|
Name |
Accession |
Description |
Interval |
E-value |
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
21-513 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 858.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEYGCIVAQARRSVKTSFPRPGWVEQDPTEVLASQIGVMMEVQFKSGIHSDRIAAIGISNQRE 100
Cdd:COG0554 4 YILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITNQRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 101 TTVVWDRISGQPIYNAIVWQCRRTAPLIDELVEQGAEELVRSRTGLTLDPYFSASKVQWILDNVDGARESAAAGDLMFGT 180
Cdd:COG0554 84 TTVVWDRKTGKPLYNAIVWQDRRTADICEELKADGLEDLIREKTGLVLDPYFSATKIKWILDNVPGARERAEAGELLFGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 181 IDTWLIYNLTGGQVFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRVASDIMTNMPPIMGVAGD 260
Cdd:COG0554 164 IDSWLIWKLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDPDLFGAEIPIAGIAGD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 261 QQASLFGHCCFHPGQTKNTYGTGCFMLMNTGDEIVESKNGLVSTIGIAADGKISYALEGSIFAAGSTMNWLRNNMGIISS 340
Cdd:COG0554 244 QQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGGKVTYALEGSIFVAGAAVQWLRDGLGLIDS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 341 VSESAQLATSINDNEGCYFVPAFAGLGAPWWDPHARGIVCGLTGASSRATIVRAACESMAYQSYDVLRAMEQDVGLSIER 420
Cdd:COG0554 324 AAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADSGIPLKE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 421 LSVDGGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLAVGYWEDLEELEQNAQIVKVFHPHMSAERRESNLAG 500
Cdd:COG0554 404 LRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEELAALWKVDRRFEPQMDEEERERLYAG 483
|
490
....*....|...
gi 2192564081 501 WRDAVKRSLNTAQ 513
Cdd:COG0554 484 WKKAVERTLGWAE 496
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
21-506 |
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: 815.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEYGCIVAQARRSVKTSFPRPGWVEQDPTEVLASQIGVMMEVQFKSGIHSDRIAAIGISNQRE 100
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 101 TTVVWDRISGQPIYNAIVWQCRRTAPLIDELVEQGAEELVRSRTGLTLDPYFSASKVQWILDNVDGARESAAAGDLMFGT 180
Cdd:cd07786 81 TTVVWDRETGKPVYNAIVWQDRRTADICEELKAEGHEEMIREKTGLVLDPYFSATKIRWILDNVPGARERAERGELAFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 181 IDTWLIYNLTGGQVFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRVASDIMTNMPPIMGVAGD 260
Cdd:cd07786 161 IDSWLIWKLTGGKVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDPDLLGAEIPIAGIAGD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 261 QQASLFGHCCFHPGQTKNTYGTGCFMLMNTGDEIVESKNGLVSTIGIAADGKISYALEGSIFAAGSTMNWLRNNMGIISS 340
Cdd:cd07786 241 QQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLGGKVTYALEGSIFIAGAAVQWLRDGLGLIES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 341 VSESAQLATSINDNEGCYFVPAFAGLGAPWWDPHARGIVCGLTGASSRATIVRAACESMAYQSYDVLRAMEQDVGLSIER 420
Cdd:cd07786 321 AAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEADSGIPLKE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 421 LSVDGGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLAVGYWEDLEELEQNAQIVKVFHPHMSAERRESNLAG 500
Cdd:cd07786 401 LRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAKLWQVDRRFEPSMSEEEREALYAG 480
|
....*.
gi 2192564081 501 WRDAVK 506
Cdd:cd07786 481 WKKAVK 486
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
21-506 |
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: 798.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEYGCIVAQARRSVKTSFPRPGWVEQDPTEVLASQIGVMMEVQFKSGIHSDRIAAIGISNQRE 100
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 101 TTVVWDRISGQPIYNAIVWQCRRTAPLIDELVEQGAEELVRSRTGLTLDPYFSASKVQWILDNVDGARESAAAGDLMFGT 180
Cdd:cd07769 81 TTVVWDKKTGKPLYNAIVWQDRRTADICEELKAKGLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAERGELLFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 181 IDTWLIYNLTGGQVFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRVASDIMTNMPPIMGVAGD 260
Cdd:cd07769 161 IDTWLIWKLTGGKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTDPEGLGAGIPIAGILGD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 261 QQASLFGHCCFHPGQTKNTYGTGCFMLMNTGDEIVESKNGLVSTIGIAADGKISYALEGSIFAAGSTMNWLRNNMGIISS 340
Cdd:cd07769 241 QQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQIGGKVTYALEGSIFIAGAAIQWLRDNLGLIED 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 341 VSESAQLATSINDNEGCYFVPAFAGLGAPWWDPHARGIVCGLTGASSRATIVRAACESMAYQSYDVLRAMEQDVGLSIER 420
Cdd:cd07769 321 AAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDSGIKLKE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 421 LSVDGGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLAVGYWEDLEELEQNAQIVKVFHPHMSAERRESNLAG 500
Cdd:cd07769 401 LRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDELASLWQVDKRFEPSMDEEERERLYRG 480
|
....*.
gi 2192564081 501 WRDAVK 506
Cdd:cd07769 481 WKKAVE 486
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
21-510 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 779.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEYGCIVAQARRSVKTSFPRPGWVEQDPTEVLASQIGVMMEVQFKSGIHSDRIAAIGISNQRE 100
Cdd:PRK00047 6 YILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGITNQRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 101 TTVVWDRISGQPIYNAIVWQCRRTAPLIDELVEQGAEELVRSRTGLTLDPYFSASKVQWILDNVDGARESAAAGDLMFGT 180
Cdd:PRK00047 86 TTVVWDKETGRPIYNAIVWQDRRTADICEELKRDGYEDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGELLFGT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 181 IDTWLIYNLTGGQVFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRVASD-IMTNMPPIMGVAG 259
Cdd:PRK00047 166 IDTWLVWKLTGGKVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYgFFGGEVPIAGIAG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 260 DQQASLFGHCCFHPGQTKNTYGTGCFMLMNTGDEIVESKNGLVSTIGIAADGKISYALEGSIFAAGSTMNWLRNNMGIIS 339
Cdd:PRK00047 246 DQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGIDGKVVYALEGSIFVAGSAIQWLRDGLKIIS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 340 SVSESAQLATSINDNEGCYFVPAFAGLGAPWWDPHARGIVCGLTGASSRATIVRAACESMAYQSYDVLRAMEQDVGLSIE 419
Cdd:PRK00047 326 DASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADSGIRLK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 420 RLSVDGGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLAVGYWEDLEELEQNAQIVKVFHPHMSAERRESNLA 499
Cdd:PRK00047 406 ELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDELKEQWKIDRRFEPQMDEEEREKLYA 485
|
490
....*....|.
gi 2192564081 500 GWRDAVKRSLN 510
Cdd:PRK00047 486 GWKKAVKRTLA 496
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
21-510 |
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: 720.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEYGCIVAQARRSVKTSFPRPGWVEQDPTEVLASQIGVMMEVQFKSGIHSDRIAAIGISNQRE 100
Cdd:TIGR01311 2 YILAIDQGTTSSRAIVFDKDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAGIKPDDIAAIGITNQRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 101 TTVVWDRISGQPIYNAIVWQCRRTAPLIDELVEQGAEELVRSRTGLTLDPYFSASKVQWILDNVDGARESAAAGDLMFGT 180
Cdd:TIGR01311 82 TTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYGEFIREKTGLPLDPYFSATKLRWLLDNVPGVREAAERGELLFGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 181 IDTWLIYNLTGGQVFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRVASDIMTNMPPIMGVAGD 260
Cdd:TIGR01311 162 IDTWLIWNLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYTDPGLLGAEIPITGVLGD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 261 QQASLFGHCCFHPGQTKNTYGTGCFMLMNTGDEIVESKNGLVSTIGIAADGKIS-YALEGSIFAAGSTMNWLRNNMGIIS 339
Cdd:TIGR01311 242 QQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKKPvYALEGSVFVAGAAVQWLRDNLKLIK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 340 SVSESAQLATSINDNEGCYFVPAFAGLGAPWWDPHARGIVCGLTGASSRATIVRAACESMAYQSYDVLRAMEQDVGLSIE 419
Cdd:TIGR01311 322 HAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTRDVLEAMEKDAGVEIT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 420 RLSVDGGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLAVGYWEDLEELEQNAQIVKVFHPHMSAERRESNLA 499
Cdd:TIGR01311 402 KLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWRVEKTFEPEMDEEEREARYA 481
|
490
....*....|.
gi 2192564081 500 GWRDAVKRSLN 510
Cdd:TIGR01311 482 GWKEAVKRSLG 492
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
21-508 |
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: 649.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEYGCIVAQARRSVKTSFPRPGWVEQDPTEVLASQIGVMMEV--QFKS-GIHSDRIAAIGISN 97
Cdd:cd07792 2 LVGAIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAveKLKAlGISPSDIKAIGITN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 98 QRETTVVWDRISGQPIYNAIVWQCRRTAPLIDELVEQ--GAEELVRSRTGLTLDPYFSASKVQWILDNVDGARESAAAGD 175
Cdd:cd07792 82 QRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELSAKtpGGKDHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDDGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 176 LMFGTIDTWLIYNLTGG---QVFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRVASDIMTNMP 252
Cdd:cd07792 162 LLFGTVDSWLIWNLTGGkngGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIASGPLAGVP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 253 pIMGVAGDQQASLFGHCCFHPGQTKNTYGTGCFMLMNTGDEIVESKNGLVSTIG--IAADGKISYALEGSIFAAGSTMNW 330
Cdd:cd07792 242 -ISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAykLGPDAPPVYALEGSIAIAGAAVQW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 331 LRNNMGIISSVSESAQLATSINDNEGCYFVPAFAGLGAPWWDPHARGIVCGLTGASSRATIVRAACESMAYQSYDVLRAM 410
Cdd:cd07792 321 LRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREILDAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 411 EQDVGLSIERLSVDGGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLAVGYWEDLEELEQNAQI-VKVFHPHM 489
Cdd:cd07792 401 NKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSLNEGgRTVFEPQI 480
|
490
....*....|....*....
gi 2192564081 490 SAERRESNLAGWRDAVKRS 508
Cdd:cd07792 481 SEEERERRYKRWKKAVERS 499
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
20-513 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 596.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 20 SYIMALDCGTTSVLATIVDEYGCIVAQARRSVKTSFPRPGWVEQDPTEVLASQIGVMMEV--QFKSGIHSDRIAAIGISN 97
Cdd:PTZ00294 2 KYIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAikKLREKGPSFKIKAIGITN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 98 QRETTVVWDRISGQPIYNAIVWQCRRTAPLIDELVEQ-GAEELVRSRTGLTLDPYFSASKVQWILDNVDGARESAAAGDL 176
Cdd:PTZ00294 82 QRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKyGGSNFFQKITGLPISTYFSAFKIRWMLENVPAVKDAVKEGTL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 177 MFGTIDTWLIYNLTGGQVFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRVASDimTNMP---- 252
Cdd:PTZ00294 162 LFGTIDTWLIWNLTGGKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTISGE--AVPLlegv 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 253 PIMGVAGDQQASLFGHCCFHPGQTKNTYGTGCFMLMNTGDEIVESKNGLVSTIG--IAADGKISYALEGSIFAAGSTMNW 330
Cdd:PTZ00294 240 PITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCyqLGPNGPTVYALEGSIAVAGAGVEW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 331 LRNNMGIISSVSESAQLATSINDNEGCYFVPAFAGLGAPWWDPHARGIVCGLTGASSRATIVRAACESMAYQSYDVLRAM 410
Cdd:PTZ00294 320 LRDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDVIESM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 411 EQDVGLSIERLSVDGGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLAVGYWEDLEELEQNAQI-VKVFHPHM 489
Cdd:PTZ00294 400 EKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVKKLIRRsNSTFSPQM 479
|
490 500
....*....|....*....|....
gi 2192564081 490 SAERRESNLAGWRDAVKRSLNTAQ 513
Cdd:PTZ00294 480 SAEERKAIYKEWNKAVERSLKWAK 503
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
21-512 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 550.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEYGCIVAQARRSVKTSFPRPGWVEQDPTEVLASQIGVMME----VQFKSGIHSDRIAAIGIS 96
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKalekAAAKGHNVDSGLKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 97 NQRETTVVWDRISGQPIYNAIVWQCRRTAPLIDELVEQ--GAEELVRSRTGLTLDPYFSASKVQWILDNVDGARESAAAG 174
Cdd:PLN02295 81 NQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKElsGGRKHFVETCGLPISTYFSATKLLWLLENVDAVKEAVKSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 175 DLMFGTIDTWLIYNLTGGQ---VFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRVASDIMTNM 251
Cdd:PLN02295 161 DALFGTIDSWLIWNLTGGAsggVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIAKGWPLAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 252 PPIMGVAGDQQASLFGHCCfHPGQTKNTYGTGCFMLMNTGDEIVESKNGLVSTIG--IAADGKISYALEGSIFAAGSTMN 329
Cdd:PLN02295 241 VPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAykLGPDAPTNYALEGSVAIAGAAVQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 330 WLRNNMGIISSVSESAQLATSINDNEGCYFVPAFAGLGAPWWDPHARGIVCGLTGASSRATIVRAACESMAYQSYDVLRA 409
Cdd:PLN02295 320 WLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQVKDVLDA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 410 MEQDVGLSIER-----LSVDGGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLAVGYWEDLEELEQNAQIV-K 483
Cdd:PLN02295 400 MRKDAGEEKSHkglflLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEEEIFASEKWKNtT 479
|
490 500
....*....|....*....|....*....
gi 2192564081 484 VFHPHMSAERRESNLAGWRDAVKRSLNTA 512
Cdd:PLN02295 480 TFRPKLDEEERAKRYASWCKAVERSFDLA 508
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
21-506 |
1.36e-178 |
|
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: 511.34 E-value: 1.36e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEYGCIVAQARRSVKTSFPRPGWVEQDPtEVLASQI-GVMMEVQFKSGIHSDRIAAIGISNQR 99
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDP-EELWQQFvKVIKEALKNAGLTPEDIAAIGISTQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 100 ETTVVWDRISGQPIYNAIVWQCRRTAPLIDEL-----------VEQGAEELVRSRTGLT-----LDPYFSASKVQWILDN 163
Cdd:cd07793 80 NTFLTWDKKTGKPLHNFITWQDLRAAELCESWnrslllkalrgGSKFLHFLTRNKRFLAasvlkFSTAHVSIRLLWILQN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 164 VDGARESAAAGDLMFGTIDTWLIYNLTGGQVFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRV 243
Cdd:cd07793 160 NPELKEAAEKGELLFGTIDTWLLWKLTGGKVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFGST 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 244 ASDIMTNMPPIMGVAGDQQASLFGHCCFHPGQTKNTYGTGCFMLMNTGDEIVESKNGLVSTIGIAADGKISYALEGSIFA 323
Cdd:cd07793 240 DPSIFGAEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGGEITYLAEGNASD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 324 AGSTMNWLRNnMGIISSVSESAQLATSINDNEGCYFVPAFAGLGAPWWDPHARGIVCGLTGASSRATIVRAACESMAYQS 403
Cdd:cd07793 320 TGTVIDWAKS-IGLFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIAFRV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 404 YDVLRAMEQDVGLSIERLSVDGGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLAVGYWEDLEELEQNAQIVK 483
Cdd:cd07793 399 KQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEELKKLRKIEK 478
|
490 500
....*....|....*....|...
gi 2192564081 484 VFHPHMSAERRESNLAGWRDAVK 506
Cdd:cd07793 479 IFEPKMDNEKREELYKNWKKAVK 501
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
21-495 |
1.10e-102 |
|
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: 316.77 E-value: 1.10e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEYGCIVAQARRSVKTSFPRPGWVEQDPTEVLASQIGVMMEVQFKSGIHSDRIAAIGISNQRE 100
Cdd:COG1070 2 YVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQMH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 101 TTVVWDRiSGQPIYNAIVWQCRRTAPLIDELVEQGAEELVRSRTGLTLDPYFSASKVQWILDNVDGARESAAagdlMFGT 180
Cdd:COG1070 82 GLVLLDA-DGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIA----KVLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 181 IDTWLIYNLTGgqVFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRVASDI--MTNMP---PIM 255
Cdd:COG1070 157 PKDYLRYRLTG--EFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAaaETGLPagtPVV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 256 GVAGDQQASLFGHCCFHPGQTKNTYGTGCFMLMNTgDEIVESKNGLVSTIGIAADGKisYALEGSIFAAGSTMNWLRNNM 335
Cdd:COG1070 235 AGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVS-DKPLPDPEGRVHTFCHAVPGR--WLPMGATNNGGSALRWFRDLF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 336 --GIISSVSESAQLATSIN-DNEGCYFVPAFAGLGAPWWDPHARGIVCGLTGASSRATIVRAACESMAYQSYDVLRAMEQ 412
Cdd:COG1070 312 adGELDDYEELNALAAEVPpGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEALEE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 413 dVGLSIERLSVDGGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLAVGYWEDLEE-LEQNAQIVKVFHPHmsA 491
Cdd:COG1070 392 -AGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEaAAAMVRVGETIEPD--P 468
|
....
gi 2192564081 492 ERRE 495
Cdd:COG1070 469 ENVA 472
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
21-489 |
5.56e-96 |
|
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: 297.51 E-value: 5.56e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEYGCIVAQARRSVKTSFPRPGWVEQDPTEVLASQIGVMMEVQFKSGIHSDRIAAIGISNQRE 100
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 101 TTVVWDRiSGQPIYNAIVWQCRRTAplidelveqgaeelvrsrtgltldpyfsaskvqwildnvdgaresaaagdlMFGT 180
Cdd:cd07779 81 TFVPVDE-DGRPLRPAISWQDKRTA---------------------------------------------------KFLT 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 181 IDTWLIYNLTGgqVFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRVASD------IMTNMPPI 254
Cdd:cd07779 109 VQDYLLYRLTG--EFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEaaeetgLPEGTPVV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 255 MGvAGDQQASLFGHCCFHPGQTKNTYGTGCFMLMNTgDEIVESKNGLVSTIGIAADGKisYALEGSIFAAGSTMNWLRNN 334
Cdd:cd07779 187 AG-GGDQQCAALGAGVLEPGTASLSLGTAAVVIAVS-DKPVEDPERRIPCNPSAVPGK--WVLEGSINTGGSAVRWFRDE 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 335 ----------MGIISSVSESAQLATSINDNEGCYFVPAFAGLGAPWWDPHARGIVCGLTGASSRATIVRAACESMAYQSY 404
Cdd:cd07779 263 fgqdevaekeLGVSPYELLNEEAAKSPPGSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELR 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 405 DVLRAMEqDVGLSIERLSVDGGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLAVGYWEDLEELEQN-AQIVK 483
Cdd:cd07779 343 DNLEAME-KAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAmVRVTD 421
|
....*.
gi 2192564081 484 VFHPHM 489
Cdd:cd07779 422 TFEPDP 427
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
21-462 |
6.04e-90 |
|
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: 280.61 E-value: 6.04e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEYGCIVAQARRSVKTSFPRPGWVEQDPTEVLASQIGVMMEVQFKSGIHSDRIAAIGISNQRE 100
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 101 TTVVWDRiSGQPIYNAIVWQCRRTAplidelveqgaeelvrsrtgltldpyfsaskvqwildnvdgaresaaagdlmFGT 180
Cdd:cd00366 81 GVVLVDA-DGNPLRPAIIWLDRRAK----------------------------------------------------FLQ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 181 IDTWLIYNLTGgqVFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRVASDI--MTNMP---PIM 255
Cdd:cd00366 108 PNDYIVFRLTG--EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAaeETGLPagtPVV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 256 GVAGDQQASLFGHCCFHPGQTKNTYGTGCFMLMNTgDEIVESkNGLVSTIGIAADGKisYALEGSIFAAGSTMNWLRNNM 335
Cdd:cd00366 186 AGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCT-DEPVPP-DPRLLNRCHVVPGL--WLLEGAINTGGASLRWFRDEF 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 336 GIISSVSESAQ----LATSINDN-EGCYFVPAFAGLGAPWWDPHARGIVCGLTGASSRATIVRAACESMAYQSYDVLRAM 410
Cdd:cd00366 262 GEEEDSDAEYEgldeLAAEVPPGsDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEIL 341
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2192564081 411 EQDvGLSIERLSVDGGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLA 462
Cdd:cd00366 342 EEL-GVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
21-467 |
6.16e-85 |
|
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: 269.46 E-value: 6.16e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEYGCIVAQARRSVKTSFPRPGWVEQDPTEVLASQIGVMMEVQfkSGIHSDRIAAIGISNQRE 100
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAA--AQAGPDPIAAISVSSQGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 101 TTVVWDRiSGQPIYNAIVWQCRRTAPLIDELVEQ-GAEELVRsRTGLTLDPYFSASKVQWILDNVDGARESAAAgdlmFG 179
Cdd:cd07773 79 SGVPVDR-DGEPLGPAIVWFDPRGKEEAEELAERiGAEELYR-ITGLPPSPMYSLAKLLWLREHEPEIFAKAAK----WL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 180 TIDTWLIYNLTGgqVFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRVASDI--MTNMPP-IMG 256
Cdd:cd07773 153 SVADYIAYRLTG--EPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAaeELGLPAgTPV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 257 VAG--DQQASLFGHCCFHPGQTKNTYGTG-CFMLMNTGDEIVESKNGLVSTIGIAADGKiSYALEGSIfAAGSTMNWLRN 333
Cdd:cd07773 231 VVGghDHLCAALGAGVIEPGDVLDSTGTAeALLAVVDEPPLDEMLAEGGLSYGHHVPGG-YYYLAGSL-PGGALLEWFRD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 334 NMGI--ISSVSESAQLATSINDNEGCYFVPAFAGLGAPWWDPHARGIVCGLTGASSRATIVRAACESMAYQSYDVLRAME 411
Cdd:cd07773 309 LFGGdeSDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEALE 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2192564081 412 QdVGLSIERLSVDGGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLAVG 467
Cdd:cd07773 389 K-AGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
21-491 |
6.29e-83 |
|
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: 265.17 E-value: 6.29e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEYGCIVAQARRSVKTSFPRPGWVEQDPTEVLASQIGVMMEVQFKSGIHSDRIAAIGISNQRE 100
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 101 TTVVWDRiSGQPIYNAIVWQCRRTAPLIDELvEQGAEELVRSRTGLTLDPYFSASKVQWILDNvdgARESAAAgdlmfgt 180
Cdd:cd07808 81 GLVLLDK-NGRPLRPAILWNDQRSAAECEEL-EARLGDEILIITGNPPLPGFTLPKLLWLKEN---EPEIFAR------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 181 IDT------WLIYNLTGgqVFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRVASDI--MTNMP 252
Cdd:cd07808 149 IRKillpkdYLRYRLTG--ELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAaeELGLP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 253 P----IMGvAGDQQASLFGHCCFHPGQTKNTYGTGCFMLMNTgDEIVESKNGLVSTIGIAADGKiSYALeGSIFAAGSTM 328
Cdd:cd07808 227 EgtpvVAG-AGDNAAAALGAGVVEPGDALISLGTSGVVFAPT-DKPVPDPKGRLHTFPHAVPGK-WYAM-GVTLSAGLSL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 329 NWLRNNMGIISSVSE--SAQLATSINDNEGCYFVPAFAGLGAPWWDPHARGIVCGLTGASSRATIVRAACESMAYQSYDV 406
Cdd:cd07808 303 RWLRDLFGPDRESFDelDAEAAKVPPGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDS 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 407 LRAMEqDVGLSIERLSVDGGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLAVGYWEDLEE-LEQNAQIVKVF 485
Cdd:cd07808 383 LEVLK-ELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEaAAACIKIEKTI 461
|
....*.
gi 2192564081 486 HPHMSA 491
Cdd:cd07808 462 EPDPER 467
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
21-267 |
1.90e-79 |
|
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: 248.41 E-value: 1.90e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEYGCIVAQARRSVKTSFPRPGWVEQDPTEVLASQIGVMMEVQFKSGIHSDRIAAIGISNQRE 100
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 101 TTVVWDRIsGQPIYNAIVWQCRRTAPLIDELVEQGAEELVRSRTGLTLDPYFSASKVQWILDNVDGARESAAAgdlmFGT 180
Cdd:pfam00370 81 GTVLLDKN-DKPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHK----FLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 181 IDTWLIYNLTGgqVFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRVASDI--MTNMP---PIM 255
Cdd:pfam00370 156 IHDYLRWRLTG--VFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELaaMWGLDegvPVV 233
|
250
....*....|..
gi 2192564081 256 GVAGDQQASLFG 267
Cdd:pfam00370 234 GGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
21-495 |
4.75e-76 |
|
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: 247.43 E-value: 4.75e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEYGCIVAQARRSVKTSFPRPGWVEQDPTEVLASQIGVMMEVQFKSGIHSDRIAAIGISNQRE 100
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 101 TTVVWDRiSGQPIYNAIVWQCRRTAPLIDELVEQ-GAEELVRSRTGLTLDPYFSASKVQWILDNvdgARESAAAGDLMFG 179
Cdd:cd07805 81 GVVPVDK-DGNPLRNAIIWSDTRAAEEAEEIAGGlGGIEGYRLGGGNPPSGKDPLAKILWLKEN---EPEIYAKTHKFLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 180 TIDtWLIYNLTGgqVFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRVASD------IMTNMPP 253
Cdd:cd07805 157 AKD-YLNFRLTG--RAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEaaaelgLPAGTPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 254 IMGvAGDQQASLFGHCCFHPGQTkNTY-GTGCFMLMNTGDEIVESKNGLVStigIAADGKISYALEGSIFAAGSTMNWLR 332
Cdd:cd07805 234 VGG-GGDAAAAALGAGAVEEGDA-HIYlGTSGWVAAHVPKPKTDPDHGIFT---LASADPGRYLLAAEQETAGGALEWAR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 333 NNMGIISSVSESA-----QLATSIN-DNEGCYFVPAFAGLGAPWWDPHARGIVCGLTGASSRATIVRAACESMAYQSYDV 406
Cdd:cd07805 309 DNLGGDEDLGADDyelldELAAEAPpGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 407 LRAMEqDVGLSIERLSVDGGASRNEFIMQFQADLLDIPVLQCET-VETTAIGAAYLAGLAVGYWEDLEELEQNAQIVKVF 485
Cdd:cd07805 389 LEALE-KLTRKIDELRLVGGGARSDLWCQILADVLGRPVEVPENpQEAGALGAALLAAVGLGLLKSFDEAKALVKVEKVF 467
|
490
....*....|
gi 2192564081 486 HPhmSAERRE 495
Cdd:cd07805 468 EP--DPENRA 475
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
21-467 |
3.02e-68 |
|
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: 225.87 E-value: 3.02e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEYGCIVAQARRSVKTSFPRPGWVEQDPT---EVLASQIGVMMEvqfKSGIHSDRIAAIGISN 97
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEvwwGAVCEIIRELLA---KAGISPKEIAAIGVSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 98 QRETTVVWDRiSGQPIYNAIVWQCRRTAPLIDELVEQGAEELVRSRTGLTLDPYFSASKVQWILDN----VDGAResaaa 173
Cdd:cd07804 78 LVPALVPVDE-NGKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSQSVGPKLLWIKRNepevFKKTR----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 174 gdlMFGTIDTWLIYNLTGgqVFATDYTNASRTA-LFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRVASDI--MTN 250
Cdd:cd07804 152 ---KFLGAYDYIVYKLTG--EYVIDYSSAGNEGgLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEAaeETG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 251 MP---PIMGVAGDQQASLFGHCCFHPGQTKNTYGT-GCFMLmntgdeIVESKNGLVSTIGIAADGKISYALEGSIFAAGS 326
Cdd:cd07804 227 LAegtPVVAGTVDAAASALSAGVVEPGDLLLMLGTaGDIGV------VTDKLPTDPRLWLDYHDIPGTYVLNGGMATSGS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 327 TMNWLRNNMGI----------ISSVSESAQLATSIN-DNEGCYFVPAFAGLGAPWWDPHARGIVCGLTGASSRATIVRAA 395
Cdd:cd07804 301 LLRWFRDEFAGeeveaeksggDSAYDLLDEEAEKIPpGSDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRAL 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2192564081 396 CESMAYQSYDVLRAMEQDvGLSIERLSVDGGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLAVG 467
Cdd:cd07804 381 LEGVAYGLRHHLEVIREA-GLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
21-487 |
4.19e-59 |
|
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: 202.79 E-value: 4.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEYGCIVAQARRSVKTSFPRPGWVEQDPTEVLASQIGVMMEVqfKSGIHSDRIAAIGISNQRE 100
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEV--LAKLGGGEVDAIGFSSAMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 101 TTVVWDRiSGQPIYNAIVWQCRRTAPLIDELVEQGAEELVRSRTGLTLDPYFSASKVQWILDNVDGARESAAagdlMFGT 180
Cdd:cd07770 79 SLLGVDE-DGEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAA----KFVS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 181 IDTWLIYNLTGgqVFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRVASDIMTNMP-----PIM 255
Cdd:cd07770 154 IKEYLLYRLTG--ELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAERLGllagtPVV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 256 GVAGDQQASLFGHCCFHPGQTKNTYGTGCFMLMNTGDEIVESKNGLVStigIAADGKiSYALEGSIFAAGSTMNWLRNNM 335
Cdd:cd07770 232 LGASDGALANLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPGRLWC---YRLDEN-RWLVGGAINNGGNVLDWLRDTL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 336 -GIISSVSE-SAQLATSINDNEGCYFVPAFAGLGAPWWDPHARGIVCGLTGASSRATIVRAACESMAYQSYDVLRAMEQD 413
Cdd:cd07770 308 lLSGDDYEElDKLAEAVPPGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEALEEL 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2192564081 414 VGlSIERLSVDGGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLAVGYWEDLEELEQNaQIVKVFHP 487
Cdd:cd07770 388 AG-PVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSLEADELV-KIGKVVEP 459
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
21-467 |
1.71e-55 |
|
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: 192.00 E-value: 1.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEYGCIVAQARRSVKTSFPRPGWVEQDPTEVLASQIGVMMEVQFKSGIHSDRIAAIGISNQRE 100
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 101 TTVVWDRiSGQPIYNAIVWQCRRTAPLIDELVEQGAEELVRSRTGLTLDPYFSASKVQWILDNvdgARESAAAGDLMFGT 180
Cdd:cd07802 81 GLYLVDK-DGKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKEN---EPERYDRIRTVLFC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 181 IDtWLIYNLTGgqVFATDYTNASrTALFNIHALDWDDDLLALFDVP--RSMMPEVRWSSGDYGRVASDI--MTNMP---P 253
Cdd:cd07802 157 KD-WIRYRLTG--EISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVTAEAaaLTGLPegtP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 254 IMGVAGDQQASLFGHCCFHPGQTKNTYGTGCfmlMNTG--DEIVESKNGLVSTIGIAADGKIsyALEGSIfAAGSTMNWL 331
Cdd:cd07802 233 VAAGAFDVVASALGAGAVDEGQLCVILGTWS---INEVvtDEPVVPDSVGSNSLHADPGLYL--IVEASP-TSASNLDWF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 332 RNNMGIISSVSESA------QLATSIN-DNEGCYFVPAFAGLGApwwDPHARGIVCGLTGASSRATIVRAACESMAYQSY 404
Cdd:cd07802 307 LDTLLGEEKEAGGSdydeldELIAAVPpGSSGVIFLPYLYGSGA---NPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHR 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2192564081 405 DVLRAMEQDVGLSIERLSvdGGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLAVG 467
Cdd:cd07802 384 DHLERLLVARKPETIRLT--GGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| XylB |
TIGR01312 |
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ... |
25-477 |
3.81e-51 |
|
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of carbohydrate kinases. The member from Klebsiella pneumoniae, designated DalK (see , was annotated erroneously in GenBank as D-arabinitol kinase but is authentic D-xylulose kinase. D-xylulose kinase (XylB) generally is found with xylose isomerase (XylA) and acts in xylose utilization. [Energy metabolism, Sugars]
Pssm-ID: 273550 [Multi-domain] Cd Length: 481 Bit Score: 181.36 E-value: 3.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 25 LDCGTTSVLATIVDEYGCIVAQARRSVKTSFPRPGWVEQDPTEVLASQIGVMMEVQFKSGIHSDRIAAIGISNQRETTVV 104
Cdd:TIGR01312 3 IDLGTSGVKALLVDEQGEVIASGSAPHTVISPHPGWSEQDPEDWWDATEEAIKELLEQASEMGQDIKGIGISGQMHGLVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 105 WDRiSGQPIYNAIVWQCRRTAPLIDELVEQGAEELVRSRTGLTLDPYFSASKVQWILDNvdgarESAAagdlmFGTIDT- 183
Cdd:TIGR01312 83 LDA-NGEVLRPAILWNDTRTAQECEELEAELGDERVLEITGNLALPGFTAPKLLWVRKH-----EPEV-----FARIAKv 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 184 -----WLIYNLTGGqvFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRVASDI--MTNMP---P 253
Cdd:TIGR01312 152 mlpkdYLRYRLTGE--YVTEYSDASGTGWFDVAKRAWSKELLDALDLPESQLPELIESSEKAGTVRPEVaaRLGLSagvP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 254 IMGVAGDQQASLFGHCCFHPGQTKNTYGTGCFMLMNTGDEIVESKnGLVSTIGIAADGkiSYALEGSIFAAGSTMNWLRN 333
Cdd:TIGR01312 230 VAAGGGDNAAGAIGTGTVDPGDAMMSLGTSGVVYAVTDKPLPDPA-GAVHGFCHALPG--GWLPMGVTLSATSSLEWFRE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 334 NMGIISSVSESAQLATSINDNEGCYFVPAFAGLGAPWWDPHARGIVCGLTGASSRATIVRAACESMAYQSYDVLRAMEQD 413
Cdd:TIGR01312 307 LFGKEDVEALNELAEQSPPGAEGVTFLPYLNGERTPHLDPQARGSFIGLTHNTTRADLTRAVLEGVTFALRDSLDILREA 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2192564081 414 VGLSIERLSVDGGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLAVGYWEDLEELEQ 477
Cdd:TIGR01312 387 GGIPIQSIRLIGGGAKSPAWRQMLADIFGTPVDVPEGEEGPALGAAILAAWALGEKDLAALCSE 450
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
21-466 |
5.87e-48 |
|
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466801 [Multi-domain] Cd Length: 429 Bit Score: 171.64 E-value: 5.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEYGCIVAQARRSVKTSFPRPGWVEQDPTEVLASQIGVMMEVqfKSGIHSDRIAAIGISNQRE 100
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLREL--PAELRPRRVVAIAVDGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 101 TTVVWDRiSGQPIYNAIVWQCRRTAPLIDELveQGAEELVRSRTGLTLDPYFSASKVQWILDNVDGARESAA----AGDl 176
Cdd:cd07783 79 TLVLVDR-EGEPLRPAIMYNDARAVAEAEEL--AEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAkflhQAD- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 177 mfgtidtWLIYNLTGGQvFATDYTNASRTaLFNIHALDWDDDLLALFDVPRSMMPEVRwSSGDY-GRVASDIM--TNMP- 252
Cdd:cd07783 155 -------WLAGRLTGDR-GVTDYNNALKL-GYDPETGRWPSWLLALLGIPPDLLPRVV-APGTViGTLTAEAAeeLGLPa 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 253 --PImgVAG--DQQASLFGHCCFHPGQTKNTYGTG-CFMLmnTGDEIVESKNGLVStigiaadgkiSYALEGSIFAAGST 327
Cdd:cd07783 225 gtPV--VAGttDSIAAFLASGAVRPGDAVTSLGTTlVLKL--LSDKRVPDPGGGVY----------SHRHGDGYWLVGGA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 328 mnwlrNNMG--IISSVSESAQLAT-----SINDNEGCYFVP-AFAGLGAPWWDPHARGIVcgLTGASSRATIVRAACESM 399
Cdd:cd07783 291 -----SNTGgaVLRWFFSDDELAElsaqaDPPGPSGLIYYPlPLRGERFPFWDPDARGFL--LPRPHDRAEFLRALLEGI 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2192564081 400 AYQSYDVLRAMEQDVGLSIERLSVDGGASRNEFIMQFQADLLDIPVLQCETvETTAIGAAYLAGLAV 466
Cdd:cd07783 364 AFIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEE-EEAALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
21-467 |
1.78e-42 |
|
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: 157.02 E-value: 1.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEYGCIVAQARRSVKTSFPRPGWVEQDPTEVLASQIGVMMEVQFKSGIHSDRIAAIGISNQRE 100
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 101 TTVVWDRiSGQPIYNAIVWQCRRTAPLIDELVEQGAEELVRSRTGLTLDPYFSASKVQWILDNvdgARESAAAGDLMFGT 180
Cdd:cd24121 81 GTWLVDE-DGRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKEN---EPERLERARTALHC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 181 IDtWLIYNLTGgqVFATDYTNASRTaLFNIHALDWDDDLLALFDVP--RSMMPEVRWSSGDYGRVASDI--MTNMP---P 253
Cdd:cd24121 157 KD-WLFYKLTG--EIATDPSDASLT-FLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAaaATGLPagtP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 254 IMGVAGDQQASLFGHCCFHPGQTKNTYGTGCFMLMNTgDEIVESKNGLVSTIGIAADGKISYALegSIFAAGSTMNWLrn 333
Cdd:cd24121 233 VVLGPFDVVATALGSGAIEPGDACSILGTTGVHEVVV-DEPDLEPEGVGYTICLGVPGRWLRAM--ANMAGTPNLDWF-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 334 nMGIISSVSESAQLATSIND--------------NEGCYFVP--AFAGLGAPWWDPHARGIVCGLTGASSRATIVRAACE 397
Cdd:cd24121 308 -LRELGEVLKEGAEPAGSDLfqdleelaassppgAEGVLYHPylSPAGERAPFVNPNARAQFTGLSLEHTRADLLRAVYE 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 398 SMAYQSYDVLRAMeqdvGLSIERLSVDGGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLAVG 467
Cdd:cd24121 387 GVALAMRDCYEHM----GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
277-465 |
7.46e-41 |
|
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: 145.55 E-value: 7.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 277 KNTYGTGCFMLMnTGDEIVESKNGLVSTIGiAADGKISYALEGSIFAAGSTMNWLRNNMGIISSVS-----ESAQLATSI 351
Cdd:pfam02782 2 AISAGTSSFVLV-ETPEPVLSVHGVWGPYT-NEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRdagnvESLAELAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 352 N---DNEGCYFVPAFAGLGAPWWDPHARGIVCGLTGASSRATIVRAACESMAYQSYDVLRAMEQDVGLSIERLSVDGGAS 428
Cdd:pfam02782 80 AavaPAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSGGGS 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 2192564081 429 RNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLA 465
Cdd:pfam02782 160 RNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
21-467 |
8.86e-41 |
|
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: 152.38 E-value: 8.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEYGCIVAQARRSVKTSFPR--PGWVEQDPTEVLASQIGVMMEVQFKSGIHSDRIAAIGISNQ 98
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDdyPDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 99 RETTVVWDRiSGQPIYnaivwqcrrTAPLID-------ELVEQGAEELVRSRTGLTLDPYFSASKVQWILDNVDGARESA 171
Cdd:cd07798 81 REGIVFLDK-DGRELY---------AGPNIDargveeaAEIDDEFGEEIYTTTGHWPTELFPAARLLWFKENRPEIFERI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 172 AAgdlmFGTIDTWLIYNLTGgqVFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRVASD----- 246
Cdd:cd07798 151 AT----VLSISDWIGYRLTG--ELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEaarel 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 247 -IMTNMPPIMGVAgDQQASLFGHCCFHPGQTKNTYGTGCFMLMNTGDEIVESKNGLVSTIGIAADGkisYALEGSIFAAG 325
Cdd:cd07798 225 gLPEGTPVVVGGA-DTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTGCHLVPGK---WVLESNAGVTG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 326 STMNWLRNNM-GIISSVSES-AQLATSINDNE-GCYfvpAFAGLGAPwwDPHARGI--------VCGLTGASSRATIVRA 394
Cdd:cd07798 301 LNYQWLKELLyGDPEDSYEVlEEEASEIPPGAnGVL---AFLGPQIF--DARLSGLknggflfpTPLSASELTRGDFARA 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2192564081 395 ACESMAYQSYDVLRAMEQDVGLSIERLSVDGGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLAVG 467
Cdd:cd07798 376 ILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
21-467 |
1.28e-37 |
|
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: 143.46 E-value: 1.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVD-EYGCIVAQARRSVKTSFPRPGWVEQDPTEVLASQIGVMMEVQFKSGIHSDRIAAIGISNQR 99
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 100 ETTVVWDRiSGQPIYNAIVWQCRRTAPLIDELVEQ-GAEELVRsrTGLTLDPYFSASKVQWILDNvdgarESAAAGDLMF 178
Cdd:cd07809 81 HGLVALDA-DGKVLRPAKLWCDTRTAPEAEELTEAlGGKKCLL--VGLNIPARFTASKLLWLKEN-----EPEHYARIAK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 179 -GTIDTWLIYNLTGGqvFATDYTNASRTALFNIHALDWDDDLLALFDVPR---SMMPEVRWSSGDYGRVASDI--MTNMP 252
Cdd:cd07809 153 iLLPHDYLNWKLTGE--KVTGLGDASGTFPIDPRTRDYDAELLAAIDPSRdlrDLLPEVLPAGEVAGRLTPEGaeELGLP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 253 PimGV-----AGDQQASLFGHCCFHPGQTKNTYGT-GCfmLMNTGDEIVESKNGLVSTigiaadgkisyalegsiFAaGS 326
Cdd:cd07809 231 A--GIpvapgEGDNMTGALGTGVVNPGTVAVSLGTsGT--AYGVSDKPVSDPHGRVAT-----------------FC-DS 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 327 TMNWL--RNNMGIISSVSESA------------QLATSI-NDNEGCYFVPAFAGLGAPWWdPHARGIVCGLTGAS-SRAT 390
Cdd:cd07809 289 TGGMLplINTTNCLTAWTELFrellgvsyeeldELAAQApPGAGGLLLLPFLNGERTPNL-PHGRASLVGLTLSNfTRAN 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2192564081 391 IVRAACESMAYQSYDVLRAMEQDvGLSIERLSVDGGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLAVG 467
Cdd:cd07809 368 LARAALEGATFGLRYGLDILREL-GVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
21-491 |
4.33e-31 |
|
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466799 [Multi-domain] Cd Length: 504 Bit Score: 126.11 E-value: 4.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVD-EYGCIVAQARRSVKTSF--PRPGWVEQDPTEVLASQIGVMMEVQFKSGIHSDRIAAIGISN 97
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 98 QRETTVVWDRiSGQPIYNAIVWQCRRTAPLIDELVEQGAEELVRSrtgltLDPY---FSA----SKVQWILDNVDGARES 170
Cdd:cd07781 81 TSSTVVPVDE-DGNPLAPAILWMDHRAQEEAAEINETAHPALEYY-----LAYYggvYSSewmwPKALWLKRNAPEVYDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 171 AA----AGDlmfgtidtWLIYNLTGGQVfatdytnASRTA-----------------LFN-IHALdwdddllalFDVPRS 228
Cdd:cd07781 155 AYtiveACD--------WINARLTGRWV-------RSRCAaghkwmynewgggppreFLAaLDPG---------LLKLRE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 229 MMPEVRWSSGD-YGRV---ASDIM---TNMPPIMGvAGDQQASLFGHCCFHPGQTKNTYGT-GCFMLMNTGDEIVEsknG 300
Cdd:cd07781 211 KLPGEVVPVGEpAGTLtaeAAERLglpAGIPVAQG-GIDAHMGAIGAGVVEPGTLALIMGTsTCHLMVSPKPVDIP---G 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 301 LvstIGIAADGKI--SYALEGSIFAAGSTMNWLRNNMGI------ISSVSESAQLATSINDNEGcyfvpafaGLGA-PWW 371
Cdd:cd07781 287 I---CGPVPDAVVpgLYGLEAGQSAVGDIFAWFVRLFVPpaeergDSIYALLSEEAAKLPPGES--------GLVAlDWF 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 372 --------DPHARGIVCGLTGASSRATIVRAACESMAYQSYDVLRAMEQDvGLSIERLSVDGG-ASRNEFIMQFQADLLD 442
Cdd:cd07781 356 ngnrtplvDPRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERFEEA-GVPVNRVVACGGiAEKNPLWMQIYADVLG 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2192564081 443 IPVLQCETVETTAIGAAYLAGLAVGYWEDLEELEQN-AQIVKVFHPHMSA 491
Cdd:cd07781 435 RPIKVPKSDQAPALGAAILAAVAAGVYADIEEAADAmVRVDRVYEPDPEN 484
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
21-488 |
2.56e-28 |
|
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: 117.82 E-value: 2.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEYGCIVAQARRS-VKTSFPR-PGWVEQDPTEVLASQIGVMMEVQFKSGIHSDRIAAIGISNQ 98
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREwRHKEVPDvPGSMDFDTEKNWKLICECIREALKKAGIAPKSIAAISTTSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 99 RETTVVWDRiSGQPIynaivWQCR----RTAPLIDELVEQ--GAEELVRSRTGLTldpyFSAS---KVQWILDNVDGARE 169
Cdd:cd07775 81 REGIVLYDN-EGEEI-----WACAnvdaRAAEEVSELKELynTLEEEVYRISGQT----FALGaipRLLWLKNNRPEIYR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 170 SAAAgdlmFGTIDTWLIYNLTGgqVFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRVASDI-- 247
Cdd:cd07775 151 KAAK----ITMLSDWIAYKLSG--ELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEAae 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 248 ----MTNMPPIMGvAGDQQASLFGHCCFHPGQTKNTYGTGCFMLMNTGDEIVESKNGLvsTIGIAADGKISYAlEGSIFA 323
Cdd:cd07775 225 etglKEGTPVVVG-GGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMNI--RVNCHVIPDMWQA-EGISFF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 324 AGSTMNWLRNNMGIissvsESAQLA--TSIND----NEGCYFVPAFA-GLGAPWWDP-------HARGIVCGLT---GAS 386
Cdd:cd07775 301 PGLVMRWFRDAFCA-----EEKEIAerLGIDAydllEEMAKDVPPGSyGIMPIFSDVmnyknwrHAAPSFLNLDidpEKC 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 387 SRATIVRAACESMAYQSYDVLRAMEQDVGLSIERLSVDGGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLAV 466
Cdd:cd07775 376 NKATFFRAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGA 455
|
490 500
....*....|....*....|...
gi 2192564081 467 GYWEDLEE-LEQNAQIVKVFHPH 488
Cdd:cd07775 456 GIYSSLEEaVESLVKWEREYLPN 478
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
21-462 |
1.76e-27 |
|
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: 114.63 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEYGCIVAqARRSVKTSFP----RPGWVEQDPTEVLASQIGVMMEVqfkSGIHSDRIAAIGIS 96
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLESGRIL-ESVSRPTPAPissdDPGRSEQDPEKILEAVRNLIDEL---PREYLSDVTGIGIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 97 NQRETTVVWDRiSGQPIYNAIVWQCRRTAPLIDELVEQGAEELvRSRTGLTLDPYFSASKVQWILDNvdgarESAAAGDL 176
Cdd:cd07777 77 GQMHGIVLWDE-DGNPVSPLITWQDQRCSEEFLGGLSTYGEEL-LPKSGMRLKPGYGLATLFWLLRN-----GPLPSKAD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 177 MFGTIDTWLIYNLTGGQVFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRwSSGD-YGRVASDIMTNMPpiM 255
Cdd:cd07777 150 RAGTIGDYIVARLTGLPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIV-PSGEiVGTLSSALPKGIP--V 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 256 GVA-GDQQASLFGhCCFHPGQTkntygtgcfMLMN--TGdeivesknGLVSTIGIAADGKISYAL----EGSIFAAGSTM 328
Cdd:cd07777 227 YVAlGDNQASVLG-SGLNEEND---------AVLNigTG--------AQLSFLTPKFELSGSVEIrpffDGRYLLVAASL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 329 N----------WLRNNMGIISSVSESAQL------ATSINDNEGCYFVPAFAGlGApwWDPHARGIVCGLTGAS-SRATI 391
Cdd:cd07777 289 PggralavlvdFLREWLRELGGSLSDDEIwekldeLAESEESSDLSVDPTFFG-ER--HDPEGRGSITNIGESNfTLGNL 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2192564081 392 VRAACESMAYQSYDVLRAMEQDvGLSIERLSVDGGASR-NEFIMQFQADLLDIPVLQCETVETTAIGAAYLA 462
Cdd:cd07777 366 FRALCRGIAENLHEMLPRLDLD-LSGIERIVGSGGALRkNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
21-496 |
6.07e-26 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 110.83 E-value: 6.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YImALDCGTTSVLATIVDEYGCIVAQARRSVKTSFPRPGWVEQDPTEVLASQIGVMMEVqfkSGIHSDR-IAAIGISNQR 99
Cdd:PRK15027 2 YI-GIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKAL---GDQHSLQdVKALGIAGQM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 100 ETTVVWDRiSGQPIYNAIVW---QCRRTAPLIDELVEQGaeelvRSRTGLTLDPYFSASKVQWIldnvdgARESAAagdl 176
Cdd:PRK15027 78 HGATLLDA-QQRVLRPAILWndgRCAQECALLEARVPQS-----RVITGNLMMPGFTAPKLLWV------QRHEPE---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 177 MFGTIDT------WLIYNLTGgqVFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRVASDIMT- 249
Cdd:PRK15027 142 IFRQIDKvllpkdYLRLRMTG--EFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAKa 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 250 -NMP--PIMGVAGDQQASLFGHCCFHPGQTKNTYGT-GCFMLMNTGdeIVESKNGLVSTIGIAADGKisYALEGSIFAAG 325
Cdd:PRK15027 220 wGMAtvPVVAGGGDNAAGAVGVGMVDANQAMLSLGTsGVYFAVSEG--FLSKPESAVHSFCHALPQR--WHLMSVMLSAA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 326 STMNWLRNNMGiISSVSESAQLATSINDNEG-CYFVPAFAGLGAPWWDPHARGIVCGLTGASSRATIVRAACESMAYQSY 404
Cdd:PRK15027 296 SCLDWAAKLTG-LSNVPALIAAAQQADESAEpVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 405 DVLRAMeQDVGLSIERLSVDGGASRNEFIMQFqadLLDIPVLQCETVE----TTAIGAAYLAGLAVGYWEDLEE------ 474
Cdd:PRK15027 375 DGMDVV-HACGIKPQSVTLIGGGARSEYWRQM---LADISGQQLDYRTggdvGPALGAARLAQIAANPEKSLIEllpqlp 450
|
490 500
....*....|....*....|..
gi 2192564081 475 LEQNAQIVKVFHPHMsAERRES 496
Cdd:PRK15027 451 LEQSHLPDAQRYAAY-QPRRET 471
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
20-487 |
9.86e-23 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 100.87 E-value: 9.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 20 SYIMALDCGTTSVLATIVDEYGCIVAQAR--RSVKTSFPRPGWVEQDPTEVLasQIGVMMEVQFKSGIHSDRIAAIGIsn 97
Cdd:PRK10331 2 DVILVLDCGATNVRAIAVDRQGKIVARAStpNASDIAAENSDWHQWSLDAIL--QRFADCCRQINSELTECHIRGITV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 98 qreTT-----VVWDRiSGQPIYNAIVWQCRRTAPLIDELVEQGAEELVRSRTGLTLDPYFSASKVQWILDNVDGARESAA 172
Cdd:PRK10331 78 ---TTfgvdgALVDK-QGNLLYPIISWKCPRTAAVMENIERYISAQQLQQISGVGAFSFNTLYKLVWLKENHPQLLEQAH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 173 AgdlmFGTIDTWLIYNLTGgqVFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRVASDI--MTN 250
Cdd:PRK10331 154 A----WLFISSLINHRLTG--EFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPSAaaLLG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 251 MP---PIMGVAGDQQASLFGhccfhPGQTKN----TYGTGcfmlmntgdEIVESKNGLVST--------IGIAADGKISY 315
Cdd:PRK10331 228 LPvgiPVISAGHDTQFALFG-----SGAGQNqpvlSSGTW---------EILMVRSAQVDTsllsqyagSTCELDSQSGL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 316 ALEGSIFAAGSTMNWLRNnmgIISSVSESAQL----ATSINDN-EGCYFVPAFAGLGapwwdphaRGIVCGLTGASSRAT 390
Cdd:PRK10331 294 YNPGMQWLASGVLEWVRK---LFWTAETPYQTmieeARAIPPGaDGVKMQCDLLACQ--------NAGWQGVTLNTTRGH 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 391 IVRAACESMAYQSYDVLRAMEQDVGLSIERLSVDGGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLAVGYWE 470
Cdd:PRK10331 363 FYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFS 442
|
490
....*....|....*...
gi 2192564081 471 DLEELEQNAQI-VKVFHP 487
Cdd:PRK10331 443 SPEQARAQMKYqYRYFYP 460
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
358-487 |
7.45e-16 |
|
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: 80.27 E-value: 7.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 358 YFVPAFAGLGAPWWDPHARGIVCGLTGASSR---ATIVRAACESMAYQSYDVLRAMEQDvGLSIERLSVDGGASRNEFIM 434
Cdd:cd07782 382 HVLPDFHGNRSPLADPTLRGMISGLTLDTSLddlALLYLATLQALAYGTRHIIEAMNAA-GHKIDTIFMCGGLSKNPLFV 460
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2192564081 435 QFQADLLDIPVLQCETVETTAIGAAYLAGLAVGYWEDLEE-LEQNAQIVKVFHP 487
Cdd:cd07782 461 QLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDaMAAMSGPGKVVEP 514
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
19-489 |
1.85e-15 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 78.89 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 19 GSYIMALDCGTTSVLATIVDEYGCIVAQARRS-VKTSFPR-PGWVEQDPTE--VLASQigVMMEVQFKSGIHSDRIAAIG 94
Cdd:PRK10939 2 MSYLMALDAGTGSIRAVIFDLNGNQIAVGQAEwRHLAVPDvPGSMEFDLEKnwQLACQ--CIRQALQKAGIPASDIAAVS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 95 ISNQRETTVVWDRiSGQPIynaivWQC----RRTAPLIDELVE--QGAEELVRSRTGLTLDpyFSA-SKVQWILDNVDGA 167
Cdd:PRK10939 80 ATSMREGIVLYDR-NGTEI-----WACanvdARASREVSELKElhNNFEEEVYRCSGQTLA--LGAlPRLLWLAHHRPDI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 168 RESAAAgdlmFGTIDTWLIYNLTGgqVFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVRWSSGDYGRVASD- 246
Cdd:PRK10939 152 YRQAHT----ITMISDWIAYMLSG--ELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAKa 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 247 -----IMTNMPPIMGvAGDQQASLFGHCCFHPGQTKNTYGTGCFMLMNTGDEIVESK----------NGLVSTIGIAadg 311
Cdd:PRK10939 226 aaetgLRAGTPVVMG-GGDVQLGCLGLGVVRPGQTAVLGGTFWQQVVNLPAPVTDPNmnirinphviPGMVQAESIS--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 312 kisyalegsiFAAGSTMNWLRNNMGiissvSESAQLATSINDNE-------------GCYFV-PAFAG---LGApWWdpH 374
Cdd:PRK10939 302 ----------FFTGLTMRWFRDAFC-----AEEKLLAERLGIDAyslleemasrvpvGSHGIiPIFSDvmrFKS-WY--H 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 375 ARGIVCGLT---GASSRATIVRAACESMAYQSYDVLRAMEQDVGLSIERLSVDGGASRNEFIMQFQADLLDIPVLQCETV 451
Cdd:PRK10939 364 AAPSFINLSidpEKCNKATLFRALEENAAIVSACNLQQIAAFSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVK 443
|
490 500 510
....*....|....*....|....*....|....*....
gi 2192564081 452 ETTAIGAAYLAGLAVGYWEDLEEL-EQNAQIVKVFHPHM 489
Cdd:PRK10939 444 EATALGCAIAAGVGAGIYSSLAETgERLVRWERTFEPNP 482
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
21-487 |
2.68e-13 |
|
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: 72.27 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 21 YIMALDCGTTSVLATIVDEY-GCIVAQARRSVKT-SFPRPGWVEQDPTEVLASQIGVMMEVQFKSGIHSDRIAAIGISN- 97
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDLYaGLEMAQEPVPYYQdSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVDAt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 98 ------QRETTVVWDRISGQPIYNAIVWQCRRT---APLIDELVEQGAEElvrsRTGLTLDPYFSASKVQWILDNVDGAR 168
Cdd:cd07768 81 cslaifDREGTPLMALIPYPNEDNVIFWMDHSAvneAQWINMQCPQQLLD----YLGGKISPEMGVPKLKYFLDEYSHLR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 169 ESAaagDLMFGTIDtWLIYNLTGgqvfatDYTNASRTALF--NIHALdwdddllalfdvprsmmpEVRWSSGDYGRVASD 246
Cdd:cd07768 157 DKH---FHIFDLHD-YIAYELTR------LYEWNICGLLGkeNLDGE------------------ESGWSSSFFKNIDPR 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 247 IMTNMPPIM-----------GVAGDQQASLFGhccFHPGQT---------KNTYGTG----------------CFMLMNT 290
Cdd:cd07768 209 LEHLTTTKNlpsnvpigttsGVALPEMAEKMG---LHPGTAvvvscidahASWFAVAsphletslfmiagtssCHMYGTT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 291 GDEIVESKNGLVSTI----------GIAADGKISYALEGSIFAAGSTMNWLRNNMGIISSVSESA-QLATSINDNEGCYF 359
Cdd:cd07768 286 ISDRIPGVWGPFDTIidpdysvyeaGQSATGKLIEHLFESHPCARKFDEALKKGADIYQVLEQTIrQIEKNNGLSIHILT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 360 VPAFAGLGAPWWDPHARGIVCGLTGASSR---ATIVRAACESMAYQSYDVLRAMEQDvGLSIERLSVDGGASRNEFIMQF 436
Cdd:cd07768 366 LDMFFGNRSEFADPRLKGSFIGESLDTSMlnlTYKYIAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKNERLLQL 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2192564081 437 QADLLDIPVLQCETVETTAIGAAYLAGLAVGYWEDLEELEQ----NAQIVKVFHP 487
Cdd:cd07768 445 IALVTNVAIIKPKENMMGILGAAVLAKVAAGKKQLADSITEadisNDRKSETFEP 499
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
369-495 |
1.24e-12 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 70.14 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 369 PWW--------DPHARGIVCGLTGASSRATIVRAACESMAYQSYDVLRAMEQDvGLSIERLSVDGGASR-NEFIMQFQAD 439
Cdd:COG1069 377 DWFngnrsplaDQRLKGVILGLTLGTDAEDIYRALVEATAFGTRAIIERFEEE-GVPIDEIIACGGIATkNPLVMQIYAD 455
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2192564081 440 LLDIPVLQCETVETTAIGAAYLAGLAVGYWEDLEEleqnAQ------IVKVFHPHmsAERRE 495
Cdd:COG1069 456 VTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEE----AMaamgsgFDKVYTPD--PENVA 511
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
109-483 |
4.65e-11 |
|
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: 64.86 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 109 SGQPIYNAIVWQCRRTAPLIDELVEQGAEELVRSRTGLTLDPYFSASKVQWILDNvdgaresaaaGDLMFGTIDTWLI-- 186
Cdd:cd07771 86 NGELLGNPVHYRDPRTEGMMEELFEKISKEELYERTGIQFQPINTLYQLYALKKE----------GPELLERADKLLMlp 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 187 ----YNLTGgqVFATDYTNASRTALFNIHALDWDDDLLALFDVPRSMMPEVrWSSGD-YGRVASDIMTNMP----PIMGV 257
Cdd:cd07771 156 dllnYLLTG--EKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPI-VPPGTvLGTLKPEVAEELGlkgiPVIAV 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 258 AGDQQASLFgHCCfhPGQTKNTY----GTGCFMlmntGdeiVESKNGLVStigiaadgKISYAL----EGSIFaaGSTMn 329
Cdd:cd07771 233 ASHDTASAV-AAV--PAEDEDAAfissGTWSLI----G---VELDEPVIT--------EEAFEAgftnEGGAD--GTIR- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 330 WLRNNMG----------------------IISSVSESAQLATSINDNEGCYFVPAfaglgapwwDPHARgIV--CGLTGA 385
Cdd:cd07771 292 LLKNITGlwllqecrreweeegkdysydeLVALAEEAPPFGAFIDPDDPRFLNPG---------DMPEA-IRayCRETGQ 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 386 S---SRATIVRAACESMAYQSYDVLRAMEQDVGLSIERLSVDGGASRNEFIMQFQADLLDIPVLQCEtVETTAIGAAYLA 462
Cdd:cd07771 362 PvpeSPGEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAGP-VEATAIGNLLVQ 440
|
410 420
....*....|....*....|.
gi 2192564081 463 GLAVGYWEDLEELeqnAQIVK 483
Cdd:cd07771 441 LIALGEIKSLEEG---RELVR 458
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
372-474 |
1.63e-08 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 57.16 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 372 DPHARGIVCGLTGASSRATIVRAACESMAYQSYDVLRAMEQDvGLSIERLSVDGG-ASRNEFIMQFQADLLDIPVLQCET 450
Cdd:PRK04123 394 DQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFEDQ-GVPVEEVIAAGGiARKNPVLMQIYADVLNRPIQVVAS 472
|
90 100
....*....|....*....|....
gi 2192564081 451 VETTAIGAAYLAGLAVGYWEDLEE 474
Cdd:PRK04123 473 DQCPALGAAIFAAVAAGAYPDIPE 496
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
352-501 |
1.13e-06 |
|
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466795 [Multi-domain] Cd Length: 514 Bit Score: 51.02 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 352 NDNEGCYF-----VPAfaGLGAPWWDPHARGIVcgltGASSRATIVRAACES--MAYQSYdvLRAMEQDVglSIERLSVD 424
Cdd:cd07776 363 NGNLGLYFdepeiTPP--VPGGGRRFFGDDGVD----AFFDPAVEVRAVVESqfLSMRLH--AERLGSDI--PPTRILAT 432
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 425 GGASRNEFIMQFQADLLDIPVLQCETVETTAIGAAYLAGLAV-----GYWEDLEELEQNAQIVKVFHPHMSAERRESNLA 499
Cdd:cd07776 433 GGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLlcagsGDFSPEFVVFSAEEPKLVAEPDPEAAEVYDKLL 512
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..
gi 2192564081 500 GW 501
Cdd:cd07776 513 ER 514
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| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
336-462 |
8.04e-05 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466792 [Multi-domain] Cd Length: 424 Bit Score: 44.94 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192564081 336 GIISSVSESAQLATSINDNE-GCYFVPAFAGLGAPWwdPHARGIVCG---LTGASSRAtivrAACESMAYQSYDVLRAME 411
Cdd:cd07772 303 RIAKSFPQLPSLADLAKLLArGTFALPSFAPGGGPF--PGSGGRGVLsafPSAEEAYA----LAILYLALMTDYALDLLG 376
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2192564081 412 QDVGlsieRLSVDGGASRNEFIMQFQADLL-DIPVLQCETVETTAIGAAYLA 462
Cdd:cd07772 377 SGVG----RIIVEGGFAKNPVFLRLLAALRpDQPVYLSDDSEGTALGAALLA 424
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