|
Name |
Accession |
Description |
Interval |
E-value |
| glpK |
PRK00047 |
glycerol kinase GlpK; |
6-495 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 1023.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 6 NKNYIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIFATQSAVMVEALAQAGLHHDQVAAIGITN 85
Cdd:PRK00047 3 MKKYILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 86 QRETTVVWDKVTGRPIYNAIVWQCRRSTEICQQLKRDGHEQYISDTTGLVTDPYFSGTKLKWILDNVEGSRERARNGELL 165
Cdd:PRK00047 83 QRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRDGYEDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGELL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 166 FGTIDSWLIWKFTGGKTHVTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRTKSG------IAIGG 239
Cdd:PRK00047 163 FGTIDTWLVWKLTGGKVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYgffggeVPIAG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 240 IAGDQQAALFGQMCVEPGQAKNTYGTGCFLLMNTGDKAVKSKHGMLTTIACGPRGEVAYALEGAVFNGGSTVQWLRDELK 319
Cdd:PRK00047 243 IAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGIDGKVVYALEGSIFVAGSAIQWLRDGLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 320 IINDAHDTEYFAGKVKDSNGVYLVPAFTGLGAPYWDPYARGALFGLTRGVRVDHIIRAALESIAYQTRDVLDAMQQDSGE 399
Cdd:PRK00047 323 IISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADSGI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 400 RLKSLRVDGGAVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLACGFWGSLEELRGKAVIEREFEPQLEEAAKEK 479
Cdd:PRK00047 403 RLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDELKEQWKIDRRFEPQMDEEEREK 482
|
490
....*....|....*.
gi 516455773 480 LYAGWQKAVSRTRDWE 495
Cdd:PRK00047 483 LYAGWKKAVKRTLAWA 498
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
7-495 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 1008.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 7 KNYIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIFATQSAVMVEALAQAGLHHDQVAAIGITNQ 86
Cdd:COG0554 2 KKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITNQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 87 RETTVVWDKVTGRPIYNAIVWQCRRSTEICQQLKRDGHEQYISDTTGLVTDPYFSGTKLKWILDNVEGSRERARNGELLF 166
Cdd:COG0554 82 RETTVVWDRKTGKPLYNAIVWQDRRTADICEELKADGLEDLIREKTGLVLDPYFSATKIKWILDNVPGARERAEAGELLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 167 GTIDSWLIWKFTGGKTHVTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRTK-----SGIAIGGIA 241
Cdd:COG0554 162 GTIDSWLIWKLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDpdlfgAEIPIAGIA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 242 GDQQAALFGQMCVEPGQAKNTYGTGCFLLMNTGDKAVKSKHGMLTTIACGPRGEVAYALEGAVFNGGSTVQWLRDELKII 321
Cdd:COG0554 242 GDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGGKVTYALEGSIFVAGAAVQWLRDGLGLI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 322 NDAHDTEYFAGKVKDSNGVYLVPAFTGLGAPYWDPYARGALFGLTRGVRVDHIIRAALESIAYQTRDVLDAMQQDSGERL 401
Cdd:COG0554 322 DSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADSGIPL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 402 KSLRVDGGAVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLACGFWGSLEELRGKAVIEREFEPQLEEAAKEKLY 481
Cdd:COG0554 402 KELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEELAALWKVDRRFEPQMDEEERERLY 481
|
490
....*....|....
gi 516455773 482 AGWQKAVSRTRDWE 495
Cdd:COG0554 482 AGWKKAVERTLGWA 495
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
9-488 |
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: 950.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 9 YIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIFATQSAVMVEALAQAGLHHDQVAAIGITNQRE 88
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 89 TTVVWDKVTGRPIYNAIVWQCRRSTEICQQLKRDGHEQYISDTTGLVTDPYFSGTKLKWILDNVEGSRERARNGELLFGT 168
Cdd:cd07786 81 TTVVWDRETGKPVYNAIVWQDRRTADICEELKAEGHEEMIREKTGLVLDPYFSATKIRWILDNVPGARERAERGELAFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 169 IDSWLIWKFTGGKTHVTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRTKS-----GIAIGGIAGD 243
Cdd:cd07786 161 IDSWLIWKLTGGKVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDPdllgaEIPIAGIAGD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 244 QQAALFGQMCVEPGQAKNTYGTGCFLLMNTGDKAVKSKHGMLTTIACGPRGEVAYALEGAVFNGGSTVQWLRDELKIIND 323
Cdd:cd07786 241 QQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLGGKVTYALEGSIFIAGAAVQWLRDGLGLIES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 324 AHDTEYFAGKVKDSNGVYLVPAFTGLGAPYWDPYARGALFGLTRGVRVDHIIRAALESIAYQTRDVLDAMQQDSGERLKS 403
Cdd:cd07786 321 AAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEADSGIPLKE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 404 LRVDGGAVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLACGFWGSLEELRGKAVIEREFEPQLEEAAKEKLYAG 483
Cdd:cd07786 401 LRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAKLWQVDRRFEPSMSEEEREALYAG 480
|
....*
gi 516455773 484 WQKAV 488
Cdd:cd07786 481 WKKAV 485
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
9-488 |
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: 941.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 9 YIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIFATQSAVMVEALAQAGLHHDQVAAIGITNQRE 88
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 89 TTVVWDKVTGRPIYNAIVWQCRRSTEICQQLKRDGHEQYISDTTGLVTDPYFSGTKLKWILDNVEGSRERARNGELLFGT 168
Cdd:cd07769 81 TTVVWDKKTGKPLYNAIVWQDRRTADICEELKAKGLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAERGELLFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 169 IDSWLIWKFTGGKTHVTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRTKS-----GIAIGGIAGD 243
Cdd:cd07769 161 IDTWLIWKLTGGKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTDPeglgaGIPIAGILGD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 244 QQAALFGQMCVEPGQAKNTYGTGCFLLMNTGDKAVKSKHGMLTTIACGPRGEVAYALEGAVFNGGSTVQWLRDELKIIND 323
Cdd:cd07769 241 QQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQIGGKVTYALEGSIFIAGAAIQWLRDNLGLIED 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 324 AHDTEYFAGKVKDSNGVYLVPAFTGLGAPYWDPYARGALFGLTRGVRVDHIIRAALESIAYQTRDVLDAMQQDSGERLKS 403
Cdd:cd07769 321 AAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDSGIKLKE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 404 LRVDGGAVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLACGFWGSLEELRGKAVIEREFEPQLEEAAKEKLYAG 483
Cdd:cd07769 401 LRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDELASLWQVDKRFEPSMDEEERERLYRG 480
|
....*
gi 516455773 484 WQKAV 488
Cdd:cd07769 481 WKKAV 485
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
9-494 |
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: 857.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 9 YIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIFATQSAVMVEALAQAGLHHDQVAAIGITNQRE 88
Cdd:TIGR01311 2 YILAIDQGTTSSRAIVFDKDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAGIKPDDIAAIGITNQRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 89 TTVVWDKVTGRPIYNAIVWQCRRSTEICQQLKRDGHEQYISDTTGLVTDPYFSGTKLKWILDNVEGSRERARNGELLFGT 168
Cdd:TIGR01311 82 TTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYGEFIREKTGLPLDPYFSATKLRWLLDNVPGVREAAERGELLFGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 169 IDSWLIWKFTGGKTHVTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRTKSG-----IAIGGIAGD 243
Cdd:TIGR01311 162 IDTWLIWNLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYTDPGllgaeIPITGVLGD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 244 QQAALFGQMCVEPGQAKNTYGTGCFLLMNTGDKAVKSKHGMLTTIACGPRGEVA-YALEGAVFNGGSTVQWLRDELKIIN 322
Cdd:TIGR01311 242 QQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKKPvYALEGSVFVAGAAVQWLRDNLKLIK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 323 DAHDTEYFAGKVKDSNGVYLVPAFTGLGAPYWDPYARGALFGLTRGVRVDHIIRAALESIAYQTRDVLDAMQQDSGERLK 402
Cdd:TIGR01311 322 HAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTRDVLEAMEKDAGVEIT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 403 SLRVDGGAVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLACGFWGSLEELRGKAVIEREFEPQLEEAAKEKLYA 482
Cdd:TIGR01311 402 KLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWRVEKTFEPEMDEEEREARYA 481
|
490
....*....|..
gi 516455773 483 GWQKAVSRTRDW 494
Cdd:TIGR01311 482 GWKEAVKRSLGW 493
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
8-491 |
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: 750.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 8 NYIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIFATQSAVMVEALAQA---GLHHDQVAAIGIT 84
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLkalGISPSDIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 85 NQRETTVVWDKVTGRPIYNAIVWQCRRSTEICQQL--KRDGHEQYISDTTGLVTDPYFSGTKLKWILDNVEGSRERARNG 162
Cdd:cd07792 81 NQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELsaKTPGGKDHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 163 ELLFGTIDSWLIWKFTGGK---THVTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRTKS----GI 235
Cdd:cd07792 161 RLLFGTVDSWLIWNLTGGKnggVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIASgplaGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 236 AIGGIAGDQQAALFGQMCVEPGQAKNTYGTGCFLLMNTGDKAVKSKHGMLTTIA--CGPRGEVAYALEGAVFNGGSTVQW 313
Cdd:cd07792 241 PISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAykLGPDAPPVYALEGSIAIAGAAVQW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 314 LRDELKIINDAHDTEYFAGKVKDSNGVYLVPAFTGLGAPYWDPYARGALFGLTRGVRVDHIIRAALESIAYQTRDVLDAM 393
Cdd:cd07792 321 LRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREILDAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 394 QQDSGERLKSLRVDGGAVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLACGFWGSLEELRGKAVIERE-FEPQL 472
Cdd:cd07792 401 NKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSLNEGGRTvFEPQI 480
|
490
....*....|....*....
gi 516455773 473 EEAAKEKLYAGWQKAVSRT 491
Cdd:cd07792 481 SEEERERRYKRWKKAVERS 499
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
7-495 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 680.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 7 KNYIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIFATQSAVMVEALAQAGLHHDQ--VAAIGIT 84
Cdd:PTZ00294 1 MKYIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKGPSfkIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 85 NQRETTVVWDKVTGRPIYNAIVWQCRRSTEICQQLKRD-GHEQYISDTTGLVTDPYFSGTKLKWILDNVEGSRERARNGE 163
Cdd:PTZ00294 81 NQRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKyGGSNFFQKITGLPISTYFSAFKIRWMLENVPAVKDAVKEGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 164 LLFGTIDSWLIWKFTGGKTHVTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRTKS-------GIA 236
Cdd:PTZ00294 161 LLFGTIDTWLIWNLTGGKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTISGeavplleGVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 237 IGGIAGDQQAALFGQMCVEPGQAKNTYGTGCFLLMNTGDKAVKSKHGMLTTIA--CGPRGEVAYALEGAVFNGGSTVQWL 314
Cdd:PTZ00294 241 ITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCyqLGPNGPTVYALEGSIAVAGAGVEWL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 315 RDELKIINDAHDTEYFAGKVKDSNGVYLVPAFTGLGAPYWDPYARGALFGLTRGVRVDHIIRAALESIAYQTRDVLDAMQ 394
Cdd:PTZ00294 321 RDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDVIESME 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 395 QDSGERLKSLRVDGGAVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLACGFWGSLEELRGKAVIE-REFEPQLE 473
Cdd:PTZ00294 401 KDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVKKLIRRSnSTFSPQMS 480
|
490 500
....*....|....*....|..
gi 516455773 474 EAAKEKLYAGWQKAVSRTRDWE 495
Cdd:PTZ00294 481 AEERKAIYKEWNKAVERSLKWA 502
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
9-494 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 674.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 9 YIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIFATQSAVMVEALAQAGLH----HDQVAAIGIT 84
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKghnvDSGLKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 85 NQRETTVVWDKVTGRPIYNAIVWQCRRSTEICQQLKRD--GHEQYISDTTGLVTDPYFSGTKLKWILDNVEGSRERARNG 162
Cdd:PLN02295 81 NQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKElsGGRKHFVETCGLPISTYFSATKLLWLLENVDAVKEAVKSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 163 ELLFGTIDSWLIWKFTGGK---THVTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRT-----KSG 234
Cdd:PLN02295 161 DALFGTIDSWLIWNLTGGAsggVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIakgwpLAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 235 IAIGGIAGDQQAALFGQMCvEPGQAKNTYGTGCFLLMNTGDKAVKSKHGMLTTIA--CGPRGEVAYALEGAVFNGGSTVQ 312
Cdd:PLN02295 241 VPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAykLGPDAPTNYALEGSVAIAGAAVQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 313 WLRDELKIINDAHDTEYFAGKVKDSNGVYLVPAFTGLGAPYWDPYARGALFGLTRGVRVDHIIRAALESIAYQTRDVLDA 392
Cdd:PLN02295 320 WLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQVKDVLDA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 393 MQQDSGE-----RLKSLRVDGGAVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLACGFWGSLEELRG-KAVIER 466
Cdd:PLN02295 400 MRKDAGEekshkGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEEEIFASeKWKNTT 479
|
490 500
....*....|....*....|....*...
gi 516455773 467 EFEPQLEEAAKEKLYAGWQKAVSRTRDW 494
Cdd:PLN02295 480 TFRPKLDEEERAKRYASWCKAVERSFDL 507
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
9-488 |
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: 564.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 9 YIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIFATQSAVMVEALAQAGLHHDQVAAIGITNQRE 88
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 89 TTVVWDKVTGRPIYNAIVWQCRRSTEICQQLKRD-----------------GHEQYISD-----TTGLVTdpyfsgTKLK 146
Cdd:cd07793 81 TFLTWDKKTGKPLHNFITWQDLRAAELCESWNRSlllkalrggskflhfltRNKRFLAAsvlkfSTAHVS------IRLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 147 WILDNVEGSRERARNGELLFGTIDSWLIWKFTGGKTHVTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSE 226
Cdd:cd07793 155 WILQNNPELKEAAEKGELLFGTIDTWLLWKLTGGKVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 227 IYGRTK-----SGIAIGGIAGDQQAALFGQMCVEPGQAKNTYGTGCFLLMNTGDKAVKSKHGMLTTIACGPRGEVAYALE 301
Cdd:cd07793 235 DFGSTDpsifgAEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGGEITYLAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 302 GAVFNGGSTVQWLRDELkIINDAHDTEYFAGKVKDSNGVYLVPAFTGLGAPYWDPYARGALFGLTRGVRVDHIIRAALES 381
Cdd:cd07793 315 GNASDTGTVIDWAKSIG-LFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILES 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 382 IAYQTRDVLDAMQQDSGERLKSLRVDGGAVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLACGFWGSLEELRGK 461
Cdd:cd07793 394 IAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEELKKL 473
|
490 500
....*....|....*....|....*..
gi 516455773 462 AVIEREFEPQLEEAAKEKLYAGWQKAV 488
Cdd:cd07793 474 RKIEKIFEPKMDNEKREELYKNWKKAV 500
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
8-493 |
3.94e-124 |
|
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: 371.47 E-value: 3.94e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 8 NYIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIFATQSAVMVEALAQAGLHHDQVAAIGITNQR 87
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 88 ETTVVWDKvTGRPIYNAIVWQCRRSTEICQQLKRDGHEQYISDTTGLVTDPYFSGTKLKWILDNVEGSRERARngelLFG 167
Cdd:COG1070 81 HGLVLLDA-DGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIA----KVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 168 TIDSWLIWKFTGgkTHVTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRTKSGIA----------- 236
Cdd:COG1070 156 LPKDYLRYRLTG--EFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAaetglpagtpv 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 237 IGGiAGDQQAALFGQMCVEPGQAKNTYGTGCFLLMNTgDKAVKSKHGMLTTIACGPRGevAYALEGAVFNGGSTVQWLRD 316
Cdd:COG1070 234 VAG-AGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVS-DKPLPDPEGRVHTFCHAVPG--RWLPMGATNNGGSALRWFRD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 317 ELkIINDAHDTEYF---AGKVK-DSNGVYLVPAFTGLGAPYWDPYARGALFGLTRGVRVDHIIRAALESIAYQTRDVLDA 392
Cdd:COG1070 310 LF-ADGELDDYEELnalAAEVPpGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 393 MQQdSGERLKSLRVDGGAVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLACGFWGSLEE-LRGKAVIEREFEPQ 471
Cdd:COG1070 389 LEE-AGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEaAAAMVRVGETIEPD 467
|
490 500
....*....|....*....|...
gi 516455773 472 LEEAAK-EKLYAGWQKAVSRTRD 493
Cdd:COG1070 468 PENVAAyDELYERYRELYPALKP 490
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
9-477 |
4.00e-121 |
|
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: 361.84 E-value: 4.00e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 9 YIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIFATQSAVMVEALAQAGLHHDQVAAIGITNQRE 88
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 89 TTVVWDKvTGRPIYNAIVWQCRRSTEICqqlkrdgheqyisdttglvtdpyfsgtklkwildnvegsrerarngellfgT 168
Cdd:cd07779 81 TFVPVDE-DGRPLRPAISWQDKRTAKFL---------------------------------------------------T 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 169 IDSWLIWKFTGgkTHVTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGR-TKS-----GIAIG---- 238
Cdd:cd07779 109 VQDYLLYRLTG--EFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTlTKEaaeetGLPEGtpvv 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 239 -GiAGDQQAALFGQMCVEPGQAKNTYGTGCFLLMNTGDKAVKSKHGMLTTIACGPRgevAYALEGAVFNGGSTVQWLRDE 317
Cdd:cd07779 187 aG-GGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPG---KWVLEGSINTGGSAVRWFRDE 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 318 L----KIINDAHDTEYF-----AGKVK-DSNGVYLVPAFTGLGAPYWDPYARGALFGLTRGVRVDHIIRAALESIAYQTR 387
Cdd:cd07779 263 FgqdeVAEKELGVSPYEllneeAAKSPpGSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELR 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 388 DVLDAMqQDSGERLKSLRVDGGAVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLACGFWGSLEELRGKAV-IER 466
Cdd:cd07779 343 DNLEAM-EKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAMVrVTD 421
|
490
....*....|.
gi 516455773 467 EFEPQLEEAAK 477
Cdd:cd07779 422 TFEPDPENVAI 432
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
9-445 |
8.02e-114 |
|
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466787 [Multi-domain] Cd Length: 392 Bit Score: 341.47 E-value: 8.02e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 9 YIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIFATQSAVMVEALAQAGLHHDQVAAIGITNQRE 88
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 89 TTVVWDKvTGRPIYNAIVWQCRRSTeicqqlkrdgheqyisdttglvtdpyfsgtklkwildnvegsrerarngellFGT 168
Cdd:cd00366 81 GVVLVDA-DGNPLRPAIIWLDRRAK----------------------------------------------------FLQ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 169 IDSWLIWKFTGgkTHVTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRT----------KSGIAIG 238
Cdd:cd00366 108 PNDYIVFRLTG--EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVtpeaaeetglPAGTPVV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 239 GIAGDQQAALFGQMCVEPGQAKNTYGTGCFLLMNTGDKavKSKHGMLTTIACGPRGevAYALEGAVFNGGSTVQWLRDEL 318
Cdd:cd00366 186 AGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEP--VPPDPRLLNRCHVVPG--LWLLEGAINTGGASLRWFRDEF 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 319 KIINDAHDTEYF----AGKVKD-SNGVYLVPAFTGLGAPYWDPYARGALFGLTRGVRVDHIIRAALESIAYQTRDVLDAM 393
Cdd:cd00366 262 GEEEDSDAEYEGldelAAEVPPgSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEIL 341
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 516455773 394 qQDSGERLKSLRVDGGAVANNFLMQFQADILGTQVERPQMRETTALGAAYLA 445
Cdd:cd00366 342 -EELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
9-450 |
6.80e-105 |
|
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: 320.30 E-value: 6.80e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 9 YIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIFATQSAVMVEALAQAGlhHDQVAAIGITNQRE 88
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAG--PDPIAAISVSSQGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 89 TTVVWDKvTGRPIYNAIVWQCRRSTEICQQLKRDGHEQYISDTTGLVTDPYFSGTKLKWILDNVEGSRERARNgellFGT 168
Cdd:cd07773 79 SGVPVDR-DGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAK----WLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 169 IDSWLIWKFTGgkTHVTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRTKSGIAIGG--------- 239
Cdd:cd07773 154 VADYIAYRLTG--EPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEELglpagtpvv 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 240 IAG-DQQAALFGQMCVEPGQAKNTYGTG-CFLLMNTGDKAVKSKHGMLTTIACGPRGEVAYALEGavFNGGSTVQWLRDE 317
Cdd:cd07773 232 VGGhDHLCAALGAGVIEPGDVLDSTGTAeALLAVVDEPPLDEMLAEGGLSYGHHVPGGYYYLAGS--LPGGALLEWFRDL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 318 L--KIINDAHDTEYFAGKVKDSNGVYLVPAFTGLGAPYWDPYARGALFGLTRGVRVDHIIRAALESIAYQTRDVLDAMQQ 395
Cdd:cd07773 310 FggDESDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEALEK 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 516455773 396 dSGERLKSLRVDGGAVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLACG 450
Cdd:cd07773 390 -AGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
9-250 |
5.54e-104 |
|
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: 310.81 E-value: 5.54e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 9 YIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIFATQSAVMVEALAQAGLHHDQVAAIGITNQRE 88
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 89 TTVVWDKVTgRPIYNAIVWQCRRSTEICQQLKRDGHEQYISDTTGLVTDPYFSGTKLKWILDNVEGSRERARngelLFGT 168
Cdd:pfam00370 81 GTVLLDKND-KPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIH----KFLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 169 IDSWLIWKFTGgkTHVTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRTKSGIA----------IG 238
Cdd:pfam00370 156 IHDYLRWRLTG--VFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAamwgldegvpVV 233
|
250
....*....|..
gi 516455773 239 GIAGDQQAALFG 250
Cdd:pfam00370 234 GGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
9-487 |
4.59e-101 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 311.78 E-value: 4.59e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 9 YIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIFATQSAVMVEALAQAGLHHDQVAAIGITNQRE 88
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 89 TTVVWDKvTGRPIYNAIVWQCRRSTEICQQLkRDGHEQYISDTTGLVTDPYFSGTKLKWILDNVEGSRERARngELLFGT 168
Cdd:cd07808 81 GLVLLDK-NGRPLRPAILWNDQRSAAECEEL-EARLGDEILIITGNPPLPGFTLPKLLWLKENEPEIFARIR--KILLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 169 iDsWLIWKFTGgkTHVTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRTKSGIA-----------I 237
Cdd:cd07808 157 -D-YLRYRLTG--ELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAAeelglpegtpvV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 238 GGiAGDQQAALFGQMCVEPGQAKNTYGTGCFLLMNTgDKAVKSKHGMLTTIACGPRGEVaYALeGAVFNGGSTVQWLRDE 317
Cdd:cd07808 233 AG-AGDNAAAALGAGVVEPGDALISLGTSGVVFAPT-DKPVPDPKGRLHTFPHAVPGKW-YAM-GVTLSAGLSLRWLRDL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 318 LKiiNDAHDTEYFAGKVKD----SNGVYLVPAFTGLGAPYWDPYARGALFGLTRGVRVDHIIRAALESIAYQTRDVLDAM 393
Cdd:cd07808 309 FG--PDRESFDELDAEAAKvppgSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 394 qQDSGERLKSLRVDGGAVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLACGFWGSLEELRGKAV-IEREFEPQL 472
Cdd:cd07808 387 -KELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACIkIEKTIEPDP 465
|
490
....*....|....*.
gi 516455773 473 EEAAK-EKLYAGWQKA 487
Cdd:cd07808 466 ERHEAyDELYARYREL 481
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
9-486 |
2.35e-91 |
|
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: 286.76 E-value: 2.35e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 9 YIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIFATqsavMVEALAQ--AGLHHDQVAAIGITNQ 86
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEA----VLEALKEvlAKLGGGEVDAIGFSSA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 87 RETTVVWDKvTGRPIYNAIVWQCRRSTEICQQLKRDGHEQYISDTTGLVTDPYFSGTKLKWILDNVEGSRERARngelLF 166
Cdd:cd07770 77 MHSLLGVDE-DGEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAA----KF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 167 GTIDSWLIWKFTGgkTHVTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRTKSGIA---------- 236
Cdd:cd07770 152 VSIKEYLLYRLTG--ELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAerlgllagtp 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 237 --IGgiAGDQQAALFGQMCVEPGQAKNTYGTgcfllmnTG------DKAVKSKHGMLTTIACGPRGevaYALEGAVFNGG 308
Cdd:cd07770 230 vvLG--ASDGALANLGSGALDPGRAALTVGT-------SGairvvsDRPVLDPPGRLWCYRLDENR---WLVGGAINNGG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 309 STVQWLRDELKIINDAHD--TEYFAGKVKDSNGVYLVPAFTGLGAPYWDPYARGALFGLTRGVRVDHIIRAALESIAYQT 386
Cdd:cd07770 298 NVLDWLRDTLLLSGDDYEelDKLAEAVPPGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 387 RDVLDAMQQDSGERlKSLRVDGGAVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLACGFWGSLeELRGKAVIER 466
Cdd:cd07770 378 KSIYEALEELAGPV-KEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSL-EADELVKIGK 455
|
490 500
....*....|....*....|.
gi 516455773 467 EFEPQLEEAAK-EKLYAGWQK 486
Cdd:cd07770 456 VVEPDPENHAIyAELYERFKK 476
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
9-482 |
1.47e-89 |
|
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Chromobacterium violaceum xylulose kinase (CvXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466807 [Multi-domain] Cd Length: 485 Bit Score: 282.10 E-value: 1.47e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 9 YIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIF-ATQSAVMvEALAQAGLHHDQVAAIGITNQR 87
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWdAVCRATR-ALLEKSGIDPSDIAAIAFSGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 88 ETTVVWDKvTGRPIYNAIVWQCRRSTEICQQL-KRDGHEQYISDTTGLVTDPYFSGTKLKWILDNvegSRERARNGELLF 166
Cdd:cd07805 80 QGVVPVDK-DGNPLRNAIIWSDTRAAEEAEEIaGGLGGIEGYRLGGGNPPSGKDPLAKILWLKEN---EPEIYAKTHKFL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 167 GTIDsWLIWKFTGgkTHVTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRTKSGIA---------- 236
Cdd:cd07805 156 DAKD-YLNFRLTG--RAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAAaelglpagtp 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 237 -IGGiAGDQQAALFGQMCVEPGQAkNTY-GTGCFLLMNTGDKAVKSKHGMlTTIACGPRGEVAYAleGAVFNGGSTVQWL 314
Cdd:cd07805 233 vVGG-GGDAAAAALGAGAVEEGDA-HIYlGTSGWVAAHVPKPKTDPDHGI-FTLASADPGRYLLA--AEQETAGGALEWA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 315 RDELKIINDAHDTEY-----FAGKVK-DSNGVYLVPAFTGLGAPYWDPYARGALFGLTRGVRVDHIIRAALESIAYQTRD 388
Cdd:cd07805 308 RDNLGGDEDLGADDYelldeLAAEAPpGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRW 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 389 VLDAMqQDSGERLKSLRVDGGAVANNFLMQFQADILGTQVERP-QMRETTALGAAYLAGLACGFWGSLEELRGKAVIERE 467
Cdd:cd07805 388 LLEAL-EKLTRKIDELRLVGGGARSDLWCQILADVLGRPVEVPeNPQEAGALGAALLAAVGLGLLKSFDEAKALVKVEKV 466
|
490
....*....|....*.
gi 516455773 468 FEPQLEEAAK-EKLYA 482
Cdd:cd07805 467 FEPDPENRARyDRLYE 482
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
9-450 |
3.71e-82 |
|
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: 262.08 E-value: 3.71e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 9 YIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIFATQSAVMVEALAQAGLHHDQVAAIGITNQRE 88
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 89 TTVVWDKvTGRPIYNAIVWQCRRSTEICQQLKRDGHEQYISDTTGLVTDPYFSGTKLKWILDNVEGSRERARngelLFGT 168
Cdd:cd07804 81 ALVPVDE-NGKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTR----KFLG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 169 IDSWLIWKFTGgkTHVTDYTNASRTM-LFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRT------KSGIAIGG-- 239
Cdd:cd07804 156 AYDYIVYKLTG--EYVIDYSSAGNEGgLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVtkeaaeETGLAEGTpv 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 240 IAG--DQQAALFGQMCVEPGQAKNTYGT-GCFLLMNtgDKAVKSKHgMLTTIACGPRGevaYALEGAVFNGGSTVQWLRD 316
Cdd:cd07804 234 VAGtvDAAASALSAGVVEPGDLLLMLGTaGDIGVVT--DKLPTDPR-LWLDYHDIPGT---YVLNGGMATSGSLLRWFRD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 317 EL-----KIINDAHDTEY-----FAGKVK-DSNGVYLVPAFTGLGAPYWDPYARGALFGLTRGVRVDHIIRAALESIAYQ 385
Cdd:cd07804 308 EFageevEAEKSGGDSAYdlldeEAEKIPpGSDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYG 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516455773 386 TRDVLDAMqQDSGERLKSLRVDGGAVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLACG 450
Cdd:cd07804 388 LRHHLEVI-REAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
9-450 |
3.23e-67 |
|
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: 222.81 E-value: 3.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 9 YIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIFATQSAVMVEALAQAGLHHDQVAAIGITNQRE 88
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 89 TTVVWDKvTGRPIYNAIVWQCRRSTEICQQLKRDGHEQYISDTTGLVTDPYFSGTKLKWILDNvegSRERARNGELLFGT 168
Cdd:cd07802 81 GLYLVDK-DGKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKEN---EPERYDRIRTVLFC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 169 IDsWLIWKFTGgkTHVTDYTNASrTMLFNIHTLEWDAKMLDILDVP--REMLPEVKSSSEIYGRT------KSGIAIG-- 238
Cdd:cd07802 157 KD-WIRYRLTG--EISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVtaeaaaLTGLPEGtp 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 239 --GIAGDQQAALFGQMCVEPGQAKNTYGTGCfllMNTG--DKAVKSKHGMLTTIACGPrgEVAYALEGAVfNGGSTVQWL 314
Cdd:cd07802 233 vaAGAFDVVASALGAGAVDEGQLCVILGTWS---INEVvtDEPVVPDSVGSNSLHADP--GLYLIVEASP-TSASNLDWF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 315 RDEL---KIINDAHDTEYFAGKVKD----SNGVYLVPAFTGLGApywDPYARGALFGLTRGVRVDHIIRAALESIAYQTR 387
Cdd:cd07802 307 LDTLlgeEKEAGGSDYDELDELIAAvppgSSGVIFLPYLYGSGA---NPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHR 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516455773 388 DVLDAMqqDSGERLKSLRVDGGAVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLACG 450
Cdd:cd07802 384 DHLERL--LVARKPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
9-449 |
2.05e-63 |
|
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: 212.47 E-value: 2.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 9 YIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIFATqsavMVEALAQ--AGLHHDQVAAIGITNQ 86
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEA----LRSLLRElpAELRPRRVVAIAVDGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 87 RETTVVWDKvTGRPIYNAIVWQCRRSTEICQQLKRdgHEQYISDTTGLVTDPYFSGTKLKWILDNVEGSRERARngelLF 166
Cdd:cd07783 77 SGTLVLVDR-EGEPLRPAIMYNDARAVAEAEELAE--AAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTA----KF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 167 GTIDSWLIWKFTGGKtHVTDYTNASRTmLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRTKSGIA---------- 236
Cdd:cd07783 150 LHQADWLAGRLTGDR-GVTDYNNALKL-GYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAAeelglpagtp 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 237 -IGGIAgDQQAALFGQMCVEPGQAKNTYGTGCFLLMNTGDKAVKSKHGmlttIACGPRGEVAYALEGAVFNGGSTVQWL- 314
Cdd:cd07783 228 vVAGTT-DSIAAFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGG----VYSHRHGDGYWLVGGASNTGGAVLRWFf 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 315 -RDELKIINDAHDTEYfagkvkdSNGVYLVP-AFTGLGAPYWDPYARGALfgLTRGVRVDHIIRAALESIAYQTRDVLDA 392
Cdd:cd07783 303 sDDELAELSAQADPPG-------PSGLIYYPlPLRGERFPFWDPDARGFL--LPRPHDRAEFLRALLEGIAFIERLGYER 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 516455773 393 MQQDSGERLKSLRVDGGAVANNFLMQFQADILGTQVERPQmRETTALGAAYLAGLAC 449
Cdd:cd07783 374 LEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAE-EEEAALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
9-450 |
2.05e-58 |
|
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: 199.76 E-value: 2.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 9 YIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQA--GWVEHDPMEIFATQSAVMVEALAQAGLHHDQVAAIGITNQ 86
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDypDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 87 RETTVVWDKvTGRPIY---N----AIVWQcrrsTEICQQlkrdgHEQYISDTTGLVTDPYFSGTKLKWILDNVEGSRERA 159
Cdd:cd07798 81 REGIVFLDK-DGRELYagpNidarGVEEA----AEIDDE-----FGEEIYTTTGHWPTELFPAARLLWFKENRPEIFERI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 160 RNgellFGTIDSWLIWKFTGGKthVTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRTKSGIA--- 236
Cdd:cd07798 151 AT----VLSISDWIGYRLTGEL--VSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAArel 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 237 ---------IGGiaGDQQAALFGQMCVEPGQAKNTYGTGCFLLMNTGDKAVKSKHGMLTTIACGPRGevaYALEGavfNG 307
Cdd:cd07798 225 glpegtpvvVGG--ADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTGCHLVPGK---WVLES---NA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 308 GST---VQWLRDEL-KIINDAHDT--EYFAGKVKDSNGVYlvpAFTGLGAPYWD--PYARGALF--------GLTRGvrv 371
Cdd:cd07798 297 GVTglnYQWLKELLyGDPEDSYEVleEEASEIPPGANGVL---AFLGPQIFDARlsGLKNGGFLfptplsasELTRG--- 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516455773 372 dHIIRAALESIAYQTRDVLDAMQQDSGERLKSLRVDGGAVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLACG 450
Cdd:cd07798 371 -DFARAILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
9-450 |
6.78e-51 |
|
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: 179.74 E-value: 6.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 9 YIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIFATQSAVMVEALAQAGLHHDQVAAIGITNQRE 88
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 89 TTVVWDKvTGRPIYNAIVWQCRRSTEICQQLKRDGHEQYISDTTGLVTDPYFSGTKLKWILDNVEGSRERARngeLLFGT 168
Cdd:cd24121 81 GTWLVDE-DGRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKENEPERLERAR---TALHC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 169 IDsWLIWKFTGGKThvTDYTNASRTMlFNIHTLEWDAKMLDILDVP--REMLPEVKSSSEIYG--RTKSGIAIGGIAG-- 242
Cdd:cd24121 157 KD-WLFYKLTGEIA--TDPSDASLTF-LDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGplTPEAAAATGLPAGtp 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 243 ------DQQAALFGQMCVEPGQAKNTYGTGCFLLMNTgDKAVKSKHGMLTTIACGPRGEVAYALegAVFNGGSTVQWLRD 316
Cdd:cd24121 233 vvlgpfDVVATALGSGAIEPGDACSILGTTGVHEVVV-DEPDLEPEGVGYTICLGVPGRWLRAM--ANMAGTPNLDWFLR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 317 EL-------KIINDAHDTEYFAGKVKD----SNGV----YLVPAftGLGAPYWDPYARGALFGLTRGVRVDHIIRAALES 381
Cdd:cd24121 310 ELgevlkegAEPAGSDLFQDLEELAASsppgAEGVlyhpYLSPA--GERAPFVNPNARAQFTGLSLEHTRADLLRAVYEG 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516455773 382 IAYQTRDVLDAMqqdsGERLKSLRVDGGAVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLACG 450
Cdd:cd24121 388 VALAMRDCYEHM----GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
9-450 |
1.03e-50 |
|
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: 178.90 E-value: 1.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 9 YIIALDQGTTSSRAIIFD-RDANVVCTAQREFAQHYPQAGWVEHDPMEIF-ATQSAVMvEALAQAGLHHDQVAAIGITNQ 86
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWdALQAAFA-QLLKDAGAELRDVAAIGISGQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 87 RETTVVWDKvTGRPIYNAIVWQCRRSTEICQQLKRD-GHEQYISdtTGLVTDPYFSGTKLKWILDNVEGSRERARNGELL 165
Cdd:cd07809 80 MHGLVALDA-DGKVLRPAKLWCDTRTAPEAEELTEAlGGKKCLL--VGLNIPARFTASKLLWLKENEPEHYARIAKILLP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 166 FGtidsWLIWKFTGGKthVTDYTNASRTMLFNIHTLEWDAKMLDILDVPR---EMLPEVKSSSEIYGR-TKSGIAIGGI- 240
Cdd:cd07809 157 HD----YLNWKLTGEK--VTGLGDASGTFPIDPRTRDYDAELLAAIDPSRdlrDLLPEVLPAGEVAGRlTPEGAEELGLp 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 241 --------AGDQQAALFGQMCVEPGQAKNTYGT-GCflLMNTGDKAVKSKHGMLTTIaCGPRGEVAYALEGAvfnGGSTV 311
Cdd:cd07809 231 agipvapgEGDNMTGALGTGVVNPGTVAVSLGTsGT--AYGVSDKPVSDPHGRVATF-CDSTGGMLPLINTT---NCLTA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 312 qWLRDELKIINDAHDT--EYFAGKVKDSNGVYLVPAFTGLGAPYWdPYARGALFGLTRGV-RVDHIIRAALESIAYQTRD 388
Cdd:cd07809 305 -WTELFRELLGVSYEEldELAAQAPPGAGGLLLLPFLNGERTPNL-PHGRASLVGLTLSNfTRANLARAALEGATFGLRY 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455773 389 VLDAMQQDsGERLKSLRVDGGAVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLACG 450
Cdd:cd07809 383 GLDILREL-GVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
259-449 |
3.76e-47 |
|
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.
Pssm-ID: 426979 [Multi-domain] Cd Length: 197 Bit Score: 162.11 E-value: 3.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 259 AKNTYGTGCFLLMnTGDKAVKSKHGMLTTI--ACGPRGevaYALEGAVFNGGSTVQWLRDEL----KIINDAHDTEYF-- 330
Cdd:pfam02782 1 LAISAGTSSFVLV-ETPEPVLSVHGVWGPYtnEMLPGY---WGLEGGQSAAGSLLAWLLQFHglreELRDAGNVESLAel 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 331 --AGKVKDSNGVYLVPAFTGLGAPYWDPYARGALFGLTRGVRVDHIIRAALESIAYQTRDVLDAMQQDSGERLKSLRVDG 408
Cdd:pfam02782 77 aaLAAVAPAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 516455773 409 GAVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLAC 449
Cdd:pfam02782 157 GGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVAA 197
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
9-484 |
2.05e-43 |
|
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: 160.19 E-value: 2.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 9 YIIALDQGTTSSRAIIFDRDANVVCTAQREFaQH-----YPqaGWVEHDPMEIFATQSAVMVEALAQAGLHHDQVAAIGI 83
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREW-RHkevpdVP--GSMDFDTEKNWKLICECIREALKKAGIAPKSIAAIST 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 84 TNQRETTVVWDKvTGRPIynaivWQCR----RSTEICQQLK--RDGHEQYISDTTGlvtDPYFSGT--KLKWILDNVEGS 155
Cdd:cd07775 78 TSMREGIVLYDN-EGEEI-----WACAnvdaRAAEEVSELKelYNTLEEEVYRISG---QTFALGAipRLLWLKNNRPEI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 156 RERARNgellFGTIDSWLIWKFTGgkTHVTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRTKSGI 235
Cdd:cd07775 149 YRKAAK----ITMLSDWIAYKLSG--ELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 236 A------------IGGiaGDQQAALFGQMCVEPGQAKNTYGTGCFLLMNTGDKAVKSKhgMLTTIACGPRGEVAYAlEGA 303
Cdd:cd07775 223 AeetglkegtpvvVGG--GDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPA--MNIRVNCHVIPDMWQA-EGI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 304 VFNGGSTVQWLRD----ELKII-----NDAHD----------------TEYFAGKVKDSNGVYLVPAFTGLGApywDP-- 356
Cdd:cd07775 298 SFFPGLVMRWFRDafcaEEKEIaerlgIDAYDlleemakdvppgsygiMPIFSDVMNYKNWRHAAPSFLNLDI---DPek 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 357 YARGALFgltrgvrvdhiiRAALESIAYQTRDVLDAMQQDSGERLKSLRVDGGAVANNFLMQFQADILGTQVERPQMRET 436
Cdd:cd07775 375 CNKATFF------------RAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEA 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 516455773 437 TALGAAYLAGLACGFWGSLEELRGKAV-IEREFEPQLEEAAK-EKLYAGW 484
Cdd:cd07775 443 TALGAAIAAGVGAGIYSSLEEAVESLVkWEREYLPNPENHEVyQDLYEKW 492
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
9-482 |
1.02e-42 |
|
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466799 [Multi-domain] Cd Length: 504 Bit Score: 158.47 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 9 YIIALDQGTTSSRAIIFD-RDANVVCTAQREFAQHY--PQAGWVEHDPMEIFATQSAVMVEALAQAGLHHDQVAAIGITN 85
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 86 QRETTVVWDKvTGRPIYNAIVWQCRRSTEICQQLKRDGHEqyisdtTGLVTDPYFSGT--------KLKWILDNVEGSRE 157
Cdd:cd07781 81 TSSTVVPVDE-DGNPLAPAILWMDHRAQEEAAEINETAHP------ALEYYLAYYGGVyssewmwpKALWLKRNAPEVYD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 158 RARngellfgTI----DsWLIWKFTGGKThvtdytnASRTM-----LFNIHTLEWDAKMLDILDVP----REMLP-EVKS 223
Cdd:cd07781 154 AAY-------TIveacD-WINARLTGRWV-------RSRCAaghkwMYNEWGGGPPREFLAALDPGllklREKLPgEVVP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 224 SSEIYGRT----------KSGIAIGGIAGDQQAALFGQMCVEPGQAKNTYGT-GCFLLMNTGDKAVKskhGMlttiaCGP 292
Cdd:cd07781 219 VGEPAGTLtaeaaerlglPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTsTCHLMVSPKPVDIP---GI-----CGP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 293 -RGEVA---YALEG---AVfngGSTVQWLRDEL-KIINDAHDTEY-----FAGKVK-DSNGVYLVPAFTGLGAPYWDPYA 358
Cdd:cd07781 291 vPDAVVpglYGLEAgqsAV---GDIFAWFVRLFvPPAEERGDSIYallseEAAKLPpGESGLVALDWFNGNRTPLVDPRL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 359 RGALFGLTRGVRVDHIIRAALESIAYQTRDVLDAMqQDSGERLKSLRVDGGAVANN-FLMQFQADILGTQVERPQMRETT 437
Cdd:cd07781 368 RGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERF-EEAGVPVNRVVACGGIAEKNpLWMQIYADVLGRPIKVPKSDQAP 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 516455773 438 ALGAAYLAGLACGFWGSLEELRGKAV-IEREFEPQLEEAAK-EKLYA 482
Cdd:cd07781 447 ALGAAILAAVAAGVYADIEEAADAMVrVDRVYEPDPENHAVyEELYA 493
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
9-445 |
9.52e-38 |
|
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: 143.52 E-value: 9.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 9 YIIALDQGTTSSRAIIFDRDANVVcTAQREFAQHYPQA----GWVEHDPMEIFATqsavMVEALAQAGLHHD-QVAAIGI 83
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLESGRI-LESVSRPTPAPISsddpGRSEQDPEKILEA----VRNLIDELPREYLsDVTGIGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 84 TNQRETTVVWDKvTGRPIYNAIVWQCRRSTEICQQLKRDGHEQYISDTT-------GLVTdpyfsgtkLKWIldnvegsr 156
Cdd:cd07777 76 TGQMHGIVLWDE-DGNPVSPLITWQDQRCSEEFLGGLSTYGEELLPKSGmrlkpgyGLAT--------LFWL-------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 157 erARNGELL-----FGTIDSWLIWKFTGGKTHVTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRT 231
Cdd:cd07777 139 --LRNGPLPskadrAGTIGDYIVARLTGLPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 232 KSGIAIG-----GIaGDQQAALFGQMCVEPGQAKNTYGTGCFLLMNTgDKAVKSKH---------GMLTTIACGPRGEVA 297
Cdd:cd07777 217 SSALPKGipvyvAL-GDNQASVLGSGLNEENDAVLNIGTGAQLSFLT-PKFELSGSveirpffdgRYLLVAASLPGGRAL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 298 YALEGAVfnggstVQWLRDELKIINDAHDTEYF--AGKVKDSNGVYLVPAFTGlGApyWDPYARGALFGLTRG-VRVDHI 374
Cdd:cd07777 295 AVLVDFL------REWLRELGGSLSDDEIWEKLdeLAESEESSDLSVDPTFFG-ER--HDPEGRGSITNIGESnFTLGNL 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455773 375 IRAALESIAYQTRDVLDAMQQDSGeRLKSLRVDGGAVA-NNFLMQFQADILGTQVERPQMRETTALGAAYLA 445
Cdd:cd07777 366 FRALCRGIAENLHEMLPRLDLDLS-GIERIVGSGGALRkNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
8-487 |
8.06e-33 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 130.90 E-value: 8.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 8 NYIIALDQGTTSSRAIIFDRDANVVCTAQREFaQHYPQ---AGWVEHDPMEIFATQSAVMVEALAQAGLHHDQVAAIGIT 84
Cdd:PRK10939 3 SYLMALDAGTGSIRAVIFDLNGNQIAVGQAEW-RHLAVpdvPGSMEFDLEKNWQLACQCIRQALQKAGIPASDIAAVSAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 85 NQRETTVVWDKvTGRPIynaivWQC----RRSTEICQQLK--RDGHEQYISDTTG----LVTDPyfsgtKLKWILDNVEG 154
Cdd:PRK10939 82 SMREGIVLYDR-NGTEI-----WACanvdARASREVSELKelHNNFEEEVYRCSGqtlaLGALP-----RLLWLAHHRPD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 155 SRERARNgellFGTIDSWLIWKFTGGKThvTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRT--- 231
Cdd:PRK10939 151 IYRQAHT----ITMISDWIAYMLSGELA--VDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVtak 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 232 ---KSGIAIG-----GiAGDQQAALFGQMCVEPGQAKNTYGTGCFLLMNTGdkAVKSKHGMLTTIACGPRGEVAYAlEGA 303
Cdd:PRK10939 225 aaaETGLRAGtpvvmG-GGDVQLGCLGLGVVRPGQTAVLGGTFWQQVVNLP--APVTDPNMNIRINPHVIPGMVQA-ESI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 304 VFNGGSTVQWLRD----ELKIIN-----DAHDT-EYFAGKVK-DSNGVylVPAFTGL--------GAPYW-----DPYA- 358
Cdd:PRK10939 301 SFFTGLTMRWFRDafcaEEKLLAerlgiDAYSLlEEMASRVPvGSHGI--IPIFSDVmrfkswyhAAPSFinlsiDPEKc 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 359 -RGALFgltrgvrvdhiiRAALESIAYQTRDVLDAMQQDSGERLKSLRVDGGAVANNFLMQFQADILGTQVERPQMRETT 437
Cdd:PRK10939 379 nKATLF------------RALEENAAIVSACNLQQIAAFSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEAT 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 516455773 438 ALGAAYLAGLACGFWGSLEELRGKAV-IEREFEPQLEEAAK-EKLYAGWQKA 487
Cdd:PRK10939 447 ALGCAIAAGVGAGIYSSLAETGERLVrWERTFEPNPENHELyQEAKEKWQAV 498
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
11-476 |
2.40e-31 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 126.24 E-value: 2.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 11 IALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIF-ATQSAVmvEAL-AQAGLHhdQVAAIGITNQRE 88
Cdd:PRK15027 3 IGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWqATDRAM--KALgDQHSLQ--DVKALGIAGQMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 89 TTVVWDKvTGRPIYNAIVWQCRRSTEICQQLkrdghEQYIS---DTTGLVTDPYFSGTKLKWIldnvegsrerARNGELL 165
Cdd:PRK15027 79 GATLLDA-QQRVLRPAILWNDGRCAQECALL-----EARVPqsrVITGNLMMPGFTAPKLLWV----------QRHEPEI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 166 FGTIDSWLIWK------FTGgkTHVTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRTKSGIA--- 236
Cdd:PRK15027 143 FRQIDKVLLPKdylrlrMTG--EFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAkaw 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 237 -------IGGiAGDQQAALFGQMCVEPGQAKNTYGT-GCFLLMNTG-----DKAVKS-KHGMlttiacgPRgevAYALEG 302
Cdd:PRK15027 221 gmatvpvVAG-GGDNAAGAVGVGMVDANQAMLSLGTsGVYFAVSEGflskpESAVHSfCHAL-------PQ---RWHLMS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 303 AVFNGGSTVQW------LRDELKIINDAHDTEYFAGKvkdsngVYLVPAFTGLGAPYWDPYARGALFGLTRGVRVDHIIR 376
Cdd:PRK15027 290 VMLSAASCLDWaakltgLSNVPALIAAAQQADESAEP------VWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELAR 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 377 AALESIAYQTRDVLDAMqQDSGERLKSLRVDGGAVANNFLMQFQADILGTQVE-RPQMRETTALGAAYLAGLACGFWGSL 455
Cdd:PRK15027 364 AVLEGVGYALADGMDVV-HACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDyRTGGDVGPALGAARLAQIAANPEKSL 442
|
490 500
....*....|....*....|.
gi 516455773 456 EELRGKAVIEREFEPQLEEAA 476
Cdd:PRK15027 443 IELLPQLPLEQSHLPDAQRYA 463
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
8-480 |
8.66e-30 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 121.67 E-value: 8.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 8 NYIIALDQGTTSSRAIIFDRDANVVctAQREFAQHYPQA----GWVEHDPMEIFATQSAVMVEALAQagLHHDQVAAIGI 83
Cdd:PRK10331 2 DVILVLDCGATNVRAIAVDRQGKIV--ARASTPNASDIAaensDWHQWSLDAILQRFADCCRQINSE--LTECHIRGITV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 84 TNQRETTVVWDKvTGRPIYNAIVWQCRRSTEICQQLkrdghEQYISDTTgLVTDpyfSGT---------KLKWILDNVEG 154
Cdd:PRK10331 78 TTFGVDGALVDK-QGNLLYPIISWKCPRTAAVMENI-----ERYISAQQ-LQQI---SGVgafsfntlyKLVWLKENHPQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 155 SRERARngELLFgtIDSWLIWKFTGGKThvTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRTKSG 234
Cdd:PRK10331 148 LLEQAH--AWLF--ISSLINHRLTGEFT--TDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 235 IA--IG---GI----AG-DQQAALFGQmcvepGQAKN----TYGTGCFLLMNTG--DKAVKSKHGMLTTIACGPRGevay 298
Cdd:PRK10331 222 AAalLGlpvGIpvisAGhDTQFALFGS-----GAGQNqpvlSSGTWEILMVRSAqvDTSLLSQYAGSTCELDSQSG---- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 299 alegaVFNGG------STVQWLRDELKIINDAHDTEYFAGKV--KDSNGVYLVPAFTGLGAPYWdpyaRGALFGLTRGvr 370
Cdd:PRK10331 293 -----LYNPGmqwlasGVLEWVRKLFWTAETPYQTMIEEARAipPGADGVKMQCDLLACQNAGW----QGVTLNTTRG-- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 371 vdHIIRAALESIAYQTRDVLDAMQQDSGERLKSLRVDGGAVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLACG 450
Cdd:PRK10331 362 --HFYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVG 439
|
490 500 510
....*....|....*....|....*....|.
gi 516455773 451 FWGSLEELRGKAVIE-REFEPQLEEAAKEKL 480
Cdd:PRK10331 440 EFSSPEQARAQMKYQyRYFYPQTEPEFIEEV 470
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
9-481 |
3.14e-25 |
|
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: 108.87 E-value: 3.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 9 YIIALDQGTTSSRAIIFDrdanvvCTAQREFAQH--------YPQAGWVEHDPMEIFATQSAVMVEALAQAGLHHDQVAA 80
Cdd:cd07768 1 YGIGVDVGTSSARAGVYD------LYAGLEMAQEpvpyyqdsSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 81 IGITN-------QRETTVVWDKVTGRPIYNAIVWQCRRSTEICQQLKRDGHEQyISDTTGLVTDPYFSGTKLKWILDnvE 153
Cdd:cd07768 75 CGVDAtcslaifDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWINMQCPQQ-LLDYLGGKISPEMGVPKLKYFLD--E 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 154 GSRERARNGELLfgTIDSWLIWKFTGgkthvtDYTNASRTMLF--NIHTLE--WDAKMLDILDVPREMLPEVKssseIYG 229
Cdd:cd07768 152 YSHLRDKHFHIF--DLHDYIAYELTR------LYEWNICGLLGkeNLDGEEsgWSSSFFKNIDPRLEHLTTTK----NLP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 230 RTKSGIAIGGIAGDQQAALFGQM--------CVE-----PGQAKNTYGTGCFLLMNTgdkavKSKHGMLTTIA------C 290
Cdd:cd07768 220 SNVPIGTTSGVALPEMAEKMGLHpgtavvvsCIDahaswFAVASPHLETSLFMIAGT-----SSCHMYGTTISdripgvW 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 291 GPRgEVAYALEGAVFNGGST-----VQWL-------RDELKIINDAHDT----EY----FAGKVKDSNGVYLVPAFTGLG 350
Cdd:cd07768 295 GPF-DTIIDPDYSVYEAGQSatgklIEHLfeshpcaRKFDEALKKGADIyqvlEQtirqIEKNNGLSIHILTLDMFFGNR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 351 APYWDPYARGALFGL---TRGVRVDHIIRAALESIAYQTRDVLDAMQQDsGERLKSLRVDGGAVANNFLMQFQADILGTQ 427
Cdd:cd07768 374 SEFADPRLKGSFIGEsldTSMLNLTYKYIAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKNERLLQLIALVTNVA 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 428 VERPQMRETTALGAAYLAGLACG---FWGSLEELRGK-AVIEREFEPQLEE--AAKEKLY 481
Cdd:cd07768 453 IIKPKENMMGILGAAVLAKVAAGkkqLADSITEADISnDRKSETFEPLAYRlgADYILLY 512
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
7-482 |
1.08e-23 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 104.04 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 7 KNYIIALDQGTTSSRAIIFD-RDANVVCTAQREFAQH------YPQAGWVEHDPMEIFATQSAVMVEALAQAGLHHDQVA 79
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDaADGEELASAVHPYPRWviglylPPPPDQARQHPLDYLEALEAAVREALAQAGVDPADVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 80 AIGItnqrETT----VVWDK----------VTGRPIYNAIVW-------QCRRSTEICqqlkRDGHEQYIsdttglvtdP 138
Cdd:COG1069 81 GIGV----DATgctpVPVDAdgtplallpeFAENPHAMVILWkdhtaqeEAERINELA----KARGEDYL---------R 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 139 YFSGT--------KLKWILDNVEGSRERArngELLFGTIDsWLIWKFTGgkthvtdytnasrTMLFNIHTL--------E 202
Cdd:COG1069 144 YVGGIissewfwpKILHLLREDPEVYEAA---DSFVELCD-WITWQLTG-------------SLKRSRCTAghkalwhaH 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 203 WDA-------KMLD-ILDVPREMLP-EVKSSSEIYGR-TKS---------GIAIGGIAGDQQAALFGQMCVEPGQ-AKNt 262
Cdd:COG1069 207 EGGypseeffAALDpLLDGLADRLGtEIYPLGEPAGTlTAEwaarlglppGTAVAVGAIDAHAGAVGAGGVEPGTlVKV- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 263 YGT-GCFLLMNTGDKAVKskhGMlttiaCGP-RGEV---AYALEG---AVfngGSTVQWLRDEL-------KIINDAHDT 327
Cdd:COG1069 286 MGTsTCHMLVSPEERFVP---GI-----CGQvDGSIvpgMWGYEAgqsAV---GDIFAWFVRLLvppleyeKEAEERGIS 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 328 --EYFAGKVK----DSNGVYLVPAFTGLGAPYWDPYARGALFGLTRGVRVDHIIRAALESIAYQTRDVLDAMQQdSGERL 401
Cdd:COG1069 355 lhPLLTEEAAklppGESGLHALDWFNGNRSPLADQRLKGVILGLTLGTDAEDIYRALVEATAFGTRAIIERFEE-EGVPI 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 402 KSLRVDGG-AVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLACGFWGSLEELRGK--AVIEREFEPQLEEAAK- 477
Cdd:COG1069 434 DEIIACGGiATKNPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMAAmgSGFDKVYTPDPENVAVy 513
|
....*
gi 516455773 478 EKLYA 482
Cdd:COG1069 514 DALYA 518
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
9-476 |
3.15e-23 |
|
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: 103.00 E-value: 3.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 9 YIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIFATQSAVMVEALAQAGLHHDQVAAIGITnqre 88
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 89 TT---VVWDK--------VTGRPIYNAIVWQCRRSTEICQQLKRDGHE--QYIsdttGLVTDPYFSGTKLKWILDNVEGS 155
Cdd:cd07782 77 ATcslVVLDAegkpvsvsPSGDDERNVILWMDHRAVEEAERINATGHEvlKYV----GGKISPEMEPPKLLWLKENLPET 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 156 RERARNgelLFGTIDsWLIWKFTGGKTHVTDYTNASRTMLFN-IHTLEWDAKMLDILDvpremLPEVksSSEIYGRtksg 234
Cdd:cd07782 153 WAKAGH---FFDLPD-FLTWKATGSLTRSLCSLVCKWTYLAHeGSEGGWDDDFFKEIG-----LEDL--VEDNFAK---- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 235 iaIGGIAGDQQAALFGQMCV----EPGQAKNT-------------YGT-GCFLLMNTGDKAVKSKHGMLT--TIAC---- 290
Cdd:cd07782 218 --IGSVVLPPGEPVGGGLTAeaakELGLPEGTpvgvslidahaggLGTlGADVGGLPCEADPLTRRLALIcgTSSChmav 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 291 -----------GP---------------------------RGEVAYA--LEGAVFNGGSTVQWLRDELKIIndAHDTEYF 330
Cdd:cd07782 296 spepvfvpgvwGPyysamlpglwlneggqsatgalldhiiETHPAYPelKEEAKAAGKSIYEYLNERLEQL--AEEKGLP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 331 AGKVkdSNGVYLVPAFTGLGAPYWDPYARGALFGLTRGVRVDHIIR---AALESIAYQTRDVLDAMQQdSGERLKSLRVD 407
Cdd:cd07782 374 LAYL--TRDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHIIEAMNA-AGHKIDTIFMC 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516455773 408 GGAVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLACGFWGSLEEL------RGKAVierefEPQLEEAA 476
Cdd:cd07782 451 GGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDAmaamsgPGKVV-----EPNEELKK 520
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
159-466 |
5.27e-21 |
|
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: 95.67 E-value: 5.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 159 ARNGELLFGTIDSWLI------WKFTGGKthVTDYTNASRTMLFNIHTLEWDAKMLDILDVPREMLPEVKSSSEIYGRTK 232
Cdd:cd07771 138 KKEGPELLERADKLLMlpdllnYLLTGEK--VAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 233 SGIA-IGGIAG---------DQQAALfgqMCVePGQAKNTY----GT----GCFLlmntgDKAVKSKHgmlttiacgprg 294
Cdd:cd07771 216 PEVAeELGLKGipviavashDTASAV---AAV-PAEDEDAAfissGTwsliGVEL-----DEPVITEE------------ 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 295 evAYAL----EGAVF---------NGGSTVQWLRDELKIINDAHDTEYFAGKVKDSNGVYLV-----PAF---------- 346
Cdd:cd07771 275 --AFEAgftnEGGADgtirllkniTGLWLLQECRREWEEEGKDYSYDELVALAEEAPPFGAFidpddPRFlnpgdmpeai 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 347 ------TGLGAPYwdpyargalfglTRGvrvdHIIRAALESIAYQTRDVLDAMQQDSGERLKSLRVDGGAVANNFLMQFQ 420
Cdd:cd07771 353 raycreTGQPVPE------------SPG----EIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLT 416
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 516455773 421 ADILGTQVER-PQmrETTALGAAYLAGLACGFWGSLEELRgkAVIER 466
Cdd:cd07771 417 ADATGLPVIAgPV--EATAIGNLLVQLIALGEIKSLEEGR--ELVRN 459
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
352-486 |
1.85e-13 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 72.57 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 352 PYWDPYARGALFGLTRGVRVDHIIRAALESIAYQTRDVLDAMQQdSGERLKSLRVDGG-AVANNFLMQFQADILGTQVER 430
Cdd:PRK04123 391 PLADQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFED-QGVPVEEVIAAGGiARKNPVLMQIYADVLNRPIQV 469
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 516455773 431 PQMRETTALGAAYLAGLACGFWGSLEELRGK--AVIEREFEPQLEEAAK-EKLYAGWQK 486
Cdd:PRK04123 470 VASDQCPALGAAIFAAVAAGAYPDIPEAQQAmaSPVEKTYQPDPENVARyEQLYQEYKQ 528
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
13-476 |
5.34e-12 |
|
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: 67.97 E-value: 5.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 13 LDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQ----AGwVEHDPMEIFATQSAVM-VEAL-------AQAGLHHDQVAA 80
Cdd:cd07776 5 LDLSTQSLKAVVIDSDLKVVAEESVNFDSDLPEygtkGG-VHRDGDGGEVTSPVLMwVEALdllleklKAAGFDFSRVKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 81 IGITNQRETTVVWDKVTGRPIYN-------------------AIVWQCRRSTEICQQL-KRDGHEQYISDTTGlvTDPY- 139
Cdd:cd07776 84 ISGSGQQHGSVYWSKGAESALANldpskslaeqlegafsvpdSPIWMDSSTTKQCRELeKAVGGPEALAKLTG--SRAYe 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 140 -FSGTK-LKWILDNVEGSRERARNGeLL--FGTidSWLIWKFTGgkthvTDYTNASRTMLFNIHTLEWDAKMLDILDVP- 214
Cdd:cd07776 162 rFTGPQiAKIAQTDPEAYENTERIS-LVssFLA--SLLLGRYAP-----IDESDGSGMNLMDIRSRKWSPELLDAATAPd 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 215 -REMLPEVKSSSEIYGRT----------KSGIAIGGIAGDQQAALFGqMCVEPGQAKNTYGTG--CFLLMNTGDKAVKSk 281
Cdd:cd07776 234 lKEKLGELVPSSTVAGGIssyfverygfSPDCLVVAFTGDNPASLAG-LGLEPGDVAVSLGTSdtVFLVLDEPKPGPEG- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 282 HgmlttIACGPRGEVAY-ALegAVF-NGGSTVQWLRDElkiINDAhDTEYFAGKVKDS----NGVylvpaftgLGAPYWD 355
Cdd:cd07776 312 H-----VFANPVDPGSYmAM--LCYkNGSLARERVRDR---YAGG-SWEKFNELLESTppgnNGN--------LGLYFDE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 356 ----PYARGALFGLTRGVRVD------HIIRAALE----SIAYQTRDVLdamqqdSGERLKSLRVDGGAVANNFLMQFQA 421
Cdd:cd07776 373 peitPPVPGGGRRFFGDDGVDaffdpaVEVRAVVEsqflSMRLHAERLG------SDIPPTRILATGGASANKAILQVLA 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455773 422 DILGTQVERPQMRETTALGAAYLA--GLAC---GFWGSLEELRGKAVIEREFEPQLEEAA 476
Cdd:cd07776 447 DVFGAPVYTLDVANSAALGAALRAahGLLCagsGDFSPEFVVFSAEEPKLVAEPDPEAAE 506
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
186-219 |
7.84e-04 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 42.01 E-value: 7.84e-04
10 20 30
....*....|....*....|....*....|....
gi 516455773 186 DYTNASRTMLFNIHTLEWDAKMLDILDVPREMLP 219
Cdd:PRK10640 157 EYTNATTTQLVNINSDDWDESLLAWSGAPKAWFG 190
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
6-83 |
2.83e-03 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 39.88 E-value: 2.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516455773 6 NKNYIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHypqagwveHDPMEIFATQSAVMVEALAQAGLHHDQVAAIGI 83
Cdd:COG1940 3 DAGYVIGIDIGGTKIKAALVDLDGEVLARERIPTPAG--------AGPEAVLEAIAELIEELLAEAGISRGRILGIGI 72
|
|
| |
