|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
3-478 |
0e+00 |
|
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: 646.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLIGTDLGTTSTKSVLYDHQGHVIASANVGYPLYHDTVTTAEEDPQEIWQAVQATIHQVSAGIDPEDIEGIAFSSAMHSL 82
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVDAIGFSSAMHSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 83 ILLDSQKQPLTRVITWADNRAAQDAAELKSQPLGDRLYHLTGTPIHPMSPLVKLHWLAHHSPELLAQTCHVVGIKEYLIY 162
Cdd:cd07770 81 LGVDEDGEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAAKFVSIKEYLLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 163 KMTGQLQMDYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIDGLTPVAASTLGLAPTTKIIMGASDGALS 242
Cdd:cd07770 161 RLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAERLGLLAGTPVVLGASDGALA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 243 NLGVGADEPGVAAITIGTSGAVRVMTKQPYLDPEGRLFCYYVAPHHWIVGGPINNGGQVFRWVRDELFTTEsqtaranqq 322
Cdd:cd07770 241 NLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPGRLWCYRLDENRWLVGGAINNGGNVLDWLRDTLLLSG--------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 323 DPYDQLTALAATVPVGAHGLLFHPYLSGERAPLWNADARGSLLGVTTTTTKADIARAVLEGIVMNLNTVLQ-LTAAAEPV 401
Cdd:cd07770 312 DDYEELDKLAEAVPPGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEaLEELAGPV 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654308591 402 HAIRATGGFARSNLWRQILTDVLGQPITIPASFESSCLAAAVIGLKALGHIDDLtAIHAMIGATETYQPNAANHQLY 478
Cdd:cd07770 392 KEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSL-EADELVKIGKVVEPDPENHAIY 467
|
|
| gntK_FGGY |
TIGR01314 |
gluconate kinase, FGGY type; Gluconate is derived from glucose in two steps. This model ... |
3-504 |
0e+00 |
|
gluconate kinase, FGGY type; Gluconate is derived from glucose in two steps. This model describes one form of gluconate kinase, belonging to the FGGY family of carbohydrate kinases. Gluconate kinase phosphoryates gluconate for entry into the Entner-Douderoff pathway. [Energy metabolism, Sugars]
Pssm-ID: 130381 [Multi-domain] Cd Length: 505 Bit Score: 576.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLIGTDLGTTSTKSVLYDHQGHVIASANVGYPLYHDTVTTAEEDPQEIWQAVQATIHQVSAGI-DPEDIEGIAFSSAMHS 81
Cdd:TIGR01314 1 YMIGVDIGTTSTKAVLFEENGKIVAKSSIGYPLYTPASGMAEENPEEIFEAVLVTIREVSINLeDEDEILFVSFSTQMHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 82 LILLDSQKQPLTRVITWADNRAAQDAAELKSQPLGDRLYHLTGTPIHPMSPLVKLHWLAHHSPELLAQTCHVVGIKEYLI 161
Cdd:TIGR01314 81 LIAFDENWQPLTRLITWADNRAVKYAEQIKESKNGFDIYRRTGTPIHPMAPLSKIIWLEAEHPDIYQKAAKYLEIKGYIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 162 YKMTGQLQMDYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIDGLTPVAASTLGLAPTTKIIMGASDGAL 241
Cdd:TIGR01314 161 QRLFGTYKIDYSTASATGMFNLFELDWDKEALELTGIKESQLPKLVPTTEIEENLPHEYAKKMGIQSSTPFVIGASDGVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 242 SNLGVGADEPGVAAITIGTSGAVRVMTKQPYLDPEGRLFCYYVAPHHWIVGGPINNGGQVFRWVRDELFTTESQTARANQ 321
Cdd:TIGR01314 241 SNLGVNAIKKGEAAVTIGTSGAIRTVIDKPKTDEKGRIFCYALTKEHWVIGGPVNNGGDVLRWARDEIFDSEIETATRLG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 322 QDPYDQLTALAATVPVGAHGLLFHPYLSGERAPLWNADARGSLLGVTTTTTKADIARAVLEGIVMNLNTV-LQLT-AAAE 399
Cdd:TIGR01314 321 IDPYDVLTEIAARVSPGADGLLFHPYLAGERAPLWNANARGSFFGLTYSHKKEHMIRAALEGVIYNLYTVaLALVeVMGD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 400 PVHAIRATGGFARSNLWRQILTDVLGQPITIPASFESSCLAAAVIGLKALGHIDDLTAIHAMIGATETYQPNAANHQLYH 479
Cdd:TIGR01314 401 PLNMIQATGGFASSEVWRQMMSDIFEQEIVVPESYESSCLGACILGLKALGLIEDFSEVSTMVGTTETHTPIEKNFEIYR 480
|
490 500
....*....|....*....|....*
gi 654308591 480 QHQVVFDHVTAQLAPLYHEIATLNR 504
Cdd:TIGR01314 481 EISPIFINLSRSLLAEYEQIADFQR 505
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
2-498 |
0e+00 |
|
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: 563.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 2 TYLIGTDLGTTSTKSVLYDHQGHVIASANVGYPLYHDTVTTAEEDPQEIWQAVQATIHQV--SAGIDPEDIEGIAFSSAM 79
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELlaKAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 80 HSLILLDSQKQPLTRVITWADNRAAQDAAELKSQPLGDRLYHLTGTPIHPMSPLVKLHWLAHHSPELLAQTCHVVGIKEY 159
Cdd:COG1070 81 HGLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAKVLLPKDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 160 LIYKMTGQLQMDYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIDGLTPVAASTLGLAPTTKIIMGASDG 239
Cdd:COG1070 161 LRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAAETGLPAGTPVVAGAGDN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 240 ALSNLGVGADEPGVAAITIGTSGAVRVMTKQPYLDPEGRLFCY-YVAPHHWIVGGPINNGGQVFRWVRDELFTTEsqtar 318
Cdd:COG1070 241 AAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFcHAVPGRWLPMGATNNGGSALRWFRDLFADGE----- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 319 anqQDPYDQLTALAATVPVGAHGLLFHPYLSGERAPLWNADARGSLLGVTTTTTKADIARAVLEGIVMNLNTVLQ-LTAA 397
Cdd:COG1070 316 ---LDDYEELNALAAEVPPGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEaLEEA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 398 AEPVHAIRATGGFARSNLWRQILTDVLGQPITIPASFESSCLAAAVIGLKALGHIDDL-TAIHAMIGATETYQPNAANHQ 476
Cdd:COG1070 393 GVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLeEAAAAMVRVGETIEPDPENVA 472
|
490 500
....*....|....*....|..
gi 654308591 477 LYHQHQVVFDHVTAQLAPLYHE 498
Cdd:COG1070 473 AYDELYERYRELYPALKPLFER 494
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
3-478 |
1.07e-163 |
|
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: 472.41 E-value: 1.07e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLIGTDLGTTSTKSVLYDHQGHVIASANVGYPLYHDTVTTAEEDPQEIWQAVQATIHQV--SAGIDPEDIEGIAFSSAMH 80
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELlaKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 81 SLILLDSQKQPLTRVITWADNRAAQDAAELKSQpLGDRLYHLTGTPIHPMSPLVKLHWLAHHSPELLAQTCHVVGIKEYL 160
Cdd:cd07808 81 GLVLLDKNGRPLRPAILWNDQRSAAECEELEAR-LGDEILIITGNPPLPGFTLPKLLWLKENEPEIFARIRKILLPKDYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 161 IYKMTGQLQMDYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIDGLTPVAASTLGLAPTTKIIMGASDGA 240
Cdd:cd07808 160 RYRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAAEELGLPEGTPVVAGAGDNA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 241 LSNLGVGADEPGVAAITIGTSGAVRVMTKQPYLDPEGRLFCY-YVAPHHWIVGGPINNGGQVFRWVRDELFTTEsqtara 319
Cdd:cd07808 240 AAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLHTFpHAVPGKWYAMGVTLSAGLSLRWLRDLFGPDR------ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 320 nqqDPYDQLTALAATVPVGAHGLLFHPYLSGERAPLWNADARGSLLGVTTTTTKADIARAVLEGIVMNLNTVLQ-LTAAA 398
Cdd:cd07808 314 ---ESFDELDAEAAKVPPGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEvLKELG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 399 EPVHAIRATGGFARSNLWRQILTDVLGQPITIPASFESSCLAAAVIGLKALGHIDDLTAIHA-MIGATETYQPNAANHQL 477
Cdd:cd07808 391 IKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAaCIKIEKTIEPDPERHEA 470
|
.
gi 654308591 478 Y 478
Cdd:cd07808 471 Y 471
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
3-479 |
1.30e-160 |
|
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: 464.69 E-value: 1.30e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLIGTDLGTTSTKSVLYDHQGHVIASANVGYPLYHDTVTTAEEDPQEIWQAVQATIHQV--SAGIDPEDIEGIAFSSAMH 80
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALleKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 81 SLILLDSQKQPLTRVITWADNRAAQDAAELKSQPLGDRLYHL-TGTPIHPMSPLVKLHWLAHHSPELLAQTCHVVGIKEY 159
Cdd:cd07805 81 GVVPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLgGGNPPSGKDPLAKILWLKENEPEIYAKTHKFLDAKDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 160 LIYKMTGQLQMDYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIDGLTPVAASTLGLAPTTKIIMGASDG 239
Cdd:cd07805 161 LNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAAAELGLPAGTPVVGGGGDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 240 ALSNLGVGADEPGVAAITIGTSGAVRVMTKQPYLDPEGRLFCY-YVAPHHWIVGGPINNGGQVFRWVRDELFTTESQTAr 318
Cdd:cd07805 241 AAAALGAGAVEEGDAHIYLGTSGWVAAHVPKPKTDPDHGIFTLaSADPGRYLLAAEQETAGGALEWARDNLGGDEDLGA- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 319 anqqDPYDQLTALAATVPVGAHGLLFHPYLSGERAPLWNADARGSLLGVTTTTTKADIARAVLEGIVMNLNTVL-QLTAA 397
Cdd:cd07805 320 ----DDYELLDELAAEAPPGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWLLeALEKL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 398 AEPVHAIRATGGFARSNLWRQILTDVLGQPITIPA-SFESSCLAAAVIGLKALGHIDDLTAIHAMIGATETYQPNAANHQ 476
Cdd:cd07805 396 TRKIDELRLVGGGARSDLWCQILADVLGRPVEVPEnPQEAGALGAALLAAVGLGLLKSFDEAKALVKVEKVFEPDPENRA 475
|
...
gi 654308591 477 LYH 479
Cdd:cd07805 476 RYD 478
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
3-478 |
2.61e-136 |
|
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: 400.74 E-value: 2.61e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLIGTDLGTTSTKSVLYDHQGHVIASANVGYPLYHDTVTTAEEDPQEIWQAVQATIHQV--SAGIDPEDIEGIAFSSAMH 80
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAvaKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 81 SLILLDSQKQPLTRVITWADNRAAqdaaelksqplgdrlyhltgtpihpmsplvklhwlahhspellaqtcHVVGIKEYL 160
Cdd:cd07779 81 TFVPVDEDGRPLRPAISWQDKRTA-----------------------------------------------KFLTVQDYL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 161 IYKMTGQLQMDYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIDGLTPVAASTLGLAPTTKIIMGASDGA 240
Cdd:cd07779 114 LYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAAEETGLPEGTPVVAGGGDQQ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 241 LSNLGVGADEPGVAAITIGTSGAVRVMTKQPYLDPEGRLFCY-YVAPHHWIVGGPINNGGQVFRWVRDELFTTESQTARA 319
Cdd:cd07779 194 CAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNpSAVPGKWVLEGSINTGGSAVRWFRDEFGQDEVAEKEL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 320 NqQDPYDQLTALAATVPVGAHGLLFHPYLSGERAPLWNADARGSLLGVTTTTTKADIARAVLEGIVMNLNTVLQLTAAAE 399
Cdd:cd07779 274 G-VSPYELLNEEAAKSPPGSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELRDNLEAMEKAG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 400 -PVHAIRATGGFARSNLWRQILTDVLGQPITIPASFESSCLAAAVIGLKALGHIDDL-TAIHAMIGATETYQPNAANHQL 477
Cdd:cd07779 353 vPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFeEAVKAMVRVTDTFEPDPENVAI 432
|
.
gi 654308591 478 Y 478
Cdd:cd07779 433 Y 433
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
3-445 |
1.80e-132 |
|
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: 389.23 E-value: 1.80e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLIGTDLGTTSTKSVLYDHQGHVIASANVGYPLYHDTVTTAEEDPQEIWQAVQATIHQV--SAGIDPEDIEGIAFSSAMH 80
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVlaKAGIDPSDIAAIGISGQMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 81 SLILLDSQKQPLTRVITWADNRAaqdaaelksqplgdrlyhltgtpihpmsplvklhwlahhspellaqtcHVVGIKEYL 160
Cdd:cd00366 81 GVVLVDADGNPLRPAIIWLDRRA------------------------------------------------KFLQPNDYI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 161 IYKMTGQLQMDYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIDGLTPVAASTLGLAPTTKIIMGASDGA 240
Cdd:cd00366 113 VFRLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGGDTA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 241 LSNLGVGADEPGVAAITIGTSGAVRVMTKQPYlDPEGRLFCYYVAPH-HWIVGGPINNGGQVFRWVRDELFTTESQTARa 319
Cdd:cd00366 193 AAALGAGVVEPGDAVDSTGTSSVLSVCTDEPV-PPDPRLLNRCHVVPgLWLLEGAINTGGASLRWFRDEFGEEEDSDAE- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 320 nqqdpYDQLTALAATVPVGAHGLLFHPYLSGERAPLWNADARGSLLGVTTTTTKADIARAVLEGIVMNLNTVLQ-LTAAA 398
Cdd:cd00366 271 -----YEGLDELAAEVPPGSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEiLEELG 345
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 654308591 399 EPVHAIRATGGFARSNLWRQILTDVLGQPITIPASFESSCLAAAVIG 445
Cdd:cd00366 346 VKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
3-450 |
5.34e-130 |
|
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: 385.34 E-value: 5.34e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLIGTDLGTTSTKSVLYDHQGHVIASANVGYPLYHDTVTTAEEDPQEIWQAVQATIHQV--SAGIDPEDIEGIAFSSAMH 80
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELlaKAGISPKEIAAIGVSGLVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 81 SLILLDSQKQPLTRVITWADNRAAQDAAELKSQPLGDRLYHLTGTPIHPMSPLVKLHWLAHHSPELLAQTCHVVGIKEYL 160
Cdd:cd07804 81 ALVPVDENGKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRKFLGAYDYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 161 IYKMTGQLQMDYSMA-NATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIDGLTPVAASTLGLAPTTKIIMGASDG 239
Cdd:cd07804 161 VYKLTGEYVIDYSSAgNEGGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEAAEETGLAEGTPVVAGTVDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 240 ALSNLGVGADEPGVAAITIGTSGAVRVMTKQPYLDPegRLFC-YYVAPHHWIVGGPINNGGQVFRWVRDELFTTESQTAR 318
Cdd:cd07804 241 AASALSAGVVEPGDLLLMLGTAGDIGVVTDKLPTDP--RLWLdYHDIPGTYVLNGGMATSGSLLRWFRDEFAGEEVEAEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 319 ANQQDPYDQLTALAATVPVGAHGLLFHPYLSGERAPLWNADARGSLLGVTTTTTKADIARAVLEGIVMNLNTVLQLTAAA 398
Cdd:cd07804 319 SGGDSAYDLLDEEAEKIPPGSDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYGLRHHLEVIREA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 654308591 399 E-PVHAIRATGGFARSNLWRQILTDVLGQPITIPASFESSCLAAAVIGLKALG 450
Cdd:cd07804 399 GlPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
3-450 |
7.80e-127 |
|
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: 376.93 E-value: 7.80e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLIGTDLGTTSTKSVLYDHQGHVIASANVGYPLYHDTVTTAEEDPQEIWQAVQATIHQVSAGIDPEDIEGIAFSSAMHSL 82
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGPDPIAAISVSSQGESG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 83 ILLDSQKQPLTRVITWADNRAAQDAAELKSQPLGDRLYHLTGTPIHPMSPLVKLHWLAHHSPELLAQTCHVVGIKEYLIY 162
Cdd:cd07773 81 VPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAKWLSVADYIAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 163 KMTGQLQMDYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIDGLTPVAASTLGLAPTTKIIMGASDGALS 242
Cdd:cd07773 161 RLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEELGLPAGTPVVVGGHDHLCA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 243 NLGVGADEPGVAAITIGTSGAVRVMTKQPYLD--PEGRLFCY--YVAPHHWIVGGPInNGGQVFRWVRDELFTTESQTAR 318
Cdd:cd07773 241 ALGAGVIEPGDVLDSTGTAEALLAVVDEPPLDemLAEGGLSYghHVPGGYYYLAGSL-PGGALLEWFRDLFGGDESDLAA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 319 ANqqdpydqltALAATVPVGAHGLLFHPYLSGERAPLWNADARGSLLGVTTTTTKADIARAVLEGIVMNLNTVLQ-LTAA 397
Cdd:cd07773 320 AD---------ELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEaLEKA 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 654308591 398 AEPVHAIRATGGFARSNLWRQILTDVLGQPITIPASFESSCLAAAVIGLKALG 450
Cdd:cd07773 391 GIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| XylB |
TIGR01312 |
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ... |
5-478 |
1.19e-115 |
|
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: 349.69 E-value: 1.19e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 5 IGTDLGTTSTKSVLYDHQGHVIASANVGYPLYHDTVTTAEEDPQEIWQAVQATIHQVS--AGIDPEDIEGIAFSSAMHSL 82
Cdd:TIGR01312 1 LGIDLGTSGVKALLVDEQGEVIASGSAPHTVISPHPGWSEQDPEDWWDATEEAIKELLeqASEMGQDIKGIGISGQMHGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 83 ILLDSQKQPLTRVITWADNRAAQDAAELKSQPLGDRLYHLTGTPIHPMSPLVKLHWLAHHSPELLAQTCHVVGIKEYLIY 162
Cdd:TIGR01312 81 VLLDANGEVLRPAILWNDTRTAQECEELEAELGDERVLEITGNLALPGFTAPKLLWVRKHEPEVFARIAKVMLPKDYLRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 163 KMTGQLQMDYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIDGLTPVAASTLGLAPTTKIIMGASDGALS 242
Cdd:TIGR01312 161 RLTGEYVTEYSDASGTGWFDVAKRAWSKELLDALDLPESQLPELIESSEKAGTVRPEVAARLGLSAGVPVAAGGGDNAAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 243 NLGVGADEPGVAAITIGTSGAVRVMTKQPYLDPEGRL--FCYYVaPHHWIVGGPINNGGQVFRWVRDELFTTEsqtaran 320
Cdd:TIGR01312 241 AIGTGTVDPGDAMMSLGTSGVVYAVTDKPLPDPAGAVhgFCHAL-PGGWLPMGVTLSATSSLEWFRELFGKED------- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 321 qqdpYDQLTALAATVPVGAHGLLFHPYLSGERAPLWNADARGSLLGVTTTTTKADIARAVLEGIVMNLNTVLQL--TAAA 398
Cdd:TIGR01312 313 ----VEALNELAEQSPPGAEGVTFLPYLNGERTPHLDPQARGSFIGLTHNTTRADLTRAVLEGVTFALRDSLDIlrEAGG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 399 EPVHAIRATGGFARSNLWRQILTDVLGQPITIPASFESSCLAAAVIGLKALGHIDDLTAIHAM-IGATETYQPNAANHQL 477
Cdd:TIGR01312 389 IPIQSIRLIGGGAKSPAWRQMLADIFGTPVDVPEGEEGPALGAAILAAWALGEKDLAALCSEAvVKQTESVLPIAENVEA 468
|
.
gi 654308591 478 Y 478
Cdd:TIGR01312 469 Y 469
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
3-450 |
7.62e-113 |
|
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: 341.07 E-value: 7.62e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLIGTDLGTTSTKSVLYDHQGHVIASANVGYPLYHDTVTTAEEDPQEIWQAVQATIHQV--SAGIDPEDIEGIAFSSAMH 80
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELleKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 81 SLILLDSQKQPLTRVITWADNRAAQDAAELKSQPLGDRLYHLTGTPIHPMSPLVKLHWLAHHSPELLAQTCHVVGIKEYL 160
Cdd:cd07802 81 GLYLVDKDGKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRIRTVLFCKDWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 161 IYKMTGQLQMDYSMANaTGLFNLYNFDWEPVALDYAHITRTQ--LPPLVDTDAVIDGLTPVAASTLGLAPTTKIIMGASD 238
Cdd:cd07802 161 RYRLTGEISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEELKdkLPPLVPSTEIAGRVTAEAAALTGLPEGTPVAAGAFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 239 GALSNLGVGADEPGVAAITIGTSGAVRVMTKQPYLDPEGRLFCYYVAPHHWIVGGPINNGGQVFRWVRDELFTTEsqtaR 318
Cdd:cd07802 240 VVASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDSVGSNSLHADPGLYLIVEASPTSASNLDWFLDTLLGEE----K 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 319 ANQQDPYDQLTALAATVPVGAHGLLFHPYLSGERAplwNADARGSLLGVTTTTTKADIARAVLEGIVMNLNTVLQLTAAA 398
Cdd:cd07802 316 EAGGSDYDELDELIAAVPPGSSGVIFLPYLYGSGA---NPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLVA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 654308591 399 EPVHAIRATGGFARSNLWRQILTDVLGQPITIPASFESSCLAAAVIGLKALG 450
Cdd:cd07802 393 RKPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
3-449 |
6.51e-104 |
|
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: 317.63 E-value: 6.51e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLIGTDLGTTSTKSVLYDHQGHVIASANVGYPLYHDTVTTAEEDPQEIWQAVQATIHQVSAGIDPEDIEGIAFSSAMHSL 82
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPRRVVAIAVDGTSGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 83 ILLDSQKQPLTRVITWADNRAAQDAAELKSqpLGDRLYHLTGTPIHPMSPLVKLHWLAHHSPELLAQTCHVVGIKEYLIY 162
Cdd:cd07783 81 VLVDREGEPLRPAIMYNDARAVAEAEELAE--AAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFLHQADWLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 163 KMTGQLQM-DYSMAnATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIDGLTPVAASTLGLAPTTKIIMGASDGAL 241
Cdd:cd07783 159 RLTGDRGVtDYNNA-LKLGYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLPAGTPVVAGTTDSIA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 242 SNLGVGADEPGVAAITIGTSGAVRVMTKQPYLDPEGRLFCYYVAPHHWIVGGPINNGGQVFRWvrdelfttesqtarANQ 321
Cdd:cd07783 238 AFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGVYSHRHGDGYWLVGGASNTGGAVLRW--------------FFS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 322 QDPYDQLTALAAtvPVGAHGLLFHPY-LSGERAPLWNADARGSLLgvTTTTTKADIARAVLEGIVMNLNTVLQL--TAAA 398
Cdd:cd07783 304 DDELAELSAQAD--PPGPSGLIYYPLpLRGERFPFWDPDARGFLL--PRPHDRAEFLRALLEGIAFIERLGYERleELGA 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 654308591 399 EPVHAIRATGGFARSNLWRQILTDVLGQPITIPASfESSCLAAAVIGLKAL 449
Cdd:cd07783 380 PPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEE-EEAALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
3-443 |
1.37e-95 |
|
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: 296.77 E-value: 1.37e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLIGTDLGTTSTKSVLYD-HQGHVIASANVGYPLYHDTVTTAEEDPQEIWQAVQATIHQV--SAGIDPEDIEGIAFSSAM 79
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLlkDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 80 HSLILLDSQKQPLTRVITWADNRAAQDAAELkSQPLGDRLYHLTGTPIHPMSPLVKLHWLAHHSPELLAQTCHVVGIKEY 159
Cdd:cd07809 81 HGLVALDADGKVLRPAKLWCDTRTAPEAEEL-TEALGGKKCLLVGLNIPARFTASKLLWLKENEPEHYARIAKILLPHDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 160 LIYKMTGQLQMDYSMANATGLFNLYNFDWEPVALDYAHITRT---QLPPLVDTDAVIDGLTPVAASTLGLAPTTKIIMGA 236
Cdd:cd07809 160 LNWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAIDPSRDlrdLLPEVLPAGEVAGRLTPEGAEELGLPAGIPVAPGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 237 SDGALSNLGVGADEPGVAAITIGTSGAVRVMTKQPYLDPEGRL--FCYyvAPHHWIvggPINNGGQVF-RWVRdelftte 313
Cdd:cd07809 240 GDNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSDPHGRVatFCD--STGGML---PLINTTNCLtAWTE------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 314 sqTARANQQDPYDQLTALAATVPVGAHGLLFHPYLSGERAPLWnADARGSLLGVTTT-TTKADIARAVLEGIVMNLNTVL 392
Cdd:cd07809 308 --LFRELLGVSYEELDELAAQAPPGAGGLLLLPFLNGERTPNL-PHGRASLVGLTLSnFTRANLARAALEGATFGLRYGL 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 654308591 393 Q-LTAAAEPVHAIRATGGFARSNLWRQILTDVLGQPITIPASFESSCLAAAV 443
Cdd:cd07809 385 DiLRELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAAL 436
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
3-450 |
7.95e-93 |
|
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: 289.91 E-value: 7.95e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLIGTDLGTTSTKSVLYDHQGHVIASANVGYPLYHDTVTTAEEDPQEIWQAVQATIHQVSAGID--PEDIEGIAFSSAMH 80
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDvlPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 81 SLILLDSQKQPLTRVITWADNRAAQDAAELKSQPLGDRLYHLTGTPIHPMSPLVKLHWLAHHSPELLAQTCHVVGIKEYL 160
Cdd:cd24121 81 GTWLVDEDGRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKENEPERLERARTALHCKDWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 161 IYKMTGQLQMDYSMANATgLFNLYNFDWEPVALDYAHIT--RTQLPPLVDTDAVIDGLTPVAASTLGLAPTTKIIMGASD 238
Cdd:cd24121 161 FYKLTGEIATDPSDASLT-FLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAAAATGLPAGTPVVLGPFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 239 GALSNLGVGADEPGVAAITIGTSGAVRVMTKQPYLDPE--GRLFCyYVAPHHWIVGGPINNGGQVFRWVRDELFTTESQT 316
Cdd:cd24121 240 VVATALGSGAIEPGDACSILGTTGVHEVVVDEPDLEPEgvGYTIC-LGVPGRWLRAMANMAGTPNLDWFLRELGEVLKEG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 317 ARANQQDPYDQLTALAATVPVGAHGLLFHPYLS--GERAPLWNADARGSLLGVTTTTTKADIARAVLEGIVMNLNTVLQl 394
Cdd:cd24121 319 AEPAGSDLFQDLEELAASSPPGAEGVLYHPYLSpaGERAPFVNPNARAQFTGLSLEHTRADLLRAVYEGVALAMRDCYE- 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 654308591 395 tAAAEPVHAIRATGGFARSNLWRQILTDVLGQPITIPASFESSCLAAAVIGLKALG 450
Cdd:cd24121 398 -HMGEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
3-480 |
1.66e-81 |
|
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: 262.09 E-value: 1.66e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLIGTDLGTTSTKSVLYD-HQGHVIASANVGYPLYHDT--VTTAEEDPQEIWQAVQATIHQV--SAGIDPEDIEGIAFSS 77
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYIPprPGWAEQNPADYWEALEEAVRGAlaEAGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 78 AMHSLILLDSQKQPLTRVITWADNRAAQDAAEL--KSQPLGDRLYHLTGTPIHPMSPLVKLHWLAHHSPELLAQTCHVVG 155
Cdd:cd07781 81 TSSTVVPVDEDGNPLAPAILWMDHRAQEEAAEIneTAHPALEYYLAYYGGVYSSEWMWPKALWLKRNAPEVYDAAYTIVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 156 IKEYLIYKMTGQLQMdySMANAT---------GLFNlYNFdWEPVALDYAHItRTQLP-PLVDTDAVIDGLTPVAASTLG 225
Cdd:cd07781 161 ACDWINARLTGRWVR--SRCAAGhkwmynewgGGPP-REF-LAALDPGLLKL-REKLPgEVVPVGEPAGTLTAEAAERLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 226 LAPTTKIIMGASDGALSNLGVGADEPGVAAITIGTSGAVRVMTKQPYLDPEgrLFCYY---VAPHHWIVggpinNGGQ-- 300
Cdd:cd07781 236 LPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTCHLMVSPKPVDIPG--ICGPVpdaVVPGLYGL-----EAGQsa 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 301 ---VFRWVRDELFTTesqtARANQQDPYDQLTALAATVPVGAHGLLFHPYLSGERAPLWNADARGSLLGVTTTTTKADIA 377
Cdd:cd07781 309 vgdIFAWFVRLFVPP----AEERGDSIYALLSEEAAKLPPGESGLVALDWFNGNRTPLVDPRLRGAIVGLTLGTTPAHIY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 378 RAVLEGIVMNLNTVL-QLTAAAEPVHAIRATGGFARSN-LWRQILTDVLGQPITIPASFESSCLAAAVIGLKALGHIDDL 455
Cdd:cd07781 385 RALLEATAFGTRAIIeRFEEAGVPVNRVVACGGIAEKNpLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVAAGVYADI 464
|
490 500
....*....|....*....|....*.
gi 654308591 456 -TAIHAMIGATETYQPNAANHQLYHQ 480
Cdd:cd07781 465 eEAADAMVRVDRVYEPDPENHAVYEE 490
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
3-478 |
8.47e-81 |
|
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: 259.96 E-value: 8.47e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLIGTDLGTTSTKSVLYDHQGHVIASANVGY-----PLYHDTVttaEEDPQEIWQAVQATIHQV--SAGIDPEDIEGIAF 75
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREWrhkevPDVPGSM---DFDTEKNWKLICECIREAlkKAGIAPKSIAAIST 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 76 SSAMHSLILLDSQKQPLtrvitWA----DNRAAQDAAELKSQPLG--DRLYHLTG-TPihPMSPLVKLHWLAHHSPELLA 148
Cdd:cd07775 78 TSMREGIVLYDNEGEEI-----WAcanvDARAAEEVSELKELYNTleEEVYRISGqTF--ALGAIPRLLWLKNNRPEIYR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 149 QTCHVVGIKEYLIYKMTGQLQMDYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIDGLTPVAASTLGLAP 228
Cdd:cd07775 151 KAAKITMLSDWIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEAAEETGLKE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 229 TTKIIMGASDGALSNLGVGADEPGVAAITIGTSGAVRVMTKQPYLDPEG--RLFCyYVAPHHWIVGGPINNGGQVFRWVR 306
Cdd:cd07775 231 GTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMniRVNC-HVIPDMWQAEGISFFPGLVMRWFR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 307 DELFTTESQTARANQQDPYDQLTALAATVPVGAHGLLfhP-------YLSGERAPL----WNADARGSllgvttttTKAD 375
Cdd:cd07775 310 DAFCAEEKEIAERLGIDAYDLLEEMAKDVPPGSYGIM--PifsdvmnYKNWRHAAPsflnLDIDPEKC--------NKAT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 376 IARAVLE--GIVMNLNtvLQLTAAAEPVHA--IRATGGFARSNLWRQILTDVLGQPITIPASFESSCLAAAVIGLKALGH 451
Cdd:cd07775 380 FFRAIMEnaAIVSAGN--LERIAEFSGIFPdsLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAGI 457
|
490 500
....*....|....*....|....*...
gi 654308591 452 IDDLT-AIHAMIGATETYQPNAANHQLY 478
Cdd:cd07775 458 YSSLEeAVESLVKWEREYLPNPENHEVY 485
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
3-245 |
6.25e-78 |
|
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: 244.17 E-value: 6.25e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLIGTDLGTTSTKSVLYDHQGHVIASANVGYPLYHDTVTTAEEDPQEIWQAVQATIHQV--SAGIDPEDIEGIAFSSAMH 80
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTlsQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 81 SLILLDSQKQPLTRVITWADNRAAQDAAELKSQPLGDRLYHLTGTPIHPMSPLVKLHWLAHHSPELLAQTCHVVGIKEYL 160
Cdd:pfam00370 81 GTVLLDKNDKPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIHDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 161 IYKMTGQLQMDYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIDGLTPVAASTLGLAPTTKIIMGASDGA 240
Cdd:pfam00370 161 RWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGGDQQ 240
|
....*
gi 654308591 241 LSNLG 245
Cdd:pfam00370 241 AAAFG 245
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
3-450 |
7.15e-78 |
|
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: 250.99 E-value: 7.15e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLIGTDLGTTSTKSVLYDHQGHVIASA--NVGY---PLYHDTVttaEEDPQEIWQAVQATIHQV--SAGIDPEDIEGIAF 75
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAyrEWEYytdDDYPDAK---EFDPEELWEKICEAIREAlkKAGISPEDISAVSS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 76 SSAMHSLILLDSQKQPLtrvitWA----DNRAAQDAAELkSQPLGDRLYHLTGTPIHPMSPLVKLHWLAHHSPELLAQTC 151
Cdd:cd07798 78 TSQREGIVFLDKDGREL-----YAgpniDARGVEEAAEI-DDEFGEEIYTTTGHWPTELFPAARLLWFKENRPEIFERIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 152 HVVGIKEYLIYKMTGQLQMDYSMANATGLFNLYNFDW-EPV--ALDYAHITrtqLPPLVDTDAVIDGLTPVAASTLGLAP 228
Cdd:cd07798 152 TVLSISDWIGYRLTGELVSEPSQASETQLFDIKKREWsQELleALGLPPEI---LPEIVPSGTVLGTVSEEAARELGLPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 229 TTKIIMGASDGALSNLGVGADEPGVAAITIGTSGAVRVMTKQPYLDPEGRLF-CYYVAPHHWIVGGpiNNG--GQVFRWV 305
Cdd:cd07798 229 GTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWtGCHLVPGKWVLES--NAGvtGLNYQWL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 306 RDELFTtesqtaraNQQDPYDQLTALAATVPVGAHGLL--FHPYLSGERA-PLWNADARGSLLGVTTTTTKADIARAVLE 382
Cdd:cd07798 307 KELLYG--------DPEDSYEVLEEEASEIPPGANGVLafLGPQIFDARLsGLKNGGFLFPTPLSASELTRGDFARAILE 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654308591 383 G----IVMNLNTVLQLTAAAEPvhAIRATGGFARSNLWRQILTDVLGQPITIPASFESSCLAAAVIGLKALG 450
Cdd:cd07798 379 NiafaIRANLEQLEEVSGREIP--YIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
3-476 |
3.34e-65 |
|
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: 218.88 E-value: 3.34e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLIGTDLGTTSTKSVLYDHQGHVIASANVGYPLYHDTVTTAEEDPQEIWQAVQATIHQV--SAGIDPEDIEGIAFSSAMH 80
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREAlaKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 81 SLILLDSQ-KQPLTRVITWADNRAAQDAAELKSQPLGDRLYHLTGTPIHPMSPLVKLHWLAHHSP---------ELLAQT 150
Cdd:cd07769 81 TTVVWDKKtGKPLYNAIVWQDRRTADICEELKAKGLEERIREKTGLPLDPYFSATKIKWILDNVPgareraergELLFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 151 chvvgIKEYLIYKMTGQLQ--MDYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAV-----IDGL---TPVA 220
Cdd:cd07769 161 -----IDTWLIWKLTGGKVhvTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVfgytdPEGLgagIPIA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 221 AstlglapttkiIMGASDGALsnLGVGADEPGVAAITIGTsGAVRVMT--KQPYLDPEGrlFCYYVAphhWIVGGP---- 294
Cdd:cd07769 236 G-----------ILGDQQAAL--FGQGCFEPGMAKNTYGT-GCFLLMNtgEKPVPSKNG--LLTTIA---WQIGGKvtya 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 295 ----INNGGQVFRWVRDELFTTESqtaranqqdpYDQLTALAATVPvGAHGLLFHPYLSGERAPLWNADARGSLLGVTTT 370
Cdd:cd07769 297 legsIFIAGAAIQWLRDNLGLIED----------AAETEELARSVE-DNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 371 TTKADIARAVLEGIVMNLNTVLQLTAAA--EPVHAIRATGGFARSNLWRQILTDVLGQPITIPASFESSCLAAAVIGLKA 448
Cdd:cd07769 366 TTKAHIVRAALESIAYQTRDVLEAMEKDsgIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLA 445
|
490 500
....*....|....*....|....*...
gi 654308591 449 LGHIDDLTAIHAMIGATETYQPNAANHQ 476
Cdd:cd07769 446 VGFWKDLDELASLWQVDKRFEPSMDEEE 473
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
5-495 |
1.76e-64 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 216.76 E-value: 1.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 5 IGTDLGTTSTKSVLYDHQGHVIAS------ANVGYPLYhdtvttAEEDPQEIWQAVQATIHQVSAGIDPEDIEGIAFSSA 78
Cdd:PRK15027 3 IGIDLGTSGVKVILLNEQGEVVASqtekltVSRPHPLW------SEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 79 MHSLILLDSQKQPLTRVITWADNRAAQDAAELKSQPLGDRlyHLTGTPIHPMSPLVKLHWLAHHSPELLAQTCHVVGIKE 158
Cdd:PRK15027 77 MHGATLLDAQQRVLRPAILWNDGRCAQECALLEARVPQSR--VITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 159 YLIYKMTGQLQMDYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIDGLTPVAASTLGLaPTTKIIMGASD 238
Cdd:PRK15027 155 YLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAKAWGM-ATVPVVAGGGD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 239 GALSNLGVGADEPGVAAITIGTSGAVRVMTKQPYLDPEGRL--FCYYVaPHHWIVGGPINNGGQVFRWvrdelfttesqT 316
Cdd:PRK15027 234 NAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVhsFCHAL-PQRWHLMSVMLSAASCLDW-----------A 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 317 ARANQQDPYDQLTALAATVPVGAHGLLFHPYLSGERAPLWNADARGSLLGVTTTTTKADIARAVLEGIVMNLNTVLQLTA 396
Cdd:PRK15027 302 AKLTGLSNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVH 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 397 AA--EPvHAIRATGGFARSNLWRQILTDVLGQPITIPASFE-SSCLAAAVIGLKALGHIDDLTAIHAMIGATETYQPNAA 473
Cdd:PRK15027 382 ACgiKP-QSVTLIGGGARSEYWRQMLADISGQQLDYRTGGDvGPALGAARLAQIAANPEKSLIELLPQLPLEQSHLPDAQ 460
|
490 500
....*....|....*....|..
gi 654308591 474 NHQLYHQHQVVFDHVTAQLAPL 495
Cdd:PRK15027 461 RYAAYQPRRETFRRLYQQLLPL 482
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
1-481 |
3.18e-64 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 217.18 E-value: 3.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 1 MTYLIGTDLGTTSTKSVLYDHQGHVIASANV--------GYPlyhdtvTTAEEDPQEIWQAVQATIHQV--SAGIDPEDI 70
Cdd:PRK10939 2 MSYLMALDAGTGSIRAVIFDLNGNQIAVGQAewrhlavpDVP------GSMEFDLEKNWQLACQCIRQAlqKAGIPASDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 71 EGIAFSSAMHSLILLDSQKQPLtrvitWA----DNRAAQDAAELKS--QPLGDRLYHLTGTPIhPMSPLVKLHWLAHHSP 144
Cdd:PRK10939 76 AAVSATSMREGIVLYDRNGTEI-----WAcanvDARASREVSELKElhNNFEEEVYRCSGQTL-ALGALPRLLWLAHHRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 145 ELLAQTCHVVGIKEYLIYKMTGQLQMDYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIDGLTPVAASTL 224
Cdd:PRK10939 150 DIYRQAHTITMISDWIAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAKAAAET 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 225 GLAPTTKIIMGASDGALSNLGVGADEPGVAAITIGTSGAVRVMTKQPYLDPEGRLfcyYVAPHhwiVGGPINNG------ 298
Cdd:PRK10939 230 GLRAGTPVVMGGGDVQLGCLGLGVVRPGQTAVLGGTFWQQVVNLPAPVTDPNMNI---RINPH---VIPGMVQAesisff 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 299 -GQVFRWVRDELFTTESQTARANQQDPYDQLTALAATVPVGAHGLLfhPYLSG--------ERAPlwnadargSLLGVT- 368
Cdd:PRK10939 304 tGLTMRWFRDAFCAEEKLLAERLGIDAYSLLEEMASRVPVGSHGII--PIFSDvmrfkswyHAAP--------SFINLSi 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 369 --TTTTKADIARAVLE--GIV--MNLNTVLQLTA--AAEPVHAiratGGFARSNLWRQILTDVLGQPITIPASFESSCLA 440
Cdd:PRK10939 374 dpEKCNKATLFRALEEnaAIVsaCNLQQIAAFSGvfPSSLVFA----GGGSKGKLWSQILADVTGLPVKVPVVKEATALG 449
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 654308591 441 AAVIGLKALGHIDDL-TAIHAMIGATETYQPNAANHQLYHQH 481
Cdd:PRK10939 450 CAIAAGVGAGIYSSLaETGERLVRWERTFEPNPENHELYQEA 491
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
1-480 |
1.03e-62 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 212.23 E-value: 1.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 1 MTYLIGTDLGTTSTKSVLYDHQGHVIASANVGYPLYHDT---VttaEEDPQEIWQAVQATIHQV--SAGIDPEDIEGIAF 75
Cdd:COG0554 2 KKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQpgwV---EHDPEEIWESVLAVIREAlaKAGISAEDIAAIGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 76 SSAMHSLILLDSQK-QPLTRVITWADNRAAQDAAELKSQPLGDRLYHLTGTPIHPMSPLVKLHWLAHHSP---------E 145
Cdd:COG0554 79 TNQRETTVVWDRKTgKPLYNAIVWQDRRTADICEELKADGLEDLIREKTGLVLDPYFSATKIKWILDNVPgareraeagE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 146 LLAQTchvvgIKEYLIYKMTGQLQ--MDYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIdGLT------ 217
Cdd:COG0554 159 LLFGT-----IDSWLIWKLTGGKVhvTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVF-GETdpdlfg 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 218 ---PVAAstlglapttkiIMGASDGALsnLGVGADEPGVAAITIGTsGAVRVMT--KQPyldpegrlfcyyVAPHH---- 288
Cdd:COG0554 233 aeiPIAG-----------IAGDQQAAL--FGQACFEPGMAKNTYGT-GCFLLMNtgDEP------------VRSKNgllt 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 289 ---WIVG--------GPINNGGQVFRWVRDEL--FTTESQTaranqqdpydqlTALAATVPvGAHGLLFHPYLSGERAPL 355
Cdd:COG0554 287 tiaWGLGgkvtyaleGSIFVAGAAVQWLRDGLglIDSAAES------------EALARSVE-DNGGVYFVPAFTGLGAPY 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 356 WNADARGSLLGVTTTTTKADIARAVLEGIVMNLNTVLQL--TAAAEPVHAIRATGGFARSNLWRQILTDVLGQPITIPAS 433
Cdd:COG0554 354 WDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAmeADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKV 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 654308591 434 FESSCLAAAVIGLKALGHIDDLTAIHAMIGATETYQPNAANHQ---LYHQ 480
Cdd:COG0554 434 TETTALGAAYLAGLAVGFWKSLEELAALWKVDRRFEPQMDEEErerLYAG 483
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
3-474 |
1.11e-56 |
|
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: 196.63 E-value: 1.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLIGTDLGTTSTKSVLYDHQGHVIASANVGYPLYHDTVTTAEEDPQEIWQAVQATIHQV--SAGIDPEDIEGIAFSSAMH 80
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEAlkNAGLTPEDIAAIGISTQRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 81 SLILLDSQK-QPLTRVITWADNRAAQDAAELKSQPL-------GDRLYHLTGTPIH---------PMSPLVKLHWLAHHS 143
Cdd:cd07793 81 TFLTWDKKTgKPLHNFITWQDLRAAELCESWNRSLLlkalrggSKFLHFLTRNKRFlaasvlkfsTAHVSIRLLWILQNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 144 PELLAQ----TCHVVGIKEYLIYKMTG--QLQMDYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTdavidglt 217
Cdd:cd07793 161 PELKEAaekgELLFGTIDTWLLWKLTGgkVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDT-------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 218 pvaASTLGLapTTKIIMGAsdgALSNLGVGAD-----------EPGVAAITIGTSGAVRVMT-KQPYLDPEGrlfcYY-- 283
Cdd:cd07793 233 ---SGDFGS--TDPSIFGA---EIPITAVVADqqaalfgeccfDKGDVKITMGTGTFIDINTgSKPHASVKG----LYpl 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 284 VAphhWIVGGPI--------NNGGQVFRWVRDE-LFTTESQTAranqqdpydqltALAATVPvGAHGLLFHPYLSGERAP 354
Cdd:cd07793 301 VG---WKIGGEItylaegnaSDTGTVIDWAKSIgLFDDPSETE------------DIAESVE-DTNGVYFVPAFSGLQAP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 355 LWNADARGSLLGVTTTTTKADIARAVLEGIVMnlnTVLQLTAAAE-----PVHAIRATGGFARSNLWRQILTDVLGQPIT 429
Cdd:cd07793 365 YNDPTACAGFIGLTPSTTKAHLVRAILESIAF---RVKQLLETMEketsiKISSIRVDGGVSNNDFILQLIADLLGKPVE 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 654308591 430 IPASFESSCLAAAVI-GLkALGHIDDLTAIHAMIGATETYQPNAAN 474
Cdd:cd07793 442 RPKNTEMSALGAAFLaGL-ASGIWKSKEELKKLRKIEKIFEPKMDN 486
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
3-442 |
2.00e-55 |
|
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: 191.67 E-value: 2.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLIGTDLGTTSTKSVLYD-HQGHVIASANV--GYPLYHDTVTTAEEDPQEIWQAVQATIHQVSAGIDPeDIEGIAFSSAM 79
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDlESGRILESVSRptPAPISSDDPGRSEQDPEKILEAVRNLIDELPREYLS-DVTGIGITGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 80 HSLILLDSQKQPLTRVITWADNRAAQDAAElKSQPLGDRLYHLTGTPIHPMSPLVKLHWLAHHSPeLLAQTCHVVGIKEY 159
Cdd:cd07777 80 HGIVLWDEDGNPVSPLITWQDQRCSEEFLG-GLSTYGEELLPKSGMRLKPGYGLATLFWLLRNGP-LPSKADRAGTIGDY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 160 LIYKMTGQLQ--MDYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIDGLTPVAASTLGLAPTtkiiMGas 237
Cdd:cd07777 158 IVARLTGLPKpvMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLSSALPKGIPVYVA----LG-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 238 DGALSNLGVGADEPGVAAITIGTSGAVRVMTKQPYLDPEGRLFCYYvAPHHWIVGGPInNGGQVFRW----VRDelfTTE 313
Cdd:cd07777 232 DNQASVLGSGLNEENDAVLNIGTGAQLSFLTPKFELSGSVEIRPFF-DGRYLLVAASL-PGGRALAVlvdfLRE---WLR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 314 SQTARANQQDPYDQLTALAAtvPVGAHGLLFHPYLSGERaplWNADARGSLLGVTTTTTK-ADIARAVLEGIVMNLNTVL 392
Cdd:cd07777 307 ELGGSLSDDEIWEKLDELAE--SEESSDLSVDPTFFGER---HDPEGRGSITNIGESNFTlGNLFRALCRGIAENLHEML 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 654308591 393 QLTAAAEP-VHAIRATGGFARSNLW-RQILTDVLGQPITIPASFESSCLAAA 442
Cdd:cd07777 382 PRLDLDLSgIERIVGSGGALRKNPVlRRIIEKRFGLPVVLSEGSEEAAVGAA 433
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
3-471 |
2.93e-55 |
|
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: 192.32 E-value: 2.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLIGTDLGTTSTKSVLYDHQGHVIASANVGYPLYHDTVTTAEEDPQEIWQAVQATIHQV--SAGIDPEDIEGIAFSSAMH 80
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREAlaKAGIRASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 81 SLILLDSQK-QPLTRVITWADNRAAQDAAELKSQPLGDRLYHLTGTPIHPMSPLVKLHWLAHHSP---------ELLAQT 150
Cdd:cd07786 81 TTVVWDRETgKPVYNAIVWQDRRTADICEELKAEGHEEMIREKTGLVLDPYFSATKIRWILDNVPgareraergELAFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 151 chvvgIKEYLIYKMT-GQLQM-DYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIdGLTpvAASTLGLA- 227
Cdd:cd07786 161 -----IDSWLIWKLTgGKVHAtDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVF-GYT--DPDLLGAEi 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 228 PTTKIImGASDGALsnLGVGADEPGVAAITIGTsGAVRVMT--KQPyldpegrlfcyyVAPHH-------WIVGGPIN-- 296
Cdd:cd07786 233 PIAGIA-GDQQAAL--FGQACFEPGMAKNTYGT-GCFMLMNtgEKP------------VRSKNgllttiaWQLGGKVTya 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 297 ------NGGQVFRWVRDEL--FTTESQTAranqqdpydqltALAATVPvGAHGLLFHPYLSGERAPLWNADARGSLLGVT 368
Cdd:cd07786 297 legsifIAGAAVQWLRDGLglIESAAETE------------ALARSVP-DNGGVYFVPAFTGLGAPYWDPDARGAIFGLT 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 369 TTTTKADIARAVLEGIVMNLNTVLQLTAAA--EPVHAIRATGGFARSNLWRQILTDVLGQPITIPASFESSCLAAAVI-G 445
Cdd:cd07786 364 RGTTRAHIARAALESIAYQTRDLLEAMEADsgIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLaG 443
|
490 500
....*....|....*....|....*.
gi 654308591 446 LKAlGHIDDLTAIHAMIGATETYQPN 471
Cdd:cd07786 444 LAV-GLWKSLDELAKLWQVDRRFEPS 468
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
4-471 |
1.96e-50 |
|
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: 179.64 E-value: 1.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 4 LIGT-DLGTTSTKSVLYDHQGHVIASANVGYPLYHDTVTTAEEDPQEIWQAVQATIHQV-----SAGIDPEDIEGIAFSS 77
Cdd:cd07792 2 LVGAiDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAveklkALGISPSDIKAIGITN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 78 AMHSLILLDSQ-KQPLTRVITWADNRAAQDAAELKSQ-PLG-DRLYHLTGTPIHPMSPLVKLHWLAHHSPE----LLAQT 150
Cdd:cd07792 82 QRETTVVWDKStGKPLYNAIVWLDTRTSDTVEELSAKtPGGkDHFRKKTGLPISTYFSAVKLRWLLDNVPEvkkaVDDGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 151 CHVVGIKEYLIYKMTGQLQM-----DYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIdGLtpVAASTLG 225
Cdd:cd07792 162 LLFGTVDSWLIWNLTGGKNGgvhvtDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVY-GK--IASGPLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 226 LAPTTKIImGASDGALsnLGVGADEPGVAAITIGT-------SGAVRVMTKQpyldpeGRL--FCYYV---APHHWIVGG 293
Cdd:cd07792 239 GVPISGCL-GDQQAAL--VGQGCFKPGEAKNTYGTgcfllynTGEEPVFSKH------GLLttVAYKLgpdAPPVYALEG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 294 PINNGGQVFRWVRDELFTTESqtaranqqdpYDQLTALAATVPvGAHGLLFHPYLSGERAPLWNADARGSLLGVTTTTTK 373
Cdd:cd07792 310 SIAIAGAAVQWLRDNLGIISS----------ASEVETLAASVP-DTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 374 ADIARAVLEGIVMNLNTVLQLTA--AAEPVHAIRATGGFARSNLWRQILTDVLGQPITIPASFESSCLAAAV---IGLKA 448
Cdd:cd07792 379 AHIARAALEAVCFQTREILDAMNkdSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIaagLAVGV 458
|
490 500
....*....|....*....|...
gi 654308591 449 LGHIDDLTAIHAmiGATETYQPN 471
Cdd:cd07792 459 WKSLDELKSLNE--GGRTVFEPQ 479
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
1-471 |
3.45e-46 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 167.51 E-value: 3.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 1 MTYLIGTDLGTTSTKSVLYDHQGHVIASANVGyplyhDTVTTAEEDPQ-------EIWQAVQATIHQVSAGIDPEDIEGI 73
Cdd:PRK10331 1 QDVILVLDCGATNVRAIAVDRQGKIVARASTP-----NASDIAAENSDwhqwsldAILQRFADCCRQINSELTECHIRGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 74 AFSSAMHSLILLDSQKQPLTRVITWADNRAAQDAAELKSQPLGDRLYHLTGTPIHPMSPLVKLHWLAHHSPELLAQTCHV 153
Cdd:PRK10331 76 TVTTFGVDGALVDKQGNLLYPIISWKCPRTAAVMENIERYISAQQLQQISGVGAFSFNTLYKLVWLKENHPQLLEQAHAW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 154 VGIKEYLIYKMTGQLQMDYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIDGLTPVAASTLGLAPTTKII 233
Cdd:PRK10331 156 LFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPSAAALLGLPVGIPVI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 234 MGASDGALSNLGVGADEpGVAAITIGTSGAVRVMTKQPYLDPEGR---LFCYYVAphhwiVGGPINNGGQ-----VFRWV 305
Cdd:PRK10331 236 SAGHDTQFALFGSGAGQ-NQPVLSSGTWEILMVRSAQVDTSLLSQyagSTCELDS-----QSGLYNPGMQwlasgVLEWV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 306 RDELFTTEsqtaranqqDPYDQLTALAATVPVGAHGLLFHPYLSGERaplwnadaRGSLLGVTTTTTKADIARAVLEGIV 385
Cdd:PRK10331 310 RKLFWTAE---------TPYQTMIEEARAIPPGADGVKMQCDLLACQ--------NAGWQGVTLNTTRGHFYRAALEGLT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 386 MNLNTVLQLTaaaEPVHAIRAT-----GGFARSNLWRQILTDVLGQPITIPASFESSCLAAAVIGLKALGHIDDL-TAIH 459
Cdd:PRK10331 373 AQLKRNLQVL---EKIGHFKASelllvGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPeQARA 449
|
490
....*....|..
gi 654308591 460 AMIGATETYQPN 471
Cdd:PRK10331 450 QMKYQYRYFYPQ 461
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
1-470 |
6.68e-45 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 164.76 E-value: 6.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 1 MTYLIGTDLGTTSTKSVLYDHQGHVIASanvgYPLYHDTVTT----AEEDPQEIWQAVQATIHQVSAGIDPED----IEG 72
Cdd:PTZ00294 1 MKYIGSIDQGTTSTRFIIFDEKGNVVSS----HQIPHEQITPhpgwLEHDPEEILRNVYKCMNEAIKKLREKGpsfkIKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 73 IAFSSAMHSLILLDSQ-KQPLTRVITWADNRAAQDAAEL-KSQPLGDRLYHLTGTPIHPMSPLVKLHWLAHHSPELLA-- 148
Cdd:PTZ00294 77 IGITNQRETVVAWDKVtGKPLYNAIVWLDTRTYDIVNELtKKYGGSNFFQKITGLPISTYFSAFKIRWMLENVPAVKDav 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 149 --QTCHVVGIKEYLIYKMTGQ--LQMDYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIDGLTPVAASTL 224
Cdd:PTZ00294 157 keGTLLFGTIDTWLIWNLTGGksHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTISGEAVPLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 225 GLAPTTKIImGASDGALsnLGVGADEPGVAAITIGTsGAVRVMT--KQPYLDPEGRL--FCYYV---APHHWIVGGPINN 297
Cdd:PTZ00294 237 EGVPITGCI-GDQQAAL--IGHGCFEKGDAKNTYGT-GCFLLMNtgTEIVFSKHGLLttVCYQLgpnGPTVYALEGSIAV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 298 GGQVFRWVRDELfttesqtaraNQQDPYDQLTALAATVPvGAHGLLFHPYLSGERAPLWNADARGSLLGVTTTTTKADIA 377
Cdd:PTZ00294 313 AGAGVEWLRDNM----------GLISHPSEIEKLARSVK-DTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 378 RAVLEGIVMNLNTVLQ--LTAAAEPVHAIRATGGFARSNLWRQILTDVLGQPITIPASFESSCLAAAVI-GLkALGHIDD 454
Cdd:PTZ00294 382 RAALEAIALQTNDVIEsmEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLaGL-AVGVWKS 460
|
490
....*....|....*..
gi 654308591 455 LTAIHAMI-GATETYQP 470
Cdd:PTZ00294 461 LEEVKKLIrRSNSTFSP 477
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
3-480 |
2.86e-44 |
|
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: 163.47 E-value: 2.86e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLIGTDLGTTSTKSVLYDHQGHVIASAnvgyplyHDTVTTAEEDP-------QEIWQAVQATIHQV--SAGIDPEDIEGI 73
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATA-------SQPITTWNPKPdfyeqssEDIWQAVCEAVKEVleGAGVDPEQVKGI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 74 AFSsAMHSLILLDSQKQPLT---------RVITWADNRAAQDAAELKSQplGDRLYHLTGTPIHPMSPLVKLHWLAHHSP 144
Cdd:cd07782 74 GFD-ATCSLVVLDAEGKPVSvspsgdderNVILWMDHRAVEEAERINAT--GHEVLKYVGGKISPEMEPPKLLWLKENLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 145 ELLAQTCHVVGIKEYLIYKMTGQL---------QMDYS--MANATG----LFNLYNFDwEPVALDYAHITRTQLPPLVdt 209
Cdd:cd07782 151 ETWAKAGHFFDLPDFLTWKATGSLtrslcslvcKWTYLahEGSEGGwdddFFKEIGLE-DLVEDNFAKIGSVVLPPGE-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 210 dAVIDGLTPVAASTLGLAPTTKIIMGASD---GALSNLGVGADEPGVA--------AITIGTSGAVRVMTKQPyldpegr 278
Cdd:cd07782 228 -PVGGGLTAEAAKELGLPEGTPVGVSLIDahaGGLGTLGADVGGLPCEadpltrrlALICGTSSCHMAVSPEP------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 279 LFC------YY--VAPHHWIvggpiNNGGQ----------VFRWVRdelFTTESQTARANQQDPYDQLTA----LAATVP 336
Cdd:cd07782 300 VFVpgvwgpYYsaMLPGLWL-----NEGGQsatgalldhiIETHPA---YPELKEEAKAAGKSIYEYLNErleqLAEEKG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 337 VGAHGLL----FHPYLSGERAPLWNADARGSLLGVTTTTTKADIAR---AVLEGIVMNLNTVLQ-LTAAAEPVHAIRATG 408
Cdd:cd07782 372 LPLAYLTrdlhVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHIIEaMNAAGHKIDTIFMCG 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654308591 409 GFARSNLWRQILTDVLGQPITIPASFESSCLAAAVIGLKALGHIDDL-TAIHAMIGATETYQPNAAnHQLYHQ 480
Cdd:cd07782 452 GLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLwDAMAAMSGPGKVVEPNEE-LKKYHD 523
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
3-470 |
9.43e-44 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 161.53 E-value: 9.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLIGTDLGTTSTKSVLYDHQGHVIASANVGYPLYHDTVTTAEEDPQEIWQAVQATIHQV--SAGIDPEDIEGIAFSSAMH 80
Cdd:PRK00047 6 YILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEAlaKAGISPDQIAAIGITNQRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 81 SLILLDSQK-QPLTRVITWADNRAAQDAAELKSQPLGDRLYHLTGTPIHPMSPLVKLHWLAHHSP---------ELLAQT 150
Cdd:PRK00047 86 TTVVWDKETgRPIYNAIVWQDRRTADICEELKRDGYEDYIREKTGLVIDPYFSGTKIKWILDNVEgareraekgELLFGT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 151 chvvgIKEYLIYKMT-GQLQM-DYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIdGLTPVAASTLGLAP 228
Cdd:PRK00047 166 -----IDTWLVWKLTgGKVHVtDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVY-GKTNPYGFFGGEVP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 229 TTKIImGASDGALsnLGVGADEPGVAAITIGTsGAVRVMT--KQPYLDPEGRLFCyyVAphhWIVGGPIN--------NG 298
Cdd:PRK00047 240 IAGIA-GDQQAAL--FGQLCFEPGMAKNTYGT-GCFMLMNtgEKAVKSENGLLTT--IA---WGIDGKVVyalegsifVA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 299 GQVFRWVRDEL--FTTESQTaranqqdpydqlTALAATVPvGAHGLLFHPYLSGERAPLWNADARGSLLGVTTTTTKADI 376
Cdd:PRK00047 311 GSAIQWLRDGLkiISDASDS------------EALARKVE-DNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 377 ARAVLEGIVMNLNTVLQLTAA--AEPVHAIRATGGFARSNLWRQILTDVLGQPITIPASFESSCLAAAVI-GLkALGHID 453
Cdd:PRK00047 378 IRATLESIAYQTRDVLDAMQAdsGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLaGL-AVGFWK 456
|
490
....*....|....*..
gi 654308591 454 DLTAIHAMIGATETYQP 470
Cdd:PRK00047 457 DLDELKEQWKIDRRFEP 473
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
8-470 |
1.88e-39 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 149.85 E-value: 1.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 8 DLGTTSTKSVLYDHQGHVIASANVGYPLYHDTVTTAEEDPQEIWQAVQATIhqvSAGIDPEDIEGIAFSSAMH------- 80
Cdd:PLN02295 6 DQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCI---AKALEKAAAKGHNVDSGLKaigitnq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 81 ---SLILLDSQKQPLTRVITWADNRAAQDAAELKSQPLGDR--LYHLTGTPIHPMSPLVKLHWLAHHSPELLA--QTCHV 153
Cdd:PLN02295 83 retTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKELSGGRkhFVETCGLPISTYFSATKLLWLLENVDAVKEavKSGDA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 154 -VG-IKEYLIYKMTGQLQ-----MDYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIDGLTPvAASTLGL 226
Cdd:PLN02295 163 lFGtIDSWLIWNLTGGASggvhvTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIAK-GWPLAGV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 227 APTTkiIMGASDGALsnLGVGADePGVAAITIGT-------SGAVRVMTKQPYL-------DPEgrlfcyyvAPHHWIVG 292
Cdd:PLN02295 242 PIAG--CLGDQHAAM--LGQRCR-PGEAKSTYGTgcfillnTGEEVVPSKHGLLttvayklGPD--------APTNYALE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 293 GPINNGGQVFRWVRDELFTTESQTaranqqdpydQLTALAATVPvGAHGLLFHPYLSGERAPLWNADARGSLLGVTTTTT 372
Cdd:PLN02295 309 GSVAIAGAAVQWLRDNLGIIKSAS----------EIEALAATVD-DTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTN 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 373 KADIARAVLEGIVMNLNTVL-------QLTAAAEPVHAIRATGGFARSNLWRQILTDVLGQPITIPASFESSCLAAAVIG 445
Cdd:PLN02295 378 KAHIARAVLESMCFQVKDVLdamrkdaGEEKSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAA 457
|
490 500
....*....|....*....|....*.
gi 654308591 446 LKALGHIDDLTAI-HAMIGATETYQP 470
Cdd:PLN02295 458 GLAVGLWTEEEIFaSEKWKNTTTFRP 483
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
254-449 |
4.21e-34 |
|
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: 127.06 E-value: 4.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 254 AAITIGTSGAVRVMTKQPYLDPEGRLFCYY--VAPHHWIVGGPINNGGQVFRWVRDELFTTESQtARANQQDPYDQLTAL 331
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSVHGVWGPYTneMLPGYWGLEGGQSAAGSLLAWLLQFHGLREEL-RDAGNVESLAELAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 332 AATVPVGahGLLFHPYLSGERAPLWNADARGSLLGVTTTTTKADIARAVLEGIVMNL-NTVLQLTAAAE-PVHAIRATGG 409
Cdd:pfam02782 80 AAVAPAG--GLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLrQILEALTKQEGhPIDTIHVSGG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 654308591 410 FARSNLWRQILTDVLGQPITIPASFESSCLAAAVIGLKAL 449
Cdd:pfam02782 158 GSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVAA 197
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
1-480 |
1.22e-32 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 130.74 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 1 MTYLIGTDLGTTSTKSVLYD-HQGHVIASANVGYP-----LYHDTVTT-AEEDPQEIWQAVQATIHQV--SAGIDPEDIE 71
Cdd:PRK04123 2 MAYVIGLDFGTDSVRALLVDcATGEELATAVVEYPhwvkgRYLDLPPNqALQHPLDYIESLEAAIPAVlkEAGVDPAAVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 72 GIAFSSAMHSLILLDSQKQPLTRVITWADN----------RAAQDAAelksqplgDRLYHLTGTPIHP------------ 129
Cdd:PRK04123 82 GIGVDFTGSTPAPVDADGTPLALLPEFAENphamvklwkdHTAQEEA--------EEINRLAHERGEAdlsryiggiyss 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 130 --MSPLVkLHWLaHHSPELLAQTCHVVGIKEYLIYKMTG-QLQMDYSMAN-ATGLFNLYNFDWE--P-----VALD--YA 196
Cdd:PRK04123 154 ewFWAKI-LHVL-REDPAVYEAAASWVEACDWVVALLTGtTDPQDIVRSRcAAGHKALWHESWGglPsadffDALDplLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 197 HITRTQLP-PLVDTDAVIDGLTPVAASTLGLAPTTKIIMGASDGALSNLGVGAdEPGVAAITIGTSgAVRVMtkqpyLDP 275
Cdd:PRK04123 232 RGLRDKLFtETWTAGEPAGTLTAEWAQRLGLPEGVAVSVGAFDAHMGAVGAGA-EPGTLVKVMGTS-TCDIL-----LAD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 276 EGRLfcyyVAPHHWIVGGPINNG-----------GQVFRWVRDELFTTESQTARANQQDP-YDQLTALAATVPVGAHGLL 343
Cdd:PRK04123 305 KQRA----VPGICGQVDGSIVPGligyeagqsavGDIFAWFARLLVPPEYKDEAEARGKQlLELLTEAAAKQPPGEHGLV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 344 FHPYLSGERAPLWNADARGSLLGVTTTTTKADIARAVLEGIVMNLNTVL-QLTAAAEPVHAIRATGGFARSN-LWRQILT 421
Cdd:PRK04123 381 ALDWFNGRRTPLADQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMeCFEDQGVPVEEVIAAGGIARKNpVLMQIYA 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654308591 422 DVLGQPITIPASFESSCLAAAVIGLKALGHIDDL-TAIHAMIGATE-TYQPNAANHQLYHQ 480
Cdd:PRK04123 461 DVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIpEAQQAMASPVEkTYQPDPENVARYEQ 521
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
3-481 |
1.25e-32 |
|
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: 130.44 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLIGTDLGTTSTKSVLYD-HQGHVIASANVgyPLYHDTVTTAE---EDPQEIWQAVQATIHQV--SAGIDPEDIEGIAFS 76
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDlYAGLEMAQEPV--PYYQDSSKKSWkfwQKSTEIIKALQKCVQKLniREGVDAYEVKGCGVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 77 sAMHSLILLDSQKQPLTR---------VITWADNRA---AQDAAELKSQPLGDRLyhltGTPIHPMSPLVKLHWLAHHSP 144
Cdd:cd07768 79 -ATCSLAIFDREGTPLMAlipypnednVIFWMDHSAvneAQWINMQCPQQLLDYL----GGKISPEMGVPKLKYFLDEYS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 145 ELLAQTCHVVGIKEYLIYKMTGQLQMdysmaNATGLFNLYNFD-----WEP-----VALDYAHITRTQL-PPLVDTDAVI 213
Cdd:cd07768 154 HLRDKHFHIFDLHDYIAYELTRLYEW-----NICGLLGKENLDgeesgWSSsffknIDPRLEHLTTTKNlPSNVPIGTTS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 214 DGLTPVAASTLGLAPTTKIIMGASDGALSNLGVG-ADEPGVAAITIGTSGAVRVMTKQPYLDPeGRLFCYYVA--PHHWI 290
Cdd:cd07768 229 GVALPEMAEKMGLHPGTAVVVSCIDAHASWFAVAsPHLETSLFMIAGTSSCHMYGTTISDRIP-GVWGPFDTIidPDYSV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 291 VGGPINNGGQVFRW-VRDELFTTESQTARANQQDPYDQLTALA---ATVPVGAHGLLFHPYLSGERAPLWNADARGSLLG 366
Cdd:cd07768 308 YEAGQSATGKLIEHlFESHPCARKFDEALKKGADIYQVLEQTIrqiEKNNGLSIHILTLDMFFGNRSEFADPRLKGSFIG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 367 VTTTTTKADIA---RAVLEGIVMNLNTVLQ-LTAAAEPVHAIRATGGFARSNLWRQILTDVLGQPITIPASFESSCLAAA 442
Cdd:cd07768 388 ESLDTSMLNLTykyIAILEALAFGTRLIIDtFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAA 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 654308591 443 VIGLKALG---HIDDLT-AIHAMIGATETYQPNAANH------------QLYHQH 481
Cdd:cd07768 468 VLAKVAAGkkqLADSITeADISNDRKSETFEPLAYRLgadyillykllcVKYHIH 522
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
84-465 |
5.64e-25 |
|
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: 107.61 E-value: 5.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 84 LLDSQKQPLTRVITWADNRAAQDAAELKSQPLGDRLYHLTGTPIHPMSPLVKLHWLAHHSPELLAQTCHVVGIKEYLIYK 163
Cdd:cd07771 82 LLDKNGELLGNPVHYRDPRTEGMMEELFEKISKEELYERTGIQFQPINTLYQLYALKKEGPELLERADKLLMLPDLLNYL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 164 MTGQLQMDYSMANATGLFNLYNFDWEPVALDYAHITRTQLPPLVDTDAVIDGLTPVAASTLGLAPtTKIIMGAS-DGALS 242
Cdd:cd07771 162 LTGEKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPEVAEELGLKG-IPVIAVAShDTASA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 243 NLGVGADEPGVAAITIGTSGAVRVMTKQPYLDPEGRLFCYyvaphhwivggpINNGG-----QVFR-----WVRDELftt 312
Cdd:cd07771 241 VAAVPAEDEDAAFISSGTWSLIGVELDEPVITEEAFEAGF------------TNEGGadgtiRLLKnitglWLLQEC--- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 313 ESQTARANQQDPYDQLTALAATV-PVGA-----HGLLFHP---------YL--SGERAPlwnadargsllgvtttTTKAD 375
Cdd:cd07771 306 RREWEEEGKDYSYDELVALAEEApPFGAfidpdDPRFLNPgdmpeairaYCreTGQPVP----------------ESPGE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 376 IARAVLEGIVMNL-NTVLQLTAAA-EPVHAIRATGGFARSNLWRQILTDVLGQP-ITIPAsfESSCLAAAVIGLKALGHI 452
Cdd:cd07771 370 IARCIYESLALKYaKTIEELEELTgKRIDRIHIVGGGSRNALLCQLTADATGLPvIAGPV--EATAIGNLLVQLIALGEI 447
|
410
....*....|...
gi 654308591 453 DDLTAIHAMIGAT 465
Cdd:cd07771 448 KSLEEGRELVRNS 460
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
3-481 |
4.23e-19 |
|
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: 89.92 E-value: 4.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 3 YLiGTDLGTTSTKSVLYDHQGHVIASANVGY----PLYHdtvTTA----EEDPQEI------W-QAVQATIHQ-VSAGID 66
Cdd:cd07776 2 YL-GLDLSTQSLKAVVIDSDLKVVAEESVNFdsdlPEYG---TKGgvhrDGDGGEVtspvlmWvEALDLLLEKlKAAGFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 67 PEDIEGIAFSSAMH---------SLIL--LDSqKQPL----------TRVITWADNRAAQDAAELKSQpLG--DRLYHLT 123
Cdd:cd07776 78 FSRVKAISGSGQQHgsvywskgaESALanLDP-SKSLaeqlegafsvPDSPIWMDSSTTKQCRELEKA-VGgpEALAKLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 124 GTPIHPMSPLVKLHWLAHHSPELLAQTCHVVGIKEYLIYKMTGQLQ-MDYSMANATGLFNLYNFDWEPVALDYA---HIt 199
Cdd:cd07776 156 GSRAYERFTGPQIAKIAQTDPEAYENTERISLVSSFLASLLLGRYApIDESDGSGMNLMDIRSRKWSPELLDAAtapDL- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 200 RTQLPPLVDTDAVIDGLTPVAASTLGLAPTTKIIMGASDGALSNLGVGAdEPGVAAITIGTSGAVRVMTKQPYLDPEGRL 279
Cdd:cd07776 235 KEKLGELVPSSTVAGGISSYFVERYGFSPDCLVVAFTGDNPASLAGLGL-EPGDVAVSLGTSDTVFLVLDEPKPGPEGHV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 280 FCYYVAPHHWIVGGPINNGGQVFRWVRDelfttesqtaRANQQDpYDQLTALAATVPVGAHGLLFHPYLSGE------RA 353
Cdd:cd07776 314 FANPVDPGSYMAMLCYKNGSLARERVRD----------RYAGGS-WEKFNELLESTPPGNNGNLGLYFDEPEitppvpGG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 354 PLWNADARgsllGVTTTTTKADIARAVLEGIVMNLNTVLQLTAAAEPVHAIRATGGFARSNLWRQILTDVLGQPITIPAS 433
Cdd:cd07776 383 GRRFFGDD----GVDAFFDPAVEVRAVVESQFLSMRLHAERLGSDIPPTRILATGGASANKAILQVLADVFGAPVYTLDV 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 654308591 434 FESSCLAAAVIGLKALGHIDDLTAIHAMIGATE-----TYQPNAANHQLYHQH 481
Cdd:cd07776 459 ANSAALGAALRAAHGLLCAGSGDFSPEFVVFSAeepklVAEPDPEAAEVYDKL 511
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
58-204 |
4.05e-13 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 71.29 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 58 IHQVSAGIDPEDIEgiafssamhsLILLDSQKQPLTRVITWADNRA----AQDAAELKSqplgDRLYHLTGTPIHPMSPL 133
Cdd:PRK10640 54 IRIDSIGIDTWGVD----------YVLLDKQGQRVGLPVSYRDSRTdgvmAQAQQQLGK----RDIYRRSGIQFLPFNTL 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654308591 134 VKLHWLAHHSPELLAQTCHVVGIKEYLIYKMTGQLQMDYSMANATGLFNLYNFDWEPVALDYAHITRTQLP 204
Cdd:PRK10640 120 YQLRALTEQQPELIAQVAHALLIPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGAPKAWFG 190
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
8-242 |
1.22e-11 |
|
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: 66.51 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 8 DLGTTSTKSVLYDHQGHVIASANV--------GYPlyhdtvttaEEDPQEIWQAVQATIHQVSAGidpEDIEGIAFSSam 79
Cdd:cd07772 6 DIGKTNKKLLLFDENGEVLAERSTpnpeieedGYP---------CEDVEAIWEWLLDSLAELAKR---HRIDAINFTT-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 80 H--SLILLDSQKQPLTRVItwaDNRAAQDAAELKS--QPLGDRLyhLTGTPIHPMSpL---VKLHWLAHHSPELLAQTCH 152
Cdd:cd07772 72 HgaTFALLDENGELALPVY---DYEKPIPDEINEAyyAERGPFE--ETGSPPLPGG-LnlgKQLYWLKREKPELFARAKT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 153 VVGIKEYLIYKMTGQLQMDY-SMANATGLfnlynfdWEPVALDYAHITRTQ-----LPPLVDTDAVIDGLTPVAASTLGL 226
Cdd:cd07772 146 ILPLPQYWAWRLTGKAASEItSLGCHTDL-------WDFEKNEYSSLVKKEgwdklFPPLRKAWEVLGPLRPDLARRTGL 218
|
250
....*....|....*.
gi 654308591 227 APTTKIIMGASDGALS 242
Cdd:cd07772 219 PKDIPVGCGIHDSNAA 234
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
4-433 |
1.16e-08 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466797 [Multi-domain] Cd Length: 544 Bit Score: 57.41 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 4 LIGTDLGTTSTKSVLYDHQGHVIASANVGYPLYHDT-----VTtaeEDPQEIWQAVQATIHQVSAGIDPEDIEGIAFsSA 78
Cdd:cd07778 2 GIGIDVGSTSVRIGIFDYHGTLLATSERPISYKQDPkdlwfVT---QSSTEIWKAIKTALKELIEELSDYIVSGIGV-SA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 79 MHSLILL--------------DSQKQPLTR-VITWADNRAAQDAAELKSQPLGDRLYHLTGTPIHPMSpLVKLHWLAHHS 143
Cdd:cd07778 78 TCSMVVMqrdsdtsylvpynvIHEKSNPDQdIIFWMDHRASEETQWLNNILPDDILDYLGGGFIPEMA-IPKLKYLIDLI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 144 PELLAQTCHVVGIKEYLIYKMTGQ--------LQMDYS--MANATGL--FNLYNFDWEPVALDYAHITRTQL--PPLVDT 209
Cdd:cd07778 157 KEDTFKKLEVFDLHDWISYMLATNlghsnivpVNAPPSigIGIDGSLkgWSKDFYSKLKISTKVCNVGNTFKeaPPLPYA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 210 DAVIDGLTPVAASTLGLAPTTKIIMGASD---GALSNLGVGADEPGVAAITIGTSGAVRVMTKQPYLDPegrlfcyyvap 286
Cdd:cd07778 237 GIPIGKVNVILASYLGIDKSTVVGHGCIDcyaGWFSTFAAAKTLDTTLFMVAGTSTCFLYATSSSQVGP----------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 287 hhwIVG--GPINN---------GGQ-----VFrwvrDELFTT-----ESQTARANQQDPYDQ-----LTALAATVPVGAH 340
Cdd:cd07778 306 ---IPGiwGPFDQllknysvyeGGQsatgkLI----EKLFNShpaiiELLKSDANFFETVEEkidkyERLLGQSIHYLTR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 341 GLLFHPYLSGERAPLWNADARGSLLGVTTTTTKADIAR---AVLEGIVMNL-NTVLQLTAAAEPVHAIRATGGFARSNLW 416
Cdd:cd07778 379 HMFFYGDYLGNRTPYNDPNMSGSFIGESTDSSLTDLVLkyiLILEFLAFQTkLIIDNFQKEKIIIQKVVISGSQAKNARL 458
|
490
....*....|....*...
gi 654308591 417 RQILTDVLGQP-ITIPAS 433
Cdd:cd07778 459 LQLLSTVLSKIhIIVPLS 476
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-128 |
8.65e-07 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 50.67 E-value: 8.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654308591 1 MTYLIGTDLGTTSTKSVLYDHQGHVIASANVGYPlyhdtvttAEEDPQEIWQAVQATIHQV--SAGIDPEDIEGIAFSSA 78
Cdd:COG1940 4 AGYVIGIDIGGTKIKAALVDLDGEVLARERIPTP--------AGAGPEAVLEAIAELIEELlaEAGISRGRILGIGIGVP 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 654308591 79 MhsliLLDSQkqplTRVITWADNRAAqdaaeLKSQPLGDRLYHLTGTPIH 128
Cdd:COG1940 76 G----PVDPE----TGVVLNAPNLPG-----WRGVPLAELLEERLGLPVF 112
|
|
| BcrAD_BadFG |
pfam01869 |
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ... |
5-75 |
9.70e-04 |
|
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are two subunits of Benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also includes an activase subunit from the enzyme 2-hydroxyglutaryl-CoA dehydratase. The protein Swiss:O66634 contains two copies of this region suggesting that the family may structurally dimerize. This family appears to be related to pfam00370.
Pssm-ID: 396441 [Multi-domain] Cd Length: 271 Bit Score: 41.19 E-value: 9.70e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654308591 5 IGTDLGTTSTKSVLYDHQGHVIASANVGYPLYHDTVTTAEEDPQEiwQAVQATIHQvsAGIDPEDIEGIAF 75
Cdd:pfam01869 1 LGIDGGSTKTKAVLMDDDGEVLGRAIAGSANFESVGVEAAERNLK--DAITEALEE--AGLKLDDIEYMFL 67
|
|
| ASKHA_NBD_BcrAD_BadFG_HgdC_HadI |
cd24036 |
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and ... |
5-73 |
2.83e-03 |
|
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and HgdC/HadI family includes BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins which are subunits of benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also contains some dehydratase activators, such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). Uncharacterized proteins, such as Escherichia coli protein YjiL and Methanocaldococcus jannaschii protein MJ0800, are also included in this family.
Pssm-ID: 466886 [Multi-domain] Cd Length: 250 Bit Score: 39.45 E-value: 2.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654308591 5 IGTDLGTTSTKSVLYDHQGHVIASANVgyPLYHDTVTTAEEDPQEIWQAvqatihqvsAGIDPEDIEGI 73
Cdd:cd24036 2 AGIDVGSTTTKAVILDDKGKILGKAVI--RTGTDPEKTAERALEEALEE---------AGLSREDIEYI 59
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
3-78 |
5.98e-03 |
|
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and similar proteins; The family includes Fusobacterium nucleatum N-acetylmannosamine kinase (NanK; EC 2.7.1.60) and beta-glucoside kinase (BglK; EC 2.7.1.85) from Klebsiella pneumoniae and Listeria innocua. NanK catalyzes the second step of the sialic acid catabolic pathway, transferring a phosphate group from adenosine 5'-triphosphate to the C6 position of N-acetylmannosamine to generate N-acetylmannosamine 6-phosphate. Unlike other NanK enzymes and ROK family members, F. nucleatum NanK does not have a conserved zinc-binding site. BglK catalyzes the ATP-dependent phosphorylation of cellobiose to produce cellobiose-6'-P. It may have a dual role of kinase and transcriptional regulator of the cellobiose-PTS operon. The subfamily belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Members of this subfamily lack the cysteine-rich zinc-binding motif, which presents in other ROK families.
Pssm-ID: 466918 [Multi-domain] Cd Length: 294 Bit Score: 38.69 E-value: 5.98e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654308591 3 YLIGTDLGTTSTKSVLYDHQGHViasanvgypLYHDTVTT-AEEDPQEIWQAVQATIHQVSAGIdpeDIEGIAFSSA 78
Cdd:cd24068 1 KILGIDIGGTKIKYGLVDADGEI---------LEKDSVPTpASKGGDAILERLLEIIAELKEKY---DIEGIGISSA 65
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
2-78 |
6.42e-03 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 38.71 E-value: 6.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654308591 2 TYLIGTDLGTTSTKSVLYDHQGHVIASANVGyPLYHDTVttaeeDPQEIWQAVQATIHQVSAGI-DPEDIEGIAFSSA 78
Cdd:COG2971 1 PYILGVDGGGTKTRAVLVDADGEVLGRGRAG-GANPQSV-----GLEEALASLREALEEALAAAgDPADIEAVGFGLA 72
|
|
| |
