|
Name |
Accession |
Description |
Interval |
E-value |
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
4-498 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 952.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 4 QKYIMALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPKPGWVEHDANEIWTTQLGVALSAMNQIGASAEDIAAIGITNQ 83
Cdd:COG0554 2 KKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITNQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 84 RETTIVWDRDTGEPVCHAIVWQCRRTSEYCDELKARGLTEKFREKTGLVIDAYFSATKLKWILDNVPGVRARAERGDLLF 163
Cdd:COG0554 82 RETTVVWDRKTGKPLYNAIVWQDRRTADICEELKADGLEDLIREKTGLVLDPYFSATKIKWILDNVPGARERAEAGELLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 164 GTVETWLIWKLTCGKIHVTDYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPKPVPNSEFYEYADPMHFGGEIKIAGAA 243
Cdd:COG0554 162 GTIDSWLIWKLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDPDLFGAEIPIAGIA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 244 GDQQAALFGQTCFTKGEAKSTFGTGGFLLMNTGEKPVFSHNGLVTTVAWGLDGKVNYALEGSIFVAGAAIQWLRDELHLL 323
Cdd:COG0554 242 GDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGGKVTYALEGSIFVAGAAVQWLRDGLGLI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 324 EDARDSEYMAQKVKDTNGCYVVPAFTGLGAPHWDQYARGAIVGLTRGVNKNHIIRATLDSLCYQINDVLTAMQADAGIPL 403
Cdd:COG0554 322 DSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADSGIPL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 404 TALKVDGGACANNYLMQTMADISARPVKRPCCVETTALGAAYLAGLAVGYWQSTDDVLKNWSVDREFVPALTEAERTRRI 483
Cdd:COG0554 402 KELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEELAALWKVDRRFEPQMDEEERERLY 481
|
490
....*....|....*
gi 2050539736 484 QGWNKAVRCSYGWAK 498
Cdd:COG0554 482 AGWKKAVERTLGWAE 496
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
1-497 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 928.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 1 MANQKYIMALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPKPGWVEHDANEIWTTQLGVALSAMNQIGASAEDIAAIGI 80
Cdd:PRK00047 1 MMMKKYILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 81 TNQRETTIVWDRDTGEPVCHAIVWQCRRTSEYCDELKARGLTEKFREKTGLVIDAYFSATKLKWILDNVPGVRARAERGD 160
Cdd:PRK00047 81 TNQRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRDGYEDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 161 LLFGTVETWLIWKLTCGKIHVTDYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPKPVPNSEFYEYADPMHF-GGEIKI 239
Cdd:PRK00047 161 LLFGTIDTWLVWKLTGGKVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYGFfGGEVPI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 240 AGAAGDQQAALFGQTCFTKGEAKSTFGTGGFLLMNTGEKPVFSHNGLVTTVAWGLDGKVNYALEGSIFVAGAAIQWLRDE 319
Cdd:PRK00047 241 AGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGIDGKVVYALEGSIFVAGSAIQWLRDG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 320 LHLLEDARDSEYMAQKVKDTNGCYVVPAFTGLGAPHWDQYARGAIVGLTRGVNKNHIIRATLDSLCYQINDVLTAMQADA 399
Cdd:PRK00047 321 LKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 400 GIPLTALKVDGGACANNYLMQTMADISARPVKRPCCVETTALGAAYLAGLAVGYWQSTDDVLKNWSVDREFVPALTEAER 479
Cdd:PRK00047 401 GIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDELKEQWKIDRRFEPQMDEEER 480
|
490
....*....|....*...
gi 2050539736 480 TRRIQGWNKAVRCSYGWA 497
Cdd:PRK00047 481 EKLYAGWKKAVKRTLAWA 498
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
6-491 |
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: 902.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 6 YIMALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPKPGWVEHDANEIWTTQLGVALSAMNQIGASAEDIAAIGITNQRE 85
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 86 TTIVWDRDTGEPVCHAIVWQCRRTSEYCDELKARGLTEKFREKTGLVIDAYFSATKLKWILDNVPGVRARAERGDLLFGT 165
Cdd:cd07786 81 TTVVWDRETGKPVYNAIVWQDRRTADICEELKAEGHEEMIREKTGLVLDPYFSATKIRWILDNVPGARERAERGELAFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 166 VETWLIWKLTCGKIHVTDYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPKPVPNSEFYEYADPMHFGGEIKIAGAAGD 245
Cdd:cd07786 161 IDSWLIWKLTGGKVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDPDLLGAEIPIAGIAGD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 246 QQAALFGQTCFTKGEAKSTFGTGGFLLMNTGEKPVFSHNGLVTTVAWGLDGKVNYALEGSIFVAGAAIQWLRDELHLLED 325
Cdd:cd07786 241 QQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLGGKVTYALEGSIFIAGAAVQWLRDGLGLIES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 326 ARDSEYMAQKVKDTNGCYVVPAFTGLGAPHWDQYARGAIVGLTRGVNKNHIIRATLDSLCYQINDVLTAMQADAGIPLTA 405
Cdd:cd07786 321 AAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEADSGIPLKE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 406 LKVDGGACANNYLMQTMADISARPVKRPCCVETTALGAAYLAGLAVGYWQSTDDVLKNWSVDREFVPALTEAERTRRIQG 485
Cdd:cd07786 401 LRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAKLWQVDRRFEPSMSEEEREALYAG 480
|
....*.
gi 2050539736 486 WNKAVR 491
Cdd:cd07786 481 WKKAVK 486
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
6-491 |
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: 894.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 6 YIMALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPKPGWVEHDANEIWTTQLGVALSAMNQIGASAEDIAAIGITNQRE 85
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 86 TTIVWDRDTGEPVCHAIVWQCRRTSEYCDELKARGLTEKFREKTGLVIDAYFSATKLKWILDNVPGVRARAERGDLLFGT 165
Cdd:cd07769 81 TTVVWDKKTGKPLYNAIVWQDRRTADICEELKAKGLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAERGELLFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 166 VETWLIWKLTCGKIHVTDYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPKPVPNSEFYEYADPMHFGGEIKIAGAAGD 245
Cdd:cd07769 161 IDTWLIWKLTGGKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTDPEGLGAGIPIAGILGD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 246 QQAALFGQTCFTKGEAKSTFGTGGFLLMNTGEKPVFSHNGLVTTVAWGLDGKVNYALEGSIFVAGAAIQWLRDELHLLED 325
Cdd:cd07769 241 QQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQIGGKVTYALEGSIFIAGAAIQWLRDNLGLIED 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 326 ARDSEYMAQKVKDTNGCYVVPAFTGLGAPHWDQYARGAIVGLTRGVNKNHIIRATLDSLCYQINDVLTAMQADAGIPLTA 405
Cdd:cd07769 321 AAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDSGIKLKE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 406 LKVDGGACANNYLMQTMADISARPVKRPCCVETTALGAAYLAGLAVGYWQSTDDVLKNWSVDREFVPALTEAERTRRIQG 485
Cdd:cd07769 401 LRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDELASLWQVDKRFEPSMDEEERERLYRG 480
|
....*.
gi 2050539736 486 WNKAVR 491
Cdd:cd07769 481 WKKAVE 486
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
5-496 |
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: 804.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 5 KYIMALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPKPGWVEHDANEIWTTQLGVALSAMNQIGASAEDIAAIGITNQR 84
Cdd:TIGR01311 1 PYILAIDQGTTSSRAIVFDKDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAGIKPDDIAAIGITNQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 85 ETTIVWDRDTGEPVCHAIVWQCRRTSEYCDELKARGLTEKFREKTGLVIDAYFSATKLKWILDNVPGVRARAERGDLLFG 164
Cdd:TIGR01311 81 ETTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYGEFIREKTGLPLDPYFSATKLRWLLDNVPGVREAAERGELLFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 165 TVETWLIWKLTCGKIHVTDYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPKPVPNSEFYEYADPMHFGGEIKIAGAAG 244
Cdd:TIGR01311 161 TIDTWLIWNLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYTDPGLLGAEIPITGVLG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 245 DQQAALFGQTCFTKGEAKSTFGTGGFLLMNTGEKPVFSHNGLVTTVAWGLDGKVN-YALEGSIFVAGAAIQWLRDELHLL 323
Cdd:TIGR01311 241 DQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKKPvYALEGSVFVAGAAVQWLRDNLKLI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 324 EDARDSEYMAQKVKDTNGCYVVPAFTGLGAPHWDQYARGAIVGLTRGVNKNHIIRATLDSLCYQINDVLTAMQADAGIPL 403
Cdd:TIGR01311 321 KHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTRDVLEAMEKDAGVEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 404 TALKVDGGACANNYLMQTMADISARPVKRPCCVETTALGAAYLAGLAVGYWQSTDDVLKNWSVDREFVPALTEAERTRRI 483
Cdd:TIGR01311 401 TKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWRVEKTFEPEMDEEEREARY 480
|
490
....*....|...
gi 2050539736 484 QGWNKAVRCSYGW 496
Cdd:TIGR01311 481 AGWKEAVKRSLGW 493
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
5-490 |
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: 678.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 5 KYIMALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPKPGWVEHDANEIWTTQ---LGVALSAMNQIGASAEDIAAIGIT 81
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVyecIEEAVEKLKALGISPSDIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 82 NQRETTIVWDRDTGEPVCHAIVWQCRRTSEYCDELKAR--GLTEKFREKTGLVIDAYFSATKLKWILDNVPGVRARAERG 159
Cdd:cd07792 81 NQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELSAKtpGGKDHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 160 DLLFGTVETWLIWKLTCGK---IHVTDYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPKPVPNSEFYEYADPMHFGGe 236
Cdd:cd07792 161 RLLFGTVDSWLIWNLTGGKnggVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIASGPLAG- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 237 IKIAGAAGDQQAALFGQTCFTKGEAKSTFGTGGFLLMNTGEKPVFSHNGLVTTVAW--GLDGKVNYALEGSIFVAGAAIQ 314
Cdd:cd07792 240 VPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAYklGPDAPPVYALEGSIAIAGAAVQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 315 WLRDELHLLEDARDSEYMAQKVKDTNGCYVVPAFTGLGAPHWDQYARGAIVGLTRGVNKNHIIRATLDSLCYQINDVLTA 394
Cdd:cd07792 320 WLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREILDA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 395 MQADAGIPLTALKVDGGACANNYLMQTMADISARPVKRPCCVETTALGAAYLAGLAVGYWQSTDDVLK-NWSVDREFVPA 473
Cdd:cd07792 400 MNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSlNEGGRTVFEPQ 479
|
490
....*....|....*..
gi 2050539736 474 LTEAERTRRIQGWNKAV 490
Cdd:cd07792 480 ISEEERERRYKRWKKAV 496
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
6-500 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 610.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 6 YIMALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPKPGWVEHDANEIWTTQLGVALSAMNQIGASAED----IAAIGIT 81
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGHNvdsgLKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 82 NQRETTIVWDRDTGEPVCHAIVWQCRRTSEYCDEL--KARGLTEKFREKTGLVIDAYFSATKLKWILDNVPGVRARAERG 159
Cdd:PLN02295 81 NQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLekELSGGRKHFVETCGLPISTYFSATKLLWLLENVDAVKEAVKSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 160 DLLFGTVETWLIWKLTCGK---IHVTDYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPKPVPNSEFYEYADPMHFGGE 236
Cdd:PLN02295 161 DALFGTIDSWLIWNLTGGAsggVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIAKGWPLAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 237 IKIAGAAGDQQAALFGQTCfTKGEAKSTFGTGGFLLMNTGEKPVFSHNGLVTTVAW--GLDGKVNYALEGSIFVAGAAIQ 314
Cdd:PLN02295 241 VPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYklGPDAPTNYALEGSVAIAGAAVQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 315 WLRDELHLLEDARDSEYMAQKVKDTNGCYVVPAFTGLGAPHWDQYARGAIVGLTRGVNKNHIIRATLDSLCYQINDVLTA 394
Cdd:PLN02295 320 WLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQVKDVLDA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 395 MQADAGIP-----LTALKVDGGACANNYLMQTMADISARPVKRPCCVETTALGAAYLAGLAVGYWqSTDDVLKN--WSVD 467
Cdd:PLN02295 400 MRKDAGEEkshkgLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLW-TEEEIFASekWKNT 478
|
490 500 510
....*....|....*....|....*....|...
gi 2050539736 468 REFVPALTEAERTRRIQGWNKAVRCSYGWAKED 500
Cdd:PLN02295 479 TTFRPKLDEEERAKRYASWCKAVERSFDLADLS 511
|
|
| 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: 602.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 4 QKYIMALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPKPGWVEHDANEIWT---TQLGVALSAMNQIGASAeDIAAIGI 80
Cdd:PTZ00294 1 MKYIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRnvyKCMNEAIKKLREKGPSF-KIKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 81 TNQRETTIVWDRDTGEPVCHAIVWQCRRTSEYCDEL-KARGLTEKFREKTGLVIDAYFSATKLKWILDNVPGVRARAERG 159
Cdd:PTZ00294 80 TNQRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELtKKYGGSNFFQKITGLPISTYFSAFKIRWMLENVPAVKDAVKEG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 160 DLLFGTVETWLIWKLTCGKIHVTDYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPKPVPNSEFYEYADPMHFGG--EI 237
Cdd:PTZ00294 160 TLLFGTIDTWLIWNLTGGKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTISGEAVPLleGV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 238 KIAGAAGDQQAALFGQTCFTKGEAKSTFGTGGFLLMNTGEKPVFSHNGLVTTVAW--GLDGKVNYALEGSIFVAGAAIQW 315
Cdd:PTZ00294 240 PITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYqlGPNGPTVYALEGSIAVAGAGVEW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 316 LRDELHLLEDARDSEYMAQKVKDTNGCYVVPAFTGLGAPHWDQYARGAIVGLTRGVNKNHIIRATLDSLCYQINDVLTAM 395
Cdd:PTZ00294 320 LRDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDVIESM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 396 QADAGIPLTALKVDGGACANNYLMQTMADISARPVKRPCCVETTALGAAYLAGLAVGYWQSTDDV--LKNWSvDREFVPA 473
Cdd:PTZ00294 400 EKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVkkLIRRS-NSTFSPQ 478
|
490 500
....*....|....*....|....*.
gi 2050539736 474 LTEAERTRRIQGWNKAVRCSYGWAKE 499
Cdd:PTZ00294 479 MSAEERKAIYKEWNKAVERSLKWAKL 504
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
6-491 |
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: 535.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 6 YIMALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPKPGWVEHDANEIWTTQLGVALSAMNQIGASAEDIAAIGITNQRE 85
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 86 TTIVWDRDTGEPVCHAIVWQCRRTSEYCDE------LKA-RG-------LTEKFREKTGLVIDayFSAT----KLKWILD 147
Cdd:cd07793 81 TFLTWDKKTGKPLHNFITWQDLRAAELCESwnrsllLKAlRGgskflhfLTRNKRFLAASVLK--FSTAhvsiRLLWILQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 148 NVPGVRARAERGDLLFGTVETWLIWKLTCGKIHVTDYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPKPVPNSEFYEY 227
Cdd:cd07793 159 NNPELKEAAEKGELLFGTIDTWLLWKLTGGKVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 228 ADPMHFGGEIKIAGAAGDQQAALFGQTCFTKGEAKSTFGTGGFLLMNTGEKPVFSHNGLVTTVAWGLDGKVNYALEGSIF 307
Cdd:cd07793 239 TDPSIFGAEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGGEITYLAEGNAS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 308 VAGAAIQWLRDELhLLEDARDSEYMAQKVKDTNGCYVVPAFTGLGAPHWDQYARGAIVGLTRGVNKNHIIRATLDSLCYQ 387
Cdd:cd07793 319 DTGTVIDWAKSIG-LFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIAFR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 388 INDVLTAMQADAGIPLTALKVDGGACANNYLMQTMADISARPVKRPCCVETTALGAAYLAGLAVGYWQSTDDVLKNWSVD 467
Cdd:cd07793 398 VKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEELKKLRKIE 477
|
490 500
....*....|....*....|....
gi 2050539736 468 REFVPALTEAERTRRIQGWNKAVR 491
Cdd:cd07793 478 KIFEPKMDNEKREELYKNWKKAVK 501
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
5-483 |
2.07e-104 |
|
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: 321.01 E-value: 2.07e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 5 KYIMALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPKPGWVEHDANEIWTTQLGVALSAMNQIGASAEDIAAIGITNQR 84
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 85 ETTIVWDRDtGEPVCHAIVWQCRRTSEYCDELKARGLTEKFREKTGLVIDAYFSATKLKWILDNVPGVRARAERgdllFG 164
Cdd:COG1070 81 HGLVLLDAD-GEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAK----VL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 165 TVETWLIWKLTcGKIhVTDYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPKPVPNSEFY-----EYADPMHFGGEIKI 239
Cdd:COG1070 156 LPKDYLRYRLT-GEF-VTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAgtltaEAAAETGLPAGTPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 240 AGAAGDQQAALFGQTCFTKGEAKSTFGTGGFLLMNTgEKPVFSHNGLVTTVAWGLDGKvnYALEGSIFVAGAAIQWLRDE 319
Cdd:COG1070 234 VAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVS-DKPLPDPEGRVHTFCHAVPGR--WLPMGATNNGGSALRWFRDL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 320 LhLLEDARDSEYMAQKVKDT----NGCYVVPAFTGLGAPHWDQYARGAIVGLTRGVNKNHIIRATLDSLCYQINDVLTAM 395
Cdd:COG1070 311 F-ADGELDDYEELNALAAEVppgaDGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEAL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 396 QAdAGIPLTALKVDGGACANNYLMQTMADISARPVKRPCCVETTALGAAYLAGLAVGYWQSTDDVLKNW-SVDREFVPAL 474
Cdd:COG1070 390 EE-AGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMvRVGETIEPDP 468
|
....*....
gi 2050539736 475 TEAERTRRI 483
Cdd:COG1070 469 ENVAAYDEL 477
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
6-472 |
4.67e-98 |
|
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: 302.52 E-value: 4.67e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 6 YIMALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPKPGWVEHDANEIWTTQLGVALSAMNQIGASAEDIAAIGITNQRE 85
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 86 TTIVWDRDtGEPVCHAIVWQCRRTSEYCdelkargltekfrektglvidayfsatklkwildnvpgvraraergdllfgT 165
Cdd:cd07779 81 TFVPVDED-GRPLRPAISWQDKRTAKFL---------------------------------------------------T 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 166 VETWLIWKLTCGkiHVTDYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPKPVPNSEFY-----EYADPMHFGGEIKIA 240
Cdd:cd07779 109 VQDYLLYRLTGE--FVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIgtltkEAAEETGLPEGTPVV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 241 GAAGDQQAALFGQTCFTKGEAKSTFGTGGFLLMNTgEKPVFSHNGLVTTVAWGLDGKvnYALEGSIFVAGAAIQWLRDEL 320
Cdd:cd07779 187 AGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVS-DKPVEDPERRIPCNPSAVPGK--WVLEGSINTGGSAVRWFRDEF 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 321 HLLEDARD----SEY-----MAQKVK-DTNGCYVVPAFTGLGAPHWDQYARGAIVGLTRGVNKNHIIRATLDSLCYQIND 390
Cdd:cd07779 264 GQDEVAEKelgvSPYellneEAAKSPpGSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELRD 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 391 VLTAMQaDAGIPLTALKVDGGACANNYLMQTMADISARPVKRPCCVETTALGAAYLAGLAVGYWQSTDDVLKNWS-VDRE 469
Cdd:cd07779 344 NLEAME-KAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAMVrVTDT 422
|
...
gi 2050539736 470 FVP 472
Cdd:cd07779 423 FEP 425
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
6-235 |
9.55e-93 |
|
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: 282.30 E-value: 9.55e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 6 YIMALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPKPGWVEHDANEIWTTQLGVALSAMNQIGASAEDIAAIGITNQRE 85
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 86 TTIVWDRDTgEPVCHAIVWQCRRTSEYCDELKARGLTEKFREKTGLVIDAYFSATKLKWILDNVPGVRARAErgdlLFGT 165
Cdd:pfam00370 81 GTVLLDKND-KPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIH----KFLT 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 166 VETWLIWKLTcGKiHVTDYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPKPVPNSEFYEYADPMHFGG 235
Cdd:pfam00370 156 IHDYLRWRLT-GV-FVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAM 223
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
6-452 |
3.34e-92 |
|
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: 287.56 E-value: 3.34e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 6 YIMALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPKPGWVEHDANEIWTTqlgvALSAMNQI--GASAEDIAAIGITNQ 83
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEA----VKEAIREAaaQAGPDPIAAISVSSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 84 RETTIVWDRDtGEPVCHAIVWQCRRTSEYCDELKARGLTEKFREKTGLVIDAYFSATKLKWILDNVPGVRARAERgdllF 163
Cdd:cd07773 77 GESGVPVDRD-GEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAK----W 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 164 GTVETWLIWKLTcGKiHVTDYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPKPVPNSEF-----YEYADPMHFGGEIK 238
Cdd:cd07773 152 LSVADYIAYRLT-GE-PVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVigtvtPEAAEELGLPAGTP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 239 IAGaagdqqaalfG---QTC-------FTKGEAKSTFGTGGFLLMNTGEKPVF-SHNGLVTTVAWGLDGKVnYALEGSIf 307
Cdd:cd07773 230 VVV----------GghdHLCaalgagvIEPGDVLDSTGTAEALLAVVDEPPLDeMLAEGGLSYGHHVPGGY-YYLAGSL- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 308 VAGAAIQWLRDEL-HLLEDARDSEYMAQKVKDT-NGCYVVPAFTGLGAPHWDQYARGAIVGLTRGVNKNHIIRATLDSLC 385
Cdd:cd07773 298 PGGALLEWFRDLFgGDESDLAAADELAEAAPPGpTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLA 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050539736 386 YQINDVLTAMQAdAGIPLTALKVDGGACANNYLMQTMADISARPVKRPCCVETTALGAAYLAGLAVG 452
Cdd:cd07773 378 FELRLNLEALEK-AGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
6-447 |
1.47e-87 |
|
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: 274.06 E-value: 1.47e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 6 YIMALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPKPGWVEHDANEIWTTQLGVALSAMNQIGASAEDIAAIGITNQRE 85
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 86 TTIVWDRDtGEPVCHAIVWQCRRTSeycdelkargltekfrektglvidayfsatklkwildnvpgvraraergdllFGT 165
Cdd:cd00366 81 GVVLVDAD-GNPLRPAIIWLDRRAK----------------------------------------------------FLQ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 166 VETWLIWKLTcGKIhVTDYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPKPVPNSEFY-----EYADPMHFGGEIKIA 240
Cdd:cd00366 108 PNDYIVFRLT-GEF-AIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVgrvtpEAAEETGLPAGTPVV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 241 GAAGDQQAALFGQTCFTKGEAKSTFGTGGFLLMNTGEKPVFSHNGLVTTVAwgLDGKvnYALEGSIFVAGAAIQWLRDEL 320
Cdd:cd00366 186 AGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVPPDPRLLNRCHV--VPGL--WLLEGAINTGGASLRWFRDEF 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 321 HLLEDARDSEY----MAQKVKD-TNGCYVVPAFTGLGAPHWDQYARGAIVGLTRGVNKNHIIRATLDSLCYQINDVLTAM 395
Cdd:cd00366 262 GEEEDSDAEYEgldeLAAEVPPgSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEIL 341
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2050539736 396 QaDAGIPLTALKVDGGACANNYLMQTMADISARPVKRPCCVETTALGAAYLA 447
Cdd:cd00366 342 E-ELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
6-483 |
8.72e-77 |
|
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: 248.62 E-value: 8.72e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 6 YIMALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPKPGWVEHDANEIWTTQLGVALSAMNQIGASaeDIAAIGITNQRE 85
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGG--EVDAIGFSSAMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 86 TTIVWDRDtGEPVCHAIVWQCRRTSEYCDELKARGLTEKFREKTGLVIDAYFSATKLKWILDNVPGVRARAERgdllFGT 165
Cdd:cd07770 79 SLLGVDED-GEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAAK----FVS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 166 VETWLIWKLTcGKiHVTDYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPKPVPNSEFY-----EYADPMHFGGEIKia 240
Cdd:cd07770 154 IKEYLLYRLT-GE-LVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLpglkpEFAERLGLLAGTP-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 241 gaagdqqaaLF-----------GQTCFTKGEAKSTFGTGGFLLMNTgEKPVFSHNGLVttvaWgldgkvNYALEGSIFVA 309
Cdd:cd07770 230 ---------VVlgasdgalanlGSGALDPGRAALTVGTSGAIRVVS-DRPVLDPPGRL----W------CYRLDENRWLV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 310 GAAI-------QWLRDELHLLEDARD--SEYMAQKVKDTNGCYVVPAFTGLGAPHWDQYARGAIVGLTRGVNKNHIIRAT 380
Cdd:cd07770 290 GGAInnggnvlDWLRDTLLLSGDDYEelDKLAEAVPPGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 381 LDSLCYQINDVLTAMQaDAGIPLTALKVDGGACANNYLMQTMADISARPVKRPCCVETTALGAAYLAGLAVGYWQStDDV 460
Cdd:cd07770 370 LEGVAFNLKSIYEALE-ELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISS-LEA 447
|
490 500
....*....|....*....|...
gi 2050539736 461 LKNWSVDREFVPALTEAERTRRI 483
Cdd:cd07770 448 DELVKIGKVVEPDPENHAIYAEL 470
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
6-472 |
1.04e-74 |
|
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: 243.58 E-value: 1.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 6 YIMALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPKPGWVEHDANEIW-----TTQlgvalSAMNQIGASAEDIAAIGI 80
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWdavcrATR-----ALLEKSGIDPSDIAAIAF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 81 TNQRETTIVWDRDtGEPVCHAIVWQCRRTSEYCDELKARGLTEKFREKTGLV-IDAYFSATKLKWILDNVPGVRARAerg 159
Cdd:cd07805 76 SGQMQGVVPVDKD-GNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLGGGNpPSGKDPLAKILWLKENEPEIYAKT--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 160 DLLFGTVEtWLIWKLTcGKIhVTDYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPKPVPNSEFY-----EYADPMHFG 234
Cdd:cd07805 152 HKFLDAKD-YLNFRLT-GRA-ATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVgeltpEAAAELGLP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 235 GEIKIAGAAGDQQAALFGQTCFTKGEAKSTFGTGGFLLMNTgEKPVFSHNGLVTTVAWGLDGKVNYAleGSIFVAGAAIQ 314
Cdd:cd07805 229 AGTPVVGGGGDAAAAALGAGAVEEGDAHIYLGTSGWVAAHV-PKPKTDPDHGIFTLASADPGRYLLA--AEQETAGGALE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 315 WLRDELHLLEDARDSEY-----MAQKVK-DTNGCYVVPAFTGLGAPHWDQYARGAIVGLTRGVNKNHIIRATLDSLCYQI 388
Cdd:cd07805 306 WARDNLGGDEDLGADDYelldeLAAEAPpGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 389 NDVLTAMQADAGiPLTALKVDGGACANNYLMQTMADISARPVKR---PccVETTALGAAYLAGLAVGYWQSTDDVLKNWS 465
Cdd:cd07805 386 RWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVpenP--QEAGALGAALLAAVGLGLLKSFDEAKALVK 462
|
....*..
gi 2050539736 466 VDREFVP 472
Cdd:cd07805 463 VEKVFEP 469
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
6-484 |
3.70e-73 |
|
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: 239.36 E-value: 3.70e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 6 YIMALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPKPGWVEHDANEIWTTQLGVALSAMNQIGASAEDIAAIGITNQRE 85
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 86 TTIVWDRDtGEPVCHAIVWQCRRTSEYCDELKARgLTEKFREKTGLVIDAYFSATKLKWILDNVPGVRARAERgdLLFgt 165
Cdd:cd07808 81 GLVLLDKN-GRPLRPAILWNDQRSAAECEELEAR-LGDEILIITGNPPLPGFTLPKLLWLKENEPEIFARIRK--ILL-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 166 VETWLIWKLTcGKIHvTDYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPKPVPNSEFY-----EYADpmHFG--GEIK 238
Cdd:cd07808 155 PKDYLRYRLT-GELA-TDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVgtltpEAAE--ELGlpEGTP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 239 IAGAAGDQQAALFGQTCFTKGEAKSTFGTGGFLLMNTgEKPVFSHNGLVTTVAWGLDGKvNYALeGSIFVAGAAIQWLRD 318
Cdd:cd07808 231 VVAGAGDNAAAALGAGVVEPGDALISLGTSGVVFAPT-DKPVPDPKGRLHTFPHAVPGK-WYAM-GVTLSAGLSLRWLRD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 319 EL-HLLEDARDSEYMAQKVKD-TNGCYVVPAFTGLGAPHWDQYARGAIVGLTRGVNKNHIIRATLDSLCYQINDVLTAMQ 396
Cdd:cd07808 308 LFgPDRESFDELDAEAAKVPPgSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVLK 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 397 aDAGIPLTALKVDGGACANNYLMQTMADISARPVKRPCCVETTALGAAYLAGLAVGYWQSTDDVLKNWS-VDREFVPalt 475
Cdd:cd07808 388 -ELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACIkIEKTIEP--- 463
|
....*....
gi 2050539736 476 EAERTRRIQ 484
Cdd:cd07808 464 DPERHEAYD 472
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
6-452 |
1.31e-67 |
|
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: 223.94 E-value: 1.31e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 6 YIMALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPKPGWVEHDANEIWTTQLGVALSAMNQIGASAEDIAAIGITNQRE 85
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 86 TTIVWDRDtGEPVCHAIVWQCRRTSEYCDELKARGLTEKFREKTGLVIDAYFSATKLKWILDNVPGVRARAERgdllFGT 165
Cdd:cd07804 81 ALVPVDEN-GKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRK----FLG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 166 VETWLIWKLTcGKIhVTDYSNASRTM-LFNIHTLDWDDEILQILDIPRCMLPKPVPNSEFYEYADP-------MHFGgeI 237
Cdd:cd07804 156 AYDYIVYKLT-GEY-VIDYSSAGNEGgLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKeaaeetgLAEG--T 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 238 KIAGAAGDQQAALFGQTCFTKGEAKSTFGTGGFLLMNTGEKPVFSHNGLVTTVAWGLdgkvnYALEGSIFVAGAAIQWLR 317
Cdd:cd07804 232 PVVAGTVDAAASALSAGVVEPGDLLLMLGTAGDIGVVTDKLPTDPRLWLDYHDIPGT-----YVLNGGMATSGSLLRWFR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 318 DEL--HLLEDAR-----DSEYMAQKVKDT----NGCYVVPAFTGLGAPHWDQYARGAIVGLTRGVNKNHIIRATLDSLCY 386
Cdd:cd07804 307 DEFagEEVEAEKsggdsAYDLLDEEAEKIppgsDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAY 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050539736 387 QINDVLTAMqADAGIPLTALKVDGGACANNYLMQTMADISARPVKRPCCVETTALGAAYLAGLAVG 452
Cdd:cd07804 387 GLRHHLEVI-REAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
6-452 |
2.12e-51 |
|
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466805 [Multi-domain] Cd Length: 444 Bit Score: 180.82 E-value: 2.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 6 YIMALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPKPGWVEHDANEIWTTQLGVALSAMNQIGASAEDIAAIGITNQRE 85
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 86 TTIVWDRDtGEPVCHAIVWQCRRTSEYCDELKARGLTEKFREKTGLVIDAYFSATKLKWILDNVPGVRARAerGDLLFgt 165
Cdd:cd07802 81 GLYLVDKD-GKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRI--RTVLF-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 166 VETWLIWKLTcGKIHvTDYSNASrTMLFNIHTLDWDDEILQILDIPRCM--LPKPVPNSEfyeyadpmhFGGEIkiagaa 243
Cdd:cd07802 156 CKDWIRYRLT-GEIS-TDYTDAG-SSLLDLDTGEYDDELLDLLGIEELKdkLPPLVPSTE---------IAGRV------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 244 gdqqaalfgqtcfTKGEAKST-------------------FGTG----GFLLMNTG---------EKPVFSHNGLVtTVA 291
Cdd:cd07802 218 -------------TAEAAALTglpegtpvaagafdvvasaLGAGavdeGQLCVILGtwsinevvtDEPVVPDSVGS-NSL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 292 WGLDGKVnYALEGSifVAGAA-IQWLRDELHLLEDARDS-------EYMAQKVKDTNGCYVVPAFTGLGAphwDQYARGA 363
Cdd:cd07802 284 HADPGLY-LIVEAS--PTSASnLDWFLDTLLGEEKEAGGsdydeldELIAAVPPGSSGVIFLPYLYGSGA---NPNARGG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 364 IVGLTRGVNKNHIIRATLDSLCYQINDVLTAMqaDAGIPLTALKVDGGACANNYLMQTMADISARPVKRPCCVETTALGA 443
Cdd:cd07802 358 FFGLTAWHTRAHLLRAVYEGIAFSHRDHLERL--LVARKPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGA 435
|
....*....
gi 2050539736 444 AYLAGLAVG 452
Cdd:cd07802 436 AICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
6-452 |
2.27e-49 |
|
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: 175.49 E-value: 2.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 6 YIMALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPK--PGWVEHDANEIWTTQLGVALSAMNQIGASAEDIAAIGITNQ 83
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDdyPDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 84 RETTIVWDRDtGEPVC-------HAIVWQcrrtSEYCDELKargltEKFREKTGLVIDAYFSATKLKWILDNVPGVRARA 156
Cdd:cd07798 81 REGIVFLDKD-GRELYagpnidaRGVEEA----AEIDDEFG-----EEIYTTTGHWPTELFPAARLLWFKENRPEIFERI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 157 ERgdllFGTVETWLIWKLtCGKIhVTDYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPKPVPNSEFY-----EYADPM 231
Cdd:cd07798 151 AT----VLSISDWIGYRL-TGEL-VSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLgtvseEAAREL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 232 HFGGEIKIAGAAGDQQAALFGQTCFTKGEAKSTFGTGGFLLMNTgEKPVFSHNGLVTTVAWGLDGKvnYALEGSIFVAGA 311
Cdd:cd07798 225 GLPEGTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVT-DEPIIDPERRLWTGCHLVPGK--WVLESNAGVTGL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 312 AIQWLRDelHLLEDARDS-----EYMAQKVKDTNGCYvvpAFTGLGAPhwDQYARGAIVGL--------TRGVNKNHIIR 378
Cdd:cd07798 302 NYQWLKE--LLYGDPEDSyevleEEASEIPPGANGVL---AFLGPQIF--DARLSGLKNGGflfptplsASELTRGDFAR 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050539736 379 ATLDSLCYQINDVLTAMQADAGIPLTALKVDGGACANNYLMQTMADISARPVKRPCCVETTALGAAYLAGLAVG 452
Cdd:cd07798 375 AILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
6-451 |
1.30e-48 |
|
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466801 [Multi-domain] Cd Length: 429 Bit Score: 173.18 E-value: 1.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 6 YIMALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPKPGWVEHDANEIWTTqlgvALSAMNQIGASA--EDIAAIGITNQ 83
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEA----LRSLLRELPAELrpRRVVAIAVDGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 84 RETTIVWDRDtGEPVCHAIVWQCRRTSEYCDELKARGltEKFREKTGLVIDAYFSATKLKWILDNVPGVRARAERgdLLF 163
Cdd:cd07783 77 SGTLVLVDRE-GEPLRPAIMYNDARAVAEAEELAEAA--GAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAK--FLH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 164 GTveTWLIWKLTcGKIHVTDYSNASRTmLFNIHTLDWDDEILQILDIPRCMLPKPVPNSEFY-----EYADPMHFGGEIK 238
Cdd:cd07783 152 QA--DWLAGRLT-GDRGVTDYNNALKL-GYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIgtltaEAAEELGLPAGTP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 239 IAGAAGDQQAALFGQTCFTKGEAKSTFGTGgfL-LMNTGEKPVFSHNGLVTTVAWGLDGkvnYALEGSIFVAGAAIQWL- 316
Cdd:cd07783 228 VVAGTTDSIAAFLASGAVRPGDAVTSLGTT--LvLKLLSDKRVPDPGGGVYSHRHGDGY---WLVGGASNTGGAVLRWFf 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 317 -RDELHLLEDARDSEYMaqkvkdtNGCYVVP-AFTGLGAPHWDQYARGAIvgLTRGVNKNHIIRATLDSLCYQINDVLTA 394
Cdd:cd07783 303 sDDELAELSAQADPPGP-------SGLIYYPlPLRGERFPFWDPDARGFL--LPRPHDRAEFLRALLEGIAFIERLGYER 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2050539736 395 MQADAGIPLTALKVDGGACANNYLMQTMADISARPVKRPCCvETTALGAAYLAGLAV 451
Cdd:cd07783 374 LEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEE-EEAALGAALLAAAGL 429
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
261-450 |
2.16e-45 |
|
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.
Pssm-ID: 426979 [Multi-domain] Cd Length: 197 Bit Score: 157.49 E-value: 2.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 261 AKSTFGTGGFLLMnTGEKPVFSHNGLVTTVAwGLDGKVNYALEGSIFVAGAAIQWLRDELHLLEDARDS---EYMAQKVK 337
Cdd:pfam02782 1 LAISAGTSSFVLV-ETPEPVLSVHGVWGPYT-NEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRDAgnvESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 338 -----DTNGCYVVPAFTGLGAPHWDQYARGAIVGLTRGVNKNHIIRATLDSLCYQINDVLTAMQADAGIPLTALKVDGGA 412
Cdd:pfam02782 79 laavaPAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSGGG 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 2050539736 413 CANNYLMQTMADISARPVKRPCCVETTALGAAYLAGLA 450
Cdd:pfam02782 159 SRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
6-452 |
3.27e-43 |
|
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: 158.94 E-value: 3.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 6 YIMALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPKPGWVEHDANEIWTTQLGVALSAMNQIGASAEDIAAIGITNQRE 85
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 86 TTIVWDRDtGEPVCHAIVWQCRRTSEYCDELKARGLTEKFREKTGLVIDAYFSATKLKWILDNVPGVRARAERgdLLFgt 165
Cdd:cd24121 81 GTWLVDED-GRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKENEPERLERART--ALH-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 166 VETWLIWKLTcGKIhVTDYSNASRTMlFNIHTLDWDDEILQILDIP--RCMLPKPVPNSEFY-----EYADPMHFGGEIK 238
Cdd:cd24121 156 CKDWLFYKLT-GEI-ATDPSDASLTF-LDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIgpltpEAAAATGLPAGTP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 239 IAGAAGDQQAALFGQTCFTKGEAKSTFGTGGFLLMNTGEkPVFSHNGLVTTVAWGLDGKVNYALegSIFVAGAAIQWLRD 318
Cdd:cd24121 233 VVLGPFDVVATALGSGAIEPGDACSILGTTGVHEVVVDE-PDLEPEGVGYTICLGVPGRWLRAM--ANMAGTPNLDWFLR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 319 EL-------HLLEDARDSEYMAQKVKD----TNGCYVVP--AFTGLGAPHWDQYARGAIVGLTRGVNKNHIIRATLDSLC 385
Cdd:cd24121 310 ELgevlkegAEPAGSDLFQDLEELAASsppgAEGVLYHPylSPAGERAPFVNPNARAQFTGLSLEHTRADLLRAVYEGVA 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050539736 386 YQINDVLTAMqadaGIPLTALKVDGGACANNYLMQTMADISARPVKRPCCVETTALGAAYLAGLAVG 452
Cdd:cd24121 390 LAMRDCYEHM----GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
6-472 |
9.19e-41 |
|
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: 152.87 E-value: 9.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 6 YIMALDAGTTSNRCILFNARGEMCSVAQKEFTQY-FPK-PGWVEHDANEIWTTQLGVALSAMNQIGASAEDIAAIGITNQ 83
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREWRHKeVPDvPGSMDFDTEKNWKLICECIREALKKAGIAPKSIAAISTTSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 84 RETTIVWDRDtGEPVchaivWQCR----RTSEYCDELKAR--GLTEKFREKTG--LVIDAyfsATKLKWILDNVPGVRAR 155
Cdd:cd07775 81 REGIVLYDNE-GEEI-----WACAnvdaRAAEEVSELKELynTLEEEVYRISGqtFALGA---IPRLLWLKNNRPEIYRK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 156 AERgdllFGTVETWLIWKLTcGKIhVTDYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPKPVPNSEFY-----EYADP 230
Cdd:cd07775 152 AAK----ITMLSDWIAYKLS-GEL-AVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIgkvtkEAAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 231 MHFGGEIKIAGAAGDQQAALFGQTCFTKGEAKSTFGTGGFLLMNTGEkPVFSHNGLVTTVAWGLDGKVNYalEGSIFVAG 310
Cdd:cd07775 226 TGLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAA-PVTDPAMNIRVNCHVIPDMWQA--EGISFFPG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 311 AAIQWLRD----ELHLLEDA---RDSEYMAQKVKDTN-GCY-VVPAFTGL-GAPHWdQYARGAIVGLT---RGVNKNHII 377
Cdd:cd07775 303 LVMRWFRDafcaEEKEIAERlgiDAYDLLEEMAKDVPpGSYgIMPIFSDVmNYKNW-RHAAPSFLNLDidpEKCNKATFF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 378 RATLDSLCYQINDVLTAMQADAGIPLTALKVDGGACANNYLMQTMADISARPVKRPCCVETTALGAAYLAGLAVGYWQST 457
Cdd:cd07775 382 RAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAGIYSSL 461
|
490
....*....|....*.
gi 2050539736 458 DDVLKNWS-VDREFVP 472
Cdd:cd07775 462 EEAVESLVkWEREYLP 477
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
6-452 |
1.03e-40 |
|
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: 151.93 E-value: 1.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 6 YIMALDAGTTSNRCILFNA-RGEMCSVAQKEFTQYFPKPGWVEHDANEIWTtQLGVALS-AMNQIGASAEDIAAIGITNQ 83
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDAeTGRVVASGSAPHENILIDPGWAEQDPEDWWD-ALQAAFAqLLKDAGAELRDVAAIGISGQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 84 RETTIVWDRDtGEPVCHAIVWQCRRTSEYCDELKARgLTEKFREKTGLVIDAYFSATKLKWILDNVPGVRARAERGDLLF 163
Cdd:cd07809 80 MHGLVALDAD-GKVLRPAKLWCDTRTAPEAEELTEA-LGGKKCLLVGLNIPARFTASKLLWLKENEPEHYARIAKILLPH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 164 GtvetWLIWKLTCGKihVTDYSNASRTMLFNIHTLDWDDEILQILD---IPRCMLPKPVPNSEFY-----EYADPMHFGG 235
Cdd:cd07809 158 D----YLNWKLTGEK--VTGLGDASGTFPIDPRTRDYDAELLAAIDpsrDLRDLLPEVLPAGEVAgrltpEGAEELGLPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 236 EIKIAGAAGDQQAALFGQTCFTKGEAKSTFGTGGFLlMNTGEKPVFSHNGLVTTVAwgldgKVNYALEGSIFVAGAAIQW 315
Cdd:cd07809 232 GIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTSGTA-YGVSDKPVSDPHGRVATFC-----DSTGGMLPLINTTNCLTAW 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 316 LRDELHLLE-DARDSEYMAQKVK-DTNGCYVVPAFTGLGAPHWDQyARGAIVGLTRGV-NKNHIIRATLDSLCYQINDVL 392
Cdd:cd07809 306 TELFRELLGvSYEELDELAAQAPpGAGGLLLLPFLNGERTPNLPH-GRASLVGLTLSNfTRANLARAALEGATFGLRYGL 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 393 TAMQaDAGIPLTALKVDGGACANNYLMQTMADISARPVKRPCCVETTALGAAYLAGLAVG 452
Cdd:cd07809 385 DILR-ELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
6-472 |
2.92e-31 |
|
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: 126.11 E-value: 2.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 6 YIMALDAGTTSNRCILFNAR-GEMCSVAQKEFTQYF--PKPGWVEHDANEIWTTqLGVAL-SAMNQIGASAEDIAAIGIT 81
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDLAdGEELASAVVPYPTGYipPRPGWAEQNPADYWEA-LEEAVrGALAEAGVDPEDVVGIGVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 82 NQRETTIVWDRDtGEPVCHAIVWQCRRTSEYCDEL--KARGLTEKFREKTGLVIDA--YFSatKLKWILDNVPGVRARA- 156
Cdd:cd07781 80 TTSSTVVPVDED-GNPLAPAILWMDHRAQEEAAEIneTAHPALEYYLAYYGGVYSSewMWP--KALWLKRNAPEVYDAAy 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 157 ---ERGDllfgtvetWLIWKLTcGKIhVTDYSNASRTMLFNIHTLDWDDEILQILD-----IPRCMLPKPVPNSEFY--- 225
Cdd:cd07781 157 tivEACD--------WINARLT-GRW-VRSRCAAGHKWMYNEWGGGPPREFLAALDpgllkLREKLPGEVVPVGEPAgtl 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 226 --EYADpmHFG--GEIKIAGAAGDQQAALFGQTCFTKGEAKSTFGTGGFLLMNTgEKPVFSHnGLvttvaWG-LDGKVN- 299
Cdd:cd07781 227 taEAAE--RLGlpAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTCHLMVS-PKPVDIP-GI-----CGpVPDAVVp 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 300 --YALEGSIFVAGAAIQWLRDELHLLEDARDS---EYMAQKVKD----TNGCYVVPAFTGLGAPHWDQYARGAIVGLTRG 370
Cdd:cd07781 298 glYGLEAGQSAVGDIFAWFVRLFVPPAEERGDsiyALLSEEAAKlppgESGLVALDWFNGNRTPLVDPRLRGAIVGLTLG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 371 VNKNHIIRATLDSLCYQINDVLTAMQaDAGIPLTALKVDGGACANN-YLMQTMADISARPVKRPCCVETTALGAAYLAGL 449
Cdd:cd07781 378 TTPAHIYRALLEATAFGTRAIIERFE-EAGVPVNRVVACGGIAEKNpLWMQIYADVLGRPIKVPKSDQAPALGAAILAAV 456
|
490 500
....*....|....*....|....
gi 2050539736 450 AVGYWQSTDDVLKNW-SVDREFVP 472
Cdd:cd07781 457 AAGVYADIEEAADAMvRVDRVYEP 480
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
6-447 |
9.43e-25 |
|
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: 106.54 E-value: 9.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 6 YIMALDAGTTSNRCILFN-ARGEMCSVAQKEFTQYFPK--PGWVEHDANEIWTTqlgvALSAMNQIGASA-EDIAAIGIT 81
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDlESGRILESVSRPTPAPISSddPGRSEQDPEKILEA----VRNLIDELPREYlSDVTGIGIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 82 NQRETTIVWDRDtGEPVCHAIVWQCRRTSE-YCDELKARGltEKFREKTGLVIDAYFSATKLKWILDNVPgVRARAERgd 160
Cdd:cd07777 77 GQMHGIVLWDED-GNPVSPLITWQDQRCSEeFLGGLSTYG--EELLPKSGMRLKPGYGLATLFWLLRNGP-LPSKADR-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 161 llFGTVETWLIWKLTCGKIHVTDYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPKPVPnsefyeyadPMHFGGEIKIA 240
Cdd:cd07777 151 --AGTIGDYIVARLTGLPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVP---------SGEIVGTLSSA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 241 GAAGDQQAALFG--QTCF------TKGEAKSTFGTGGFL--LMNTGEKPV------FSHNGLVTTVAwGLDGKVNYA-LE 303
Cdd:cd07777 220 LPKGIPVYVALGdnQASVlgsglnEENDAVLNIGTGAQLsfLTPKFELSGsveirpFFDGRYLLVAA-SLPGGRALAvLV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 304 GsiFVAgaaiQWLRDELHLLEDARDSEYMAQKVKDTNGC--YVVPAFTGlgaPHWDQYARGAIVGLTrgvNKN----HII 377
Cdd:cd07777 299 D--FLR----EWLRELGGSLSDDEIWEKLDELAESEESSdlSVDPTFFG---ERHDPEGRGSITNIG---ESNftlgNLF 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050539736 378 RATLDSLCYQINDVLTAMQADaGIPLTALKVDGGACANNYLMQTM-ADISARPVKRPCCVETTALGAAYLA 447
Cdd:cd07777 367 RALCRGIAENLHEMLPRLDLD-LSGIERIVGSGGALRKNPVLRRIiEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
6-484 |
4.46e-24 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 105.05 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 6 YImALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPKPGWVEHDANEIWTTqlgvALSAMNQIGA--SAEDIAAIGITNQ 83
Cdd:PRK15027 2 YI-GIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQA----TDRAMKALGDqhSLQDVKALGIAGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 84 RETTIVWDRDTgEPVCHAIVWQCRRTSEYCDELKARglTEKFREKTGLVIDAYFSATKLKWILDNVPGVRARAERGDLlf 163
Cdd:PRK15027 77 MHGATLLDAQQ-RVLRPAILWNDGRCAQECALLEAR--VPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLL-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 164 gtVETWLIWKLTcGKIhVTDYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPKPVPNSEFY-----EYAD-------PM 231
Cdd:PRK15027 152 --PKDYLRLRMT-GEF-ASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITgallpEVAKawgmatvPV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 232 HFGGeikiagaaGDQQAALFGQTCFTKGEAKSTFGTGG-FLLMNTG--EKPvfshNGLVTTVAWGLDGKvnYALEGSIFV 308
Cdd:PRK15027 228 VAGG--------GDNAAGAVGVGMVDANQAMLSLGTSGvYFAVSEGflSKP----ESAVHSFCHALPQR--WHLMSVMLS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 309 AGAAIQW------LRDELHLLEDARDSEYMAQKVkdtngcYVVPAFTGLGAPHWDQYARGAIVGLTRGVNKNHIIRATLD 382
Cdd:PRK15027 294 AASCLDWaakltgLSNVPALIAAAQQADESAEPV------WFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 383 SLCYQINDVLTAMQAdAGIPLTALKVDGGACANNYLMQTMADISARPVK-RPCCVETTALGAAYLAGLAVGYWQSTDDVL 461
Cdd:PRK15027 368 GVGYALADGMDVVHA-CGIKPQSVTLIGGGARSEYWRQMLADISGQQLDyRTGGDVGPALGAARLAQIAANPEKSLIELL 446
|
490 500
....*....|....*....|...
gi 2050539736 462 KNWSVDREFVPaltEAERTRRIQ 484
Cdd:PRK15027 447 PQLPLEQSHLP---DAQRYAAYQ 466
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
4-458 |
7.09e-21 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 95.10 E-value: 7.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 4 QKYIMALDAGTTSNRCILFNARGEMCSVA-QKEFTQYFP-KPGWVEHDANEIWTTQLGVALSAMNQIgaSAEDIAAIGIT 81
Cdd:PRK10331 1 QDVILVLDCGATNVRAIAVDRQGKIVARAsTPNASDIAAeNSDWHQWSLDAILQRFADCCRQINSEL--TECHIRGITVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 82 NQRETTIVWDrDTGEPVCHAIVWQCRRTSEYCDELKARGLTEKFREKTGlvIDAYFSAT--KLKWILDNVPGVRARAERg 159
Cdd:PRK10331 79 TFGVDGALVD-KQGNLLYPIISWKCPRTAAVMENIERYISAQQLQQISG--VGAFSFNTlyKLVWLKENHPQLLEQAHA- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 160 dLLFgtVETWLIWKLTcgKIHVTDYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPKPVPNSEFY-----EYADPMHFG 234
Cdd:PRK10331 155 -WLF--ISSLINHRLT--GEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIgtlqpSAAALLGLP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 235 GEIKIAGAAGDQQAALFGQTCfTKGEAKSTFGTGGFLLMNTGE-KP--VFSHNGLVTTvawgLDGKVNYALEGSIFVAGA 311
Cdd:PRK10331 230 VGIPVISAGHDTQFALFGSGA-GQNQPVLSSGTWEILMVRSAQvDTslLSQYAGSTCE----LDSQSGLYNPGMQWLASG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 312 AIQWLRDELHLLEDARDSeyM---AQKV-KDTNGCYVVPAFTGLGaphwdqyaRGAIVGLTRGVNKNHIIRATLDSLCYQ 387
Cdd:PRK10331 305 VLEWVRKLFWTAETPYQT--MieeARAIpPGADGVKMQCDLLACQ--------NAGWQGVTLNTTRGHFYRAALEGLTAQ 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050539736 388 INDVLTAMQADAGIPLTALKVDGGACANNYLMQTMADISARPVKRPCCVETTALGAAYLAGLAVGYWQSTD 458
Cdd:PRK10331 375 LKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPE 445
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
5-489 |
4.88e-19 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 90.07 E-value: 4.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 5 KYIMALDAGTTSNRCILFNARGEMCSVAQKEFT-QYFPK-PGWVEHDANEIWTTQLGVALSAMNQIGASAEDIAAIGITN 82
Cdd:PRK10939 3 SYLMALDAGTGSIRAVIFDLNGNQIAVGQAEWRhLAVPDvPGSMEFDLEKNWQLACQCIRQALQKAGIPASDIAAVSATS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 83 QRETTIVWDRDtGEPvchaiVWQC----RRTSEYCDELKAR--GLTEKFREKTGLVIdAYFSATKLKWILDNVPGVRARA 156
Cdd:PRK10939 83 MREGIVLYDRN-GTE-----IWACanvdARASREVSELKELhnNFEEEVYRCSGQTL-ALGALPRLLWLAHHRPDIYRQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 157 ERgdllFGTVETWLIWKLtCGKIHVtDYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPkpvpnsefyeyadPMHFGGE 236
Cdd:PRK10939 156 HT----ITMISDWIAYML-SGELAV-DPSNAGTTGLLDLVTRDWDPALLEMAGLRADILP-------------PVKETGT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 237 ikiagaagdqqaaLFGQTcfTKGEAKSTfGtggfLLMNTgekPVFSHNGLVTTVAWGLdGKVNYA--------------- 301
Cdd:PRK10939 217 -------------VLGHV--TAKAAAET-G----LRAGT---PVVMGGGDVQLGCLGL-GVVRPGqtavlggtfwqqvvn 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 302 ------------------------LEGSIFVAGAAIQWLRD----ELHLLEDARDS------EYMAQKVKdtNGCY-VVP 346
Cdd:PRK10939 273 lpapvtdpnmnirinphvipgmvqAESISFFTGLTMRWFRDafcaEEKLLAERLGIdaysllEEMASRVP--VGSHgIIP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 347 AFTglGAPHWDQYARGAIVGLTRGV-----NKNHIIRATLDSLCY--QINdvLTAMQADAGIPLTALKVDGGACANNYLM 419
Cdd:PRK10939 351 IFS--DVMRFKSWYHAAPSFINLSIdpekcNKATLFRALEENAAIvsACN--LQQIAAFSGVFPSSLVFAGGGSKGKLWS 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050539736 420 QTMADISARPVKRPCCVETTALGAAYLAGLAVGYWQSTDDVLKNW-SVDREFVPALTEAERTRRI-QGWNKA 489
Cdd:PRK10939 427 QILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSLAETGERLvRWERTFEPNPENHELYQEAkEKWQAV 498
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
4-472 |
1.70e-17 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 85.17 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 4 QKYIMALDAGTTSNRCILFNAR-GEMCSVAQKEFTQY------FPKPGWVEHDANEIWTtQLGVAL-SAMNQIGASAEDI 75
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDAAdGEELASAVHPYPRWviglylPPPPDQARQHPLDYLE-ALEAAVrEALAQAGVDPADV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 76 AAIGItnqrETT----IVWDRDtGEPVC---------HA--IVWQCRRTSEYCDEL----KARGltEKFREKTGLVIDA- 135
Cdd:COG1069 80 VGIGV----DATgctpVPVDAD-GTPLAllpefaenpHAmvILWKDHTAQEEAERInelaKARG--EDYLRYVGGIISSe 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 136 -YFSatKLKWILDNVPGVRARAER----GDllfgtvetWLIWKLTcGKIHvtdYSNASRT--MLFNIHTLDW-DDEILQI 207
Cdd:COG1069 153 wFWP--KILHLLREDPEVYEAADSfvelCD--------WITWQLT-GSLK---RSRCTAGhkALWHAHEGGYpSEEFFAA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 208 LDiPRcmlpkpvpnseFYEYADPMhfGGEIkiagaagdqqaalfgqtcFTKGE---------------------AKSTF- 265
Cdd:COG1069 219 LD-PL-----------LDGLADRL--GTEI------------------YPLGEpagtltaewaarlglppgtavAVGAId 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 266 ------GTG----GFLL---------MNTGEKPVFshnglVTTVaWG------LDGKvnYALEGSIFVAGAAIQWLRD-- 318
Cdd:COG1069 267 ahagavGAGgvepGTLVkvmgtstchMLVSPEERF-----VPGI-CGqvdgsiVPGM--WGYEAGQSAVGDIFAWFVRll 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 319 --ELHLLEDARDS-----EYMAQKVK----DTNGCYVVPAFTGLGAPHWDQYARGAIVGLTRGVNKNHIIRATLDSLCY- 386
Cdd:COG1069 339 vpPLEYEKEAEERgislhPLLTEEAAklppGESGLHALDWFNGNRSPLADQRLKGVILGLTLGTDAEDIYRALVEATAFg 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 387 --QINDVltamQADAGIPLTALKVDGGACANN-YLMQTMADISARPVKRPCCVETTALGAAYLAGLAVGYWQSTDDVLKN 463
Cdd:COG1069 419 trAIIER----FEEEGVPIDEIIACGGIATKNpLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMAA 494
|
570
....*....|.
gi 2050539736 464 WS--VDREFVP 472
Cdd:COG1069 495 MGsgFDKVYTP 505
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
62-442 |
6.75e-16 |
|
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.
Pssm-ID: 466791 [Multi-domain] Cd Length: 460 Bit Score: 79.88 E-value: 6.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 62 LSAMNQIGASAEDIAAIGItnqrettivwdrDT---------------GEPVCHaivwqcR--RTSEYCDELKARGLTEK 124
Cdd:cd07771 55 KEGLKKAAEQGGDIDSIGI------------DTwgvdfglldkngellGNPVHY------RdpRTEGMMEELFEKISKEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 125 FREKTGLVIDAYFSATKLKWILDNVPGVRARAER----GDLLfgtvetwlIWKLTcGKIhVTDYSNASRTMLFNIHTLDW 200
Cdd:cd07771 117 LYERTGIQFQPINTLYQLYALKKEGPELLERADKllmlPDLL--------NYLLT-GEK-VAEYTIASTTQLLDPRTKDW 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 201 DDEILQILDIPRCMLPKPVPnsefyeyadPMHFGGEIkiagaagdqqaalfgqtcftKGEAKSTFGTGGFLLMNTGEK-- 278
Cdd:cd07771 187 SEELLEKLGLPRDLFPPIVP---------PGTVLGTL--------------------KPEVAEELGLKGIPVIAVASHdt 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 279 -------PVFSHNGLV----TtvaWGLDG-------------KVNYALEGSIF--------VAGAaiqWLRDELH--LLE 324
Cdd:cd07771 238 asavaavPAEDEDAAFissgT---WSLIGveldepviteeafEAGFTNEGGADgtirllknITGL---WLLQECRreWEE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 325 DARDSEY-----MAQKVKDtNGCYVVPA----FTGLGAPHW-DQYAR--GAIVGLTRGvnknHIIRATLDSLCYQINDVL 392
Cdd:cd07771 312 EGKDYSYdelvaLAEEAPP-FGAFIDPDdprfLNPGDMPEAiRAYCRetGQPVPESPG----EIARCIYESLALKYAKTI 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2050539736 393 TAMQADAGIPLTALKVDGGACANNYLMQTMADISARPVKR-PccVETTALG 442
Cdd:cd07771 387 EELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAgP--VEATAIG 435
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
6-462 |
1.78e-15 |
|
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: 78.73 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 6 YIMALDAGTTSNRCILFNARGEMCSVAQKEFTQYFPKPGWVEHDANEIWTTQLGVALSAMNQIGASAEDIAAIGITnqre 85
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 86 TT---IVWDRD--------TGEPVCHAIVWQCRRTSEYCDELKARGltEKFREKTGLVIDAYFSATKLKWILDNVPGVRA 154
Cdd:cd07782 77 ATcslVVLDAEgkpvsvspSGDDERNVILWMDHRAVEEAERINATG--HEVLKYVGGKISPEMEPPKLLWLKENLPETWA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 155 RAERG-DLlfgtvETWLIWKLTcGKihvTDYSNASRT--MLFNIHTLD---WDDEILQILD-----------IPRCMLPK 217
Cdd:cd07782 155 KAGHFfDL-----PDFLTWKAT-GS---LTRSLCSLVckWTYLAHEGSeggWDDDFFKEIGledlvednfakIGSVVLPP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 218 PVPN----SEfyEYADPM---------------HFG--GEIKIAGAAGDQQAALFGQ---------TCFtkgeakstfgt 267
Cdd:cd07782 226 GEPVggglTA--EAAKELglpegtpvgvslidaHAGglGTLGADVGGLPCEADPLTRrlalicgtsSCH----------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 268 ggfllMNTGEKPVFshnglVTTVaWG------LDGKvnYALEGSIFVAGAAIQWLRDElH-----LLEDARDS-----EY 331
Cdd:cd07782 293 -----MAVSPEPVF-----VPGV-WGpyysamLPGL--WLNEGGQSATGALLDHIIET-HpaypeLKEEAKAAgksiyEY 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 332 MAQKVKD------------TNGCYVVPAFTGLGAPHWDQYARGAIVGLTRGVNKNHIIR---ATLDSLCYQINDVLTAMQ 396
Cdd:cd07782 359 LNERLEQlaeekglplaylTRDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHIIEAMN 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050539736 397 AdAGIPLTALKVDGGACANNYLMQTMADISARPVKRPCCVETTALGAAYLAGLAVGYWQSTDDVLK 462
Cdd:cd07782 439 A-AGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDAMA 503
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
6-472 |
2.66e-14 |
|
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466788 [Multi-domain] Cd Length: 522 Bit Score: 75.35 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 6 YIMALDAGTTSNRCILFN-ARGEMCSVAQKEFTQY-FPKPGWVEHDANEIWTTQLGVALSAMNQIGASAEDIAAIGItNQ 83
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDlYAGLEMAQEPVPYYQDsSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGV-DA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 84 RETTIVWDRDtGEPVC---------HAIVWQCRRTSEYCDELKARGlTEKFREKTGLVIDAYFSATKLKWILDNVPGVRA 154
Cdd:cd07768 80 TCSLAIFDRE-GTPLMalipypnedNVIFWMDHSAVNEAQWINMQC-PQQLLDYLGGKISPEMGVPKLKYFLDEYSHLRD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 155 RAERgdllFGTVETWLIWKLTcgKIHVTDYSNASRTMLFNIHTLDWDDEILQILDiprcmlPKPVPNSEFYEYADPMHFG 234
Cdd:cd07768 158 KHFH----IFDLHDYIAYELT--RLYEWNICGLLGKENLDGEESGWSSSFFKNID------PRLEHLTTTKNLPSNVPIG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 235 GEIKIAGAAGDQQAALFGQTCFTKG---EAKSTFGTGGF-----LLMNTGEKPVFSHNGLVTTVAWGLDGKVNYALEGSI 306
Cdd:cd07768 226 TTSGVALPEMAEKMGLHPGTAVVVScidAHASWFAVASPhletsLFMIAGTSSCHMYGTTISDRIPGVWGPFDTIIDPDY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 307 FV-------AGAAIQWL-------RDELHLLEDARD-SEYMAQKVKD-------TNGCYVVPAFTGLGAPHWDQYARGAI 364
Cdd:cd07768 306 SVyeagqsaTGKLIEHLfeshpcaRKFDEALKKGADiYQVLEQTIRQieknnglSIHILTLDMFFGNRSEFADPRLKGSF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 365 VGL---TRGVNKNHIIRATLDSLCYQINDVLTAMQADaGIPLTALKVDGGACANNYLMQTMADISARPVKRPCCVETTAL 441
Cdd:cd07768 386 IGEsldTSMLNLTYKYIAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGIL 464
|
490 500 510
....*....|....*....|....*....|....*
gi 2050539736 442 GAAYLAGLAVGYWQSTDDV----LKNWSVDREFVP 472
Cdd:cd07768 465 GAAVLAKVAAGKKQLADSIteadISNDRKSETFEP 499
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
103-465 |
8.15e-07 |
|
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; 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. The subfamily includes XKs mainly from eukaryote. 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: 466795 [Multi-domain] Cd Length: 514 Bit Score: 51.40 E-value: 8.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 103 VWQCRRTSEYCDEL-KARGLTEKFREKTGlvIDAY--FSATKLKWILDNVPGVRARAERGDLL--FGTvetwliwKLTCG 177
Cdd:cd07776 128 IWMDSSTTKQCRELeKAVGGPEALAKLTG--SRAYerFTGPQIAKIAQTDPEAYENTERISLVssFLA-------SLLLG 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 178 KIHVTDYSNASRTMLFNIHTLDWDDEILQILDIP--RCMLPKPVPN--------SEFYEYadpmhFGgeikiagaagdqq 247
Cdd:cd07776 199 RYAPIDESDGSGMNLMDIRSRKWSPELLDAATAPdlKEKLGELVPSstvaggisSYFVER-----YG------------- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 248 aalFGQTC----FTkGEAKSTF--------------GTGGFLLMNTGEKPVfshnglvttvawGLDGKV--NYALEGSIF 307
Cdd:cd07776 261 ---FSPDClvvaFT-GDNPASLaglglepgdvavslGTSDTVFLVLDEPKP------------GPEGHVfaNPVDPGSYM 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 308 V------AGAAIQWLRDELHLLEDARDSEYMAQKVKDTNGC----YVVPAFT--GLGAPHWDQYARGAIVGLTRGVNknh 375
Cdd:cd07776 325 AmlcyknGSLARERVRDRYAGGSWEKFNELLESTPPGNNGNlglyFDEPEITppVPGGGRRFFGDDGVDAFFDPAVE--- 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 376 iIRATLDSlcyQindvLTAMQADA-----GIPLTALKVDGGACANNYLMQTMADISARPVKRPCCVETTALGAAYLAGLA 450
Cdd:cd07776 402 -VRAVVES---Q----FLSMRLHAerlgsDIPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHG 473
|
410
....*....|....*
gi 2050539736 451 VGYWQSTDDVLKNWS 465
Cdd:cd07776 474 LLCAGSGDFSPEFVV 488
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
357-452 |
2.54e-06 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 49.84 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050539736 357 DQYARGAIVGLTRGVNKNHIIRATLDSLCYQINDVLTAMQaDAGIPLTALKVDGG-ACANNYLMQTMADISARPVKRPCC 435
Cdd:PRK04123 394 DQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFE-DQGVPVEEVIAAGGiARKNPVLMQIYADVLNRPIQVVAS 472
|
90
....*....|....*..
gi 2050539736 436 VETTALGAAYLAGLAVG 452
Cdd:PRK04123 473 DQCPALGAAIFAAVAAG 489
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
183-219 |
1.09e-04 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 44.71 E-value: 1.09e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2050539736 183 DYSNASRTMLFNIHTLDWDDEILQILDIPRCMLPKPV 219
Cdd:PRK10640 157 EYTNATTTQLVNINSDDWDESLLAWSGAPKAWFGRPT 193
|
|
| |
