|
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: 1066.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 1 MEKYILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVINENDVRADQIAGIGITN 80
Cdd:PRK00047 3 MKKYILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 81 QRETTVVWDKHTGRPIYHAIVWQSRQTQSICSELKQQGYEQTFRDKTGLLLDPYFAGTKVKWILDNVEGAREKAENGDLL 160
Cdd:PRK00047 83 QRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRDGYEDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGELL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 161 FGTIDTWLVWKLSGKAAHITDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGKTIDYHFYGQEVPIAG 240
Cdd:PRK00047 163 FGTIDTWLVWKLTGGKVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYGFFGGEVPIAG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 241 VAGDQQAALFGQACFERGDVKNTYGTGGFMLMNTGDKAVKSESGLLTTIAYGIDGKVNYALEGSIFVSGSAIQWLRDGLR 320
Cdd:PRK00047 243 IAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGIDGKVVYALEGSIFVAGSAIQWLRDGLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 321 MINSAPQSESYATRVDSTEGVYVVPAFVGLGTPYWDSEARGAIFGLTRGTEKEHFIRATLESLCYQTRDVMEAMSKDSGI 400
Cdd:PRK00047 323 IISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADSGI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 401 DVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLAVGFWESKDDIAKNWKLEEKFDPKMDEGEREK 480
Cdd:PRK00047 403 RLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDELKEQWKIDRRFEPQMDEEEREK 482
|
490
....*....|....*.
gi 446339515 481 LYRGWKKAVEATQVFK 496
Cdd:PRK00047 483 LYAGWKKAVKRTLAWA 498
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
1-493 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 1023.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 1 MEKYILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVINENDVRADQIAGIGITN 80
Cdd:COG0554 1 MKKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 81 QRETTVVWDKHTGRPIYHAIVWQSRQTQSICSELKQQGYEQTFRDKTGLLLDPYFAGTKVKWILDNVEGAREKAENGDLL 160
Cdd:COG0554 81 QRETTVVWDRKTGKPLYNAIVWQDRRTADICEELKADGLEDLIREKTGLVLDPYFSATKIKWILDNVPGARERAEAGELL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 161 FGTIDTWLVWKLSGKAAHITDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGKTIDYHFyGQEVPIAG 240
Cdd:COG0554 161 FGTIDSWLIWKLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDPDLF-GAEIPIAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 241 VAGDQQAALFGQACFERGDVKNTYGTGGFMLMNTGDKAVKSESGLLTTIAYGIDGKVNYALEGSIFVSGSAIQWLRDGLR 320
Cdd:COG0554 240 IAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGGKVTYALEGSIFVAGAAVQWLRDGLG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 321 MINSAPQSESYATRVDSTEGVYVVPAFVGLGTPYWDSEARGAIFGLTRGTEKEHFIRATLESLCYQTRDVMEAMSKDSGI 400
Cdd:COG0554 320 LIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADSGI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 401 DVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLAVGFWESKDDIAKNWKLEEKFDPKMDEGEREK 480
Cdd:COG0554 400 PLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEELAALWKVDRRFEPQMDEEERER 479
|
490
....*....|...
gi 446339515 481 LYRGWKKAVEATQ 493
Cdd:COG0554 480 LYAGWKKAVERTL 492
|
|
| 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: 989.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVINENDVRADQIAGIGITNQRE 83
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 84 TTVVWDKHTGRPIYHAIVWQSRQTQSICSELKQQGYEQTFRDKTGLLLDPYFAGTKVKWILDNVEGAREKAENGDLLFGT 163
Cdd:cd07786 81 TTVVWDRETGKPVYNAIVWQDRRTADICEELKAEGHEEMIREKTGLVLDPYFSATKIRWILDNVPGARERAERGELAFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 164 IDTWLVWKLSGKAAHITDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGKTiDYHFYGQEVPIAGVAG 243
Cdd:cd07786 161 IDSWLIWKLTGGKVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYT-DPDLLGAEIPIAGIAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 244 DQQAALFGQACFERGDVKNTYGTGGFMLMNTGDKAVKSESGLLTTIAYGIDGKVNYALEGSIFVSGSAIQWLRDGLRMIN 323
Cdd:cd07786 240 DQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLGGKVTYALEGSIFIAGAAVQWLRDGLGLIE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 324 SAPQSESYATRVDSTEGVYVVPAFVGLGTPYWDSEARGAIFGLTRGTEKEHFIRATLESLCYQTRDVMEAMSKDSGIDVQ 403
Cdd:cd07786 320 SAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEADSGIPLK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 404 SLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLAVGFWESKDDIAKNWKLEEKFDPKMDEGEREKLYR 483
Cdd:cd07786 400 ELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAKLWQVDRRFEPSMSEEEREALYA 479
|
....*..
gi 446339515 484 GWKKAVE 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: 960.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVINENDVRADQIAGIGITNQRE 83
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 84 TTVVWDKHTGRPIYHAIVWQSRQTQSICSELKQQGYEQTFRDKTGLLLDPYFAGTKVKWILDNVEGAREKAENGDLLFGT 163
Cdd:cd07769 81 TTVVWDKKTGKPLYNAIVWQDRRTADICEELKAKGLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAERGELLFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 164 IDTWLVWKLSGKAAHITDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGKTIDYHFyGQEVPIAGVAG 243
Cdd:cd07769 161 IDTWLIWKLTGGKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTDPEGL-GAGIPIAGILG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 244 DQQAALFGQACFERGDVKNTYGTGGFMLMNTGDKAVKSESGLLTTIAYGIDGKVNYALEGSIFVSGSAIQWLRDGLRMIN 323
Cdd:cd07769 240 DQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQIGGKVTYALEGSIFIAGAAIQWLRDNLGLIE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 324 SAPQSESYATRVDSTEGVYVVPAFVGLGTPYWDSEARGAIFGLTRGTEKEHFIRATLESLCYQTRDVMEAMSKDSGIDVQ 403
Cdd:cd07769 320 DAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDSGIKLK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 404 SLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLAVGFWESKDDIAKNWKLEEKFDPKMDEGEREKLYR 483
Cdd:cd07769 400 ELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDELASLWQVDKRFEPSMDEEERERLYR 479
|
....*..
gi 446339515 484 GWKKAVE 490
Cdd:cd07769 480 GWKKAVE 486
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
3-493 |
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: 860.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 3 KYILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVINENDVRADQIAGIGITNQR 82
Cdd:TIGR01311 1 PYILAIDQGTTSSRAIVFDKDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAGIKPDDIAAIGITNQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 83 ETTVVWDKHTGRPIYHAIVWQSRQTQSICSELKQQGYEQTFRDKTGLLLDPYFAGTKVKWILDNVEGAREKAENGDLLFG 162
Cdd:TIGR01311 81 ETTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYGEFIREKTGLPLDPYFSATKLRWLLDNVPGVREAAERGELLFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 163 TIDTWLVWKLSGKAAHITDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGKTIDYHFyGQEVPIAGVA 242
Cdd:TIGR01311 161 TIDTWLIWNLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYTDPGLL-GAEIPITGVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 243 GDQQAALFGQACFERGDVKNTYGTGGFMLMNTGDKAVKSESGLLTTIAYGIDGKVN-YALEGSIFVSGSAIQWLRDGLRM 321
Cdd:TIGR01311 240 GDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKKPvYALEGSVFVAGAAVQWLRDNLKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 322 INSAPQSESYATRVDSTEGVYVVPAFVGLGTPYWDSEARGAIFGLTRGTEKEHFIRATLESLCYQTRDVMEAMSKDSGID 401
Cdd:TIGR01311 320 IKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTRDVLEAMEKDAGVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 402 VQSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLAVGFWESKDDIAKNWKLEEKFDPKMDEGEREKL 481
Cdd:TIGR01311 400 ITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWRVEKTFEPEMDEEEREAR 479
|
490
....*....|..
gi 446339515 482 YRGWKKAVEATQ 493
Cdd:TIGR01311 480 YAGWKEAVKRSL 491
|
|
| 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: 729.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 3 KYILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVI---NENDVRADQIAGIGIT 79
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVeklKALGISPSDIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 80 NQRETTVVWDKHTGRPIYHAIVWQSRQTQSICSELKQQ--GYEQTFRDKTGLLLDPYFAGTKVKWILDNVEGAREKAENG 157
Cdd:cd07792 81 NQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELSAKtpGGKDHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 158 DLLFGTIDTWLVWKLSG---KAAHITDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGKTIDYHFYGq 234
Cdd:cd07792 161 RLLFGTVDSWLIWNLTGgknGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIASGPLAG- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 235 eVPIAGVAGDQQAALFGQACFERGDVKNTYGTGGFMLMNTGDKAVKSESGLLTTIAY--GIDGKVNYALEGSIFVSGSAI 312
Cdd:cd07792 240 -VPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAYklGPDAPPVYALEGSIAIAGAAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 313 QWLRDGLRMINSAPQSESYATRVDSTEGVYVVPAFVGLGTPYWDSEARGAIFGLTRGTEKEHFIRATLESLCYQTRDVME 392
Cdd:cd07792 319 QWLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREILD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 393 AMSKDSGIDVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLAVGFWESKDDI-AKNWKLEEKFDP 471
Cdd:cd07792 399 AMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELkSLNEGGRTVFEP 478
|
490
....*....|....*....
gi 446339515 472 KMDEGEREKLYRGWKKAVE 490
Cdd:cd07792 479 QISEEERERRYKRWKKAVE 497
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
3-496 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 660.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 3 KYILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVIN--ENDVRADQIAGIGITN 80
Cdd:PTZ00294 2 KYIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKklREKGPSFKIKAIGITN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 81 QRETTVVWDKHTGRPIYHAIVWQSRQTQSICSELKQQGYEQT-FRDKTGLLLDPYFAGTKVKWILDNVEGAREKAENGDL 159
Cdd:PTZ00294 82 QRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKYGGSNfFQKITGLPISTYFSAFKIRWMLENVPAVKDAVKEGTL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 160 LFGTIDTWLVWKLSGKAAHITDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGK-TIDYHFYGQEVPI 238
Cdd:PTZ00294 162 LFGTIDTWLIWNLTGGKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTiSGEAVPLLEGVPI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 239 AGVAGDQQAALFGQACFERGDVKNTYGTGGFMLMNTGDKAVKSESGLLTTIAY--GIDGKVNYALEGSIFVSGSAIQWLR 316
Cdd:PTZ00294 242 TGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYqlGPNGPTVYALEGSIAVAGAGVEWLR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 317 DGLRMINSAPQSESYATRVDSTEGVYVVPAFVGLGTPYWDSEARGAIFGLTRGTEKEHFIRATLESLCYQTRDVMEAMSK 396
Cdd:PTZ00294 322 DNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDVIESMEK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 397 DSGIDVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLAVGFWESKDDIAKNWKLE-EKFDPKMDE 475
Cdd:PTZ00294 402 DAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVKKLIRRSnSTFSPQMSA 481
|
490 500
....*....|....*....|.
gi 446339515 476 GEREKLYRGWKKAVEATQVFK 496
Cdd:PTZ00294 482 EERKAIYKEWNKAVERSLKWA 502
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
4-492 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 639.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVINENDVRA----DQIAGIGIT 79
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGhnvdSGLKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 80 NQRETTVVWDKHTGRPIYHAIVWQSRQTQSICSELKQQ--GYEQTFRDKTGLLLDPYFAGTKVKWILDNVEGAREKAENG 157
Cdd:PLN02295 81 NQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKElsGGRKHFVETCGLPISTYFSATKLLWLLENVDAVKEAVKSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 158 DLLFGTIDTWLVWKLSGKAA---HITDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGkTIDYHFYGQ 234
Cdd:PLN02295 161 DALFGTIDSWLIWNLTGGASggvHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIG-TIAKGWPLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 235 EVPIAGVAGDQQAALFGQACfERGDVKNTYGTGGFMLMNTGDKAVKSESGLLTTIAY--GIDGKVNYALEGSIFVSGSAI 312
Cdd:PLN02295 240 GVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYklGPDAPTNYALEGSVAIAGAAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 313 QWLRDGLRMINSAPQSESYATRVDSTEGVYVVPAFVGLGTPYWDSEARGAIFGLTRGTEKEHFIRATLESLCYQTRDVME 392
Cdd:PLN02295 319 QWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQVKDVLD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 393 AMSKDSGIDVQS-----LRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLAVGFWESKDDIAK-NWKLE 466
Cdd:PLN02295 399 AMRKDAGEEKSHkglflLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEEEIFASeKWKNT 478
|
490 500
....*....|....*....|....*.
gi 446339515 467 EKFDPKMDEGEREKLYRGWKKAVEAT 492
Cdd:PLN02295 479 TTFRPKLDEEERAKRYASWCKAVERS 504
|
|
| 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: 584.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVINENDVRADQIAGIGITNQRE 83
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 84 TTVVWDKHTGRPIYHAIVWQSRQTQSICSELKQQGYEQTFRDKTGLL----------------LDPYFAGTKVKWILDNV 147
Cdd:cd07793 81 TFLTWDKKTGKPLHNFITWQDLRAAELCESWNRSLLLKALRGGSKFLhfltrnkrflaasvlkFSTAHVSIRLLWILQNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 148 EGAREKAENGDLLFGTIDTWLVWKLSGKAAHITDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGKTi 227
Cdd:cd07793 161 PELKEAAEKGELLFGTIDTWLLWKLTGGKVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFGST- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 228 DYHFYGQEVPIAGVAGDQQAALFGQACFERGDVKNTYGTGGFMLMNTGDKAVKSESGLLTTIAYGIDGKVNYALEGSIFV 307
Cdd:cd07793 240 DPSIFGAEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGGEITYLAEGNASD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 308 SGSAIQWLRDGLrMINSAPQSESYATRVDSTEGVYVVPAFVGLGTPYWDSEARGAIFGLTRGTEKEHFIRATLESLCYQT 387
Cdd:cd07793 320 TGTVIDWAKSIG-LFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIAFRV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 388 RDVMEAMSKDSGIDVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLAVGFWESKDDIAKNWKLEE 467
Cdd:cd07793 399 KQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEELKKLRKIEK 478
|
490 500
....*....|....*....|...
gi 446339515 468 KFDPKMDEGEREKLYRGWKKAVE 490
Cdd:cd07793 479 IFEPKMDNEKREELYKNWKKAVK 501
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
3-493 |
5.81e-123 |
|
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: 368.39 E-value: 5.81e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 3 KYILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVINENDVRADQIAGIGITNQR 82
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 83 ETTVVWDKHtGRPIYHAIVWQSRQTQSICSELKQQGYEQTFRDKTGLLLDPYFAGTKVKWILDNVEGAREKAEngdlLFG 162
Cdd:COG1070 81 HGLVLLDAD-GEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIA----KVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 163 TIDTWLVWKLSGKAAhiTDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGKT---------IDyhfyg 233
Cdd:COG1070 156 LPKDYLRYRLTGEFV--TDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLtaeaaaetgLP----- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 234 QEVPIAGVAGDQQAALFGQACFERGDVKNTYGTGGFMLMNTgDKAVKSESGLLTTIAYGIDGKvnYALEGSIFVSGSAIQ 313
Cdd:COG1070 229 AGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVS-DKPLPDPEGRVHTFCHAVPGR--WLPMGATNNGGSALR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 314 WLRD--GLRMINSAPQSESYATRVD-STEGVYVVPAFVGLGTPYWDSEARGAIFGLTRGTEKEHFIRATLESLCYQTRDV 390
Cdd:COG1070 306 WFRDlfADGELDDYEELNALAAEVPpGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 391 MEAMsKDSGIDVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLAVGFWESKDDIAKNW-KLEEKF 469
Cdd:COG1070 386 LEAL-EEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMvRVGETI 464
|
490 500
....*....|....*....|....*
gi 446339515 470 DPKMDEGER-EKLYRGWKKAVEATQ 493
Cdd:COG1070 465 EPDPENVAAyDELYERYRELYPALK 489
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
4-474 |
4.65e-114 |
|
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: 343.35 E-value: 4.65e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVINENDVRADQIAGIGITNQRE 83
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 84 TTVVWDKHtGRPIYHAIVWQsrqtqsicselkqqgyeqtfrDKtgllldpyfagtKVKWILdnvegarekaengdllfgT 163
Cdd:cd07779 81 TFVPVDED-GRPLRPAISWQ---------------------DK------------RTAKFL------------------T 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 164 IDTWLVWKLSGKAAhiTDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYG--------KTidyhfyG-- 233
Cdd:cd07779 109 VQDYLLYRLTGEFV--TDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGtltkeaaeET------Glp 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 234 QEVPIAGVAGDQQAALFGQACFERGDVKNTYGTGGFMLMNTgDKAVKSESGLLTTIAYGIDGKvnYALEGSIFVSGSAIQ 313
Cdd:cd07779 181 EGTPVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVS-DKPVEDPERRIPCNPSAVPGK--WVLEGSINTGGSAVR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 314 WLRD---GLRMINSAPQSESY--------ATRVDStEGVYVVPAFVGLGTPYWDSEARGAIFGLTRGTEKEHFIRATLES 382
Cdd:cd07779 258 WFRDefgQDEVAEKELGVSPYellneeaaKSPPGS-DGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 383 LCYQTRDVMEAMsKDSGIDVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLAVGFWESKDDIAKN 462
Cdd:cd07779 337 IAFELRDNLEAM-EKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKA 415
|
490
....*....|...
gi 446339515 463 W-KLEEKFDPKMD 474
Cdd:cd07779 416 MvRVTDTFEPDPE 428
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
4-446 |
5.76e-113 |
|
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: 339.16 E-value: 5.76e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVINENDVRADQIAGIGITNQRE 83
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 84 TTVVWDKHtGRPIYHAIVWqsrqtqsicselkqqgyeqtfrdktgllldpyfagtkvkwiLDNvegaREKaengdllFGT 163
Cdd:cd00366 81 GVVLVDAD-GNPLRPAIIW-----------------------------------------LDR----RAK-------FLQ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 164 IDTWLVWKLSGKAAhiTDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGKTIDYhfYGQE------VP 237
Cdd:cd00366 108 PNDYIVFRLTGEFA--IDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPE--AAEEtglpagTP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 238 IAGVAGDQQAALFGQACFERGDVKNTYGTGGFMLMNTGDKavKSESGLLTTIAYGIDGKvnYALEGSIFVSGSAIQWLRD 317
Cdd:cd00366 184 VVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEP--VPPDPRLLNRCHVVPGL--WLLEGAINTGGASLRWFRD 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 318 glrMINSAPQSESYATRVDS--------TEGVYVVPAFVGLGTPYWDSEARGAIFGLTRGTEKEHFIRATLESLCYQTRD 389
Cdd:cd00366 260 ---EFGEEEDSDAEYEGLDElaaevppgSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRD 336
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 446339515 390 VMEAMsKDSGIDVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLA 446
Cdd:cd00366 337 NLEIL-EELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
4-251 |
1.85e-106 |
|
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: 317.36 E-value: 1.85e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVINENDVRADQIAGIGITNQRE 83
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 84 TTVVWDKHTgRPIYHAIVWQSRQTQSICSELKQQGYEQTFRDKTGLLLDPYFAGTKVKWILDNVEGAREKAEngdlLFGT 163
Cdd:pfam00370 81 GTVLLDKND-KPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIH----KFLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 164 IDTWLVWKLSGKaaHITDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGKTIDYHFYG----QEVPIA 239
Cdd:pfam00370 156 IHDYLRWRLTGV--FVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMwgldEGVPVV 233
|
250
....*....|..
gi 446339515 240 GVAGDQQAALFG 251
Cdd:pfam00370 234 GGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
4-451 |
7.16e-104 |
|
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466793 [Multi-domain] Cd Length: 443 Bit Score: 317.61 E-value: 7.16e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVINenDVRADQIAGIGITNQRE 83
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAA--QAGPDPIAAISVSSQGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 84 TTVVWDKHtGRPIYHAIVWQSRQTQSICSELKQQGYEQTFRDKTGLLLDPYFAGTKVKWILDNVEGAREKAENgdllFGT 163
Cdd:cd07773 79 SGVPVDRD-GEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAK----WLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 164 IDTWLVWKLSGKAAhiTDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGKTIDYHFYG----QEVPIA 239
Cdd:cd07773 154 VADYIAYRLTGEPV--TDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEElglpAGTPVV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 240 gVAG-DQQAALFGQACFERGDVKNTYGTGGfMLMNTGDKAVKSES--GLLTTIAYGIDGKVnYALEGSIfVSGSAIQWLR 316
Cdd:cd07773 232 -VGGhDHLCAALGAGVIEPGDVLDSTGTAE-ALLAVVDEPPLDEMlaEGGLSYGHHVPGGY-YYLAGSL-PGGALLEWFR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 317 D--GLRMINSAPQSESYATRVDSTEGVYVVPAFVGLGTPYWDSEARGAIFGLTRGTEKEHFIRATLESLCYQTRDVMEAM 394
Cdd:cd07773 308 DlfGGDESDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEAL 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 446339515 395 SKdSGIDVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLAVG 451
Cdd:cd07773 388 EK-AGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
4-488 |
5.58e-100 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 309.08 E-value: 5.58e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVINENDVRADQIAGIGITNQRE 83
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 84 TTVVWDKHtGRPIYHAIVWQSRQTQSICSELKQQgYEQTFRDKTGLLLDPYFAGTKVKWIldnvegAREKAENgdllFGT 163
Cdd:cd07808 81 GLVLLDKN-GRPLRPAILWNDQRSAAECEELEAR-LGDEILIITGNPPLPGFTLPKLLWL------KENEPEI----FAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 164 IDT------WLVWKLSGKAAhiTDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGKT---------ID 228
Cdd:cd07808 149 IRKillpkdYLRYRLTGELA--TDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLtpeaaeelgLP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 229 yhfygQEVPIAGVAGDQQAALFGQACFERGDVKNTYGTGGFMLMNTgDKAVKSESGLLTTIAYGIDGKvNYALeGSIFVS 308
Cdd:cd07808 227 -----EGTPVVAGAGDNAAAALGAGVVEPGDALISLGTSGVVFAPT-DKPVPDPKGRLHTFPHAVPGK-WYAM-GVTLSA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 309 GSAIQWLRDGL--------RMINSAPQSESYAtrvdstEGVYVVPAFVGLGTPYWDSEARGAIFGLTRGTEKEHFIRATL 380
Cdd:cd07808 299 GLSLRWLRDLFgpdresfdELDAEAAKVPPGS------EGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 381 ESLCYQTRDVMEAMsKDSGIDVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLAVGFWESKDDIA 460
Cdd:cd07808 373 EGVAFSLRDSLEVL-KELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAA 451
|
490 500 510
....*....|....*....|....*....|
gi 446339515 461 KNW-KLEEKFDPKMDEGER-EKLYRGWKKA 488
Cdd:cd07808 452 AACiKIEKTIEPDPERHEAyDELYARYREL 481
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
4-486 |
5.19e-89 |
|
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Chromobacterium violaceum xylulose kinase (CvXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466807 [Multi-domain] Cd Length: 485 Bit Score: 280.56 E-value: 5.19e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVINENDVRADQIAGIGITNQRE 83
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 84 TTVVWDKHtGRPIYHAIVWQSRQTQSICSELKQQ-GYEQTFRDKTGLLLDPYFAGTKVKWILDNvegAREKAENGDLLFG 162
Cdd:cd07805 81 GVVPVDKD-GNPLRNAIIWSDTRAAEEAEEIAGGlGGIEGYRLGGGNPPSGKDPLAKILWLKEN---EPEIYAKTHKFLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 163 TIDtWLVWKLSGKAAhiTDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGK-----TIDYHFYgQEVP 237
Cdd:cd07805 157 AKD-YLNFRLTGRAA--TDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGEltpeaAAELGLP-AGTP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 238 IAGVAGDQQAALFGQACFERGDVkNTY-GTGGFMLMNTGDKAVKSESGlLTTIAYGIDGKVNYAleGSIFVSGSAIQWLR 316
Cdd:cd07805 233 VVGGGGDAAAAALGAGAVEEGDA-HIYlGTSGWVAAHVPKPKTDPDHG-IFTLASADPGRYLLA--AEQETAGGALEWAR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 317 DGLRMINSAPQS-----ESYATRVD-STEGVYVVPAFVGLGTPYWDSEARGAIFGLTRGTEKEHFIRATLESLCYQTRDV 390
Cdd:cd07805 309 DNLGGDEDLGADdyellDELAAEAPpGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 391 MEAMSKDSGiDVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEI-QETTALGAAYLAGLAVGFWESKDDIAKNWKLEEKF 469
Cdd:cd07805 389 LEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVPENpQEAGALGAALLAAVGLGLLKSFDEAKALVKVEKVF 467
|
490
....*....|....*...
gi 446339515 470 DPKMDEGER-EKLYRGWK 486
Cdd:cd07805 468 EPDPENRARyDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
4-451 |
2.46e-85 |
|
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: 270.17 E-value: 2.46e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVINENDVRADQIAGIGITNQRE 83
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 84 TTVVWDKHtGRPIYHAIVWQSRQTQSICSELKQQGYEQTFRDKTGLLLDPYFAGTKVKWILDN----VEGARekaengdl 159
Cdd:cd07804 81 ALVPVDEN-GKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSQSVGPKLLWIKRNepevFKKTR-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 160 LFGTIDTWLVWKLSGKAAhiTDYSNASRT-LMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGKTIDyhfygqEV-- 236
Cdd:cd07804 152 KFLGAYDYIVYKLTGEYV--IDYSSAGNEgGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTK------EAae 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 237 --------PIAGVAGDQQAALFGQACFERGDVKNTYGTGGFMLMNTgDKAVKSESGLLTtiAYGIDGKvnYALEGSIFVS 308
Cdd:cd07804 224 etglaegtPVVAGTVDAAASALSAGVVEPGDLLLMLGTAGDIGVVT-DKLPTDPRLWLD--YHDIPGT--YVLNGGMATS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 309 GSAIQWLRDGL----RMINSAPQSESY------ATRVDST-EGVYVVPAFVGLGTPYWDSEARGAIFGLTRGTEKEHFIR 377
Cdd:cd07804 299 GSLLRWFRDEFageeVEAEKSGGDSAYdlldeeAEKIPPGsDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYR 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446339515 378 ATLESLCYQTRDVMEAMsKDSGIDVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLAVG 451
Cdd:cd07804 379 ALLEGVAYGLRHHLEVI-REAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
4-487 |
1.66e-83 |
|
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: 266.34 E-value: 1.66e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVIneNDVRADQIAGIGITNQRE 83
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVL--AKLGGGEVDAIGFSSAMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 84 TTVVWDKHtGRPIYHAIVWQSRQTQSICSELKQQGYEQTFRDKTGLLLDPYFAGTKVKWILDNVEGAREKAEngdlLFGT 163
Cdd:cd07770 79 SLLGVDED-GEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAA----KFVS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 164 IDTWLVWKLSGKaaHITDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGKTIDYhfYGQEVPI-AGV- 241
Cdd:cd07770 154 IKEYLLYRLTGE--LVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPE--FAERLGLlAGTp 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 242 ----AGDQQAALFGQACFERGDVKNTYGTGGFMLMNTgDKAVKSESGLLTTiaygidgkvnYALEGSIFVSGSAI----- 312
Cdd:cd07770 230 vvlgASDGALANLGSGALDPGRAALTVGTSGAIRVVS-DRPVLDPPGRLWC----------YRLDENRWLVGGAInnggn 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 313 --QWLRDGLRMINSAPQS-ESYATRVDST-EGVYVVPAFVGLGTPYWDSEARGAIFGLTRGTEKEHFIRATLESLCYQTR 388
Cdd:cd07770 299 vlDWLRDTLLLSGDDYEElDKLAEAVPPGsHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 389 DVMEAMsKDSGIDVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLAVGFWESKdDIAKNWKLEEK 468
Cdd:cd07770 379 SIYEAL-EELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSL-EADELVKIGKV 456
|
490 500
....*....|....*....|
gi 446339515 469 FDPKMDEGER-EKLYRGWKK 487
Cdd:cd07770 457 VEPDPENHAIyAELYERFKK 476
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
4-451 |
1.39e-64 |
|
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: 215.88 E-value: 1.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVINENDVRADQIAGIGITNQRE 83
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 84 TTVVWDKHtGRPIYHAIVWQSRQTQSICSELKQQGYEQTFRDKTGLLLDPYFAGTKVKWILDNvegAREKAENGDLLFGT 163
Cdd:cd07802 81 GLYLVDKD-GKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKEN---EPERYDRIRTVLFC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 164 IDtWLVWKLSGKAAhiTDYSNASrTLMFNIHDLEWDDELLELLTVP--KNMLPEVKASSEVYGKTIdyhfygQEV----- 236
Cdd:cd07802 157 KD-WIRYRLTGEIS--TDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVT------AEAaaltg 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 237 -----PIAGVAGDQQAALFGQACFERGDVKNTYGTGGfmlMNTG--DKAVKSESGLLtTIAYGIDGKVnYALEGSIfVSG 309
Cdd:cd07802 227 lpegtPVAAGAFDVVASALGAGAVDEGQLCVILGTWS---INEVvtDEPVVPDSVGS-NSLHADPGLY-LIVEASP-TSA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 310 SAIQWLRD---GLRMINSAPQSESYATRVDSTE----GVYVVPaFVgLGTPYwDSEARGAIFGLTRGTEKEHFIRATLES 382
Cdd:cd07802 301 SNLDWFLDtllGEEKEAGGSDYDELDELIAAVPpgssGVIFLP-YL-YGSGA-NPNARGGFFGLTAWHTRAHLLRAVYEG 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446339515 383 LCYQTRDVMEAMSKDSGIDvqSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLAVG 451
Cdd:cd07802 378 IAFSHRDHLERLLVARKPE--TIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
4-451 |
2.56e-61 |
|
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: 207.46 E-value: 2.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFP--QSGWVEHDANEIWTSVLAVMTEVINENDVRADQIAGIGITNQ 81
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDddYPDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 82 RETTVVWDKhTGRPIY-------HAIVWQSrqtqsicsELKQQGYEQtFRDKTGLLLDPYFAGTKVKWILDNVEGAREKA 154
Cdd:cd07798 81 REGIVFLDK-DGRELYagpnidaRGVEEAA--------EIDDEFGEE-IYTTTGHWPTELFPAARLLWFKENRPEIFERI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 155 ENgdllFGTIDTWLVWKLSGKAAhiTDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGK--------- 225
Cdd:cd07798 151 AT----VLSISDWIGYRLTGELV--SEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTvseeaarel 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 226 TIDyhfygQEVPIAGVAGDQQAALFGQACFERGDVKNTYGTGGFMLMNTgDKAVKSESGLLTTIAYGIDGKvnYALEGSI 305
Cdd:cd07798 225 GLP-----EGTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVT-DEPIIDPERRLWTGCHLVPGK--WVLESNA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 306 FVSGSAIQWLRDGLRMINSAPQS---ESYATRVDSTEGVYvvpAFVGLGTPYWDSEA--RGAIF----GLTRGTEKEHFI 376
Cdd:cd07798 297 GVTGLNYQWLKELLYGDPEDSYEvleEEASEIPPGANGVL---AFLGPQIFDARLSGlkNGGFLfptpLSASELTRGDFA 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446339515 377 RATLESLCYQTRDVMEAMSKDSGIDVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLAVG 451
Cdd:cd07798 374 RAILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
4-450 |
5.17e-61 |
|
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466801 [Multi-domain] Cd Length: 429 Bit Score: 205.92 E-value: 5.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVINEndVRADQIAGIGITNQRE 83
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAE--LRPRRVVAIAVDGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 84 TTVVWDKHtGRPIYHAIVWQSRQTQSICSELKQQGYEQTFRdkTGLLLDPYFAGTKVKWILDNVEGAREKAEngdlLFGT 163
Cdd:cd07783 79 TLVLVDRE-GEPLRPAIMYNDARAVAEAEELAEAAGAVAPR--TGLAVSPSSSLAKLLWLKRHEPEVLAKTA----KFLH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 164 IDTWLVWKLSGKAAhITDYSNASRTLmFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGkTIDYHF---YG--QEVPI 238
Cdd:cd07783 152 QADWLAGRLTGDRG-VTDYNNALKLG-YDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIG-TLTAEAaeeLGlpAGTPV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 239 agVAG--DQQAALFGQACFERGDVKNTYGTG-GFMLmnTGDKAVKSESGLLTTIAYGIDGkvnYALEGSIFVSGSAIQWL 315
Cdd:cd07783 229 --VAGttDSIAAFLASGAVRPGDAVTSLGTTlVLKL--LSDKRVPDPGGGVYSHRHGDGY---WLVGGASNTGGAVLRWF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 316 RDGLRMinsaPQSESYATRVDSTeGVYVVPaFVGLG--TPYWDSEARGAIfgLTRGTEKEHFIRATLESLCYQTRDVMEA 393
Cdd:cd07783 302 FSDDEL----AELSAQADPPGPS-GLIYYP-LPLRGerFPFWDPDARGFL--LPRPHDRAEFLRALLEGIAFIERLGYER 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 446339515 394 MSKDSGIDVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEiQETTALGAAYLAGLAV 450
Cdd:cd07783 374 LEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAE-EEEAALGAALLAAAGL 429
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
260-449 |
7.43e-53 |
|
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: 177.13 E-value: 7.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 260 VKNTYGTGGFMLMnTGDKAVKSESGLLTTIaYGIDGKVNYALEGSIFVSGSAIQWLRDGLRM---------INSAPQSES 330
Cdd:pfam02782 1 LAISAGTSSFVLV-ETPEPVLSVHGVWGPY-TNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLreelrdagnVESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 331 YATRVDsTEGVYVVPAFVGLGTPYWDSEARGAIFGLTRGTEKEHFIRATLESLCYQTRDVMEAMSKDSGIDVQSLRVDGG 410
Cdd:pfam02782 79 LAAVAP-AGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSGG 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 446339515 411 AVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLA 449
Cdd:pfam02782 158 GSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
4-451 |
2.55e-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: 180.44 E-value: 2.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAILFN-QKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVINENDVRADQIAGIGITNQR 82
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 83 ETTVVWDKHtGRPIYHAIVWQSRQTQSICSELKQQ-GYEQTFrdKTGLLLDPYFAGTKVKWILDNVEGAREKAENGDLLF 161
Cdd:cd07809 81 HGLVALDAD-GKVLRPAKLWCDTRTAPEAEELTEAlGGKKCL--LVGLNIPARFTASKLLWLKENEPEHYARIAKILLPH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 162 GtidtWLVWKLSGKAahITDYSNASRTLMFNIHDLEWDDELLELLTVPKNM---LPEVKASSEVYGKTIDYH--FYG--Q 234
Cdd:cd07809 158 D----YLNWKLTGEK--VTGLGDASGTFPIDPRTRDYDAELLAAIDPSRDLrdlLPEVLPAGEVAGRLTPEGaeELGlpA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 235 EVPIAGVAGDQQAALFGQACFERGDVKNTYGTGGFmLMNTGDKAVKSESGLLTTIAygidgKVNYALEGSIFVSGSAIQW 314
Cdd:cd07809 232 GIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTSGT-AYGVSDKPVSDPHGRVATFC-----DSTGGMLPLINTTNCLTAW 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 315 LRDGLRMIN-SAPQ--SESYATRVDStEGVYVVPAFVGLGTPYWdSEARGAIFGLTRG-TEKEHFIRATLESLCYQTRDV 390
Cdd:cd07809 306 TELFRELLGvSYEEldELAAQAPPGA-GGLLLLPFLNGERTPNL-PHGRASLVGLTLSnFTRANLARAALEGATFGLRYG 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446339515 391 MEAMSKDsGIDVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLAVG 451
Cdd:cd07809 384 LDILREL-GVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
4-451 |
6.04e-47 |
|
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: 168.96 E-value: 6.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVINENDVRADQIAGIGITNQRE 83
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 84 TTVVWDKHtGRPIYHAIVWQSRQTQSICSELKQQG-YEQTFRdKTGLLLDPYFAGTKVKWILDNvegAREKAENGDLLFG 162
Cdd:cd24121 81 GTWLVDED-GRPVRDAILWLDGRAADIVERWQADGiAEAVFE-ITGTGLFPGSQAAQLAWLKEN---EPERLERARTALH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 163 TIDtWLVWKLSGKAAhiTDYSNASRTlMFNIHDLEWDDELLELLTVP--KNMLPEVKASSEVYGKTIDYH--FYG--QEV 236
Cdd:cd24121 156 CKD-WLFYKLTGEIA--TDPSDASLT-FLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAaaATGlpAGT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 237 PIAGVAGDQQAALFGQACFERGDVKNTYGTGGFMLMNTgDKAVKSESGLLTTIAYGIDGKVNYALegSIFVSGSAIQWLr 316
Cdd:cd24121 232 PVVLGPFDVVATALGSGAIEPGDACSILGTTGVHEVVV-DEPDLEPEGVGYTICLGVPGRWLRAM--ANMAGTPNLDWF- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 317 dgLRMINSAPQSESYATRVDS--------------TEGV----YVVPAfvGLGTPYWDSEARGAIFGLTRGTEKEHFIRA 378
Cdd:cd24121 308 --LRELGEVLKEGAEPAGSDLfqdleelaassppgAEGVlyhpYLSPA--GERAPFVNPNARAQFTGLSLEHTRADLLRA 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446339515 379 TLESLCYQTRDVMEAMskdsGIDVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLAVG 451
Cdd:cd24121 384 VYEGVALAMRDCYEHM----GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
4-492 |
7.68e-43 |
|
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466799 [Multi-domain] Cd Length: 504 Bit Score: 158.85 E-value: 7.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAILFN-QKGEIAGVAQREFKQYF--PQSGWVEHDANEIWTSVLAVMTEVINENDVRADQIAGIGI-- 78
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVdt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 79 TnqrETTVVWDKHTGRPIYHAIVWQ----SRQTQSIcSELkqqgyeqtfRDKTGLLLDPYFAGT--------KVKWILDN 146
Cdd:cd07781 81 T---SSTVVPVDEDGNPLAPAILWMdhraQEEAAEI-NET---------AHPALEYYLAYYGGVyssewmwpKALWLKRN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 147 VEGAREKA----ENGDllfgtidtWLVWKLSGK-AAHItdySNASRTLMFNIHDLEWDDELLE-----LLTVPKNMLPEV 216
Cdd:cd07781 148 APEVYDAAytivEACD--------WINARLTGRwVRSR---CAAGHKWMYNEWGGGPPREFLAaldpgLLKLREKLPGEV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 217 KASSEVYGkTIDYHF---YG--QEVPIAGVAGDQQAALFGQACFERGDVKNTYGTGG-FMLMNTGDKAVKsesgllttia 290
Cdd:cd07781 217 VPVGEPAG-TLTAEAaerLGlpAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTcHLMVSPKPVDIP---------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 291 yGIDGKVN-------YALEGSIFVSGSAIQWLRDGLRMINSAPQSESY------ATRVDSTE-GVYVVPAFVGLGTPYWD 356
Cdd:cd07781 286 -GICGPVPdavvpglYGLEAGQSAVGDIFAWFVRLFVPPAEERGDSIYallseeAAKLPPGEsGLVALDWFNGNRTPLVD 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 357 SEARGAIFGLTRGTEKEHFIRATLESLCYQTRDVMEAMsKDSGIDVQSLRVDGG-AVKNNFIMQFQADIVNTSVERPEIQ 435
Cdd:cd07781 365 PRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERF-EEAGVPVNRVVACGGiAEKNPLWMQIYADVLGRPIKVPKSD 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 446339515 436 ETTALGAAYLAGLAVGFWESKDDIAKNWKLEEK-FDPKMDEGER-EKLYRGWKKAVEAT 492
Cdd:cd07781 444 QAPALGAAILAAVAAGVYADIEEAADAMVRVDRvYEPDPENHAVyEELYALYKELYDAL 502
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
4-446 |
1.72e-40 |
|
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: 151.22 E-value: 1.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAILFN-QKGEIAGVAQREFKQYFPQ--SGWVEHDANEIWTSVLAVMTEVINENDVRadqIAGIGITN 80
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDlESGRILESVSRPTPAPISSddPGRSEQDPEKILEAVRNLIDELPREYLSD---VTGIGITG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 81 QRETTVVWDKHtGRPIYHAIVWQ-SRQTQSICSELKQqgYEQTFRDKTGLLLDPYFAGTKVKWIldnvegarekAENGDL 159
Cdd:cd07777 78 QMHGIVLWDED-GNPVSPLITWQdQRCSEEFLGGLST--YGEELLPKSGMRLKPGYGLATLFWL----------LRNGPL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 160 L-----FGTIDTWLVWKLSGKAAHITDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGKTIdyHFYGQ 234
Cdd:cd07777 145 PskadrAGTIGDYIVARLTGLPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLS--SALPK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 235 EVPIAGVAGDQQAALFGQACFERGDVKNTYGTGGFMLMNTgDKAVKSES---------GLLTTIAyGIDGKVNYAlegsI 305
Cdd:cd07777 223 GIPVYVALGDNQASVLGSGLNEENDAVLNIGTGAQLSFLT-PKFELSGSveirpffdgRYLLVAA-SLPGGRALA----V 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 306 FVsgsaiQWLRDGLRMINSAPQSES-Y-----ATRVDSTEGVYVVPAFvgLGTPyWDSEARGAIFGLTRGTEK-EHFIRA 378
Cdd:cd07777 297 LV-----DFLREWLRELGGSLSDDEiWekldeLAESEESSDLSVDPTF--FGER-HDPEGRGSITNIGESNFTlGNLFRA 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446339515 379 TLESLCYQTRDVMEAMSKDSGiDVQSLRVDGGAV-KNNFIMQFQADIVNTSVERPEIQETTALGAAYLA 446
Cdd:cd07777 369 LCRGIAENLHEMLPRLDLDLS-GIERIVGSGGALrKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
4-485 |
5.57e-39 |
|
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: 147.86 E-value: 5.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAILFNQKGEIAGVAQREF--KQYFPQSGWVEHDANEIWTSVLAVMTEVINENDVRADQIAGIGITNQ 81
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREWrhKEVPDVPGSMDFDTEKNWKLICECIREALKKAGIAPKSIAAISTTSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 82 RETTVVWDKHtGRPIYHAIVWQSRQTQSIcSELKQQ--GYEQTFRDKTG--LLLDpyfAGTKVKWILDNVEGAREKAENg 157
Cdd:cd07775 81 REGIVLYDNE-GEEIWACANVDARAAEEV-SELKELynTLEEEVYRISGqtFALG---AIPRLLWLKNNRPEIYRKAAK- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 158 dllFGTIDTWLVWKLSGKAAhiTDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGK-TIDYHF---YG 233
Cdd:cd07775 155 ---ITMLSDWIAYKLSGELA--VEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKvTKEAAEetgLK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 234 QEVPIAGVAGDQQAALFGQacferGDVKNTYGT---GGF--MLMNTgDKAVKSESGLLTTIAYGIDGKVNYalEGSIFVS 308
Cdd:cd07775 230 EGTPVVVGGGDVQLGCLGL-----GVVRPGQTAvlgGSFwqQEVNT-AAPVTDPAMNIRVNCHVIPDMWQA--EGISFFP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 309 GSAIQWLRDGL--------------------RMINSAPQSE-----SYATRVDSTEGVYVVPAFVGLGTpywDSEargai 363
Cdd:cd07775 302 GLVMRWFRDAFcaeekeiaerlgidaydlleEMAKDVPPGSygimpIFSDVMNYKNWRHAAPSFLNLDI---DPE----- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 364 fgltrGTEKEHFIRATLESLCYQTRDVMEAMSKDSGIDVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAA 443
Cdd:cd07775 374 -----KCNKATFFRAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAA 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 446339515 444 YLAGLAVGFWESKDDIAKNW-KLEEKFDPKMDEGER-EKLYRGW 485
Cdd:cd07775 449 IAAGVGAGIYSSLEEAVESLvKWEREYLPNPENHEVyQDLYEKW 492
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
4-471 |
4.91e-33 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 131.24 E-value: 4.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YIlSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVINENDVRadQIAGIGITNQRE 83
Cdd:PRK15027 2 YI-GIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQ--DVKALGIAGQMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 84 TTVVWDKHTgRPIYHAIVWQSRQTQSICSELKQQgyEQTFRDKTGLLLDPYFAGTKVKWIldnvegAREKAEngdlLFGT 163
Cdd:PRK15027 79 GATLLDAQQ-RVLRPAILWNDGRCAQECALLEAR--VPQSRVITGNLMMPGFTAPKLLWV------QRHEPE----IFRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 164 IDT------WLVWKLSGKAAhiTDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGKTID--YHFYGQ- 234
Cdd:PRK15027 146 IDKvllpkdYLRLRMTGEFA--SDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPevAKAWGMa 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 235 EVPIAGVAGDQQAALFGQACFERGDVKNTYGTGGFMLMNTGDKAVKSESGLlTTIAYGIDGKvnYALEGSIFVSGSAIQW 314
Cdd:PRK15027 224 TVPVVAGGGDNAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAV-HSFCHALPQR--WHLMSVMLSAASCLDW 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 315 ------LRDGLRMINSAPQSEsyatrvDSTEGVYVVPAFVGLGTPYWDSEARGAIFGLTRGTEKEHFIRATLESLCYQTR 388
Cdd:PRK15027 301 aakltgLSNVPALIAAAQQAD------ESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 389 DVMEAMsKDSGIDVQSLRVDGGAVKNNFIMQFQADIVNTSVE-RPEIQETTALGAAYLAGLAVGFWESKDDIAKNWKLEE 467
Cdd:PRK15027 375 DGMDVV-HACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDyRTGGDVGPALGAARLAQIAANPEKSLIELLPQLPLEQ 453
|
....
gi 446339515 468 KFDP 471
Cdd:PRK15027 454 SHLP 457
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
4-457 |
9.17e-28 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 115.51 E-value: 9.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAILFNQKGEIAGVAQ--REFKQYFPQSGWVEHDANEIWTSVLAVMTEVINEndVRADQIAGIGITNQ 81
Cdd:PRK10331 3 VILVLDCGATNVRAIAVDRQGKIVARAStpNASDIAAENSDWHQWSLDAILQRFADCCRQINSE--LTECHIRGITVTTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 82 RETTVVWDKHtGRPIYHAIVWQSRQTQSICSELKQQGYEQTFRDKTGLllDPYFAGT--KVKWILDNVEGAREKAENgdL 159
Cdd:PRK10331 81 GVDGALVDKQ-GNLLYPIISWKCPRTAAVMENIERYISAQQLQQISGV--GAFSFNTlyKLVWLKENHPQLLEQAHA--W 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 160 LFgtIDTWLVWKLSGKAAhiTDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGKTI----DYHFYGQE 235
Cdd:PRK10331 156 LF--ISSLINHRLTGEFT--TDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQpsaaALLGLPVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 236 VPIAGVAGDQQAALFGQACFERGDVKNTyGTGGFMLMNTG--DKAVKSESGLLTTIAYGIDGKVNYALEgsiFVSGSAIQ 313
Cdd:PRK10331 232 IPVISAGHDTQFALFGSGAGQNQPVLSS-GTWEILMVRSAqvDTSLLSQYAGSTCELDSQSGLYNPGMQ---WLASGVLE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 314 WLRDGLrminsAPQSESYATRVDS-------TEGVYVVPAFVGLGTpywdsearGAIFGLTRGTEKEHFIRATLESLCYQ 386
Cdd:PRK10331 308 WVRKLF-----WTAETPYQTMIEEaraippgADGVKMQCDLLACQN--------AGWQGVTLNTTRGHFYRAALEGLTAQ 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446339515 387 TRDVMEAMSKDSGIDVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLAVGFWESKD 457
Cdd:PRK10331 375 LKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPE 445
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
4-483 |
9.66e-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: 113.10 E-value: 9.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAILFN-QKGEIAGVAQREFKQY-FPQSGWVEHDANEIWTSVLAVMTEVINENDVRADQIAGIGITN- 80
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDlYAGLEMAQEPVPYYQDsSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVDAt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 81 ------QRETTVVWDKHTGRPIYHAIVWQSRQTQSICSELKQQGyEQTFRDKTGLLLDPYFAGTKVKWILDNVEGAREKA 154
Cdd:cd07768 81 cslaifDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWINMQC-PQQLLDYLGGKISPEMGVPKLKYFLDEYSHLRDKH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 155 engDLLFGTIDtWLVWKLSGkaahitDYSNASRTLMF--NIHDLE--WDDEL-------LELLTVPKNmLPEVKASSEVY 223
Cdd:cd07768 160 ---FHIFDLHD-YIAYELTR------LYEWNICGLLGkeNLDGEEsgWSSSFfknidprLEHLTTTKN-LPSNVPIGTTS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 224 GKTIDYHF--YGQEVPIAGVAG--DQQAALFGQAcfergdVKNTYGTGgFMLMNTgdkavKSESGLLTTIAY---GIDGK 296
Cdd:cd07768 229 GVALPEMAekMGLHPGTAVVVSciDAHASWFAVA------SPHLETSL-FMIAGT-----SSCHMYGTTISDripGVWGP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 297 VNYALEGSIFV-------SGSAIQWLrdglrmINSAPQSESYATRVDSTEGVYVV---------------------PAFV 348
Cdd:cd07768 297 FDTIIDPDYSVyeagqsaTGKLIEHL------FESHPCARKFDEALKKGADIYQVleqtirqieknnglsihiltlDMFF 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 349 GLGTPYWDSEARGAIFGLTRGTEKEHF---IRATLESLCYQTRDVMEAMSKDsGIDVQSLRVDGGAVKNNFIMQFQADIV 425
Cdd:cd07768 371 GNRSEFADPRLKGSFIGESLDTSMLNLtykYIAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKNERLLQLIALVT 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446339515 426 NTSVERPEIQETTALGAAYLAGLAVGFWESKDDI----AKNWKLEEKFDPKMDE--GEREKLYR 483
Cdd:cd07768 450 NVAIIKPKENMMGILGAAVLAKVAAGKKQLADSIteadISNDRKSETFEPLAYRlgADYILLYK 513
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
4-461 |
4.29e-26 |
|
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: 111.47 E-value: 4.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVINENDVRADQIAGIGITnqre 83
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 84 TT---VVWDKH--------TGRPIYHAIVWQ----SRQTQSICSelkqQGYEqtfrdktglLLDpYFAGT--------KV 140
Cdd:cd07782 77 ATcslVVLDAEgkpvsvspSGDDERNVILWMdhraVEEAERINA----TGHE---------VLK-YVGGKispemeppKL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 141 KWILDNVEGAREKAENgdlLFGTIDtWLVWKLSGKAAHitdySNASRT-----LMFNIHDLEWDDELLELL--------- 206
Cdd:cd07782 143 LWLKENLPETWAKAGH---FFDLPD-FLTWKATGSLTR----SLCSLVckwtyLAHEGSEGGWDDDFFKEIgledlvedn 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 207 ------------TVPKNMLPEvKASSE--------VYGKTIDYHfygqevpiAGVAGDQQAALFGQACfERGDVKNTY-- 264
Cdd:cd07782 215 fakigsvvlppgEPVGGGLTA-EAAKElglpegtpVGVSLIDAH--------AGGLGTLGADVGGLPC-EADPLTRRLal 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 265 --GTGG-FMLMNTGDKAVKsesgllttiayGIDGKVNYAL-------EGSIFVSGSAIQWL------------------- 315
Cdd:cd07782 285 icGTSScHMAVSPEPVFVP-----------GVWGPYYSAMlpglwlnEGGQSATGALLDHIiethpaypelkeeakaagk 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 316 -------RDGLRMINSAPQSESYATRvdsteGVYVVPAFVGLGTPYWDSEARGAIFGLTRGTEKEHFIR---ATLESLCY 385
Cdd:cd07782 354 siyeylnERLEQLAEEKGLPLAYLTR-----DLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAY 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446339515 386 QTRDVMEAMSKdSGIDVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLAVGFWESKDDIAK 461
Cdd:cd07782 429 GTRHIIEAMNA-AGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDAMA 503
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
1-488 |
2.17e-25 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 109.33 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 1 MEKYILSIDQGTTSSRAILFNQKGEIAGVAQREFKQY----FPQSgwVEHDANEIWTSVLAVMTEVINENDVRADQIAGI 76
Cdd:PRK10939 1 SMSYLMALDAGTGSIRAVIFDLNGNQIAVGQAEWRHLavpdVPGS--MEFDLEKNWQLACQCIRQALQKAGIPASDIAAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 77 GITNQRETTVVWDKhTGRPIYHAIVWQSRQTQSIcSELKQ--QGYEQTFRDKTG--LLLDpyfAGTKVKWILDNVEGARE 152
Cdd:PRK10939 79 SATSMREGIVLYDR-NGTEIWACANVDARASREV-SELKElhNNFEEEVYRCSGqtLALG---ALPRLLWLAHHRPDIYR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 153 KAENgdllFGTIDTWLVWKLSGKAAhiTDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGKTIDYhfY 232
Cdd:PRK10939 154 QAHT----ITMISDWIAYMLSGELA--VDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAK--A 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 233 GQE------VPIAGVAGDQQAALFGQACFERGDVKNTYGTGGFMLMNTGDKAVKSESGLLTTiAYGIDGKVNYalEGSIF 306
Cdd:PRK10939 226 AAEtglragTPVVMGGGDVQLGCLGLGVVRPGQTAVLGGTFWQQVVNLPAPVTDPNMNIRIN-PHVIPGMVQA--ESISF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 307 VSGSAIQWLRD----GLRMINSAPQSESYATRVDSTEGVYV---------------------VPAFVGLGTpywDSEA-- 359
Cdd:PRK10939 303 FTGLTMRWFRDafcaEEKLLAERLGIDAYSLLEEMASRVPVgshgiipifsdvmrfkswyhaAPSFINLSI---DPEKcn 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 360 RGAIFgltrgtekehfiRATLESLCYQTRDVMEAMSKDSGIDVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTA 439
Cdd:PRK10939 380 KATLF------------RALEENAAIVSACNLQQIAAFSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATA 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 446339515 440 LGAAYLAGLAVGFWESKDDIAKNW-KLEEKFDPKMDEGE-REKLYRGWKKA 488
Cdd:PRK10939 448 LGCAIAAGVGAGIYSSLAETGERLvRWERTFEPNPENHElYQEAKEKWQAV 498
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
2-455 |
3.15e-23 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 102.89 E-value: 3.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 2 EKYILSIDQGTTSSRAILFN-QKGEIAGVAQREFKQY------FPQSGWVEHDANEIWTSVLAVMTEVINENDVRADQIA 74
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDaADGEELASAVHPYPRWviglylPPPPDQARQHPLDYLEALEAAVREALAQAGVDPADVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 75 GIGItnqrETT----VVWDKH----------TGRPiyHA--IVWQ----SRQTQSICSELKQQGYEQTfrdktgllldPY 134
Cdd:COG1069 81 GIGV----DATgctpVPVDADgtplallpefAENP--HAmvILWKdhtaQEEAERINELAKARGEDYL----------RY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 135 FAGT--------KVKWILDNVEGAREKA----ENGDllfgtidtWLVWKLSGKAAhitdYSNASRT--LMFNIHDLEW-D 199
Cdd:COG1069 145 VGGIissewfwpKILHLLREDPEVYEAAdsfvELCD--------WITWQLTGSLK----RSRCTAGhkALWHAHEGGYpS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 200 DELLE----LLTVPKNMLP-EVKASSEVYGK--------------------TIDYHfygqevpiAGVAG------DQQAA 248
Cdd:COG1069 213 EEFFAaldpLLDGLADRLGtEIYPLGEPAGTltaewaarlglppgtavavgAIDAH--------AGAVGaggvepGTLVK 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 249 LFG-QACfergDvkntygtggfMLMNTGDKAVKsesgllttiayGIDGKVN-------YALEG--SIFvsGSAIQWLRDG 318
Cdd:COG1069 285 VMGtSTC----H----------MLVSPEERFVP-----------GICGQVDgsivpgmWGYEAgqSAV--GDIFAWFVRL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 319 L-----------RMINSAPQ--SESYATRVDSTEGVYVVPAFVGLGTPYWDSEARGAIFGLTRGTEKEHFIRATLESLCY 385
Cdd:COG1069 338 LvppleyekeaeERGISLHPllTEEAAKLPPGESGLHALDWFNGNRSPLADQRLKGVILGLTLGTDAEDIYRALVEATAF 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446339515 386 QTRDVMEAMsKDSGIDVQSLRVDGG-AVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLAVGFWES 455
Cdd:COG1069 418 GTRAIIERF-EEEGVPIDEIIACGGiATKNPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPD 487
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
172-484 |
2.98e-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: 81.06 E-value: 2.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 172 LSGKAAHItDYSNASRTLMFNIHDLEWDDELLELLTVP--KNMLPEVKASSEVYGKTIDYHF--YG--QEVPIAGVAGDQ 245
Cdd:cd07776 196 LLGRYAPI-DESDGSGMNLMDIRSRKWSPELLDAATAPdlKEKLGELVPSSTVAGGISSYFVerYGfsPDCLVVAFTGDN 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 246 QAALFGQACfERGDVKNTYGTGGFMLMNTgDKAVKSESGLLTtiaygidgkVNYALEGSIFV-----SGS-AIQWLRDGL 319
Cdd:cd07776 275 PASLAGLGL-EPGDVAVSLGTSDTVFLVL-DEPKPGPEGHVF---------ANPVDPGSYMAmlcykNGSlARERVRDRY 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 320 ---------RMINSAPQSEsyatrvdstEGVyvvpafvgLGTPYWDSE----------ARGAIFGLTRGTEKEHFIRATL 380
Cdd:cd07776 344 aggswekfnELLESTPPGN---------NGN--------LGLYFDEPEitppvpgggrRFFGDDGVDAFFDPAVEVRAVV 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 381 ESLCYQTRDVMEAMSkdSGIDVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAYLAGLAVGFWESKDDIA 460
Cdd:cd07776 407 ESQFLSMRLHAERLG--SDIPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSP 484
|
330 340
....*....|....*....|....*.
gi 446339515 461 KNWKLEEKFDPKMDEGERE--KLYRG 484
Cdd:cd07776 485 EFVVFSAEEPKLVAEPDPEaaEVYDK 510
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
4-441 |
6.86e-16 |
|
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.
Pssm-ID: 466791 [Multi-domain] Cd Length: 460 Bit Score: 79.88 E-value: 6.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 4 YILSIDQGTTSSRAIL--FNQKG-EIAGVAQreFKQYFPQSG----WvehDANEIWTSVLAVMTEVINendvRADQIAGI 76
Cdd:cd07771 1 NYLAVDLGASSGRVILgsLDGGKlELEEIHR--FPNRPVEINghlyW---DIDRLFDEIKEGLKKAAE----QGGDIDSI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 77 GITnqretTvvW-------DKHtGRPIYHAIVWQSRQTQSICSELKQQGYEQTFRDKTGLLLDPYFAGTKVKWIldnveg 149
Cdd:cd07771 72 GID-----T--WgvdfgllDKN-GELLGNPVHYRDPRTEGMMEELFEKISKEELYERTGIQFQPINTLYQLYAL------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 150 arekAENGDLLFGTIDTWL------VWKLSGKAAhiTDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVY 223
Cdd:cd07771 138 ----KKEGPELLERADKLLmlpdllNYLLTGEKV--AEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 224 GK---TIDYHFYGQEVPIAGVAG-DQQAALFGQACFERGDVkntY---GTggFMLMntGdkaVKSESGLLTTIAY----- 291
Cdd:cd07771 212 GTlkpEVAEELGLKGIPVIAVAShDTASAVAAVPAEDEDAA---FissGT--WSLI--G---VELDEPVITEEAFeagft 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 292 ---GIDGKVNYA--LEGSIFVSGSAIQWLRDGLR-----MINSAPQSESYATRVDSTEgvyvvPAFvglGTPywdSEARG 361
Cdd:cd07771 282 negGADGTIRLLknITGLWLLQECRREWEEEGKDysydeLVALAEEAPPFGAFIDPDD-----PRF---LNP---GDMPE 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 362 AI------FGLTRGTEKEHFIRATLESLCYQTRDVMEAMSKDSGIDVQSLRVDGGAVKNNFIMQFQADIVNTSVER-PEi 434
Cdd:cd07771 351 AIraycreTGQPVPESPGEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAgPV- 429
|
....*..
gi 446339515 435 qETTALG 441
Cdd:cd07771 430 -EATAIG 435
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
352-451 |
4.16e-15 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 77.58 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 352 TPYWDSEARGAIFGLTRGTEKEHFIRATLESLCYQTRDVMEAMsKDSGIDVQSLRVDGG-AVKNNFIMQFQADIVNTSVE 430
Cdd:PRK04123 390 TPLADQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECF-EDQGVPVEEVIAAGGiARKNPVLMQIYADVLNRPIQ 468
|
90 100
....*....|....*....|.
gi 446339515 431 RPEIQETTALGAAYLAGLAVG 451
Cdd:PRK04123 469 VVASDQCPALGAAIFAAVAAG 489
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
6-446 |
3.85e-08 |
|
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: 55.87 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 6 LSIDQGTTSSRAILFNQKGEIAGVAQRE--FKQYFPQSGWVEHDANEIWTSVL-AVMTEVINENDVradQIAGIGIT--- 79
Cdd:cd07778 3 IGIDVGSTSVRIGIFDYHGTLLATSERPisYKQDPKDLWFVTQSSTEIWKAIKtALKELIEELSDY---IVSGIGVSatc 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 80 -----NQRETTVVW-----DKHTGRPIYHAIVWQSRQTQSICSELKQQgYEQTFRDKTGLLLDPYFAGTKVKWILDNVEG 149
Cdd:cd07778 80 smvvmQRDSDTSYLvpynvIHEKSNPDQDIIFWMDHRASEETQWLNNI-LPDDILDYLGGGFIPEMAIPKLKYLIDLIKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 150 AREKaengDLLFGTIDTWLVWKLSGKAAHITDYSNASRTLMFNIHDLE---WDDELLELLTVP----------KNMLPEV 216
Cdd:cd07778 159 DTFK----KLEVFDLHDWISYMLATNLGHSNIVPVNAPPSIGIGIDGSlkgWSKDFYSKLKIStkvcnvgntfKEAPPLP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 217 KASSEV-YGKTIDYHFYGQEVPIAGVAG--DQQAALFgqACFERGDVKNTY-----GTGGFMLMNTGDKAVKSESGLLTT 288
Cdd:cd07778 235 YAGIPIgKVNVILASYLGIDKSTVVGHGciDCYAGWF--STFAAAKTLDTTlfmvaGTSTCFLYATSSSQVGPIPGIWGP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 289 IAYGIDGKVNY-------------------ALEGSIFVSGSAIQWLRDGLRMI-NSAPQSESYATRVDSTEGVYvvpafV 348
Cdd:cd07778 313 FDQLLKNYSVYeggqsatgklieklfnshpAIIELLKSDANFFETVEEKIDKYeRLLGQSIHYLTRHMFFYGDY-----L 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 349 GLGTPYWDSEARGAIFGLTRGTEKE----HFIrATLESLCYQTRDVMEAMSKDSGIdVQSLRVDGGAVKNNFIMQ---FQ 421
Cdd:cd07778 388 GNRTPYNDPNMSGSFIGESTDSSLTdlvlKYI-LILEFLAFQTKLIIDNFQKEKII-IQKVVISGSQAKNARLLQllsTV 465
|
490 500
....*....|....*....|....*
gi 446339515 422 ADIVNTSVERPEIQETTALGAAYLA 446
Cdd:cd07778 466 LSKIHIIVPLSDSKYAVVKGAALLG 490
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
5-446 |
1.55e-06 |
|
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: 50.34 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 5 ILSIDQGTTSSRAILFNQKGEIagVAQREFKQYF-PQSGWVEHDANEIWTSVLAVMTEVINENDVRAdqiagIGITNQRE 83
Cdd:cd07772 2 IAVFDIGKTNKKLLLFDENGEV--LAERSTPNPEiEEDGYPCEDVEAIWEWLLDSLAELAKRHRIDA-----INFTTHGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 84 TTVVWDKHTGR--PIY---HAIVwqsrqtQSICSELKQQ--GYEQTFrdkTGLLLDPYFAGTKVKWIldnvegAREKAEn 156
Cdd:cd07772 75 TFALLDENGELalPVYdyeKPIP------DEINEAYYAErgPFEETG---SPPLPGGLNLGKQLYWL------KREKPE- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 157 gdlLFGTIDTWL------VWKLSGKAAhiTDYSNAS-RTLMFNIHDLEWDDELLELLTvpKNMLPEVKASSEVYGKTI-- 227
Cdd:cd07772 139 ---LFARAKTILplpqywAWRLTGKAA--SEITSLGcHTDLWDFEKNEYSSLVKKEGW--DKLFPPLRKAWEVLGPLRpd 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 228 --DYHFYGQEVPI-AGVAgDQQAALFG-QACFERGDVKNTYGTGgFMLMNTGDKAVKSESGLLTTIAYGID--GKVnyaL 301
Cdd:cd07772 212 laRRTGLPKDIPVgCGIH-DSNAALLPyLAAGKEPFTLLSTGTW-CIAMNPGNDLPLTELDLARDCLYNLDvfGRP---V 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446339515 302 EGSIFVSGSAIQWLRDGLRMINSAPQSESYATRVDStEGVYVVPAFVGLGTPYwdSEARGAIFGLTRGTEKEHFIRATLe 381
Cdd:cd07772 287 KTARFMGGREYERLVERIAKSFPQLPSLADLAKLLA-RGTFALPSFAPGGGPF--PGSGGRGVLSAFPSAEEAYALAIL- 362
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446339515 382 SLCYQTRDVMEAMSKDsgidVQSLRVDGGAVKNNFIMQF-QADIVNTSVERPEIQETTALGAAYLA 446
Cdd:cd07772 363 YLALMTDYALDLLGSG----VGRIIVEGGFAKNPVFLRLlAALRPDQPVYLSDDSEGTALGAALLA 424
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
164-242 |
7.18e-05 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 45.10 E-value: 7.18e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446339515 164 IDTWLVWKLSGKAAhiTDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGKTIDYHfyGQEVPIAGVA 242
Cdd:PRK10640 142 IPDYFSYRLTGKMN--WEYTNATTTQLVNINSDDWDESLLAWSGAPKAWFGRPTHPGNVIGHWICPQ--GNEIPVVAVA 216
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-78 |
1.11e-03 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 41.04 E-value: 1.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446339515 1 MEKYILSIDQGTTSSRAILFNQKGEIagVAQREFKqyFPQsgwvEHDANEIWTSVLAVMTEVINENDVRADQIAGIGI 78
Cdd:COG1940 3 DAGYVIGIDIGGTKIKAALVDLDGEV--LARERIP--TPA----GAGPEAVLEAIAELIEELLAEAGISRGRILGIGI 72
|
|
| |
