGWVEHDPMEIWASQSSTLVEALAKADINSDQIAAIGIT 81
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREW--RHKEvpdvPGSMDFDTEKNWKLICECIREALKKAGIAPKSIAAISTT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 82 NQRETVVVWEREtGKPIynaivWQCR----RTAEICEQLK--RDGMEEYIRKATGlvvDPYFSGT--KVKWILDHVEGSR 153
Cdd:cd07775 79 SMREGIVLYDNE-GEEI-----WACAnvdaRAAEEVSELKelYNTLEEEVYRISG---QTFALGAipRLLWLKNNRPEIY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 154 ERAKRgellFGTVDTWLIWKMTQgrVHVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYGQTN---- 229
Cdd:cd07775 150 RKAAK----ITMLSDWIAYKLSG--ELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTkeaa 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 230 --IGGKGGTRIpIAGIaGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVTSTHGLLTTIACGPrGEVNYalEGAV 307
Cdd:cd07775 224 eeTGLKEGTPV-VVGG-GDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMNIRVNCHVIP-DMWQA--EGIS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 308 FMAGASIQWLRD----EMKLIS-----DAFDseYFATKVKDT------------------NGVYVVPAFTGLGApywDP- 359
Cdd:cd07775 299 FFPGLVMRWFRDafcaEEKEIAerlgiDAYD--LLEEMAKDVppgsygimpifsdvmnykNWRHAAPSFLNLDI---DPe 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 360 -YARGAIFgltrgvnsnhiiRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVRE 438
Cdd:cd07775 374 kCNKATFF------------RAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKE 441
|
490 500 510
....*....|....*....|....*....|....*....
gi 496082303 439 VTALGAAYLAGLAVGFWQNLDELQEKAV-IEREFRPGIE 476
Cdd:cd07775 442 ATALGAAIAAGVGAGIYSSLEEAVESLVkWEREYLPNPE 480
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
6-480 |
2.61e-42 |
|
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: 157.70 E-value: 2.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMD-HDANIVSVSQREFEQIY--PKPGWVEHDPMEIWASQSSTLVEALAKADINSDQIAAIGITN 82
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 83 QRETVVVWEREtGKPIYNAIVW-------QCRRTAEICeqlkRDGMEEYIRKATGLV-VDPYFSgtKVKWILDHVEGSRE 154
Cdd:cd07781 81 TSSTVVPVDED-GNPLAPAILWmdhraqeEAAEINETA----HPALEYYLAYYGGVYsSEWMWP--KALWLKRNAPEVYD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 155 RAKR-GELlfgtVDtWLIWKMTqGRVhVTDYTNASRTMLFNIHELDWDDKMLDALDIP----RAMLP-EVRKSSEVYGQT 228
Cdd:cd07781 154 AAYTiVEA----CD-WINARLT-GRW-VRSRCAAGHKWMYNEWGGGPPREFLAALDPGllklREKLPgEVVPVGEPAGTL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 229 N------IGGKGGTRIPIAGIagDQQAALFGQLCVKEG-MAKNTyGT-GCFMLMNTGEKAVtstHGLlttiaCGP-RGEV 299
Cdd:cd07781 227 TaeaaerLGLPAGIPVAQGGI--DAHMGAIGAGVVEPGtLALIM-GTsTCHLMVSPKPVDI---PGI-----CGPvPDAV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 300 N---YALEGAVFMAGASIQWLRDEMKLISDAFDSEYF------ATKVK-DTNGVYVVPAFTGLGAPYWDPYARGAIFGLT 369
Cdd:cd07781 296 VpglYGLEAGQSAVGDIFAWFVRLFVPPAEERGDSIYallseeAAKLPpGESGLVALDWFNGNRTPLVDPRLRGAIVGLT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 370 RGVNSNHIIRATLESIAYQTRDVLEAMQaDSGIRLHALRVDGGAVANN-FLMQFQSDILGTRVERPEVREVTALGAAYLA 448
Cdd:cd07781 376 LGTTPAHIYRALLEATAFGTRAIIERFE-EAGVPVNRVVACGGIAEKNpLWMQIYADVLGRPIKVPKSDQAPALGAAILA 454
|
490 500 510
....*....|....*....|....*....|...
gi 496082303 449 GLAVGFWQNLDELQEKAV-IEREFRPGIETTER 480
Cdd:cd07781 455 AVAAGVYADIEEAADAMVrVDRVYEPDPENHAV 487
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
8-493 |
9.27e-36 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 138.95 E-value: 9.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 8 VALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPmEIWASQSSTLVEALAKADINSDqIAAIGITNQRETV 87
Cdd:PRK15027 3 IGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDP-EQWWQATDRAMKALGDQHSLQD-VKALGIAGQMHGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 88 VVWERETgKPIYNAIVWQCRRTAEICEQLkrdgmEEYI---RKATGLVVDPYFSGTKVKWILDH-VEGSRERAKrgELLf 163
Cdd:PRK15027 81 TLLDAQQ-RVLRPAILWNDGRCAQECALL-----EARVpqsRVITGNLMMPGFTAPKLLWVQRHePEIFRQIDK--VLL- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 164 gtVDTWLIWKMTQgrVHVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYG--QTNIGGKGGT-RIPI 240
Cdd:PRK15027 152 --PKDYLRLRMTG--EFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGalLPEVAKAWGMaTVPV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 241 AGIAGDQQAALFGQLCVKEGMAKNTYGT-GCFMLMNTG-----EKAVTS-THGLlttiacgPRgevNYALEGAVFMAGAS 313
Cdd:PRK15027 228 VAGGGDNAAGAVGVGMVDANQAMLSLGTsGVYFAVSEGflskpESAVHSfCHAL-------PQ---RWHLMSVMLSAASC 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 314 IQW------LRDEMKLISDAFDSEyfatkvKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAY 387
Cdd:PRK15027 298 LDWaakltgLSNVPALIAAAQQAD------ESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 388 QTRDVLEAMQAdSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREV-TALGAAYLAGLAVGFWQNLDELQEKAV 466
Cdd:PRK15027 372 ALADGMDVVHA-CGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTGGDVgPALGAARLAQIAANPEKSLIELLPQLP 450
|
490 500
....*....|....*....|....*..
gi 496082303 467 IEREFRPgieTTERNYRYSGWKKAVKR 493
Cdd:PRK15027 451 LEQSHLP---DAQRYAAYQPRRETFRR 474
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
6-448 |
1.09e-34 |
|
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: 135.04 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMD-HDANIVSVSQREFEQI--YPKPGWVEHDPMEIWasqsSTLVEALAK--ADINSDqIAAIGI 80
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDlESGRILESVSRPTPAPisSDDPGRSEQDPEKIL----EAVRNLIDElpREYLSD-VTGIGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 81 TNQRETVVVWeRETGKPIYNAIVWQCRRTAEICEQLKRDGMEEYIRKaTGLVVDPYFSGTKVKWIldhvegsrerAKRGE 160
Cdd:cd07777 76 TGQMHGIVLW-DEDGNPVSPLITWQDQRCSEEFLGGLSTYGEELLPK-SGMRLKPGYGLATLFWL----------LRNGP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 161 LL-----FGTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYGQTNIGGKGG 235
Cdd:cd07777 144 LPskadrAGTIGDYIVARLTGLPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLSSALPKG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 236 trIPI-AGIaGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTgEKAVTSTH---------GLLTTIA--CGPRgevnyAL 303
Cdd:cd07777 224 --IPVyVAL-GDNQASVLGSGLNEENDAVLNIGTGAQLSFLT-PKFELSGSveirpffdgRYLLVAAslPGGR-----AL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 304 egAVFmagasIQWLRDEMKLISDAFDSEYF------ATKVKDTNGVYVVPAFTGlGApyWDPYARGAIFGLTrgvNSN-- 375
Cdd:cd07777 295 --AVL-----VDFLREWLRELGGSLSDDEIwekldeLAESEESSDLSVDPTFFG-ER--HDPEGRGSITNIG---ESNft 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082303 376 --HIIRATLESIAYQTRDVLEAMQAD-SGIRlhALRVDGGAVA-NNFLMQFQSDILGTRVERPEVREVTALGAAYLA 448
Cdd:cd07777 362 lgNLFRALCRGIAENLHEMLPRLDLDlSGIE--RIVGSGGALRkNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
5-496 |
9.20e-33 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 130.90 E-value: 9.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 5 KYIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPK--PGWVEHDPMEIWASQSSTLVEALAKADINSDQIAAIGITN 82
Cdd:PRK10939 3 SYLMALDAGTGSIRAVIFDLNGNQIAVGQAEWRHLAVPdvPGSMEFDLEKNWQLACQCIRQALQKAGIPASDIAAVSATS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 83 QRETVVVWEReTGKPIynaivWQC-----RRTAEICEqLK--RDGMEEYIRKATG----LVVDPyfsgtKVKWILDHVEG 151
Cdd:PRK10939 83 MREGIVLYDR-NGTEI-----WACanvdaRASREVSE-LKelHNNFEEEVYRCSGqtlaLGALP-----RLLWLAHHRPD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 152 SRERAKRgellFGTVDTWLIWKMTQgrVHVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYG----- 226
Cdd:PRK10939 151 IYRQAHT----ITMISDWIAYMLSG--ELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGhvtak 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 227 ---QTniGGKGGTRIPIAGiaGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVTSTHGLltTIACGPRGEVNYAl 303
Cdd:PRK10939 225 aaaET--GLRAGTPVVMGG--GDVQLGCLGLGVVRPGQTAVLGGTFWQQVVNLPAPVTDPNMNI--RINPHVIPGMVQA- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 304 EGAVFMAGASIQWLRD----EMKLIS-----DAFDS-EYFATKVKdtNGVY-VVPAFTGL--------GAPYW-----DP 359
Cdd:PRK10939 298 ESISFFTGLTMRWFRDafcaEEKLLAerlgiDAYSLlEEMASRVP--VGSHgIIPIFSDVmrfkswyhAAPSFinlsiDP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 360 YA--RGAIFgltrgvnsnhiiRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVR 437
Cdd:PRK10939 376 EKcnKATLF------------RALEENAAIVSACNLQQIAAFSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVK 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082303 438 EVTALGAAYLAGLAVGFWQNLDELQEKAV-IEREFRPGIETTERnYR--YSGWKKAVKRALA 496
Cdd:PRK10939 444 EATALGCAIAAGVGAGIYSSLAETGERLVrWERTFEPNPENHEL-YQeaKEKWQAVYADQLG 504
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
6-473 |
2.78e-29 |
|
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: 120.81 E-value: 2.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMDHDANI-VSVSQREFEQ-IYPKPGWVEHDPMEIWASQSSTLVEALAKADINSDQIAAIGItNQ 83
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDLYAGLeMAQEPVPYYQdSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGV-DA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 84 RETVVVWERE--------TGKPIYNAIVW-------QCRRTAEICEQLkrdgMEEYIrkatGLVVDPYFSGTKVKWILDH 148
Cdd:cd07768 80 TCSLAIFDREgtplmaliPYPNEDNVIFWmdhsavnEAQWINMQCPQQ----LLDYL----GGKISPEMGVPKLKYFLDE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 149 VEGSRERAKRgelLFGTVDtWLIWKMTQgrvhvtDYTNASRTML----FNIHELDWDDKMLDALDIPRAML--PEVRKSS 222
Cdd:cd07768 152 YSHLRDKHFH---IFDLHD-YIAYELTR------LYEWNICGLLgkenLDGEESGWSSSFFKNIDPRLEHLttTKNLPSN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 223 EVYGQTNIGG------KGGTRIPIAGIAG--DQQAALFgqlcvkeGMAKNTYGTGCFMLMNTgekavTSTHGLLTTIA-- 292
Cdd:cd07768 222 VPIGTTSGVAlpemaeKMGLHPGTAVVVSciDAHASWF-------AVASPHLETSLFMIAGT-----SSCHMYGTTISdr 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 293 ----CGPRGEV---NYAL-EGAVFMAGASIQWL-------RDEMKLISDAFDS----EYFATKVKD----TNGVYVVPAF 349
Cdd:cd07768 290 ipgvWGPFDTIidpDYSVyEAGQSATGKLIEHLfeshpcaRKFDEALKKGADIyqvlEQTIRQIEKnnglSIHILTLDMF 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 350 TGLGAPYWDPYARGAIFGL---TRGVNSNHIIRATLESIAYQTRDVLEAMQaDSGIRLHALRVDGGAVANNFLMQFQSDI 426
Cdd:cd07768 370 FGNRSEFADPRLKGSFIGEsldTSMLNLTYKYIAILEALAFGTRLIIDTFQ-NEGIHIKELRASGGQAKNERLLQLIALV 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 496082303 427 LGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAV----IEREFRP 473
Cdd:cd07768 449 TNVAIIKPKENMMGILGAAVLAKVAAGKKQLADSITEADIsndrKSETFEP 499
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
6-482 |
3.48e-29 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 119.75 E-value: 3.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMDHDANIV-SVSQREFEQIYP-KPGWVEHDPMEIWASQSSTLVEALAKadINSDQIAAIGITnq 83
Cdd:PRK10331 3 VILVLDCGATNVRAIAVDRQGKIVaRASTPNASDIAAeNSDWHQWSLDAILQRFADCCRQINSE--LTECHIRGITVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 84 reTVVV---WERETGKPIYNAIVWQCRRTAEICEQLKR--DGMEEYIRKATGlvvdpYFS-GT--KVKWILDHvegsrer 155
Cdd:PRK10331 79 --TFGVdgaLVDKQGNLLYPIISWKCPRTAAVMENIERyiSAQQLQQISGVG-----AFSfNTlyKLVWLKEN------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 156 akrGELLFGTVDTWL-IWKMTQGR---VHVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYG--QTN 229
Cdd:PRK10331 145 ---HPQLLEQAHAWLfISSLINHRltgEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGtlQPS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 230 IGGKGG--TRIPIAGIAGDQQAALFGQlcvkeGMAKN----TYGTgCFMLMNTGEKAVTSTHGLLTTIACGPRGEVNYAL 303
Cdd:PRK10331 222 AAALLGlpVGIPVISAGHDTQFALFGS-----GAGQNqpvlSSGT-WEILMVRSAQVDTSLLSQYAGSTCELDSQSGLYN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 304 EGAVFMAGASIQWLRdemKLISDAfdSEYFATKVKD-------TNGVYVVPAFTGLGapywdpyaRGAIFGLTRGVNSNH 376
Cdd:PRK10331 296 PGMQWLASGVLEWVR---KLFWTA--ETPYQTMIEEaraippgADGVKMQCDLLACQ--------NAGWQGVTLNTTRGH 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 377 IIRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQ 456
Cdd:PRK10331 363 FYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFS 442
|
490 500
....*....|....*....|....*..
gi 496082303 457 NLDELQEKAVIE-REFRPGieTTERNY 482
Cdd:PRK10331 443 SPEQARAQMKYQyRYFYPQ--TEPEFI 467
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
4-480 |
2.39e-27 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 115.21 E-value: 2.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 4 KKYIVALDQGTTSSRAVVMD-HDANIVSVSQREF------EQIYPKPGWVEHDPMEIWASQSSTLVEALAKADINSDQIA 76
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDaADGEELASAVHPYprwvigLYLPPPPDQARQHPLDYLEALEAAVREALAQAGVDPADVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 77 AIGITNQRETVVVWEREtGKPI-----------YNAIVW-------QCRRTAEICEQLKrdgmEEYIRKATGlVVDP--Y 136
Cdd:COG1069 81 GIGVDATGCTPVPVDAD-GTPLallpefaenphAMVILWkdhtaqeEAERINELAKARG----EDYLRYVGG-IISSewF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 137 FSgtKVKWILDHVEGSRERAKRgelLFGTVDtWLIWKMTqGRVHvtdytnASRT-----MLFNIHELDW-DDKMLDALDI 210
Cdd:COG1069 155 WP--KILHLLREDPEVYEAADS---FVELCD-WITWQLT-GSLK------RSRCtaghkALWHAHEGGYpSEEFFAALDP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 211 PRAMLPEvRKSSEVYgqtNIGGKGGT-------------RIPIAGIAGDQQAALFGQLCVKEG-MAKNtYGT-GCFMLMN 275
Cdd:COG1069 222 LLDGLAD-RLGTEIY---PLGEPAGTltaewaarlglppGTAVAVGAIDAHAGAVGAGGVEPGtLVKV-MGTsTCHMLVS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 276 TGEKAVtstHGLlttiaCGPrgeVN-------YALEG---AVfmaGASIQWLRDE-------MKLISDAFDS--EYFATK 336
Cdd:COG1069 297 PEERFV---PGI-----CGQ---VDgsivpgmWGYEAgqsAV---GDIFAWFVRLlvppleyEKEAEERGISlhPLLTEE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 337 VK----DTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLEAMQAdSGIRLHALRVDGG 412
Cdd:COG1069 363 AAklppGESGLHALDWFNGNRSPLADQRLKGVILGLTLGTDAEDIYRALVEATAFGTRAIIERFEE-EGVPIDEIIACGG 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082303 413 -AVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEK--AVIEREFRPGIETTER 480
Cdd:COG1069 442 iATKNPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMAAmgSGFDKVYTPDPENVAV 512
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
6-460 |
3.32e-22 |
|
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.
Pssm-ID: 466800 [Multi-domain] Cd Length: 540 Bit Score: 99.92 E-value: 3.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEALAKADINSDQIAAIG------ 79
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGfdatcs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 80 ---ITNQRETVVVWEreTGKPIYNAIVWQCRRTAEiceqlkrdgMEEYIrKATGLVVDPYFSGT--------KVKWILDH 148
Cdd:cd07782 81 lvvLDAEGKPVSVSP--SGDDERNVILWMDHRAVE---------EAERI-NATGHEVLKYVGGKispemeppKLLWLKEN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 149 VEGSRERAKRgelLFGTVDtWLIWKMTQGRvhvtdytnaSRT-------MLFNIHELD---WDDKMLDALDIPRAMLPEV 218
Cdd:cd07782 149 LPETWAKAGH---FFDLPD-FLTWKATGSL---------TRSlcslvckWTYLAHEGSeggWDDDFFKEIGLEDLVEDNF 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 219 RKSSEV--YGQTNIGG------------KGGTRIPIAGIagDQQAALFGQLCVKEGMAKNTY-----------GTG-CFM 272
Cdd:cd07782 216 AKIGSVvlPPGEPVGGgltaeaakelglPEGTPVGVSLI--DAHAGGLGTLGADVGGLPCEAdpltrrlalicGTSsCHM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 273 LMNtgEKAV------------------------TSTHGLL----TTIACGPrgevnyALEGAVFMAGASI-QWLRDEMKL 323
Cdd:cd07782 294 AVS--PEPVfvpgvwgpyysamlpglwlneggqSATGALLdhiiETHPAYP------ELKEEAKAAGKSIyEYLNERLEQ 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 324 ISDA--FDSEYFatkvkdTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIR---ATLESIAYQTRDVLEAMQA 398
Cdd:cd07782 366 LAEEkgLPLAYL------TRDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHIIEAMNA 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082303 399 dSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDE 460
Cdd:cd07782 440 -AGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWD 500
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
6-463 |
8.23e-18 |
|
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: 85.66 E-value: 8.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 6 YIVALDQGTTSSRAVVMDHDANIVsvsqrEFEQIYPkpgwVEHDPMEI-------WASQSSTLVEALAKADINSDQIAAI 78
Cdd:cd07771 1 NYLAVDLGASSGRVILGSLDGGKL-----ELEEIHR----FPNRPVEInghlywdIDRLFDEIKEGLKKAAEQGGDIDSI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 79 GIT---------NQRetvvvweretGKPIYNAIVWQCRRTAEICEQLKRDGMEEYIRKATGLVVDPYFSgtkvkwiLDHV 149
Cdd:cd07771 72 GIDtwgvdfgllDKN----------GELLGNPVHYRDPRTEGMMEELFEKISKEELYERTGIQFQPINT-------LYQL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 150 egsRERAKRGELLFGTVDTWLI------WKMTqGRVhVTDYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSE 223
Cdd:cd07771 135 ---YALKKEGPELLERADKLLMlpdllnYLLT-GEK-VAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 224 VYGQTN---IGGKGGTRIPIAGIAG-DQQAALFGQLCVKEGMAkntY---GTGCFMlmntGekaVTSTHGLLTTIACgpr 296
Cdd:cd07771 210 VLGTLKpevAEELGLKGIPVIAVAShDTASAVAAVPAEDEDAA---FissGTWSLI----G---VELDEPVITEEAF--- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 297 gEVNYALEGAVF--------MAGASI------QWLRDEMK-----LISDAFDSEYFATKVkDTNGvyvvPAF-------- 349
Cdd:cd07771 277 -EAGFTNEGGADgtirllknITGLWLlqecrrEWEEEGKDysydeLVALAEEAPPFGAFI-DPDD----PRFlnpgdmpe 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 350 --------TGLGAPYwdpyargaifglTRGvnsnHIIRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLMQ 421
Cdd:cd07771 351 airaycreTGQPVPE------------SPG----EIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQ 414
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 496082303 422 FQSDILGTRVER-PEvrEVTALGAAYLAGLAVGFWQNLDELQE 463
Cdd:cd07771 415 LTADATGLPVIAgPV--EATAIGNLLVQLIALGEIKSLEEGRE 455
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
355-480 |
4.46e-12 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 68.33 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 355 PYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLEAMQaDSGIRLHALRVDGG-AVANNFLMQFQSDILGTRVER 433
Cdd:PRK04123 391 PLADQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFE-DQGVPVEEVIAAGGiARKNPVLMQIYADVLNRPIQV 469
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 496082303 434 PEVREVTALGAAYLAGLAVGFWQNLDELQEK--AVIEREFRPGIETTER 480
Cdd:PRK04123 470 VASDQCPALGAAIFAAVAAGAYPDIPEAQQAmaSPVEKTYQPDPENVAR 518
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
11-448 |
2.07e-07 |
|
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: 53.56 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 11 DQGTTSSRAVVMDHDANIVSVSQREFE-QIYPKPGW-VEHDPMEIWASqsstLVEALAKADINSDQ--IAAIGITnqrET 86
Cdd:cd07778 6 DVGSTSVRIGIFDYHGTLLATSERPISyKQDPKDLWfVTQSSTEIWKA----IKTALKELIEELSDyiVSGIGVS---AT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 87 --VVVWERETGK--------------PIYNAIVWQCRRTAEICEQLKRDGMEEYIRKATGLVVdPYFSGTKVKWILDHVe 150
Cdd:cd07778 79 csMVVMQRDSDTsylvpynviheksnPDQDIIFWMDHRASEETQWLNNILPDDILDYLGGGFI-PEMAIPKLKYLIDLI- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 151 gSRERAKrgELLFGTVDTWLIWKMTQGRVHVTD-YTNASRTMLFNIH-ELD-WDDKMLDALDIprAMLPEVRKSsevygq 227
Cdd:cd07778 157 -KEDTFK--KLEVFDLHDWISYMLATNLGHSNIvPVNAPPSIGIGIDgSLKgWSKDFYSKLKI--STKVCNVGN------ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 228 tniGGKGGTRIPIAGIA-GDQQAALFGQLcvkeGMAKNTY-GTGCfmlmntgekaVTSTHGLLTTIACGPRgevnyaLEG 305
Cdd:cd07778 226 ---TFKEAPPLPYAGIPiGKVNVILASYL----GIDKSTVvGHGC----------IDCYAGWFSTFAAAKT------LDT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 306 AVFM-AGAS----------------------IQWLRDEM----------KLISDAFDS---------------EYFATKV 337
Cdd:cd07778 283 TLFMvAGTStcflyatsssqvgpipgiwgpfDQLLKNYSvyeggqsatgKLIEKLFNShpaiiellksdanffETVEEKI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082303 338 KD------TNGVYVVPAFTGLG------APYWDPYARGAIFGltrGVNSNHIIR------ATLESIAYQTRDVLEAMQaD 399
Cdd:cd07778 363 DKyerllgQSIHYLTRHMFFYGdylgnrTPYNDPNMSGSFIG---ESTDSSLTDlvlkyiLILEFLAFQTKLIIDNFQ-K 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 496082303 400 SGIRLHALRVDGGAVANNFLMQFQS---DILGTRVERPEVREVTALGAAYLA 448
Cdd:cd07778 439 EKIIIQKVVISGSQAKNARLLQLLStvlSKIHIIVPLSDSKYAVVKGAALLG 490
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
183-244 |
5.44e-06 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 48.95 E-value: 5.44e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082303 183 DYTNASRTMLFNIHELDWDDKMLDALDIPRAMLPEVRKSSEVYGqtNIGGKGGTRIPIAGIA 244
Cdd:PRK10640 157 EYTNATTTQLVNINSDDWDESLLAWSGAPKAWFGRPTHPGNVIG--HWICPQGNEIPVVAVA 216
|
|
| |
