|
Name |
Accession |
Description |
Interval |
E-value |
| glpK |
PRK00047 |
glycerol kinase GlpK; |
1-496 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 1098.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 1 METYVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPKPGWVEHNANEIWGSILSVIATSLSESGIKPEQIAGIGITN 80
Cdd:PRK00047 3 MKKYILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 81 QRETAVVWDKNTGQPVYNAIVWQSRQTADICEELKAKGLNDTFREKTGLLIDAYFSGTKVKWILDHVEGAREKAERGELL 160
Cdd:PRK00047 83 QRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRDGYEDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGELL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 161 FGTIDTWLIWKLSGGKAHVTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPSSEIYAHTVPYHFFGQEVPISG 240
Cdd:PRK00047 163 FGTIDTWLVWKLTGGKVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYGFFGGEVPIAG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 241 AAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVASNHGLLTTIAWGLNGKVEYALEGSIFVAGSAIQWLRDGLR 320
Cdd:PRK00047 243 IAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGIDGKVVYALEGSIFVAGSAIQWLRDGLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 321 MLKNAADSEQYAERVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTQKEHFVRATLESLAYQTKDVLTAMEADSGI 400
Cdd:PRK00047 323 IISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADSGI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 401 SLKTLRVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLAVGYWKDQSEIATQWNIDRTFEPSMNEEKRNK 480
Cdd:PRK00047 403 RLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDELKEQWKIDRRFEPQMDEEEREK 482
|
490
....*....|....*.
gi 1229100168 481 LYEGWQKAVKAAMAFK 496
Cdd:PRK00047 483 LYAGWKKAVKRTLAWA 498
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
1-496 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 1059.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 1 METYVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPKPGWVEHNANEIWGSILSVIATSLSESGIKPEQIAGIGITN 80
Cdd:COG0554 1 MKKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 81 QRETAVVWDKNTGQPVYNAIVWQSRQTADICEELKAKGLNDTFREKTGLLIDAYFSGTKVKWILDHVEGAREKAERGELL 160
Cdd:COG0554 81 QRETTVVWDRKTGKPLYNAIVWQDRRTADICEELKADGLEDLIREKTGLVLDPYFSATKIKWILDNVPGARERAEAGELL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 161 FGTIDTWLIWKLSGGKAHVTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPSSEIYAHTVPyHFFGQEVPISG 240
Cdd:COG0554 161 FGTIDSWLIWKLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDP-DLFGAEIPIAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 241 AAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVASNHGLLTTIAWGLNGKVEYALEGSIFVAGSAIQWLRDGLR 320
Cdd:COG0554 240 IAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGGKVTYALEGSIFVAGAAVQWLRDGLG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 321 MLKNAADSEQYAERVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTQKEHFVRATLESLAYQTKDVLTAMEADSGI 400
Cdd:COG0554 320 LIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADSGI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 401 SLKTLRVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLAVGYWKDQSEIATQWNIDRTFEPSMNEEKRNK 480
Cdd:COG0554 400 PLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEELAALWKVDRRFEPQMDEEERER 479
|
490
....*....|....*.
gi 1229100168 481 LYEGWQKAVKAAMAFK 496
Cdd:COG0554 480 LYAGWKKAVERTLGWA 495
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
4-490 |
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: 1005.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPKPGWVEHNANEIWGSILSVIATSLSESGIKPEQIAGIGITNQRE 83
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 84 TAVVWDKNTGQPVYNAIVWQSRQTADICEELKAKGLNDTFREKTGLLIDAYFSGTKVKWILDHVEGAREKAERGELLFGT 163
Cdd:cd07786 81 TTVVWDRETGKPVYNAIVWQDRRTADICEELKAEGHEEMIREKTGLVLDPYFSATKIRWILDNVPGARERAERGELAFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 164 IDTWLIWKLSGGKAHVTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPSSEIYAHTVPYhFFGQEVPISGAAG 243
Cdd:cd07786 161 IDSWLIWKLTGGKVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDPD-LLGAEIPIAGIAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 244 DQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVASNHGLLTTIAWGLNGKVEYALEGSIFVAGSAIQWLRDGLRMLK 323
Cdd:cd07786 240 DQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLGGKVTYALEGSIFIAGAAVQWLRDGLGLIE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 324 NAADSEQYAERVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTQKEHFVRATLESLAYQTKDVLTAMEADSGISLK 403
Cdd:cd07786 320 SAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEADSGIPLK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 404 TLRVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLAVGYWKDQSEIATQWNIDRTFEPSMNEEKRNKLYE 483
Cdd:cd07786 400 ELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAKLWQVDRRFEPSMSEEEREALYA 479
|
....*..
gi 1229100168 484 GWQKAVK 490
Cdd:cd07786 480 GWKKAVK 486
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
4-490 |
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: 991.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPKPGWVEHNANEIWGSILSVIATSLSESGIKPEQIAGIGITNQRE 83
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 84 TAVVWDKNTGQPVYNAIVWQSRQTADICEELKAKGLNDTFREKTGLLIDAYFSGTKVKWILDHVEGAREKAERGELLFGT 163
Cdd:cd07769 81 TTVVWDKKTGKPLYNAIVWQDRRTADICEELKAKGLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAERGELLFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 164 IDTWLIWKLSGGKAHVTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPSSEIYAHTVPYHFfGQEVPISGAAG 243
Cdd:cd07769 161 IDTWLIWKLTGGKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTDPEGL-GAGIPIAGILG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 244 DQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVASNHGLLTTIAWGLNGKVEYALEGSIFVAGSAIQWLRDGLRMLK 323
Cdd:cd07769 240 DQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQIGGKVTYALEGSIFIAGAAIQWLRDNLGLIE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 324 NAADSEQYAERVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTQKEHFVRATLESLAYQTKDVLTAMEADSGISLK 403
Cdd:cd07769 320 DAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDSGIKLK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 404 TLRVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLAVGYWKDQSEIATQWNIDRTFEPSMNEEKRNKLYE 483
Cdd:cd07769 400 ELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDELASLWQVDKRFEPSMDEEERERLYR 479
|
....*..
gi 1229100168 484 GWQKAVK 490
Cdd:cd07769 480 GWKKAVE 486
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
4-495 |
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: 886.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPKPGWVEHNANEIWGSILSVIATSLSESGIKPEQIAGIGITNQRE 83
Cdd:TIGR01311 2 YILAIDQGTTSSRAIVFDKDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAGIKPDDIAAIGITNQRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 84 TAVVWDKNTGQPVYNAIVWQSRQTADICEELKAKGLNDTFREKTGLLIDAYFSGTKVKWILDHVEGAREKAERGELLFGT 163
Cdd:TIGR01311 82 TTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYGEFIREKTGLPLDPYFSATKLRWLLDNVPGVREAAERGELLFGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 164 IDTWLIWKLSGGKAHVTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPSSEIYAHTVPYhFFGQEVPISGAAG 243
Cdd:TIGR01311 162 IDTWLIWNLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYTDPG-LLGAEIPITGVLG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 244 DQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVASNHGLLTTIAWGLNGKV-EYALEGSIFVAGSAIQWLRDGLRML 322
Cdd:TIGR01311 241 DQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKKpVYALEGSVFVAGAAVQWLRDNLKLI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 323 KNAADSEQYAERVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTQKEHFVRATLESLAYQTKDVLTAMEADSGISL 402
Cdd:TIGR01311 321 KHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTRDVLEAMEKDAGVEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 403 KTLRVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLAVGYWKDQSEIATQWNIDRTFEPSMNEEKRNKLY 482
Cdd:TIGR01311 401 TKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWRVEKTFEPEMDEEEREARY 480
|
490
....*....|...
gi 1229100168 483 EGWQKAVKAAMAF 495
Cdd:TIGR01311 481 AGWKEAVKRSLGW 493
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
3-490 |
0e+00 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466802 [Multi-domain] Cd Length: 499 Bit Score: 747.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 3 TYVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPKPGWVEHNANEIWGSILSVI---ATSLSESGIKPEQIAGIGIT 79
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIeeaVEKLKALGISPSDIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 80 NQRETAVVWDKNTGQPVYNAIVWQSRQTADICEELKAK--GLNDTFREKTGLLIDAYFSGTKVKWILDHVEGAREKAERG 157
Cdd:cd07792 81 NQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELSAKtpGGKDHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 158 ELLFGTIDTWLIWKLSGGK---AHVTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPSSEIYAHTVPYHFFGq 234
Cdd:cd07792 161 RLLFGTVDSWLIWNLTGGKnggVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIASGPLAG- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 235 eVPISGAAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVASNHGLLTTIAW--GLNGKVEYALEGSIFVAGSAI 312
Cdd:cd07792 240 -VPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAYklGPDAPPVYALEGSIAIAGAAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 313 QWLRDGLRMLKNAADSEQYAERVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTQKEHFVRATLESLAYQTKDVLT 392
Cdd:cd07792 319 QWLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREILD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 393 AMEADSGISLKTLRVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLAVGYWK-DQSEIATQWNIDRTFEP 471
Cdd:cd07792 399 AMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKsLDELKSLNEGGRTVFEP 478
|
490
....*....|....*....
gi 1229100168 472 SMNEEKRNKLYEGWQKAVK 490
Cdd:cd07792 479 QISEEERERRYKRWKKAVE 497
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
4-496 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 682.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPKPGWVEHNANEIWGSILSVIATSLSESGIKPEQ--IAGIGITNQ 81
Cdd:PTZ00294 3 YIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKGPSfkIKAIGITNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 82 RETAVVWDKNTGQPVYNAIVWQSRQTADICEELKAKGLNDT-FREKTGLLIDAYFSGTKVKWILDHVEGAREKAERGELL 160
Cdd:PTZ00294 83 RETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKYGGSNfFQKITGLPISTYFSAFKIRWMLENVPAVKDAVKEGTLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 161 FGTIDTWLIWKLSGGKAHVTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPSSEIYAHTVPYHFFGQE-VPIS 239
Cdd:PTZ00294 163 FGTIDTWLIWNLTGGKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTISGEAVPLLEgVPIT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 240 GAAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVASNHGLLTTIAW--GLNGKVEYALEGSIFVAGSAIQWLRD 317
Cdd:PTZ00294 243 GCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYqlGPNGPTVYALEGSIAVAGAGVEWLRD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 318 GLRMLKNAADSEQYAERVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTQKEHFVRATLESLAYQTKDVLTAMEAD 397
Cdd:PTZ00294 323 NMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDVIESMEKD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 398 SGISLKTLRVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLAVGYWKDQSEI-ATQWNIDRTFEPSMNEE 476
Cdd:PTZ00294 403 AGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVkKLIRRSNSTFSPQMSAE 482
|
490 500
....*....|....*....|
gi 1229100168 477 KRNKLYEGWQKAVKAAMAFK 496
Cdd:PTZ00294 483 ERKAIYKEWNKAVERSLKWA 502
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
4-489 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 644.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPKPGWVEHNANEIWGSILSVIATSLSESGIK----PEQIAGIGIT 79
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKghnvDSGLKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 80 NQRETAVVWDKNTGQPVYNAIVWQSRQTADICEEL--KAKGLNDTFREKTGLLIDAYFSGTKVKWILDHVEGAREKAERG 157
Cdd:PLN02295 81 NQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLekELSGGRKHFVETCGLPISTYFSATKLLWLLENVDAVKEAVKSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 158 ELLFGTIDTWLIWKLSGGKA---HVTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPSSEIYAHTVPYHFFGQ 234
Cdd:PLN02295 161 DALFGTIDSWLIWNLTGGASggvHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIAKGWPLAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 235 eVPISGAAGDQQAALFGQACfEEGMAKNTYGTGCFMLMNTGEKAVASNHGLLTTIAWGLNGK--VEYALEGSIFVAGSAI 312
Cdd:PLN02295 241 -VPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYKLGPDapTNYALEGSVAIAGAAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 313 QWLRDGLRMLKNAADSEQYAERVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTQKEHFVRATLESLAYQTKDVLT 392
Cdd:PLN02295 319 QWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQVKDVLD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 393 AMEAD-----SGISLKTLRVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLAVGYWKDQSEIATQ-WNID 466
Cdd:PLN02295 399 AMRKDageekSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEEEIFASEkWKNT 478
|
490 500
....*....|....*....|...
gi 1229100168 467 RTFEPSMNEEKRNKLYEGWQKAV 489
Cdd:PLN02295 479 TTFRPKLDEEERAKRYASWCKAV 501
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
4-490 |
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: 603.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPKPGWVEHNANEIWGSILSVIATSLSESGIKPEQIAGIGITNQRE 83
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 84 TAVVWDKNTGQPVYNAIVWQSRQTADICEE----LKAKGLN------DTFREKTGLLIDAYFSGT------KVKWILDHV 147
Cdd:cd07793 81 TFLTWDKKTGKPLHNFITWQDLRAAELCESwnrsLLLKALRggskflHFLTRNKRFLAASVLKFStahvsiRLLWILQNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 148 EGAREKAERGELLFGTIDTWLIWKLSGGKAHVTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPSSEIYAHTV 227
Cdd:cd07793 161 PELKEAAEKGELLFGTIDTWLLWKLTGGKVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFGSTD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 228 PyHFFGQEVPISGAAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVASNHGLLTTIAWGLNGKVEYALEGSIFV 307
Cdd:cd07793 241 P-SIFGAEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGGEITYLAEGNASD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 308 AGSAIQWLRDGLrMLKNAADSEQYAERVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTQKEHFVRATLESLAYQT 387
Cdd:cd07793 320 TGTVIDWAKSIG-LFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIAFRV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 388 KDVLTAMEADSGISLKTLRVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLAVGYWKDQSEIATQWNIDR 467
Cdd:cd07793 399 KQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEELKKLRKIEK 478
|
490 500
....*....|....*....|...
gi 1229100168 468 TFEPSMNEEKRNKLYEGWQKAVK 490
Cdd:cd07793 479 IFEPKMDNEKREELYKNWKKAVK 501
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
3-491 |
6.30e-125 |
|
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: 373.40 E-value: 6.30e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 3 TYVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPKPGWVEHNANEIWGSILSVIATSLSESGIKPEQIAGIGITNQR 82
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 83 ETAVVWDKNtGQPVYNAIVWQSRQTADICEELKAKGLNDTFREKTGLLIDAYFSGTKVKWILDHVEGAREKAERgellFG 162
Cdd:COG1070 81 HGLVLLDAD-GEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAK----VL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 163 TIDTWLIWKLSGgkAHVTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPSSEIyAHTVPYHF-----FGQEVP 237
Cdd:COG1070 156 LPKDYLRYRLTG--EFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEV-AGTLTAEAaaetgLPAGTP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 238 ISGAAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTgEKAVASNHGLLTTIAWGLNGKveYALEGSIFVAGSAIQWLRD 317
Cdd:COG1070 233 VVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVS-DKPLPDPEGRVHTFCHAVPGR--WLPMGATNNGGSALRWFRD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 318 --GLRMLKNAADSEQYAERVE-STDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTQKEHFVRATLESLAYQTKDVLTAM 394
Cdd:COG1070 310 lfADGELDDYEELNALAAEVPpGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEAL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 395 EAdSGISLKTLRVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLAVGYWKDQSEIATQW-NIDRTFEPSM 473
Cdd:COG1070 390 EE-AGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMvRVGETIEPDP 468
|
490
....*....|....*....
gi 1229100168 474 NEEKR-NKLYEGWQKAVKA 491
Cdd:COG1070 469 ENVAAyDELYERYRELYPA 487
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
4-482 |
9.72e-118 |
|
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466798 [Multi-domain] Cd Length: 433 Bit Score: 352.98 E-value: 9.72e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPKPGWVEHNANEIWGSILSVIATSLSESGIKPEQIAGIGITNQRE 83
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 84 TAVVWDKNtGQPVYNAIVWQSRQTADICeelkakglndtfrektgllidayfsgtkvkwildhvegarekaergellfgT 163
Cdd:cd07779 81 TFVPVDED-GRPLRPAISWQDKRTAKFL---------------------------------------------------T 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 164 IDTWLIWKLSGGkaHVTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPSSEIYAHTVPY---HF-FGQEVPIS 239
Cdd:cd07779 109 VQDYLLYRLTGE--FVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEaaeETgLPEGTPVV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 240 GAAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVASNHGLLTTIAwGLNGKveYALEGSIFVAGSAIQWLRD-- 317
Cdd:cd07779 187 AGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPS-AVPGK--WVLEGSINTGGSAVRWFRDef 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 318 -GLRMLKNAADSEQYA---ERVEST----DGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTQKEHFVRATLESLAYQTKD 389
Cdd:cd07779 264 gQDEVAEKELGVSPYEllnEEAAKSppgsDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELRD 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 390 VLTAMEaDSGISLKTLRVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLAVGYWKDQSEIATQW-NIDRT 468
Cdd:cd07779 344 NLEAME-KAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAMvRVTDT 422
|
490
....*....|....
gi 1229100168 469 FEPsmNEEKRnKLY 482
Cdd:cd07779 423 FEP--DPENV-AIY 433
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
4-251 |
9.24e-115 |
|
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.
Pssm-ID: 395295 [Multi-domain] Cd Length: 245 Bit Score: 338.16 E-value: 9.24e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPKPGWVEHNANEIWGSILSVIATSLSESGIKPEQIAGIGITNQRE 83
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 84 TAVVWDKNTgQPVYNAIVWQSRQTADICEELKAKGLNDTFREKTGLLIDAYFSGTKVKWILDHVEGAREKAErgelLFGT 163
Cdd:pfam00370 81 GTVLLDKND-KPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIH----KFLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 164 IDTWLIWKLSGgkAHVTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPSSEIYAHTVPYHFFG----QEVPIS 239
Cdd:pfam00370 156 IHDYLRWRLTG--VFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMwgldEGVPVV 233
|
250
....*....|..
gi 1229100168 240 GAAGDQQAALFG 251
Cdd:pfam00370 234 GGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
4-446 |
4.35e-108 |
|
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: 326.83 E-value: 4.35e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPKPGWVEHNANEIWGSILSVIATSLSESGIKPEQIAGIGITNQRE 83
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 84 TAVVWDKNtGQPVYNAIVWqsrqtadiceelkakglndtfrektgllidayfsgtkvkwiLDHvegaREKaergellFGT 163
Cdd:cd00366 81 GVVLVDAD-GNPLRPAIIW-----------------------------------------LDR----RAK-------FLQ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 164 IDTWLIWKLSGgkAHVTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPSSEIYAHTVPYHF----FGQEVPIS 239
Cdd:cd00366 108 PNDYIVFRLTG--EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAAeetgLPAGTPVV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 240 GAAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVAsnHGLLTTIAWGLNGKveYALEGSIFVAGSAIQWLRDGL 319
Cdd:cd00366 186 AGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVPP--DPRLLNRCHVVPGL--WLLEGAINTGGASLRWFRDEF 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 320 -RMLKNAADSEQYAERVEST----DGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTQKEHFVRATLESLAYQTKDVLTAM 394
Cdd:cd00366 262 gEEEDSDAEYEGLDELAAEVppgsDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEIL 341
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1229100168 395 EADsGISLKTLRVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLA 446
Cdd:cd00366 342 EEL-GVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
4-451 |
2.73e-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: 321.46 E-value: 2.73e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPKPGWVEHNANEIWGSILSVIATSLSESGikPEQIAGIGITNQRE 83
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAG--PDPIAAISVSSQGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 84 TAVVWDKNtGQPVYNAIVWQSRQTADICEELKAKGLNDTFREKTGLLIDAYFSGTKVKWILDHVEGAREKAERgellFGT 163
Cdd:cd07773 79 SGVPVDRD-GEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAK----WLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 164 IDTWLIWKLSGgkAHVTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPSSEI-------YAHTVPyhfFGQEV 236
Cdd:cd07773 154 VADYIAYRLTG--EPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVigtvtpeAAEELG---LPAGT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 237 PISGAAGDQQAALFGQACFEEGMAKNTYGTG-CFMLMNTGEKAVASNHGLLTTIAWGLNGKVeYALEGSIfVAGSAIQWL 315
Cdd:cd07773 229 PVVVGGHDHLCAALGAGVIEPGDVLDSTGTAeALLAVVDEPPLDEMLAEGGLSYGHHVPGGY-YYLAGSL-PGGALLEWF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 316 RD--GLRMLKNAADSEQYAERVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTQKEHFVRATLESLAYQTKDVLTA 393
Cdd:cd07773 307 RDlfGGDESDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEA 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1229100168 394 MEAdSGISLKTLRVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLAVG 451
Cdd:cd07773 387 LEK-AGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
4-488 |
3.70e-96 |
|
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: 299.07 E-value: 3.70e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPKPGWVEHNANEIWGSILSVIATSLSESGIKPEQIAGIGITNQRE 83
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 84 TAVVWDKNtGQPVYNAIVWQSRQTADICEELKAKgLNDTFREKTGLLIDAYFSGTKVKWILDHVEGAREKAERgeLLFGT 163
Cdd:cd07808 81 GLVLLDKN-GRPLRPAILWNDQRSAAECEELEAR-LGDEILIITGNPPLPGFTLPKLLWLKENEPEIFARIRK--ILLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 164 iDtWLIWKLSGgkAHVTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPSSEIyAHTVPYHF---FG--QEVPI 238
Cdd:cd07808 157 -D-YLRYRLTG--ELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEI-VGTLTPEAaeeLGlpEGTPV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 239 SGAAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTgEKAVASNHGLLTTIAWGLNGKvEYALeGSIFVAGSAIQWLRDG 318
Cdd:cd07808 232 VAGAGDNAAAALGAGVVEPGDALISLGTSGVVFAPT-DKPVPDPKGRLHTFPHAVPGK-WYAM-GVTLSAGLSLRWLRDL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 319 LRMLKNAADS-EQYAERVE-STDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTQKEHFVRATLESLAYQTKDVLTAMEa 396
Cdd:cd07808 309 FGPDRESFDElDAEAAKVPpGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVLK- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 397 DSGISLKTLRVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLAVGYWKDQSEIATQWN-IDRTFEPSMNE 475
Cdd:cd07808 388 ELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACIkIEKTIEPDPER 467
|
490
....*....|....
gi 1229100168 476 EKR-NKLYEGWQKA 488
Cdd:cd07808 468 HEAyDELYARYREL 481
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
4-483 |
6.28e-92 |
|
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: 288.26 E-value: 6.28e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPKPGWVEHNANEIWGSILSVIATSLSESGIKPEQIAGIGITNQRE 83
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 84 TAVVWDKNtGQPVYNAIVWQSRQTADICEELKAKGLNDTFREKTGL-LIDAYFSGTKVKWILDHvegAREKAERGELLFG 162
Cdd:cd07805 81 GVVPVDKD-GNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLGGGnPPSGKDPLAKILWLKEN---EPEIYAKTHKFLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 163 TIDtWLIWKLSGgkAHVTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPSSEIyAHTV----------Pyhff 232
Cdd:cd07805 157 AKD-YLNFRLTG--RAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEV-VGELtpeaaaelglP---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 233 gQEVPISGAAGDQQAALFGQACFEEGMAkNTY-GTGCFMLMNTGEKAVASNHGlLTTIAWGLNGKveYALEGSIFVAGSA 311
Cdd:cd07805 229 -AGTPVVGGGGDAAAAALGAGAVEEGDA-HIYlGTSGWVAAHVPKPKTDPDHG-IFTLASADPGR--YLLAAEQETAGGA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 312 IQWLRDGLRMLKNAADS-----EQYAERVE-STDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTQKEHFVRATLESLAY 385
Cdd:cd07805 304 LEWARDNLGGDEDLGADdyellDELAAEAPpGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 386 QTKDVLTAMEADSGiSLKTLRVDGGAVKNNFLMQFQSDLLGVPVERPVV-NETTALGAAYLAGLAVGYWKDQSEIATQWN 464
Cdd:cd07805 384 NLRWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVPENpQEAGALGAALLAAVGLGLLKSFDEAKALVK 462
|
490 500
....*....|....*....|
gi 1229100168 465 IDRTFEPSM-NEEKRNKLYE 483
Cdd:cd07805 463 VEKVFEPDPeNRARYDRLYE 482
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
4-451 |
1.23e-86 |
|
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Rhodospirillum rubrum xylulose kinase (RrXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466806 [Multi-domain] Cd Length: 451 Bit Score: 273.63 E-value: 1.23e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPKPGWVEHNANEIWGSILSVIATSLSESGIKPEQIAGIGITNQRE 83
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 84 TAVVWDKNtGQPVYNAIVWQSRQTADICEELKAKGLNDTFREKTGLLIDAYFSGTKVKWILDHvegAREKAERGELLFgT 163
Cdd:cd07804 81 ALVPVDEN-GKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSQSVGPKLLWIKRN---EPEVFKKTRKFL-G 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 164 IDTWLIWKLSGgkAHVTDYSNASRT-LMFNIHELKWDDELLEILTVPKSMLPEVRPSSEIYAHTVPyhffgqEV------ 236
Cdd:cd07804 156 AYDYIVYKLTG--EYVIDYSSAGNEgGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTK------EAaeetgl 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 237 ----PISGAAGDQQAALFGQACFEEG--MAKntYGTGCFMLMNTGEKAVASNHGLLTTIAWGLngkveYALEGSIFVAGS 310
Cdd:cd07804 228 aegtPVVAGTVDAAASALSAGVVEPGdlLLM--LGTAGDIGVVTDKLPTDPRLWLDYHDIPGT-----YVLNGGMATSGS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 311 AIQWLRDGL-RMLKNAADS------EQYAERVEST----DGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTQKEHFVRAT 379
Cdd:cd07804 301 LLRWFRDEFaGEEVEAEKSggdsayDLLDEEAEKIppgsDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRAL 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229100168 380 LESLAYQTKDVLTAMEaDSGISLKTLRVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLAVG 451
Cdd:cd07804 381 LEGVAYGLRHHLEVIR-EAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
4-487 |
1.14e-84 |
|
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: 269.04 E-value: 1.14e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPKPGWVEHNANEIWGSILSVIATSLSESGikPEQIAGIGITNQRE 83
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLG--GGEVDAIGFSSAMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 84 TAVVWDKNtGQPVYNAIVWQSRQTADICEELKAKGLNDTFREKTGLLIDAYFSGTKVKWILDHVEGAREKAERgellFGT 163
Cdd:cd07770 79 SLLGVDED-GEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAAK----FVS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 164 IDTWLIWKLSGgkAHVTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPSSEIYAHTVPY--HFFG--QEVPIS 239
Cdd:cd07770 154 IKEYLLYRLTG--ELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEfaERLGllAGTPVV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 240 GAAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVASNHGLLTtiawglngkveYALEGSIFVAGSAI------- 312
Cdd:cd07770 232 LGASDGALANLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPGRLWC-----------YRLDENRWLVGGAInnggnvl 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 313 QWLRDGLRMLKNA-ADSEQYAERVEST-DGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTQKEHFVRATLESLAYQTKDV 390
Cdd:cd07770 301 DWLRDTLLLSGDDyEELDKLAEAVPPGsHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 391 LTAMEaDSGISLKTLRVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLAVGYWKDQsEIATQWNIDRTFE 470
Cdd:cd07770 381 YEALE-ELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSL-EADELVKIGKVVE 458
|
490
....*....|....*...
gi 1229100168 471 PSMNEEKR-NKLYEGWQK 487
Cdd:cd07770 459 PDPENHAIyAELYERFKK 476
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
4-450 |
1.56e-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: 1.56e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPKPGWVEHNANEIWGSILSVIATSLSEsgIKPEQIAGIGITNQRE 83
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAE--LRPRRVVAIAVDGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 84 TAVVWDKNtGQPVYNAIVWQSRQTADICEELKAKGLNdtFREKTGLLIDAYFSGTKVKWILDHVEGAREKAERgeLLFGT 163
Cdd:cd07783 79 TLVLVDRE-GEPLRPAIMYNDARAVAEAEELAEAAGA--VAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAK--FLHQA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 164 idTWLIWKLSGGKAhVTDYSNASRTLmFNIHELKWDDELLEILTVPKSMLPEVRPSSEIYAHT---VPYHF-FGQEVPIS 239
Cdd:cd07783 154 --DWLAGRLTGDRG-VTDYNNALKLG-YDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLtaeAAEELgLPAGTPVV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 240 GAAGDQQAALFGQACFEEGMAKNTYGTG-CFMLmnTGEKAVASNHGLLTT--IAWGLngkveYALEGSIFVAGSAIQWLR 316
Cdd:cd07783 230 AGTTDSIAAFLASGAVRPGDAVTSLGTTlVLKL--LSDKRVPDPGGGVYShrHGDGY-----WLVGGASNTGGAVLRWFF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 317 DglrmLKNAADSEQYAERvESTDGVYVVPaFVGLG--TPYWDSDVRGAIfgLTRGTQKEHFVRATLESLAYQTKDVLTAM 394
Cdd:cd07783 303 S----DDELAELSAQADP-PGPSGLIYYP-LPLRGerFPFWDPDARGFL--LPRPHDRAEFLRALLEGIAFIERLGYERL 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1229100168 395 EADSGISLKTLRVDGGAVKNNFLMQFQSDLLGVPVERPvVNETTALGAAYLAGLAV 450
Cdd:cd07783 375 EELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIA-EEEEAALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
4-451 |
1.17e-62 |
|
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: 210.49 E-value: 1.17e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPKPGWVEHNANEIWGSILSVIATSLSESGIKPEQIAGIGITNQRE 83
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 84 TAVVWDKNtGQPVYNAIVWQSRQTADICEELKAKGLNDTFREKTGLLIdayFSGTKV---KWILDHvegAREKAERgell 160
Cdd:cd07802 81 GLYLVDKD-GKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPL---WPGQPVallRWLKEN---EPERYDR---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 161 fgtIDT------WLIWKLSGgkAHVTDYSNASrTLMFNIHELKWDDELLEILTVP--KSMLPEVRPSSEIyAHTV----- 227
Cdd:cd07802 150 ---IRTvlfckdWIRYRLTG--EISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEI-AGRVtaeaa 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 228 -----PyhffgQEVPISGAAGDQQAALFGQACFEEGMAKNTYGTGCfmlMNTGE-KAVASNHGLLTTIAWGLNGKVeYAL 301
Cdd:cd07802 223 altglP-----EGTPVAAGAFDVVASALGAGAVDEGQLCVILGTWS---INEVVtDEPVVPDSVGSNSLHADPGLY-LIV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 302 EGSIfVAGSAIQWLRD---GLRMLKNAADSEQYAERVES----TDGVYVVPaFVgLGTPYwDSDVRGAIFGLTRGTQKEH 374
Cdd:cd07802 294 EASP-TSASNLDWFLDtllGEEKEAGGSDYDELDELIAAvppgSSGVIFLP-YL-YGSGA-NPNARGGFFGLTAWHTRAH 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229100168 375 FVRATLESLAYQTKDVLTAMeaDSGISLKTLRVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLAVG 451
Cdd:cd07802 370 LLRAVYEGIAFSHRDHLERL--LVARKPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
4-451 |
7.74e-60 |
|
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: 203.22 E-value: 7.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPK--PGWVEHNANEIWGSILSVIATSLSESGIKPEQIAGIGITNQ 81
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDdyPDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 82 RETAVVWDKNtGQPVY---N----AIVWQSRQTADICEELKAKglndtfrekTGLLIDAYFSGTKVKWILDHVEGAREKA 154
Cdd:cd07798 81 REGIVFLDKD-GRELYagpNidarGVEEAAEIDDEFGEEIYTT---------TGHWPTELFPAARLLWFKENRPEIFERI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 155 ERgellFGTIDTWLIWKLSGGKahVTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPS----SEIYAHTVPYH 230
Cdd:cd07798 151 AT----VLSISDWIGYRLTGEL--VSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSgtvlGTVSEEAAREL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 231 FFGQEVPISGAAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVASNHGLLTTiAWGLNGKveYALEGSIFVAGS 310
Cdd:cd07798 225 GLPEGTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTG-CHLVPGK--WVLESNAGVTGL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 311 AIQWLRDGLrmLKNAADS-----EQYAERVESTDGVYvvpAFVGLGTPYWDSDV--RGAIF----GLTRGTQKEHFVRAT 379
Cdd:cd07798 302 NYQWLKELL--YGDPEDSyevleEEASEIPPGANGVL---AFLGPQIFDARLSGlkNGGFLfptpLSASELTRGDFARAI 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229100168 380 LESLAYQTKDVLTAMEADSGISLKTLRVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLAVG 451
Cdd:cd07798 377 LENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
260-449 |
1.56e-51 |
|
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: 173.66 E-value: 1.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 260 AKNTYGTGCFMLMnTGEKAVASNHGLLTTIAwGLNGKVEYALEGSIFVAGSAIQWLRDGLRMLKNAADSE------QYAE 333
Cdd:pfam02782 1 LAISAGTSSFVLV-ETPEPVLSVHGVWGPYT-NEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRDAGnveslaELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 334 RVESTD--GVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTQKEHFVRATLESLAYQTKDVLTAMEADSGISLKTLRVDGGA 411
Cdd:pfam02782 79 LAAVAPagGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSGGG 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1229100168 412 VKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLA 449
Cdd:pfam02782 159 SRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
4-451 |
4.36e-51 |
|
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: 180.05 E-value: 4.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFN-KKGEIVHISQKEFAQYFPKPGWVEHNANEIWGSILSVIATSLSESGIKPEQIAGIGITNQR 82
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 83 ETAVVWDKNtGQPVYNAIVWQSRQTADICEELKAKgLNDTFREKTGLLIDAYFSGTKVKWILDHVEGAREKAERGELLFG 162
Cdd:cd07809 81 HGLVALDAD-GKVLRPAKLWCDTRTAPEAEELTEA-LGGKKCLLVGLNIPARFTASKLLWLKENEPEHYARIAKILLPHD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 163 tidtWLIWKLSGGKahVTDYSNASRTLMFNIHELKWDDELLEILTV---PKSMLPEVRPSSEIYAHTVPYH--FFG--QE 235
Cdd:cd07809 159 ----YLNWKLTGEK--VTGLGDASGTFPIDPRTRDYDAELLAAIDPsrdLRDLLPEVLPAGEVAGRLTPEGaeELGlpAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 236 VPISGAAGDQQAALFGQACFEEGMAKNTYGT-GCfmLMNTGEKAVASNHGLLTT-----IAW-----GLNgkveyalegs 304
Cdd:cd07809 233 IPVAPGEGDNMTGALGTGVVNPGTVAVSLGTsGT--AYGVSDKPVSDPHGRVATfcdstGGMlplinTTN---------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 305 ifVAGSAIQWLRDGLRMLKNAADSEQYAERVEStDGVYVVPAFVGLGTPYWdSDVRGAIFGLTRG-TQKEHFVRATLESL 383
Cdd:cd07809 301 --CLTAWTELFRELLGVSYEELDELAAQAPPGA-GGLLLLPFLNGERTPNL-PHGRASLVGLTLSnFTRANLARAALEGA 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229100168 384 AYQTKDVLTAMEADsGISLKTLRVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLAVG 451
Cdd:cd07809 377 TFGLRYGLDILREL-GVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
4-483 |
2.49e-50 |
|
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: 179.27 E-value: 2.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFN-KKGEIVHISQKEFAQYF--PKPGWVEHNANEIWGSILSVIATSLSESGIKPEQIAGIGITN 80
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 81 QRETAVVWDKNtGQPVYNAIVWQ----SRQTADICEelKAKGLNDTFREKTGLLIDA--YFSgtKVKWILDHVEGAREKA 154
Cdd:cd07781 81 TSSTVVPVDED-GNPLAPAILWMdhraQEEAAEINE--TAHPALEYYLAYYGGVYSSewMWP--KALWLKRNAPEVYDAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 155 ER-GELlfgtIDtWLIWKLSGG-KAHVtdySNASRTLMFNIHELKWDDELLE-----ILTVPKSMLPEVRPSSEIYAHTV 227
Cdd:cd07781 156 YTiVEA----CD-WINARLTGRwVRSR---CAAGHKWMYNEWGGGPPREFLAaldpgLLKLREKLPGEVVPVGEPAGTLT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 228 PYH--FFG--QEVPISGAAGDQQAALFGQACFEEG-MAKNTyGT-GCFMLMNTGEKAVAsnhgllttiawGLNGKVE--- 298
Cdd:cd07781 228 AEAaeRLGlpAGIPVAQGGIDAHMGAIGAGVVEPGtLALIM-GTsTCHLMVSPKPVDIP-----------GICGPVPdav 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 299 ----YALEGSIFVAGSAIQWLRDGLRMLKNAADSEQY------AERVE-STDGVYVVPAFVGLGTPYWDSDVRGAIFGLT 367
Cdd:cd07781 296 vpglYGLEAGQSAVGDIFAWFVRLFVPPAEERGDSIYallseeAAKLPpGESGLVALDWFNGNRTPLVDPRLRGAIVGLT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 368 RGTQKEHFVRATLESLAYQTKDVLTAMEaDSGISLKTLRVDGG-AVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLA 446
Cdd:cd07781 376 LGTTPAHIYRALLEATAFGTRAIIERFE-EAGVPVNRVVACGGiAEKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILA 454
|
490 500 510
....*....|....*....|....*....|....*....
gi 1229100168 447 GLAVGYWKDQSEIATQW-NIDRTFEPSM-NEEKRNKLYE 483
Cdd:cd07781 455 AVAAGVYADIEEAADAMvRVDRVYEPDPeNHAVYEELYA 493
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
4-485 |
6.09e-48 |
|
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: 172.52 E-value: 6.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQ-YFPK-PGWVEHNANEIWGSILSVIATSLSESGIKPEQIAGIGITNQ 81
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREWRHkEVPDvPGSMDFDTEKNWKLICECIREALKKAGIAPKSIAAISTTSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 82 RETAVVWDKNtGQPVY---NAIVWQSRQTadicEELKAK--GLNDTFREKTG--LLIDAyfsGTKVKWILDHVEGAREKA 154
Cdd:cd07775 81 REGIVLYDNE-GEEIWacaNVDARAAEEV----SELKELynTLEEEVYRISGqtFALGA---IPRLLWLKNNRPEIYRKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 155 ERgellFGTIDTWLIWKLSGgkAHVTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPSSEIYAHTVPYHFF-- 232
Cdd:cd07775 153 AK----ITMLSDWIAYKLSG--ELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEAAEet 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 233 --GQEVPISGAAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVASNhGLLTTIAWGLNGKVEYalEGSIFVAGS 310
Cdd:cd07775 227 glKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPA-MNIRVNCHVIPDMWQA--EGISFFPGL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 311 AIQWLRDGL---------RMLKNAADS-EQYAERVEStdGVY-VVPAFvglgtpywdSDVRG---------AIFGLT--- 367
Cdd:cd07775 304 VMRWFRDAFcaeekeiaeRLGIDAYDLlEEMAKDVPP--GSYgIMPIF---------SDVMNyknwrhaapSFLNLDidp 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 368 RGTQKEHFVRATLESLAYQTKDVLTAMEADSGISLKTLRVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAG 447
Cdd:cd07775 373 EKCNKATFFRAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAG 452
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1229100168 448 LAVGYWKDQSEIATQW-NIDRTFEPSM-NEEKRNKLYEGW 485
Cdd:cd07775 453 VGAGIYSSLEEAVESLvKWEREYLPNPeNHEVYQDLYEKW 492
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
4-451 |
8.82e-46 |
|
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: 165.88 E-value: 8.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPKPGWVEHNANEIWGSILSVIATSLSESGIKPEQIAGIGITNQRE 83
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 84 TAVVWDKNtGQPVYNAIVWQSRQTADICEELKAKGLNDTFREKTGLLIDAYFSGTKVKWILDHvegAREKAERGELLFGT 163
Cdd:cd24121 81 GTWLVDED-GRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKEN---EPERLERARTALHC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 164 IDtWLIWKLSGgkAHVTDYSNASRTlMFNIHELKWDDELLEILTVP--KSMLPEVRPSSEIYAHTVPYHF----FGQEVP 237
Cdd:cd24121 157 KD-WLFYKLTG--EIATDPSDASLT-FLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAAaatgLPAGTP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 238 ISGAAGDQQAALFGQACFEEGMAKNTYGTGCF--MLMNtgeKAVASNHGLLTTIAWGLNGKVEYALegSIFVAGSAIQWL 315
Cdd:cd24121 233 VVLGPFDVVATALGSGAIEPGDACSILGTTGVheVVVD---EPDLEPEGVGYTICLGVPGRWLRAM--ANMAGTPNLDWF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 316 RDGL------RMLKNAADSEQYAERVES-----TDGV----YVVPAfvGLGTPYWDSDVRGAIFGLTRGTQKEHFVRATL 380
Cdd:cd24121 308 LRELgevlkeGAEPAGSDLFQDLEELAAssppgAEGVlyhpYLSPA--GERAPFVNPNARAQFTGLSLEHTRADLLRAVY 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229100168 381 ESLAYQTKDVLTAMeadsGISLKTLRVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLAVG 451
Cdd:cd24121 386 EGVALAMRDCYEHM----GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
4-446 |
2.62e-41 |
|
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: 153.15 E-value: 2.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFN-KKGEIVHISQKEFAQYFPK--PGWVEHNANEIWGSILSVIATSLSESGIKpeqIAGIGITN 80
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDlESGRILESVSRPTPAPISSddPGRSEQDPEKILEAVRNLIDELPREYLSD---VTGIGITG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 81 QRETAVVWDKNtGQPVYNAIVWQ-SRQTADICEELKAKGLNdtFREKTGLLIDAYFSGTKVKWILDHvEGAREKAERgel 159
Cdd:cd07777 78 QMHGIVLWDED-GNPVSPLITWQdQRCSEEFLGGLSTYGEE--LLPKSGMRLKPGYGLATLFWLLRN-GPLPSKADR--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 160 lFGTIDTWLIWKLSGGKAHVTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPSSEIYAHTVpyHFFGQEVPIS 239
Cdd:cd07777 151 -AGTIGDYIVARLTGLPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLS--SALPKGIPVY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 240 GAAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTgEKAVASNH---------GLLTTIAwGLNGkveyalegsifvaGS 310
Cdd:cd07777 228 VALGDNQASVLGSGLNEENDAVLNIGTGAQLSFLT-PKFELSGSveirpffdgRYLLVAA-SLPG-------------GR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 311 AIQWL----RDGLRMLKNAADSEQ-Y-----AERVESTDGVYVVPAFvgLGTPyWDSDVRGAIFGLTRGTQK-EHFVRAT 379
Cdd:cd07777 293 ALAVLvdflREWLRELGGSLSDDEiWekldeLAESEESSDLSVDPTF--FGER-HDPEGRGSITNIGESNFTlGNLFRAL 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229100168 380 LESLAYQTKDVLTAMEADSGiSLKTLRVDGGAV-KNNFLMQFQSDLLGVPVERPVVNETTALGAAYLA 446
Cdd:cd07777 370 CRGIAENLHEMLPRLDLDLS-GIERIVGSGGALrKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
1-488 |
1.18e-31 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 127.43 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 1 METYVLALDQGTTSSRAIIFNKKGEIVHISQKEFaQYFPKPGW-------VEHNaneiWGSILSVIATSLSESGIKPEQI 73
Cdd:PRK10939 1 SMSYLMALDAGTGSIRAVIFDLNGNQIAVGQAEW-RHLAVPDVpgsmefdLEKN----WQLACQCIRQALQKAGIPASDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 74 AGIGITNQRETAVVWDKNtGQPVYNAIVWQSRQTADIcEELKAkgLNDTFREktglliDAY-FSGT--------KVKWIL 144
Cdd:PRK10939 76 AAVSATSMREGIVLYDRN-GTEIWACANVDARASREV-SELKE--LHNNFEE------EVYrCSGQtlalgalpRLLWLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 145 DHVEGAREKAERgellFGTIDTWLIWKLSGGKAhvTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPSSEIYA 224
Cdd:PRK10939 146 HHRPDIYRQAHT----ITMISDWIAYMLSGELA--VDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 225 HTvpyhffGQEV----------PISGAAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVASNHGLLTTiAWGLN 294
Cdd:PRK10939 220 HV------TAKAaaetglragtPVVMGGGDVQLGCLGLGVVRPGQTAVLGGTFWQQVVNLPAPVTDPNMNIRIN-PHVIP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 295 GKVEYalEGSIFVAGSAIQWLRDGL-RMLKNAADS---------EQYAERVEStdGVYVV-----------------PAF 347
Cdd:PRK10939 293 GMVQA--ESISFFTGLTMRWFRDAFcAEEKLLAERlgidaysllEEMASRVPV--GSHGIipifsdvmrfkswyhaaPSF 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 348 VGLGTpywDSDV--RGAIFgltrgtqkehfvRATLESLAYQTKDVLTAMEADSGISLKTLRVDGGAVKNNFLMQFQSDLL 425
Cdd:PRK10939 369 INLSI---DPEKcnKATLF------------RALEENAAIVSACNLQQIAAFSGVFPSSLVFAGGGSKGKLWSQILADVT 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229100168 426 GVPVERPVVNETTALGAAYLAGLAVGYWKDQSEIATQW-NIDRTFEPSM-NEEKRNKLYEGWQKA 488
Cdd:PRK10939 434 GLPVKVPVVKEATALGCAIAAGVGAGIYSSLAETGERLvRWERTFEPNPeNHELYQEAKEKWQAV 498
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
6-471 |
2.50e-30 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 123.15 E-value: 2.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 6 LALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPKPGWVEHNANEIWgsilsvIATSLSESGIKPEQ----IAGIGITNQ 81
Cdd:PRK15027 3 IGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWW------QATDRAMKALGDQHslqdVKALGIAGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 82 RETAVVWDKNTgQPVYNAIVWQSRQTADICEELKAKGlnDTFREKTGLLIDAYFSGTKVKWIldhvegAREKAErgelLF 161
Cdd:PRK15027 77 MHGATLLDAQQ-RVLRPAILWNDGRCAQECALLEARV--PQSRVITGNLMMPGFTAPKLLWV------QRHEPE----IF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 162 GTIDTWLIWK------LSGGKAhvTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPSSEIYAHTVP--YHFFG 233
Cdd:PRK15027 144 RQIDKVLLPKdylrlrMTGEFA--SDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPevAKAWG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 234 Q-EVPISGAAGDQQAALFGQACFEEGMAKNTYGT-GCFMLMNTG-----EKAVASnhgllttIAWGLNGKveYALEGSIF 306
Cdd:PRK15027 222 MaTVPVVAGGGDNAAGAVGVGMVDANQAMLSLGTsGVYFAVSEGflskpESAVHS-------FCHALPQR--WHLMSVML 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 307 VAGSAIQWLRD--GLRMLKNAADSEQYAErvESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTQKEHFVRATLESLA 384
Cdd:PRK15027 293 SAASCLDWAAKltGLSNVPALIAAAQQAD--ESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 385 YQTKDVLTAMEAdSGISLKTLRVDGGAVKNNFLMQFQSDLLGVPVE-RPVVNETTALGAAYLAGLAVGYWKDQSEIATQW 463
Cdd:PRK15027 371 YALADGMDVVHA-CGIKPQSVTLIGGGARSEYWRQMLADISGQQLDyRTGGDVGPALGAARLAQIAANPEKSLIELLPQL 449
|
....*...
gi 1229100168 464 NIDRTFEP 471
Cdd:PRK15027 450 PLEQSHLP 457
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
4-483 |
2.68e-29 |
|
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: 120.72 E-value: 2.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFNKKGEIVHISQKEFAQYFPKPGWVEHNANEIWGSILSVIATSLSESGIKPEQIAGIGITnqre 83
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 84 tA----VVWDKN--------TGQPVYNAIVWQ----SRQTADIceelkakglNDTFREktgLLidAYFSGT--------K 139
Cdd:cd07782 77 -AtcslVVLDAEgkpvsvspSGDDERNVILWMdhraVEEAERI---------NATGHE---VL--KYVGGKispemeppK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 140 VKWILDHVEGAREKAERgelLFGTIDtWLIWKLSGGKAHvtdySNASRT-----LMFNIHELKWDDELLEILTvpksmLP 214
Cdd:cd07782 142 LLWLKENLPETWAKAGH---FFDLPD-FLTWKATGSLTR----SLCSLVckwtyLAHEGSEGGWDDDFFKEIG-----LE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 215 EVrpSSEIYAHtvpyhfFGQEVPISGAAGDQqaALFGQACFEEGMAKNT---------Y----GT-GCFMLMNTGEKAVA 280
Cdd:cd07782 209 DL--VEDNFAK------IGSVVLPPGEPVGG--GLTAEAAKELGLPEGTpvgvslidaHagglGTlGADVGGLPCEADPL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 281 SNHglLTTIA-------------------WG-----------LNgkveyalEGSIFVAGSAIQWLrdgLRM------LKN 324
Cdd:cd07782 279 TRR--LALICgtsschmavspepvfvpgvWGpyysamlpglwLN-------EGGQSATGALLDHI---IEThpaypeLKE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 325 AADSEQY------AERVES------------TDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTQKEHFVR---ATLESL 383
Cdd:cd07782 347 EAKAAGKsiyeylNERLEQlaeekglplaylTRDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQAL 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 384 AYQTKDVLTAMEAdSGISLKTLRVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLAVGYWKDQSEIATQW 463
Cdd:cd07782 427 AYGTRHIIEAMNA-AGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDAMAAM 505
|
570 580
....*....|....*....|...
gi 1229100168 464 N-IDRTFEPSmNEEKR--NKLYE 483
Cdd:cd07782 506 SgPGKVVEPN-EELKKyhDRKYE 527
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
2-483 |
2.03e-28 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 118.29 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 2 ETYVLALDQGTTSSRAIIFN-KKGEIVHISQKEFAQY------FPKPGWVEHNANEIWGSILSVIATSLSESGIKPEQIA 74
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDaADGEELASAVHPYPRWviglylPPPPDQARQHPLDYLEALEAAVREALAQAGVDPADVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 75 GIGITNQRETAVVWDKNtGQPV-----------YNAIVWQ----SRQTADICEELKAKGLNDTfrektgllidAYFSGT- 138
Cdd:COG1069 81 GIGVDATGCTPVPVDAD-GTPLallpefaenphAMVILWKdhtaQEEAERINELAKARGEDYL----------RYVGGIi 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 139 -------KVKWILDHVEGAREKAERG-ELLfgtiDtWLIWKLSGgkahvtdysNASRTL-------MFNIHELKW-DDEL 202
Cdd:COG1069 150 ssewfwpKILHLLREDPEVYEAADSFvELC----D-WITWQLTG---------SLKRSRctaghkaLWHAHEGGYpSEEF 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 203 LEILTVPKSMLPEvRPSSEIYAHTVPyhfFGQ-------------EVPISGAAGDQQAALFGQACFEEG-MAKNtYGT-G 267
Cdd:COG1069 216 FAALDPLLDGLAD-RLGTEIYPLGEP---AGTltaewaarlglppGTAVAVGAIDAHAGAVGAGGVEPGtLVKV-MGTsT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 268 CFMLMNTGEKAVAsnhgllttiawGLNGKVE-------YALEGSIFVAGSAIQWLRDGL---RMLKNAAD---------- 327
Cdd:COG1069 291 CHMLVSPEERFVP-----------GICGQVDgsivpgmWGYEAGQSAVGDIFAWFVRLLvppLEYEKEAEergislhpll 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 328 SEQYAERVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTQKEHFVRATLESLAYQTKDVLTAMEAdSGISLKTLRV 407
Cdd:COG1069 360 TEEAAKLPPGESGLHALDWFNGNRSPLADQRLKGVILGLTLGTDAEDIYRALVEATAFGTRAIIERFEE-EGVPIDEIIA 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 408 DGG-AVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLAVGYWKDQSEIATQWN--IDRTFEPsmNEEKR---NKL 481
Cdd:COG1069 439 CGGiATKNPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMAAMGsgFDKVYTP--DPENVavyDAL 516
|
..
gi 1229100168 482 YE 483
Cdd:COG1069 517 YA 518
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
4-477 |
5.35e-27 |
|
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: 113.87 E-value: 5.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFN-KKGEIVHISQKEFAQY-FPKPGWVEHNANEIWGSILSVIATSLSESGIKPEQIAGIGItNQ 81
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDlYAGLEMAQEPVPYYQDsSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGV-DA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 82 RETAVVWDK----NTGQPVY----NAIVWQSRQTADICEELKAKGlNDTFREKTGLLIDAYFSGTKVKWILDHVEGAREK 153
Cdd:cd07768 80 TCSLAIFDRegtpLMALIPYpnedNVIFWMDHSAVNEAQWINMQC-PQQLLDYLGGKISPEMGVPKLKYFLDEYSHLRDK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 154 AERgelLFGTIDtWLIWKLSGgkahvtDYSNASRTLM----FNIHELKWDDEL-------LEILTVPKsMLPEVRPSSEI 222
Cdd:cd07768 159 HFH---IFDLHD-YIAYELTR------LYEWNICGLLgkenLDGEESGWSSSFfknidprLEHLTTTK-NLPSNVPIGTT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 223 YAHTVPYHFFGQEVPISGAAG----DQQAALFGqacfeegMAKNTYGTGCFMLMNTgekavASNHGLLTTIAW---GLNG 295
Cdd:cd07768 228 SGVALPEMAEKMGLHPGTAVVvsciDAHASWFA-------VASPHLETSLFMIAGT-----SSCHMYGTTISDripGVWG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 296 KVEYALEGSIFV-------AGSAIQWL-------RDGLRMLKNAADSEQYAERVES--------TDGVYVVPAFVGLGTP 353
Cdd:cd07768 296 PFDTIIDPDYSVyeagqsaTGKLIEHLfeshpcaRKFDEALKKGADIYQVLEQTIRqieknnglSIHILTLDMFFGNRSE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 354 YWDSDVRGAIFGLTRGTQKEHFV---RATLESLAYQTKDVLTAMEADsGISLKTLRVDGGAVKNNFLMQFQSDLLGVPVE 430
Cdd:cd07768 376 FADPRLKGSFIGESLDTSMLNLTykyIAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKNERLLQLIALVTNVAII 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1229100168 431 RPVVNETTALGAAYLAGLAVGYWKDQSEI----ATQWNIDRTFEPSMNEEK 477
Cdd:cd07768 455 KPKENMMGILGAAVLAKVAAGKKQLADSIteadISNDRKSETFEPLAYRLG 505
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
4-476 |
5.64e-26 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 110.50 E-value: 5.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFNKKGEIV--HISQKEFAQYFPKPGWVEHNANEIWGSiLSVIATSLSeSGIKPEQIAGIGITNQ 81
Cdd:PRK10331 3 VILVLDCGATNVRAIAVDRQGKIVarASTPNASDIAAENSDWHQWSLDAILQR-FADCCRQIN-SELTECHIRGITVTTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 82 RETAVVWDKNtGQPVYNAIVWQSRQTADICEELKAKGLNDTFREKTGllIDAYFSGT--KVKWILDHVEGAREKAERgeL 159
Cdd:PRK10331 81 GVDGALVDKQ-GNLLYPIISWKCPRTAAVMENIERYISAQQLQQISG--VGAFSFNTlyKLVWLKENHPQLLEQAHA--W 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 160 LFgtIDTWLIWKLSGGKAhvTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPSSEIYAHTVP----YHFFGQE 235
Cdd:PRK10331 156 LF--ISSLINHRLTGEFT--TDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPsaaaLLGLPVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 236 VPISGAAGDQQAALFGQacfeeGMAKN----TYGTGCFMLMNTG--EKAVASNHGLLTtiawglngkVEYALEGSIFVAG 309
Cdd:PRK10331 232 IPVISAGHDTQFALFGS-----GAGQNqpvlSSGTWEILMVRSAqvDTSLLSQYAGST---------CELDSQSGLYNPG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 310 saIQWLRDG-LRMLKNAA-DSEQY-------AERVES-TDGVYVVPAFVGLGTpywdsdvrGAIFGLTRGTQKEHFVRAT 379
Cdd:PRK10331 298 --MQWLASGvLEWVRKLFwTAETPyqtmieeARAIPPgADGVKMQCDLLACQN--------AGWQGVTLNTTRGHFYRAA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 380 LESLAYQTKDVLTAMEADSGISLKTLRVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLAVGYWKDQSEI 459
Cdd:PRK10331 368 LEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQA 447
|
490
....*....|....*...
gi 1229100168 460 ATQWNID-RTFEPSMNEE 476
Cdd:PRK10331 448 RAQMKYQyRYFYPQTEPE 465
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
4-459 |
4.14e-22 |
|
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: 98.75 E-value: 4.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAII--FNKKG---EIVHisqkefaqYFPKPG--------WvehNANEIWGSILSVIATSLSESGikp 70
Cdd:cd07771 1 NYLAVDLGASSGRVILgsLDGGKlelEEIH--------RFPNRPveinghlyW---DIDRLFDEIKEGLKKAAEQGG--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 71 eQIAGIGITnqreTavvW-------DKNtGQPVYNAIVWQSRQTADICEELKAK-GLNDTFrEKTGLLIDAYFSGTKVKW 142
Cdd:cd07771 67 -DIDSIGID----T---WgvdfgllDKN-GELLGNPVHYRDPRTEGMMEELFEKiSKEELY-ERTGIQFQPINTLYQLYA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 143 ILDHVEGAREKAERgeLLFgtIDTWLIWKLSGGKahVTDYSNASRTLMFNIHELKWDDELLEILTVPKSMLPEVRPSSEI 222
Cdd:cd07771 137 LKKEGPELLERADK--LLM--LPDLLNYLLTGEK--VAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 223 YAH---TVPYHFFGQEVP-ISGAAGDQQAALFGQACFEEGmakntygtgcFMLMNTGEKAVA---SNHGLLTTIAWGLNG 295
Cdd:cd07771 211 LGTlkpEVAEELGLKGIPvIAVASHDTASAVAAVPAEDED----------AAFISSGTWSLIgveLDEPVITEEAFEAGF 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 296 KVEYALEGSIF----VAGSAI------QWLRDGLR-----MLKNAADSEQYAERVESTDgvyvvPAFvglGTPywdSDVR 360
Cdd:cd07771 281 TNEGGADGTIRllknITGLWLlqecrrEWEEEGKDysydeLVALAEEAPPFGAFIDPDD-----PRF---LNP---GDMP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 361 GAIFGLTRGTQ------KEHFVRATLESLAYQTKDVLTAMEADSGISLKTLRVDGGAVKNNFLMQFQSDLLGVPVER-PV 433
Cdd:cd07771 350 EAIRAYCRETGqpvpesPGEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAgPV 429
|
490 500
....*....|....*....|....*.
gi 1229100168 434 vnETTALGAAYLAGLAVGYWKDQSEI 459
Cdd:cd07771 430 --EATAIGNLLVQLIALGEIKSLEEG 453
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
4-464 |
8.28e-16 |
|
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: 79.91 E-value: 8.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 4 YVLALDQGTTSSRAIIFNKKGEIVHISQ----KEFAQYFPKPGWVEHNANEI-------WGSILSVIATSLSESGIKPEQ 72
Cdd:cd07776 1 LYLGLDLSTQSLKAVVIDSDLKVVAEESvnfdSDLPEYGTKGGVHRDGDGGEvtspvlmWVEALDLLLEKLKAAGFDFSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 73 IAGIGITNQRETAVVWDK---------NTGQPVYNAI----------VWQSRQTADICEEL-KAKGLNDTFREKTGllID 132
Cdd:cd07776 81 VKAISGSGQQHGSVYWSKgaesalanlDPSKSLAEQLegafsvpdspIWMDSSTTKQCRELeKAVGGPEALAKLTG--SR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 133 AY--FSGTKV-KWILDHVEgAREKAERGELL--FGTidTWLIWKLSGgkahvTDYSNASRTLMFNIHELKWDDELLEILT 207
Cdd:cd07776 159 AYerFTGPQIaKIAQTDPE-AYENTERISLVssFLA--SLLLGRYAP-----IDESDGSGMNLMDIRSRKWSPELLDAAT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 208 VP--KSMLPEVRPSSEIYAHTVPYHF----FGQEVPISGAAGDQQAALFGQACfEEGMAKNTYGTG--CFMLMNTGEKav 279
Cdd:cd07776 231 APdlKEKLGELVPSSTVAGGISSYFVerygFSPDCLVVAFTGDNPASLAGLGL-EPGDVAVSLGTSdtVFLVLDEPKP-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 280 asnhgllttiawglngkveyALEGSIFVA---------------GS-AIQWLRDGLrmlkNAADSEQYAERVEST----D 339
Cdd:cd07776 308 --------------------GPEGHVFANpvdpgsymamlcyknGSlARERVRDRY----AGGSWEKFNELLESTppgnN 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 340 GVyvvpafvgLGTPYWDSD----------VRGAIFGLTRGTQKEHFVRATLE----SLAYQTKDVLtameadSGISLKTL 405
Cdd:cd07776 364 GN--------LGLYFDEPEitppvpgggrRFFGDDGVDAFFDPAVEVRAVVEsqflSMRLHAERLG------SDIPPTRI 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1229100168 406 RVDGGAVKNNFLMQFQSDLLGVPVERPVVNETTALGAAYLAGLAVGYWKDQSEIATQWN 464
Cdd:cd07776 430 LATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVV 488
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
1-487 |
1.36e-15 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 79.12 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 1 METYVLALDQGTTSSRAIIFN-KKGEIVHISQKEFA-----QYFPKPG-WVEHNANEIWGSILSVIATSLSESGIKPEQI 73
Cdd:PRK04123 1 MMAYVIGLDFGTDSVRALLVDcATGEELATAVVEYPhwvkgRYLDLPPnQALQHPLDYIESLEAAIPAVLKEAGVDPAAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 74 AGIGITNQRETAVVWDKNtGQPVYNAIVWQSRQTADIC--------EElkAKGLNDTFREKTGLLIDAYFSGT------- 138
Cdd:PRK04123 81 VGIGVDFTGSTPAPVDAD-GTPLALLPEFAENPHAMVKlwkdhtaqEE--AEEINRLAHERGEADLSRYIGGIyssewfw 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 139 -KVKWILDHVEGAREKAERG-ELLfgtiDtWLIWKLSGgkahVTDYSNASRT-------LMFniHElKWD---------- 199
Cdd:PRK04123 158 aKILHVLREDPAVYEAAASWvEAC----D-WVVALLTG----TTDPQDIVRSrcaaghkALW--HE-SWGglpsadffda 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 200 -DELLEILTVPKsMLPEVRPSSEIYAHTVPY--HFFG--QEVPISGAAGDQQAALFGQACfEEGMAKNTYGTG-CFMLMN 273
Cdd:PRK04123 226 lDPLLARGLRDK-LFTETWTAGEPAGTLTAEwaQRLGlpEGVAVSVGAFDAHMGAVGAGA-EPGTLVKVMGTStCDILLA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 274 TGEKAVAsnhgllttiawGLNGKVE-------YALE------GSIFvagsaiQWLRD--GLRMLKNAAD----------S 328
Cdd:PRK04123 304 DKQRAVP-----------GICGQVDgsivpglIGYEagqsavGDIF------AWFARllVPPEYKDEAEargkqllellT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 329 EQYAERVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTQKEHFVRATLESLAYQTKDVLTAMEaDSGISLKTLRVD 408
Cdd:PRK04123 367 EAAAKQPPGEHGLVALDWFNGRRTPLADQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFE-DQGVPVEEVIAA 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 409 GG-AVKNNFLMQFQSDLLGVPVErpVV--NETTALGAAYLAGLAVGYWKD----QSEIATqwNIDRTFEPsmNEEKR--- 478
Cdd:PRK04123 446 GGiARKNPVLMQIYADVLNRPIQ--VVasDQCPALGAAIFAAVAAGAYPDipeaQQAMAS--PVEKTYQP--DPENVary 519
|
....*....
gi 1229100168 479 NKLYEGWQK 487
Cdd:PRK04123 520 EQLYQEYKQ 528
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
6-446 |
2.74e-14 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466797 [Multi-domain] Cd Length: 544 Bit Score: 75.13 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 6 LALDQGTTSSRAIIFNKKGEIVHISQKE--FAQYFPKPGWVEHNANEIWGSILSVIATSLSESGIKpeQIAGIGIT---- 79
Cdd:cd07778 3 IGIDVGSTSVRIGIFDYHGTLLATSERPisYKQDPKDLWFVTQSSTEIWKAIKTALKELIEELSDY--IVSGIGVSatcs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 80 ---NQRETavvwDKNTGQPvYNAIVWQSRQTADI-------CEELkAKGLNDTFREKTGLLIDAYFSGT----KVKWILD 145
Cdd:cd07778 81 mvvMQRDS----DTSYLVP-YNVIHEKSNPDQDIifwmdhrASEE-TQWLNNILPDDILDYLGGGFIPEmaipKLKYLID 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 146 HVEGAREKaergELLFGTIDTWLIWKLSGGKAHVTD-YSNAS-RTLMFNIHELK-WDDELLEilTVPKSMLPEVRPSSEI 222
Cdd:cd07778 155 LIKEDTFK----KLEVFDLHDWISYMLATNLGHSNIvPVNAPpSIGIGIDGSLKgWSKDFYS--KLKISTKVCNVGNTFK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 223 YAHTVPY-------------HFFGQEVPISGAAG--DQQAALFGQACfEEGMAKNTY----GTG-CFMLMNTgekavASN 282
Cdd:cd07778 229 EAPPLPYagipigkvnvilaSYLGIDKSTVVGHGciDCYAGWFSTFA-AAKTLDTTLfmvaGTStCFLYATS-----SSQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 283 HGLLTTIaWG-----LNGKVEYalEGSIFVAGSAIQWL----RDGLRMLKNAADSEQYAERV------ESTDGVYVVPA- 346
Cdd:cd07778 303 VGPIPGI-WGpfdqlLKNYSVY--EGGQSATGKLIEKLfnshPAIIELLKSDANFFETVEEKidkyerLLGQSIHYLTRh 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 347 --FVG--LG--TPYWDSDVRGAIFGLTRGTQKEHFVR---ATLESLAYQTKDVLTAMEaDSGISLKTLRVDGGAVKNNFL 417
Cdd:cd07778 380 mfFYGdyLGnrTPYNDPNMSGSFIGESTDSSLTDLVLkyiLILEFLAFQTKLIIDNFQ-KEKIIIQKVVISGSQAKNARL 458
|
490 500 510
....*....|....*....|....*....|..
gi 1229100168 418 MQFQSDLLGVP---VERPVVNETTALGAAYLA 446
Cdd:cd07778 459 LQLLSTVLSKIhiiVPLSDSKYAVVKGAALLG 490
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
181-441 |
1.15e-07 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 53.95 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 181 DYSNASRTLMFNIHELKWDDELLEILTVPKSMLPE-VRPSSEIYAHTVPYhffGQEVP-ISGAAGDQQAALFGQACFEEG 258
Cdd:PRK10640 157 EYTNATTTQLVNINSDDWDESLLAWSGAPKAWFGRpTHPGNVIGHWICPQ---GNEIPvVAVASHDTASAVIASPLNDSD 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 259 MAKNTYGTGCFMLMN-----TGEKAVASNhgllTTIAWGLNGKveYALEGSIFvagsaiqwlrdGLRMLKNAADSEQYAE 333
Cdd:PRK10640 234 AAYLSSGTWSLMGFEsqtpfTNDTALAAN----ITNEGGAEGR--YRVLKNIM-----------GLWLLQRVLQERQITD 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 334 RVESTDGVYVVPAFVGLGTPYWD-----SDVRGAIFGLTRGTQK------EHFVRATLESLAYQTKDVLTAMEADSGISL 402
Cdd:PRK10640 297 LPALIAATAALPACRFLINPNDDrfinpPSMCSEIQAACRETAQpvpesdAELARCIFDSLALLYADVLHELAQLRGEPF 376
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1229100168 403 KTLRVDGGAVKNNFLMQFQSDLLGVPV-ERPVvnETTALG 441
Cdd:PRK10640 377 SQLHIVGGGCQNALLNQLCADACGIRViAGPV--EASTLG 414
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
5-446 |
2.08e-05 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466792 [Multi-domain] Cd Length: 424 Bit Score: 46.87 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 5 VLALDQGTTSSRAIIFNKKGEIVHISQKEFAqYFPKPGWVEHNANEIWGSILSVIATSLSEsgikpEQIAGIGITNQRET 84
Cdd:cd07772 2 IAVFDIGKTNKKLLLFDENGEVLAERSTPNP-EIEEDGYPCEDVEAIWEWLLDSLAELAKR-----HRIDAINFTTHGAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 85 AVVWDKNTG--QPVYNaivWQSRQTADICEELKAK--GLNDTFrekTGLLIDAYFSGTKVKWIldhvegAREKAErgelL 160
Cdd:cd07772 76 FALLDENGElaLPVYD---YEKPIPDEINEAYYAErgPFEETG---SPPLPGGLNLGKQLYWL------KREKPE----L 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 161 FGTIDTWL------IWKLSGGKahVTDYSNAS-RTLMFNIHELKWDDELLEILTvpKSMLPEVRPSSE----IYAHTVPY 229
Cdd:cd07772 140 FARAKTILplpqywAWRLTGKA--ASEITSLGcHTDLWDFEKNEYSSLVKKEGW--DKLFPPLRKAWEvlgpLRPDLARR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 230 HFFGQEVPIsgAAG--DQQAALFG-QACFEEGMAKNTYGTGCfMLMNTGEKAVASNHGLLTTIAWGLN--GKVeyaLEGS 304
Cdd:cd07772 216 TGLPKDIPV--GCGihDSNAALLPyLAAGKEPFTLLSTGTWC-IAMNPGNDLPLTELDLARDCLYNLDvfGRP---VKTA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229100168 305 IFVAGSAIQWLRDGLRMLKNAADSEQYAERVEStDGVYVVPAFVGLGTPYwdSDVRGAIFGLTRGTQKEHFVRATLeSLA 384
Cdd:cd07772 290 RFMGGREYERLVERIAKSFPQLPSLADLAKLLA-RGTFALPSFAPGGGPF--PGSGGRGVLSAFPSAEEAYALAIL-YLA 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229100168 385 YQTKDVLTAMEADSGislkTLRVDGGAVKNNFLMQFQSDLL-GVPVERPVVNETTALGAAYLA 446
Cdd:cd07772 366 LMTDYALDLLGSGVG----RIIVEGGFAKNPVFLRLLAALRpDQPVYLSDDSEGTALGAALLA 424
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-78 |
7.40e-04 |
|
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: 41.42 E-value: 7.40e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229100168 1 METYVLALDQGTTSSRAIIFNKKGEIVHisqkefAQYFPKPgwVEHNANEIWGSILSVIATSLSESGIKPEQIAGIGI 78
Cdd:COG1940 3 DAGYVIGIDIGGTKIKAALVDLDGEVLA------RERIPTP--AGAGPEAVLEAIAELIEELLAEAGISRGRILGIGI 72
|
|
| |
