|
Name |
Accession |
Description |
Interval |
E-value |
| gntK_FGGY |
TIGR01314 |
gluconate kinase, FGGY type; Gluconate is derived from glucose in two steps. This model ... |
3-508 |
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: 893.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 3 YMIGVDIGTTSTKSVLYDEKGQFIMKHNIGYPLHTPNVEVSEENPDELFDAVLMTIKYIMREADIaKEDLKLISFSAQMH 82
Cdd:TIGR01314 1 YMIGVDIGTTSTKAVLFEENGKIVAKSSIGYPLYTPASGMAEENPEEIFEAVLVTIREVSINLED-EDEILFVSFSTQMH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 83 SLIAMDASHQRLTENLTWADNRASRYAEAIKTKHNGDAIYQRTGTPIHPMSPLSKIFWMKHEQQEIFNQTATFADIKTYI 162
Cdd:TIGR01314 80 SLIAFDENWQPLTRLITWADNRAVKYAEQIKESKNGFDIYRRTGTPIHPMAPLSKIIWLEAEHPDIYQKAAKYLEIKGYI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 163 FYQLFETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHILKGMKRRYAALMGIDENTPVVVGASDGV 242
Cdd:TIGR01314 160 FQRLFGTYKIDYSTASATGMFNLFELDWDKEALELTGIKESQLPKLVPTTEIEENLPHEYAKKMGIQSSTPFVIGASDGV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 243 LSNLGVNAFKKGEVAVTIGTSGAIRTVIDKPRTDYKGRIFCYVLTEDHYVIGGPVNNGGVVLRWLRDELLASEVETAKRL 322
Cdd:TIGR01314 240 LSNLGVNAIKKGEAAVTIGTSGAIRTVIDKPKTDEKGRIFCYALTKEHWVIGGPVNNGGDVLRWARDEIFDSEIETATRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 323 GVDSYDVLTKIANNVKPGADGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIEVMN 402
Cdd:TIGR01314 320 GIDPYDVLTEIAARVSPGADGLLFHPYLAGERAPLWNANARGSFFGLTYSHKKEHMIRAALEGVIYNLYTVALALVEVMG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 403 ETPKTIKATGGFAKSEVWRQMMADIFDTDLIVPESYESSCLGACVLGMKALGEIDDFSIIEDMVGTTNKHHPNEDNVRTY 482
Cdd:TIGR01314 400 DPLNMIQATGGFASSEVWRQMMSDIFEQEIVVPESYESSCLGACILGLKALGLIEDFSEVSTMVGTTETHTPIEKNFEIY 479
|
490 500
....*....|....*....|....*.
gi 499621649 483 QQLISIFINLSRSLEARYTEIAAFQR 508
Cdd:TIGR01314 480 REISPIFINLSRSLLAEYEQIADFQR 505
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
3-492 |
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: 697.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 3 YMIGVDIGTTSTKSVLYDEKGQFIMKHNIGYPLHTPNVEVSEENPDELFDAVLMTIKYIMreADIAKEDLKLISFSAQMH 82
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVL--AKLGGGEVDAIGFSSAMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 83 SLIAMDASHQRLTENLTWADNRASRYAEAIKTKHNGDAIYQRTGTPIHPMSPLSKIFWMKHEQQEIFNQTATFADIKTYI 162
Cdd:cd07770 79 SLLGVDEDGEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAAKFVSIKEYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 163 FYQLFETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHILKGMKRRYAALMGIDENTPVVVGASDGV 242
Cdd:cd07770 159 LYRLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAERLGLLAGTPVVLGASDGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 243 LSNLGVNAFKKGEVAVTIGTSGAIRTVIDKPRTDYKGRIFCYVLTEDHYVIGGPVNNGGVVLRWLRDELlasevetakRL 322
Cdd:cd07770 239 LANLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPGRLWCYRLDENRWLVGGAINNGGNVLDWLRDTL---------LL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 323 GVDSYDVLTKIANNVKPGADGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIEVMN 402
Cdd:cd07770 310 SGDDYEELDKLAEAVPPGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEALEELAG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 403 EtPKTIKATGGFAKSEVWRQMMADIFDTDLIVPESYESSCLGACVLGMKALGEIDDFSiIEDMVGTTNKHHPNEDNVRTY 482
Cdd:cd07770 390 P-VKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSLE-ADELVKIGKVVEPDPENHAIY 467
|
490
....*....|
gi 499621649 483 QQLISIFINL 492
Cdd:cd07770 468 AELYERFKKL 477
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
2-500 |
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: 576.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 2 KYMIGVDIGTTSTKSVLYDEKGQFIMKHNIGYPLHTPNVEVSEENPDELFDAVLMTIKYIMREADIAKEDLKLISFSAQM 81
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 82 HSLIAMDASHQRLTENLTWADNRASRYAEAIKTKHNGDAIYQRTGTPIHPMSPLSKIFWMKHEQQEIFNQTATFADIKTY 161
Cdd:COG1070 81 HGLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAKVLLPKDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 162 IFYQLFETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHILKGMKRRYAALMGIDENTPVVVGASDG 241
Cdd:COG1070 161 LRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAAETGLPAGTPVVAGAGDN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 242 VLSNLGVNAFKKGEVAVTIGTSGAIRTVIDKPRTDYKGRI--FCYVLtEDHYVIGGPVNNGGVVLRWLRDELLASEveta 319
Cdd:COG1070 241 AAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVhtFCHAV-PGRWLPMGATNNGGSALRWFRDLFADGE---- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 320 krlgVDSYDVLTKIANNVKPGADGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIE 399
Cdd:COG1070 316 ----LDDYEELNALAAEVPPGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEALEE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 400 vMNETPKTIKATGGFAKSEVWRQMMADIFDTDLIVPESYESSCLGACVLGMKALGEIDDF-SIIEDMVGTTNKHHPNEDN 478
Cdd:COG1070 392 -AGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLeEAAAAMVRVGETIEPDPEN 470
|
490 500
....*....|....*....|..
gi 499621649 479 VRTYQQLISIFINLSRSLEARY 500
Cdd:COG1070 471 VAAYDELYERYRELYPALKPLF 492
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
3-493 |
1.24e-155 |
|
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: 451.99 E-value: 1.24e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 3 YMIGVDIGTTSTKSVLYDEKGQFIMKHNIGYPLHTPNVEVSEENPDELFDAVLMTIKYIMREADIAKEDLKLISFSAQMH 82
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 83 SLIAMDASHQRLTENLTWADNRASRYAEAIKTKHnGDAIYQRTGTPIHPMSPLSKIFWMKHEQQEIFNQTATFADIKTYI 162
Cdd:cd07808 81 GLVLLDKNGRPLRPAILWNDQRSAAECEELEARL-GDEILIITGNPPLPGFTLPKLLWLKENEPEIFARIRKILLPKDYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 163 FYQLFETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHILKGMKRRYAALMGIDENTPVVVGASDGV 242
Cdd:cd07808 160 RYRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAAEELGLPEGTPVVAGAGDNA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 243 LSNLGVNAFKKGEVAVTIGTSGAIRTVIDKPRTDYKGRI--FCYVLTEDHYVIGGpVNNGGVVLRWLRDELLASEvetak 320
Cdd:cd07808 240 AAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLhtFPHAVPGKWYAMGV-TLSAGLSLRWLRDLFGPDR----- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 321 rlgvDSYDVLTKIANNVKPGADGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIEv 400
Cdd:cd07808 314 ----ESFDELDAEAAKVPPGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVLKE- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 401 MNETPKTIKATGGFAKSEVWRQMMADIFDTDLIVPESYESSCLGACVLGMKALGEIDDF-SIIEDMVGTTNKHHPNEDNV 479
Cdd:cd07808 389 LGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLeEAAAACIKIEKTIEPDPERH 468
|
490
....*....|....
gi 499621649 480 RTYQQLISIFINLS 493
Cdd:cd07808 469 EAYDELYARYRELY 482
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
3-489 |
1.67e-155 |
|
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: 451.97 E-value: 1.67e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 3 YMIGVDIGTTSTKSVLYDEKGQFIMKHNIGYPLHTPNVEVSEENPDELFDAVLMTIKYIMREADIAKEDLKLISFSAQMH 82
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 83 SLIAMDASHQRLTENLTWADNRASRYAEAIKTKHNGDAIYQR-TGTPIHPMSPLSKIFWMKHEQQEIFNQTATFADIKTY 161
Cdd:cd07805 81 GVVPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLgGGNPPSGKDPLAKILWLKENEPEIYAKTHKFLDAKDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 162 IFYQLFETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHILKGMKRRYAALMGIDENTPVVVGASDG 241
Cdd:cd07805 161 LNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAAAELGLPAGTPVVGGGGDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 242 VLSNLGVNAFKKGEVAVTIGTSGAIRTVIDKPRTDYKGRIFCYV-LTEDHYVIGGPVNNGGVVLRWLRDELLASEvetak 320
Cdd:cd07805 241 AAAALGAGAVEEGDAHIYLGTSGWVAAHVPKPKTDPDHGIFTLAsADPGRYLLAAEQETAGGALEWARDNLGGDE----- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 321 RLGVDSYDVLTKIANNVKPGADGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVyLALIEV 400
Cdd:cd07805 316 DLGADDYELLDELAAEAPPGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWL-LEALEK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 401 MNETPKTIKATGGFAKSEVWRQMMADIFDTDLIVPE-SYESSCLGACVLGMKALGEIDDFSIIEDMVGTTNKHHPNEDNV 479
Cdd:cd07805 395 LTRKIDELRLVGGGARSDLWCQILADVLGRPVEVPEnPQEAGALGAALLAAVGLGLLKSFDEAKALVKVEKVFEPDPENR 474
|
490
....*....|
gi 499621649 480 RTYQQLISIF 489
Cdd:cd07805 475 ARYDRLYEVF 484
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
3-449 |
1.33e-130 |
|
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: 384.99 E-value: 1.33e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 3 YMIGVDIGTTSTKSVLYDEKGQFIMKHNIGYPLHTPNVEVSEENPDELFDAVLMTIKYIMREADIAKEDLKLISFSAQMH 82
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 83 SLIAMDASHQRLTENLTWADNRAsryaeaiktkhngdaiyqrtgtpihpmsplskifwmkheqqeifnqtaTFADIKTYI 162
Cdd:cd00366 81 GVVLVDADGNPLRPAIIWLDRRA------------------------------------------------KFLQPNDYI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 163 FYQLFETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHILKGMKRRYAALMGIDENTPVVVGASDGV 242
Cdd:cd00366 113 VFRLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGGDTA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 243 LSNLGVNAFKKGEVAVTIGTSGAIRTVIDKPRtDYKGRIFC-YVLTEDHYVIGGPVNNGGVVLRWLRDELLASEVETAKR 321
Cdd:cd00366 193 AAALGAGVVEPGDAVDSTGTSSVLSVCTDEPV-PPDPRLLNrCHVVPGLWLLEGAINTGGASLRWFRDEFGEEEDSDAEY 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 322 LGvdsydvLTKIANNVKPGADGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTvYLALIEVM 401
Cdd:cd00366 272 EG------LDELAAEVPPGSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRD-NLEILEEL 344
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 499621649 402 NETPKTIKATGGFAKSEVWRQMMADIFDTDLIVPESYESSCLGACVLG 449
Cdd:cd00366 345 GVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
3-482 |
2.24e-129 |
|
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: 383.41 E-value: 2.24e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 3 YMIGVDIGTTSTKSVLYDEKGQFIMKHNIGYPLHTPNVEVSEENPDELFDAVLMTIKYIMREADIAKEDLKLISFSAQMH 82
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 83 SLIAMDASHQRLTENLTWADNRasryaeaiktkhngdaiyqrtgtpihpmsplskifwmkheqqeifnqTATFADIKTYI 162
Cdd:cd07779 81 TFVPVDEDGRPLRPAISWQDKR-----------------------------------------------TAKFLTVQDYL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 163 FYQLFETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHILKGMKRRYAALMGIDENTPVVVGASDGV 242
Cdd:cd07779 114 LYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAAEETGLPEGTPVVAGGGDQQ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 243 LSNLGVNAFKKGEVAVTIGTSGAIRTVIDKPRTDYKGRIFCYV-LTEDHYVIGGPVNNGGVVLRWLRDELLASEVEtAKR 321
Cdd:cd07779 194 CAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPsAVPGKWVLEGSINTGGSAVRWFRDEFGQDEVA-EKE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 322 LGVDSYDVLTKIANNVKPGADGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTvYLALIEVM 401
Cdd:cd07779 273 LGVSPYELLNEEAAKSPPGSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELRD-NLEAMEKA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 402 NETPKTIKATGGFAKSEVWRQMMADIFDTDLIVPESYESSCLGACVLGMKALGEIDDF-SIIEDMVGTTNKHHPNEDNVR 480
Cdd:cd07779 352 GVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFeEAVKAMVRVTDTFEPDPENVA 431
|
..
gi 499621649 481 TY 482
Cdd:cd07779 432 IY 433
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
3-454 |
6.44e-127 |
|
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: 377.64 E-value: 6.44e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 3 YMIGVDIGTTSTKSVLYDEKGQFIMKHNIGYPLHTPNVEVSEENPDELFDAVLMTIKYIMREADIAKEDLKLISFSAQMH 82
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 83 SLIAMDASHQRLTENLTWADNRASRYAEAIKTKHNGDAIYQRTGTPIHPMSPLSKIFWMKHEQQEIFNQTATFADIKTYI 162
Cdd:cd07804 81 ALVPVDENGKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRKFLGAYDYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 163 FYQLFETFVIDQSMASST-GMLNLESLEWDKEALSLLGITESQLPEIVPTTHILKGMKRRYAALMGIDENTPVVVGASDG 241
Cdd:cd07804 161 VYKLTGEYVIDYSSAGNEgGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEAAEETGLAEGTPVVAGTVDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 242 VLSNLGVNAFKKGEVAVTIGTSGAIRTVIDKPRTDykGRIF-CYVLTEDHYVIGGPVNNGGVVLRWLRDELLASEVETAK 320
Cdd:cd07804 241 AASALSAGVVEPGDLLLMLGTAGDIGVVTDKLPTD--PRLWlDYHDIPGTYVLNGGMATSGSLLRWFRDEFAGEEVEAEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 321 RLGVDSYDVLTKIANNVKPGADGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVylalIEV 400
Cdd:cd07804 319 SGGDSAYDLLDEEAEKIPPGSDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYGLRHH----LEV 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 499621649 401 MNE---TPKTIKATGGFAKSEVWRQMMADIFDTDLIVPESYESSCLGACVLGMKALG 454
Cdd:cd07804 395 IREaglPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
3-454 |
2.44e-122 |
|
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: 365.76 E-value: 2.44e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 3 YMIGVDIGTTSTKSVLYDEKGQFIMKHNIGYPLHTPNVEVSEENPDELFDAVLMTIKYIMREAdiAKEDLKLISFSAQMH 82
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQA--GPDPIAAISVSSQGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 83 SLIAMDASHQRLTENLTWADNRASRYAEAIKTKHNGDAIYQRTGTPIHPMSPLSKIFWMKHEQQEIFNQTATFADIKTYI 162
Cdd:cd07773 79 SGVPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAKWLSVADYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 163 FYQLFETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHILKGMKRRYAALMGIDENTPVVVGASDGV 242
Cdd:cd07773 159 AYRLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEELGLPAGTPVVVGGHDHL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 243 LSNLGVNAFKKGEVAVTIGTSGAIRTVIDKPRTD----YKGRIFCYVLTEDHYVIGGPVnNGGVVLRWLRDELLASEvet 318
Cdd:cd07773 239 CAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLDemlaEGGLSYGHHVPGGYYYLAGSL-PGGALLEWFRDLFGGDE--- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 319 akrlgvDSYDVLTKIANNVKPGADGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVyLALI 398
Cdd:cd07773 315 ------SDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLN-LEAL 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 499621649 399 EVMNETPKTIKATGGFAKSEVWRQMMADIFDTDLIVPESYESSCLGACVLGMKALG 454
Cdd:cd07773 388 EKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| XylB |
TIGR01312 |
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ... |
5-489 |
7.20e-109 |
|
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: 332.36 E-value: 7.20e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 5 IGVDIGTTSTKSVLYDEKGQFIMKHNIGYPLHTPNVEVSEENPDELFDAVLMTIKYIMREADIAKEDLKLISFSAQMHSL 84
Cdd:TIGR01312 1 LGIDLGTSGVKALLVDEQGEVIASGSAPHTVISPHPGWSEQDPEDWWDATEEAIKELLEQASEMGQDIKGIGISGQMHGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 85 IAMDASHQRLTENLTWADNRASRYAEAIKTKHNGDAIYQRTGTPIHPMSPLSKIFWMKHEQQEIFNQTATFADIKTYIFY 164
Cdd:TIGR01312 81 VLLDANGEVLRPAILWNDTRTAQECEELEAELGDERVLEITGNLALPGFTAPKLLWVRKHEPEVFARIAKVMLPKDYLRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 165 QLFETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHILKGMKRRYAALMGIDENTPVVVGASDGVLS 244
Cdd:TIGR01312 161 RLTGEYVTEYSDASGTGWFDVAKRAWSKELLDALDLPESQLPELIESSEKAGTVRPEVAARLGLSAGVPVAAGGGDNAAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 245 NLGVNAFKKGEVAVTIGTSGAIRTVIDKPRTDYKGRI--FCYVLTEDHYVIGgPVNNGGVVLRWLRDELLASEVETakrl 322
Cdd:TIGR01312 241 AIGTGTVDPGDAMMSLGTSGVVYAVTDKPLPDPAGAVhgFCHALPGGWLPMG-VTLSATSSLEWFRELFGKEDVEA---- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 323 gvdsydvLTKIANNVKPGADGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIEVMN 402
Cdd:TIGR01312 316 -------LNELAEQSPPGAEGVTFLPYLNGERTPHLDPQARGSFIGLTHNTTRADLTRAVLEGVTFALRDSLDILREAGG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 403 ETPKTIKATGGFAKSEVWRQMMADIFDTDLIVPESYESSCLGACVLGMKALGEIDDFSIIEDMV-GTTNKHHPNEDNVRT 481
Cdd:TIGR01312 389 IPIQSIRLIGGGAKSPAWRQMLADIFGTPVDVPEGEEGPALGAAILAAWALGEKDLAALCSEAVvKQTESVLPIAENVEA 468
|
....*...
gi 499621649 482 YQQLISIF 489
Cdd:TIGR01312 469 YEELYERY 476
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
3-454 |
1.90e-104 |
|
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: 319.88 E-value: 1.90e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 3 YMIGVDIGTTSTKSVLYDEKGQFIMKHNIGYPLHTPNVEVSEENPDELFDAVLMTIKYIMREADIAKEDLKLISFSAQMH 82
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 83 SLIAMDASHQRLTENLTWADNRASRYAEAIKTKHNGDAIYQRTGTPIHPMSPLSKIFWMKHEQQEIFNQTATFADIKTYI 162
Cdd:cd07802 81 GLYLVDKDGKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRIRTVLFCKDWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 163 FYQLFETFVIDQSMAsSTGMLNLESLEWDKEALSLLGITE--SQLPEIVPTTHILKGMKRRYAALMGIDENTPVVVGASD 240
Cdd:cd07802 161 RYRLTGEISTDYTDA-GSSLLDLDTGEYDDELLDLLGIEElkDKLPPLVPSTEIAGRVTAEAAALTGLPEGTPVAAGAFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 241 GVLSNLGVNAFKKGEVAVTIGTSGAIRTVIDKPRTDYKGRIFCYVLTEDHYVIGGPVNNGGVVLRWLRDELLASEvetaK 320
Cdd:cd07802 240 VVASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDSVGSNSLHADPGLYLIVEASPTSASNLDWFLDTLLGEE----K 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 321 RLGVDSYDVLTKIANNVKPGADGLIFHPYLAGERAplwNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIEv 400
Cdd:cd07802 316 EAGGSDYDELDELIAAVPPGSSGVIFLPYLYGSGA---NPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLV- 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 499621649 401 mNETPKTIKATGGFAKSEVWRQMMADIFDTDLIVPESYESSCLGACVLGMKALG 454
Cdd:cd07802 392 -ARKPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
5-453 |
5.71e-93 |
|
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: 289.89 E-value: 5.71e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 5 IGVDIGTTSTKSVLYDEKGQFIMKHNIGYPLHTPNVEVSEENPDELFDAVLMTIKYIMREADIAkeDLKLISFSAQMHSL 84
Cdd:cd07783 3 LGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPR--RVVAIAVDGTSGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 85 IAMDASHQRLTENLTWADNRASRYAEAIKTKhnGDAIYQRTGTPIHPMSPLSKIFWMKHEQQEIFNQTATFADIKTYIFY 164
Cdd:cd07783 81 VLVDREGEPLRPAIMYNDARAVAEAEELAEA--AGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFLHQADWLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 165 QLFETFVI-DQSMASSTGmLNLESLEWDKEALSLLGITESQLPEIVPTTHILKGMKRRYAALMGIDENTPVVVGASDGVL 243
Cdd:cd07783 159 RLTGDRGVtDYNNALKLG-YDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLPAGTPVVAGTTDSIA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 244 SNLGVNAFKKGEVAVTIGTSGAIRTVIDKPRTDYKGRIFCYVLTEDHYVIGGPVNNGGVVLRWLrdellasevetakrLG 323
Cdd:cd07783 238 AFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGVYSHRHGDGYWLVGGASNTGGAVLRWF--------------FS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 324 VDSYDVLTKIANnvKPGADGLIFHPY-LAGERAPLWNADARGSFfgLTLSHKKEHMIRAALEGVLYNLYTVYLALIEVMN 402
Cdd:cd07783 304 DDELAELSAQAD--PPGPSGLIYYPLpLRGERFPFWDPDARGFL--LPRPHDRAEFLRALLEGIAFIERLGYERLEELGA 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 499621649 403 ETPKTIKATGGFAKSEVWRQMMADIFDTDLIVPESyESSCLGACVLGMKAL 453
Cdd:cd07783 380 PPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEE-EEAALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
3-448 |
1.27e-88 |
|
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: 279.05 E-value: 1.27e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 3 YMIGVDIGTTSTKSVLYD-EKGQFIMKHNIGYPLHTPNVEVSEENPDELFDAVLMTIKYIMREADIAKEDLKLISFSAQM 81
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 82 HSLIAMDASHQRLTENLTWADNRASRYAEAIkTKHNGDAIYQRTGTPIHPMSPLSKIFWMKHEQQEIFNQTATF---ADi 158
Cdd:cd07809 81 HGLVALDADGKVLRPAKLWCDTRTAPEAEEL-TEALGGKKCLLVGLNIPARFTASKLLWLKENEPEHYARIAKIllpHD- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 159 ktYIFYQLFETFVIDQSMASSTGMLNLESLEWDKEALSLLGIT---ESQLPEIVPTTHILKGMKRRYAALMGIDENTPVV 235
Cdd:cd07809 159 --YLNWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAIDPSrdlRDLLPEVLPAGEVAGRLTPEGAEELGLPAGIPVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 236 VGASDGVLSNLGVNAFKKGEVAVTIGTSGAIRTVIDKPRTDYKGRI--FCYVLteDHYViggPVNNG-GVVLRWlrdell 312
Cdd:cd07809 237 PGEGDNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSDPHGRVatFCDST--GGML---PLINTtNCLTAW------ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 313 aseVETAKRLGVDSYDVLTKIANNVKPGADGLIFHPYLAGERAPLWnADARGSFFGLTLS-HKKEHMIRAALEGVLYNLY 391
Cdd:cd07809 306 ---TELFRELLGVSYEELDELAAQAPPGAGGLLLLPFLNGERTPNL-PHGRASLVGLTLSnFTRANLARAALEGATFGLR 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 499621649 392 tvY-LALIEVMNETPKTIKATGGFAKSEVWRQMMADIFDTDLIVPESYESSCLGACVL 448
Cdd:cd07809 382 --YgLDILRELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQ 437
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
3-454 |
2.92e-84 |
|
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: 267.95 E-value: 2.92e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 3 YMIGVDIGTTSTKSVLYDEKGQFIMKHNIGYPLHTPNVEVSEENPDELFDAVLMTIKYIMREADIAKEDLKLISFSAQMH 82
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 83 SLIAMDASHQRLTENLTWADNRASRYAEAIKTKHNGDAIYQRTGTPIHPMSPLSKIFWMKHEQQEIFNQTATFADIKTYI 162
Cdd:cd24121 81 GTWLVDEDGRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKENEPERLERARTALHCKDWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 163 FYQLFETFVIDQSMASSTgMLNLESLEWDKEALSLLGITESQ--LPEIVPTTHILKGMKRRYAALMGIDENTPVVVGASD 240
Cdd:cd24121 161 FYKLTGEIATDPSDASLT-FLDFRTRQYDDEVLDLLGLEELRhlLPPIRPGTEVIGPLTPEAAAATGLPAGTPVVLGPFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 241 GVLSNLGVNAFKKGEVAVTIGTSGAIRTVIDKPRTDYK--GRIFCYVLtEDHYVIGGPVNNGGVVLRWLRDELLASEVET 318
Cdd:cd24121 240 VVATALGSGAIEPGDACSILGTTGVHEVVVDEPDLEPEgvGYTICLGV-PGRWLRAMANMAGTPNLDWFLRELGEVLKEG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 319 AKRLGVDSYDVLTKIANNVKPGADGLIFHPYL--AGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYla 396
Cdd:cd24121 319 AEPAGSDLFQDLEELAASSPPGAEGVLYHPYLspAGERAPFVNPNARAQFTGLSLEHTRADLLRAVYEGVALAMRDCY-- 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 499621649 397 liEVMNETPKTIKATGGFAKSEVWRQMMADIFDTDLIVPESYESSCLGACVLGMKALG 454
Cdd:cd24121 397 --EHMGEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
3-497 |
6.38e-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: 260.93 E-value: 6.38e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 3 YMIGVDIGTTSTKSVLYD-EKGQFIMKHNIGYPLH--TPNVEVSEENPDELFDAVLMTIKYIMREADIAKEDLKLISFSA 79
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGyiPPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 80 QMHSLIAMDASHQRLTENLTWADNRASRYAEAI-KTKHNGDAIY-QRTGTPIHPMSPLSKIFWMKHEQQEIFNQTATFAD 157
Cdd:cd07781 81 TSSTVVPVDEDGNPLAPAILWMDHRAQEEAAEInETAHPALEYYlAYYGGVYSSEWMWPKALWLKRNAPEVYDAAYTIVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 158 IKTYIFYQLFETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPE-----IVPTTHILKGMKRRYAALMGIDENT 232
Cdd:cd07781 161 ACDWINARLTGRWVRSRCAAGHKWMYNEWGGGPPREFLAALDPGLLKLREklpgeVVPVGEPAGTLTAEAAERLGLPAGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 233 PVVVGASDGVLSNLGVNAFKKGEVAVTIGTSGAIRTVIDKPrTDYKGriFCYV----LTEDHYVI-GGPVNNGGVvLRWL 307
Cdd:cd07781 241 PVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTCHLMVSPKP-VDIPG--ICGPvpdaVVPGLYGLeAGQSAVGDI-FAWF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 308 RDELlaseVETAKRLGVDSYDVLTKIANNVKPGADGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVL 387
Cdd:cd07781 317 VRLF----VPPAEERGDSIYALLSEEAAKLPPGESGLVALDWFNGNRTPLVDPRLRGAIVGLTLGTTPAHIYRALLEATA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 388 YNLytvyLALIEVMNE---TPKTIKATGGFA-KSEVWRQMMADIFDTDLIVPESYESSCLGACVLGMKALGEIDDF-SII 462
Cdd:cd07781 393 FGT----RAIIERFEEagvPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVAAGVYADIeEAA 468
|
490 500 510
....*....|....*....|....*....|....*
gi 499621649 463 EDMVGTTNKHHPNEDNVRTYQQLISIFINLSRSLE 497
Cdd:cd07781 469 DAMVRVDRVYEPDPENHAVYEELYALYKELYDALG 503
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
3-247 |
3.17e-79 |
|
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.
Pssm-ID: 395295 [Multi-domain] Cd Length: 245 Bit Score: 248.02 E-value: 3.17e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 3 YMIGVDIGTTSTKSVLYDEKGQFIMKHNIGYPLHTPNVEVSEENPDELFDAVLMTIKYIMREADIAKEDLKLISFSAQMH 82
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 83 SLIAMDASHQRLTENLTWADNRASRYAEAIKTKHNGDAIYQRTGTPIHPMSPLSKIFWMKHEQQEIFNQTATFADIKTYI 162
Cdd:pfam00370 81 GTVLLDKNDKPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIHDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 163 FYQLFETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHILKGMKRRYAALMGIDENTPVVVGASDGV 242
Cdd:pfam00370 161 RWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGGDQQ 240
|
....*
gi 499621649 243 LSNLG 247
Cdd:pfam00370 241 AAAFG 245
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
3-454 |
1.09e-76 |
|
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: 248.29 E-value: 1.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 3 YMIGVDIGTTSTKSVLYDEKGQ--FIMKHNIGYplHTPNVE--VSEENPDELFDAVLMTIKYIMREADIAKEDLKLISFS 78
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKivAIAYREWEY--YTDDDYpdAKEFDPEELWEKICEAIREALKKAGISPEDISAVSST 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 79 AQMHSLIAMDASHQRL--TENLtwaDNRASRYAEAIKTKHnGDAIYQRTGTPIHPMSPLSKIFWMKHEQQEIFNQTATFA 156
Cdd:cd07798 79 SQREGIVFLDKDGRELyaGPNI---DARGVEEAAEIDDEF-GEEIYTTTGHWPTELFPAARLLWFKENRPEIFERIATVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 157 DIKTYIFYQLFETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHILKGMKRRYAALMGIDENTPVVV 236
Cdd:cd07798 155 SISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAARELGLPEGTPVVV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 237 GASDGVLSNLGVNAFKKGEVAVTIGTSGAIRTVIDKPRTDYKGRIF--CYVLtEDHYVI---GGPVnngGVVLRWLRDEL 311
Cdd:cd07798 235 GGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWtgCHLV-PGKWVLesnAGVT---GLNYQWLKELL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 312 LASevetakrlGVDSYDVLTKIANNVKPGADGLI--FHPYLAGERAplwNADARGSFFGLTLSH----KKEHMIRAALEG 385
Cdd:cd07798 311 YGD--------PEDSYEVLEEEASEIPPGANGVLafLGPQIFDARL---SGLKNGGFLFPTPLSaselTRGDFARAILEN 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499621649 386 VLYNLYTVYLALIEVMNETPKTIKATGGFAKSEVWRQMMADIFDTDLIVPESYESSCLGACVLGMKALG 454
Cdd:cd07798 380 IAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
3-465 |
3.26e-68 |
|
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: 226.96 E-value: 3.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 3 YMIGVDIGTTSTKSVLYDEKGQFIMKHNIGYPLHTPNVEVSEENPDELFDAVLMTIKYIMREADIAKEDLKLISFSAQMH 82
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 83 SLIAMDASHQR-LTENLTWADNRASRYAEAIKTKHNGDAIYQRTGTPIHPMSPLSKIFWM----KHEQQEIFNQTATFAD 157
Cdd:cd07769 81 TTVVWDKKTGKpLYNAIVWQDRRTADICEELKAKGLEERIREKTGLPLDPYFSATKIKWIldnvPGARERAERGELLFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 158 IKTYIFYQL--FETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHILkGMKRRYAALMGIdentPV- 234
Cdd:cd07769 161 IDTWLIWKLtgGKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVF-GYTDPEGLGAGI----PIa 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 235 -VVGASDGVLsnLGVNAFKKGEVAVTIGT-------SGairtviDKPRTDYKGRI--FCYVLTED-HYVIGGPVNNGGVV 303
Cdd:cd07769 236 gILGDQQAAL--FGQGCFEPGMAKNTYGTgcfllmnTG------EKPVPSKNGLLttIAWQIGGKvTYALEGSIFIAGAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 304 LRWLRDELL----ASEVEtakrlgvdsydvltKIANNVkPGADGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMI 379
Cdd:cd07769 308 IQWLRDNLGliedAAETE--------------ELARSV-EDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 380 RAALEGVLYNLYTVYLALIEVMNETPKTIKATGGFAKSEVWRQMMADIFDTDLIVPESYESSCLGACVLGMKALGEIDDF 459
Cdd:cd07769 373 RAALESIAYQTRDVLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDL 452
|
....*.
gi 499621649 460 SIIEDM 465
Cdd:cd07769 453 DELASL 458
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
1-478 |
6.14e-63 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 213.68 E-value: 6.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 1 MKYMIGVDIGTTSTKSVLYDEKGQFIMKHNIGYPLHTPNVEVSEENPDELFDAVLMTIKYIMR--EADIAKEDLKLISFS 78
Cdd:PTZ00294 1 MKYIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKklREKGPSFKIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 79 AQMHSLIAMDASHQRLTEN-LTWADNRASRYAEAIKTKHNGDAIYQ-RTGTPIHPMSPLSKIFWM----KHEQQEIFNQT 152
Cdd:PTZ00294 81 NQRETVVAWDKVTGKPLYNaIVWLDTRTYDIVNELTKKYGGSNFFQkITGLPISTYFSAFKIRWMlenvPAVKDAVKEGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 153 ATFADIKTYIFYQLFE--TFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHILKGMKRRYAALMgidE 230
Cdd:PTZ00294 161 LLFGTIDTWLIWNLTGgkSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTISGEAVPLL---E 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 231 NTPVVVGASDGVLSNLGVNAFKKGEVAVTIGTSGAIRTVI-DKPRTDYKGRI--FCYVLTEDH---YVIGGPVNNGGVVL 304
Cdd:PTZ00294 238 GVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTgTEIVFSKHGLLttVCYQLGPNGptvYALEGSIAVAGAGV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 305 RWLRDELlasevetakrlG-VDSYDVLTKIANNVKpGADGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAAL 383
Cdd:PTZ00294 318 EWLRDNM-----------GlISHPSEIEKLARSVK-DTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAAL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 384 EGVLYNLYTVYLALIEVMNETPKTIKATGGFAKSEVWRQMMADIFDTDLIVPESYESSCLGACV---LGMKALGEIDDFS 460
Cdd:PTZ00294 386 EAIALQTNDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALlagLAVGVWKSLEEVK 465
|
490
....*....|....*...
gi 499621649 461 IIEDMVGTTNKHHPNEDN 478
Cdd:PTZ00294 466 KLIRRSNSTFSPQMSAEE 483
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
3-487 |
5.10e-60 |
|
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: 205.64 E-value: 5.10e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 3 YMIGVDIGTTSTKSVLYDEKGQFIMKHNIGYpLHT--PNVEVS-----EENPDELFDavlmTIKYIMREADIAKEDLKLI 75
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREW-RHKevPDVPGSmdfdtEKNWKLICE----CIREALKKAGIAPKSIAAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 76 SFSAQMHSLIAMDASHQRLtenltWA----DNRASRYAEAIKTKHNG--DAIYQRTG-TPihPMSPLSKIFWMKHEQQEI 148
Cdd:cd07775 76 STTSMREGIVLYDNEGEEI-----WAcanvDARAAEEVSELKELYNTleEEVYRISGqTF--ALGAIPRLLWLKNNRPEI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 149 FNQTATFADIKTYIFYQLFETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHILKGMKRRYAALMGI 228
Cdd:cd07775 149 YRKAAKITMLSDWIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEAAEETGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 229 DENTPVVVGASDGVLSNLGVNAFKKGEVAVTIGTSGAIRTVIDKPRTDYKG--RIFCYVLtEDHYVIGGPVNNGGVVLRW 306
Cdd:cd07775 229 KEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMniRVNCHVI-PDMWQAEGISFFPGLVMRW 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 307 LRDELLASEVETAKRLGVDSYDVLTKIANNVKPGADGL--IF----------HPylagerAPlwnadargSFFGLTLSHK 374
Cdd:cd07775 308 FRDAFCAEEKEIAERLGIDAYDLLEEMAKDVPPGSYGImpIFsdvmnyknwrHA------AP--------SFLNLDIDPE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 375 KehmiraalegvlYNLYTVYLALIE----VMNETPKTIKA-----------TGGFAKSEVWRQMMADIFDTDLIVPESYE 439
Cdd:cd07775 374 K------------CNKATFFRAIMEnaaiVSAGNLERIAEfsgifpdslvfAGGASKGKLWCQILADVLGLPVKVPVVKE 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 499621649 440 SSCLGACVLGMKALGEIDDF-SIIEDMVGTTNKHHPNEDNVRTYQQLIS 487
Cdd:cd07775 442 ATALGAAIAAGVGAGIYSSLeEAVESLVKWEREYLPNPENHEVYQDLYE 490
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
1-454 |
2.33e-58 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 201.06 E-value: 2.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 1 MKYMIGVDIGTTSTKSVLYDEKGQFIMKHNIGYPLHTPN---VEvseENPDELFDAVLMTIKYIMREADIAKEDLKLISF 77
Cdd:COG0554 2 KKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQpgwVE---HDPEEIWESVLAVIREALAKAGISAEDIAAIGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 78 SAQMHSLIAMDashqRLT----EN-LTWADNRASRYAEAIKTKHNGDAIYQRTGTPIHPMSPLSKIFWM---------KH 143
Cdd:COG0554 79 TNQRETTVVWD----RKTgkplYNaIVWQDRRTADICEELKADGLEDLIREKTGLVLDPYFSATKIKWIldnvpgareRA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 144 EQQEIFnqtatFADIKTYIFYQLfeT----FVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHILkGMK 219
Cdd:COG0554 155 EAGELL-----FGTIDSWLIWKL--TggkvHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVF-GET 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 220 RRYAALMGIdentPVVvgasdGVL----SNL-GVNAFKKGEVAVTIGTSGAIRTVI-DKPRTDYKGrifcyVLT------ 287
Cdd:COG0554 227 DPDLFGAEI----PIA-----GIAgdqqAALfGQACFEPGMAKNTYGTGCFLLMNTgDEPVRSKNG-----LLTtiawgl 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 288 --EDHYVIGGPVNNGGVVLRWLRDEL----LASEVETakrlgvdsydvltkIANNVKPgADGLIFHPYLAGERAPLWNAD 361
Cdd:COG0554 293 ggKVTYALEGSIFVAGAAVQWLRDGLglidSAAESEA--------------LARSVED-NGGVYFVPAFTGLGAPYWDPD 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 362 ARGSFFGLTLSHKKEHMIRAALEGVLYNLYtvylALIEVMNE----TPKTIKATGGFAKSEVWRQMMADIFDTDLIVPES 437
Cdd:COG0554 358 ARGAIFGLTRGTTRAHIARAALESIAYQTR----DVLDAMEAdsgiPLKELRVDGGASANDLLMQFQADILGVPVERPKV 433
|
490
....*....|....*..
gi 499621649 438 YESSCLGACVLGMKALG 454
Cdd:COG0554 434 TETTALGAAYLAGLAVG 450
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
3-480 |
1.99e-54 |
|
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: 190.85 E-value: 1.99e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 3 YMIGVDIGTTSTKSVLYDEK----GQFIMKHNIGYPlhTPNVevSEENPDELFDAVLMTIKYIMREADIAKEDLKLISFS 78
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKgkiiGSSSEKVEVLYP--EPGW--VEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 79 AQMHSLIAMDA-SHQRLTENLTWADNRASRYAEAI---------------------KTKHNGDAIYQRTgtPIHPMSPLS 136
Cdd:cd07793 77 TQRNTFLTWDKkTGKPLHNFITWQDLRAAELCESWnrslllkalrggskflhfltrNKRFLAASVLKFS--TAHVSIRLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 137 KIFwMKHE--QQEIFNQTATFADIKTYIFYQL--FETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPT- 211
Cdd:cd07793 155 WIL-QNNPelKEAAEKGELLFGTIDTWLLWKLtgGKVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 212 ---THILKGmkrryaalmGIDENTPVVVGASDGVLSNLGVNAFKKGEVAVTIGTSgairTVID-----KPRTDYKGrifC 283
Cdd:cd07793 234 gdfGSTDPS---------IFGAEIPITAVVADQQAALFGECCFDKGDVKITMGTG----TFIDintgsKPHASVKG---L 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 284 YVLT------EDHYVIGGPVNNGGVVLRWLRDELLasevetakrlgVDSYDVLTKIANNVkPGADGLIFHPYLAGERAPL 357
Cdd:cd07793 298 YPLVgwkiggEITYLAEGNASDTGTVIDWAKSIGL-----------FDDPSETEDIAESV-EDTNGVYFVPAFSGLQAPY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 358 WNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIEVMNETPKTIKATGGFAKSEVWRQMMADIFDTDLIVPES 437
Cdd:cd07793 366 NDPTACAGFIGLTPSTTKAHLVRAILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKN 445
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 499621649 438 YESSCLGACVLGMKALGEIDDFSIIEDMVGTTNKHHPNEDNVR 480
Cdd:cd07793 446 TEMSALGAAFLAGLASGIWKSKEELKKLRKIEKIFEPKMDNEK 488
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
3-452 |
5.85e-53 |
|
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: 186.54 E-value: 5.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 3 YMIGVDIGTTSTKSVLYDEKGQFIMKHNIGYPLHTPN---VEvseENPDELFDAVLMTIKYIMREADIAKEDLKLISFSA 79
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKpgwVE---HDPEEIWESQLAVAREALAKAGIRASDIAAIGITN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 80 QMHSLIAMD-ASHQRLTENLTWADNRASRYAEAIKTKHNGDAIYQRTGTPIHPMSPLSKIFWM---------KHEQQEIF 149
Cdd:cd07786 78 QRETTVVWDrETGKPVYNAIVWQDRRTADICEELKAEGHEEMIREKTGLVLDPYFSATKIRWIldnvpgareRAERGELA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 150 nqtatFADIKTYIFYQLF--ETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHILkGMKRRYAALMG 227
Cdd:cd07786 158 -----FGTIDSWLIWKLTggKVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVF-GYTDPDLLGAE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 228 IdentPV--VVGASDGVLsnLGVNAFKKGEVAVTIGTSGAIRTVI-DKPRTDYKGrifcyVLT--------EDHYVIGGP 296
Cdd:cd07786 232 I----PIagIAGDQQAAL--FGQACFEPGMAKNTYGTGCFMLMNTgEKPVRSKNG-----LLTtiawqlggKVTYALEGS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 297 VNNGGVVLRWLRDELL----ASEVETakrlgvdsydvltkIANNVkPGADGLIFHPYLAGERAPLWNADARGSFFGLTLS 372
Cdd:cd07786 301 IFIAGAAVQWLRDGLGliesAAETEA--------------LARSV-PDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 373 HKKEHMIRAALEGVLYNLYTVYLALIEVMNETPKTIKATGGFAKSEVWRQMMADIFDTDLIVPESYESSCLGACVL-GMK 451
Cdd:cd07786 366 TTRAHIARAALESIAYQTRDLLEAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLaGLA 445
|
.
gi 499621649 452 A 452
Cdd:cd07786 446 V 446
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
5-446 |
6.95e-53 |
|
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: 185.12 E-value: 6.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 5 IGVDIGTTSTKSVLYD-EKGQFI--MKHNIGYPLHTPNVEVSEENPDELFDAVLMTIKYIMREADiakEDLKLISFSAQM 81
Cdd:cd07777 3 LGIDIGTTSIKAALLDlESGRILesVSRPTPAPISSDDPGRSEQDPEKILEAVRNLIDELPREYL---SDVTGIGITGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 82 HSLIAMDASHQRLTENLTWADNRASRyAEAIKTKHNGDAIYQRTGTPIHPMSPLSKIFWMKHeQQEIFNQTATFADIKTY 161
Cdd:cd07777 80 HGIVLWDEDGNPVSPLITWQDQRCSE-EFLGGLSTYGEELLPKSGMRLKPGYGLATLFWLLR-NGPLPSKADRAGTIGDY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 162 IFYQL--FETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHILkGMKRRyaalmGIDENTPVVVGAS 239
Cdd:cd07777 158 IVARLtgLPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIV-GTLSS-----ALPKGIPVYVALG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 240 DGVLSNLGVNAFKKGEVAVTIGTSGAIRTVIDKPRTDYKGRIFCYVltEDHYVIGGPVNNGGVVLRWLRDELlaseVETA 319
Cdd:cd07777 232 DNQASVLGSGLNEENDAVLNIGTGAQLSFLTPKFELSGSVEIRPFF--DGRYLLVAASLPGGRALAVLVDFL----REWL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 320 KRLGVDS-----YDVLTKIANNvkPGADGLIFHPYLAGERaplWNADARGSFFGLTLSH-KKEHMIRAALEGVLYNLYTV 393
Cdd:cd07777 306 RELGGSLsddeiWEKLDELAES--EESSDLSVDPTFFGER---HDPEGRGSITNIGESNfTLGNLFRALCRGIAENLHEM 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 499621649 394 YLALIEVMNEtPKTIKATGGFA-KSEVWRQMMADIFDTDLIVPESYESSCLGAC 446
Cdd:cd07777 381 LPRLDLDLSG-IERIVGSGGALrKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAA 433
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
7-462 |
3.33e-52 |
|
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: 184.65 E-value: 3.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 7 VDIGTTSTKSVLYDEKGQFIMKHNIGYPLHTPNVEVSEENPDELFDAVLMTIKYI---MREADIAKEDLKLISFSAQMHS 83
Cdd:cd07792 6 IDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAvekLKALGISPSDIKAIGITNQRET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 84 LIAMDASH-QRLTENLTWADNRASRYAEAIKTKHNG--DAIYQRTGTPIHPMSPLSKIFWM----KHEQQEIFNQTATFA 156
Cdd:cd07792 86 TVVWDKSTgKPLYNAIVWLDTRTSDTVEELSAKTPGgkDHFRKKTGLPISTYFSAVKLRWLldnvPEVKKAVDDGRLLFG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 157 DIKTYIFYQL-----FETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHILKGMKRryAALMGIden 231
Cdd:cd07792 166 TVDSWLIWNLtggknGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIAS--GPLAGV--- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 232 tPVVvgasdGVL-----SNLGVNAFKKGEVAVTIGT----------------SGAIRTVidkprtdykgrifCYVLTED- 289
Cdd:cd07792 241 -PIS-----GCLgdqqaALVGQGCFKPGEAKNTYGTgcfllyntgeepvfskHGLLTTV-------------AYKLGPDa 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 290 --HYVIGGPVNNGGVVLRWLRDELL----ASEVETakrlgvdsydvltkIANNVkPGADGLIFHPYLAGERAPLWNADAR 363
Cdd:cd07792 302 ppVYALEGSIAIAGAAVQWLRDNLGiissASEVET--------------LAASV-PDTGGVYFVPAFSGLFAPYWRPDAR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 364 GSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIEVMNETPKTIKATGGFAKSEVWRQMMADIFDTDLIVPESYESSCL 443
Cdd:cd07792 367 GTIVGLTQFTTKAHIARAALEAVCFQTREILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTAL 446
|
490 500
....*....|....*....|..
gi 499621649 444 GACV---LGMKALGEIDDFSII 462
Cdd:cd07792 447 GAAIaagLAVGVWKSLDELKSL 468
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
5-496 |
1.21e-51 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 182.86 E-value: 1.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 5 IGVDIGTTSTKSVLYDEKGQFIMKHNIGYPLHTPNVEVSEENPDELFDAVLMTIKYIMREADIakEDLKLISFSAQMHSL 84
Cdd:PRK15027 3 IGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSL--QDVKALGIAGQMHGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 85 IAMDASHQRLTENLTWADNRASRYAEAIKTKhnGDAIYQRTGTPIHPMSPLSKIFWMKHEQQEIFNQTATFADIKTYIFY 164
Cdd:PRK15027 81 TLLDAQQRVLRPAILWNDGRCAQECALLEAR--VPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 165 QLFETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHILKGMKRRYAALMGIdENTPVVVGASDGVLS 244
Cdd:PRK15027 159 RMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAKAWGM-ATVPVVAGGGDNAAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 245 NLGVNAFKKGEVAVTIGTSGAIRTVID----KPRTDYKGriFCYVLTEdhyviggpvnnggvvlRW-LRDELL--ASEVE 317
Cdd:PRK15027 238 AVGVGMVDANQAMLSLGTSGVYFAVSEgflsKPESAVHS--FCHALPQ----------------RWhLMSVMLsaASCLD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 318 TAKRL-GVDSYDVLTKIANNVKPGADGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTvYLA 396
Cdd:PRK15027 300 WAAKLtGLSNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALAD-GMD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 397 LIEVMNETPKTIKATGGFAKSEVWRQMMADIFDTDLivpeSYESS-----CLGACVLGMKALGEIDDFSIIEDMVGTTNK 471
Cdd:PRK15027 379 VVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQL----DYRTGgdvgpALGAARLAQIAANPEKSLIELLPQLPLEQS 454
|
490 500
....*....|....*....|....*
gi 499621649 472 HHPNEDNVRTYQQLISIFINLSRSL 496
Cdd:PRK15027 455 HLPDAQRYAAYQPRRETFRRLYQQL 479
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
2-448 |
1.32e-45 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 166.54 E-value: 1.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 2 KYMIGVDIGTTSTKSVLYDEKGQFIMKHNIGYPLHTPNVEVSEENPDELFDAVLMTIKYIMREADIAKEDLKLISFSAQM 81
Cdd:PRK00047 5 KYILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGITNQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 82 HSLIAMDASHQRLTEN-LTWADNRASRYAEAIKTKHNGDAIYQRTGTPIHPMSPLSKIFWM---------KHEQQEifnq 151
Cdd:PRK00047 85 ETTVVWDKETGRPIYNaIVWQDRRTADICEELKRDGYEDYIREKTGLVIDPYFSGTKIKWIldnvegareRAEKGE---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 152 tATFADIKTYIFYQLF--ETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHIlkgmkrrYA---ALM 226
Cdd:PRK00047 161 -LLFGTIDTWLVWKLTggKVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEV-------YGktnPYG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 227 GIDENTPVVVGASDGVLSNLGVNAFKKGEVAVTIGT-------SGairtviDKPRTDYKGrifcyVLTEDHYVIGGPVN- 298
Cdd:PRK00047 233 FFGGEVPIAGIAGDQQAALFGQLCFEPGMAKNTYGTgcfmlmnTG------EKAVKSENG-----LLTTIAWGIDGKVVy 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 299 -------NGGVVLRWLRDELL----ASEVETAKRLgVDSydvltkiannvkpgADGLIFHPYLAGERAPLWNADARGSFF 367
Cdd:PRK00047 302 alegsifVAGSAIQWLRDGLKiisdASDSEALARK-VED--------------NDGVYVVPAFTGLGAPYWDSDARGAIF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 368 GLTLSHKKEHMIRAALEGVLYNLYTVYLALIEVMNETPKTIKATGGFAKSEVWRQMMADIFDTDLIVPESYESSCLGACV 447
Cdd:PRK00047 367 GLTRGTTKEHIIRATLESIAYQTRDVLDAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAY 446
|
.
gi 499621649 448 L 448
Cdd:PRK00047 447 L 447
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
1-485 |
5.03e-44 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 162.87 E-value: 5.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 1 MKYMIGVDIGTTSTKSVLYDEKGQFIM------KHnigypLHTPNVEVSEEnpdelFDA------VLMTIKYIMREADIA 68
Cdd:PRK10939 2 MSYLMALDAGTGSIRAVIFDLNGNQIAvgqaewRH-----LAVPDVPGSME-----FDLeknwqlACQCIRQALQKAGIP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 69 KEDLKLISFSAQMHSLIAMDASHQRLtenltWA----DNRASRYAEAIKTKHNG--DAIYQRTGTPIhPMSPLSKIFWMK 142
Cdd:PRK10939 72 ASDIAAVSATSMREGIVLYDRNGTEI-----WAcanvDARASREVSELKELHNNfeEEVYRCSGQTL-ALGALPRLLWLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 143 HEQQEIFNQTATFADIKTYIFYQLFETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHILKGMKRRY 222
Cdd:PRK10939 146 HHRPDIYRQAHTITMISDWIAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAKA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 223 AALMGIDENTPVVVGASDGVLSNLGVNAFKKGEVAVTIGTSGAIRTVIDKPRTDYKG--RIFCYVLTedhyviggPVNNG 300
Cdd:PRK10939 226 AAETGLRAGTPVVMGGGDVQLGCLGLGVVRPGQTAVLGGTFWQQVVNLPAPVTDPNMniRINPHVIP--------GMVQA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 301 -------GVVLRWLRDELLASEVETAKRLGVDSYDVLTKIANNVKPGADGLI------------FHPylagerAPlwnad 361
Cdd:PRK10939 298 esisfftGLTMRWFRDAFCAEEKLLAERLGIDAYSLLEEMASRVPVGSHGIIpifsdvmrfkswYHA------AP----- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 362 argSFFGLTL----SHKKEhMIRAALEgvlyNLYTVY---LALIEVM-NETPKTIKATGGFAKSEVWRQMMADIFDTDLI 433
Cdd:PRK10939 367 ---SFINLSIdpekCNKAT-LFRALEE----NAAIVSacnLQQIAAFsGVFPSSLVFAGGGSKGKLWSQILADVTGLPVK 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 499621649 434 VPESYESSCLGACVLGMKALGEIDDFS-IIEDMVGTTNKHHPNEDNVRTYQQL 485
Cdd:PRK10939 439 VPVVKEATALGCAIAAGVGAGIYSSLAeTGERLVRWERTFEPNPENHELYQEA 491
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
7-469 |
2.29e-41 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 155.24 E-value: 2.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 7 VDIGTTSTKSVLYDEKGQFIMKHNIGYPLHTPNVEVSEENPDELFDAVLMTIKYIMREADIAKED----LKLISFSAQMH 82
Cdd:PLN02295 5 IDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGHNvdsgLKAIGITNQRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 83 SLIAMDASHQRLTEN-LTWADNRASRYAEAIKTKHNGD--AIYQRTGTPIHPMSPLSKIFWMKHE----QQEIFNQTATF 155
Cdd:PLN02295 85 TTVAWSKSTGRPLYNaIVWMDSRTSSICRRLEKELSGGrkHFVETCGLPISTYFSATKLLWLLENvdavKEAVKSGDALF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 156 ADIKTYIFYQL-----FETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHILKgmkrryaalmGIDE 230
Cdd:PLN02295 165 GTIDSWLIWNLtggasGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIG----------TIAK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 231 NTPVVVGASDGVLSN-----LGvNAFKKGEVAVTIGTsGA--IRTVIDKPRTDYKGRI--FCYVLTED---HYVIGGPVN 298
Cdd:PLN02295 235 GWPLAGVPIAGCLGDqhaamLG-QRCRPGEAKSTYGT-GCfiLLNTGEEVVPSKHGLLttVAYKLGPDaptNYALEGSVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 299 NGGVVLRWLRDEL----LASEVETakrlgvdsydvltkIANNVkPGADGLIFHPYLAGERAPLWNADARGSFFGLTLSHK 374
Cdd:PLN02295 313 IAGAAVQWLRDNLgiikSASEIEA--------------LAATV-DDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTN 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 375 KEHMIRAALEGVLYNLYTVYLALI-----EVMNETPKTIKATGGFAKSEVWRQMMADIFDTDLIVPESYESSCLGACV-- 447
Cdd:PLN02295 378 KAHIARAVLESMCFQVKDVLDAMRkdageEKSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYaa 457
|
490 500
....*....|....*....|...
gi 499621649 448 -LGMKALGEIDDFSIIEDMVGTT 469
Cdd:PLN02295 458 gLAVGLWTEEEIFASEKWKNTTT 480
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
256-453 |
1.03e-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: 128.98 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 256 VAVTIGTSGAIRTVIDKPRTDYKGRI--FCYVLTEDHYVIGGPVNNGGVVLRWLRDELLASEVETAKRlGVDSYDVLTKI 333
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSVHGVWgpYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRDAG-NVESLAELAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 334 AnnVKPGADGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIEVMNETPKTIKATGG 413
Cdd:pfam02782 80 A--AVAPAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSGG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499621649 414 FAKSEVWRQMMADIFDTDLIVPESYESSCLGACVLGMKAL 453
Cdd:pfam02782 158 GSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVAA 197
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
3-489 |
1.10e-28 |
|
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: 119.27 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 3 YMIGVDIGTTSTKSVLYD-EKGQFIMKHNIGY-PLHTPNVEVSEENPDELFDAVLMTIKYIMREADIAKEDLKLISFSAQ 80
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDlYAGLEMAQEPVPYyQDSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 81 MhSLIAMDASHQRLTENLT---------WADNRASRYAEAIK-TKHNgdAIYQRTGTPIHPMSPLSKIFWMKHEQQEIFN 150
Cdd:cd07768 81 C-SLAIFDREGTPLMALIPypnednvifWMDHSAVNEAQWINmQCPQ--QLLDYLGGKISPEMGVPKLKYFLDEYSHLRD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 151 QTATFADIKTYIFYQLfeTFVIDQSMASSTGMLNLESLE--WDKEALSLLGI------TESQLPEIVPTTHILKGMKRRY 222
Cdd:cd07768 158 KHFHIFDLHDYIAYEL--TRLYEWNICGLLGKENLDGEEsgWSSSFFKNIDPrlehltTTKNLPSNVPIGTTSGVALPEM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 223 AALMGIDENTPVVVGASDGVLSNLGV-NAFKKGEVAVTIGTSGAirtvidkprtdykgriFCYVLTEDHYVIG--GPVNN 299
Cdd:cd07768 236 AEKMGLHPGTAVVVSCIDAHASWFAVaSPHLETSLFMIAGTSSC----------------HMYGTTISDRIPGvwGPFDT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 300 G---------------GVVLRWL-RDELLASEVETAKRLGVDSYDVLTKIANNVKP---GADGLIFHPYLAGERAPLWNA 360
Cdd:cd07768 300 IidpdysvyeagqsatGKLIEHLfESHPCARKFDEALKKGADIYQVLEQTIRQIEKnngLSIHILTLDMFFGNRSEFADP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 361 DARGSFFGLTLS---HKKEHMIRAALEGVLYNLYtvylALIEVMNETP---KTIKATGGFAKSEVWRQMMADIFDTDLIV 434
Cdd:cd07768 380 RLKGSFIGESLDtsmLNLTYKYIAILEALAFGTR----LIIDTFQNEGihiKELRASGGQAKNERLLQLIALVTNVAIIK 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499621649 435 PESYESSCLGACVLGMKALGEIDDFSIIE------DMVGTTNKHHPNE---DNVRTYQQLISIF 489
Cdd:cd07768 456 PKENMMGILGAAVLAKVAAGKKQLADSITeadisnDRKSETFEPLAYRlgaDYILLYKLLCVKY 519
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
3-482 |
1.29e-28 |
|
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: 119.18 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 3 YMIGVDIGTTSTKSVLYDEKGQFIMKHNIGYPLHTPNVEVSEENPDELFDAVLMTIKYIMREADIAKEDLKLISFSAQMh 82
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFDATC- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 83 SLIAMDASHQRLTENLT---------WADNRASRYAEAI-KTKHNgdaIYQRTGTPIHPMSPLSKIFWMKHEQQEIFNQT 152
Cdd:cd07782 80 SLVVLDAEGKPVSVSPSgddernvilWMDHRAVEEAERInATGHE---VLKYVGGKISPEMEPPKLLWLKENLPETWAKA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 153 ATF---ADIKTYIFyqlfeTFVIDQSMAS----STGMLNLESLE-WDKEALSLLGITE------SQLPEIV--PTTHILK 216
Cdd:cd07782 157 GHFfdlPDFLTWKA-----TGSLTRSLCSlvckWTYLAHEGSEGgWDDDFFKEIGLEDlvednfAKIGSVVlpPGEPVGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 217 GMKRRYAALMGIDENTPV-------------VVGASDGVLSNLGVNAFKKgeVAVTIGTSGAIRTVIDKPRT------DY 277
Cdd:cd07782 232 GLTAEAAKELGLPEGTPVgvslidahagglgTLGADVGGLPCEADPLTRR--LALICGTSSCHMAVSPEPVFvpgvwgPY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 278 KGRIFC-YVLTEdhyviGGPVNNGGvvlrwLRDELLASEV------ETAKRLGVDSYDVLTKI----ANNVKPGADGLI- 345
Cdd:cd07782 310 YSAMLPgLWLNE-----GGQSATGA-----LLDHIIETHPaypelkEEAKAAGKSIYEYLNERleqlAEEKGLPLAYLTr 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 346 ---FHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIraalegVLYnLYTV-YLAL-----IEVMNE---TPKTIKATGG 413
Cdd:cd07782 380 dlhVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLA------LLY-LATLqALAYgtrhiIEAMNAaghKIDTIFMCGG 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499621649 414 FAKSEVWRQMMADIFDTDLIVPESYESSCLGACVLGMKALGEIDdfSIIEDMVGTTNKH---HPNEdNVRTY 482
Cdd:cd07782 453 LSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFP--SLWDAMAAMSGPGkvvEPNE-ELKKY 521
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
3-486 |
1.58e-27 |
|
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: 115.73 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 3 YMIGVDIGTTSTKSVLYDEKGQFIMKHNIGY----P-LHTPNVEVSEENPDELFDAVLMTIKYI------MREADIAKED 71
Cdd:cd07776 1 LYLGLDLSTQSLKAVVIDSDLKVVAEESVNFdsdlPeYGTKGGVHRDGDGGEVTSPVLMWVEALdlllekLKAAGFDFSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 72 LKLISFSAQMH----------SLIAMDASHQRLTENL----------TWADNRASRYAEAIKTKHNG-DAIYQRTGTPIH 130
Cdd:cd07776 81 VKAISGSGQQHgsvywskgaeSALANLDPSKSLAEQLegafsvpdspIWMDSSTTKQCRELEKAVGGpEALAKLTGSRAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 131 PMSPLSKIFWMKHEQQEIFNQTATFAdiktyifyqLFETFV----------IDQSMASSTGMLNLESLEWDKEALSLLGI 200
Cdd:cd07776 161 ERFTGPQIAKIAQTDPEAYENTERIS---------LVSSFLaslllgryapIDESDGSGMNLMDIRSRKWSPELLDAATA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 201 T--ESQLPEIVPTTHILKGMKRRYAALMGIDENTPVVVGASDGVLSNLGVNAfKKGEVAVTIGTSGAIRTVIDKPRTDYK 278
Cdd:cd07776 232 PdlKEKLGELVPSSTVAGGISSYFVERYGFSPDCLVVAFTGDNPASLAGLGL-EPGDVAVSLGTSDTVFLVLDEPKPGPE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 279 GRIFCYVLTEDHYVIGGPVNNGGVVLRWLRDellasevetakRLGVDSYDVLTKIANNVKPGADGLIFHPYLAGE----- 353
Cdd:cd07776 311 GHVFANPVDPGSYMAMLCYKNGSLARERVRD-----------RYAGGSWEKFNELLESTPPGNNGNLGLYFDEPEitppv 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 354 -RAPLWNADARGSFFGLTlshkKEHMIRAALEGVLYNLYtVYLALIEvMNETPKTIKATGGFAKSEVWRQMMADIFDTDL 432
Cdd:cd07776 380 pGGGRRFFGDDGVDAFFD----PAVEVRAVVESQFLSMR-LHAERLG-SDIPPTRILATGGASANKAILQVLADVFGAPV 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 499621649 433 IVPESYESSCLGACVLGMKALGEIDDFSIIEDMVGTTNKH-----HPNEDNVRTYQQLI 486
Cdd:cd07776 454 YTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVVFSAEEpklvaEPDPEAAEVYDKLL 512
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
1-458 |
1.32e-26 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 112.43 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 1 MKYMIGVDIGTTSTKSVLYDEKGQFIMKHnigyplHTPN-VEVSEENPDEL---FDAVLMTIKYIMRE--ADIAKEDLKL 74
Cdd:PRK10331 1 QDVILVLDCGATNVRAIAVDRQGKIVARA------STPNaSDIAAENSDWHqwsLDAILQRFADCCRQinSELTECHIRG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 75 ISFSAQMHSLIAMDASHQRLTENLTWADNRASRYAEAIKTKHNGDAIYQRTGTPIHPMSPLSKIFWMKHEQQEIFNQTAT 154
Cdd:PRK10331 75 ITVTTFGVDGALVDKQGNLLYPIISWKCPRTAAVMENIERYISAQQLQQISGVGAFSFNTLYKLVWLKENHPQLLEQAHA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 155 FADIKTYIFYQLFETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHILKGMKRRYAALMGIDENTPV 234
Cdd:PRK10331 155 WLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPSAAALLGLPVGIPV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 235 VVGASDGVLSNLGVNAfKKGEVAVTIGTSGAIRTVIDKPRTD----YKGrifcyvLTEDHYVIGGPVNNG-----GVVLR 305
Cdd:PRK10331 235 ISAGHDTQFALFGSGA-GQNQPVLSSGTWEILMVRSAQVDTSllsqYAG------STCELDSQSGLYNPGmqwlaSGVLE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 306 WLRDELLASEvetakrlgvDSYDVLTKIANNVKPGADGLIFHPYLAGERaplwnadaRGSFFGLTLSHKKEHMIRAALEG 385
Cdd:PRK10331 308 WVRKLFWTAE---------TPYQTMIEEARAIPPGADGVKMQCDLLACQ--------NAGWQGVTLNTTRGHFYRAALEG 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499621649 386 VLYNLYTVYLALIEVMNETPKTIKATGGFAKSEVWRQMMADIFDTDLIVPESYESSCLGACVLGMKALGEIDD 458
Cdd:PRK10331 371 LTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSS 443
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
1-485 |
1.58e-21 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 97.99 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 1 MKYMIGVDIGTTSTKSVLYD-EKGQFIMKHNIGYPLHT------PNVEVSEENPDELFDAVLMTIKYIMREADIAKEDLK 73
Cdd:PRK04123 2 MAYVIGLDFGTDSVRALLVDcATGEELATAVVEYPHWVkgryldLPPNQALQHPLDYIESLEAAIPAVLKEAGVDPAAVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 74 LISFSAQMHSLIAMDASHQRLTENLTWADN-----------RASRYAEAIKT--KHNGDAIYQR-TGTPIHPMSPLSKIF 139
Cdd:PRK04123 82 GIGVDFTGSTPAPVDADGTPLALLPEFAENphamvklwkdhTAQEEAEEINRlaHERGEADLSRyIGGIYSSEWFWAKIL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 140 WMKHEQQEIFNQTATFADIKTYIFYQLFETFVIDQSMAS--STGMLNLESLEWD----KEALSLL-----GITESQLP-E 207
Cdd:PRK04123 162 HVLREDPAVYEAAASWVEACDWVVALLTGTTDPQDIVRSrcAAGHKALWHESWGglpsADFFDALdpllaRGLRDKLFtE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 208 IVPTTHILKGMKRRYAALMGIDENTPVVVGASDGVLSNLGVNAfKKGEVAVTIGTSGAIRTVIDKPRTdYKGrifcyvlt 287
Cdd:PRK04123 242 TWTAGEPAGTLTAEWAQRLGLPEGVAVSVGAFDAHMGAVGAGA-EPGTLVKVMGTSTCDILLADKQRA-VPG-------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 288 edhyvIGGPVNNG---------------GVVLRWLRDELL-ASEVETAKRLGVDSYDVLTKIANNVKPGADGLIFHPYLA 351
Cdd:PRK04123 312 -----ICGQVDGSivpgligyeagqsavGDIFAWFARLLVpPEYKDEAEARGKQLLELLTEAAAKQPPGEHGLVALDWFN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 352 GERAPLWNADARGSFFGLTLSHKKEHMIRAALEGvlynlyTVY--LALIEVMNET--P-KTIKATGGFA-KSEVWRQMMA 425
Cdd:PRK04123 387 GRRTPLADQRLKGVITGLTLGTDAPDIYRALIEA------TAFgtRAIMECFEDQgvPvEEVIAAGGIArKNPVLMQIYA 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499621649 426 DIFDTDLIVPESYESSCLGACVLGMKALGEIDDfsiIED----M-VGTTNKHHPNEDNVRTYQQL 485
Cdd:PRK04123 461 DVLNRPIQVVASDQCPALGAAIFAAVAAGAYPD---IPEaqqaMaSPVEKTYQPDPENVARYEQL 522
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
102-469 |
4.81e-20 |
|
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: 92.59 E-value: 4.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 102 DNRASRYAEAIKTKHNGDAIYQRTGTPIHPMSPLSKIFWMKHEQQEIFNQTATF---ADIKTYIFyqlfeT--FVIDQSM 176
Cdd:cd07771 98 DPRTEGMMEELFEKISKEELYERTGIQFQPINTLYQLYALKKEGPELLERADKLlmlPDLLNYLL-----TgeKVAEYTI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 177 ASSTGMLNLESLEWDKEALSLLGITESQLPEIVPTTHILkGMKRRYAALMGIDENTPVVVGAS-D---GVLSnlgVNAFK 252
Cdd:cd07771 173 ASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVL-GTLKPEVAEELGLKGIPVIAVAShDtasAVAA---VPAED 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 253 KGEVAVTIGTSGAIRTVIDKPrtdykgrifcyVLTEDHYvIGGPVNNGGV-----VLR-----WLRDELLAsevETAKRL 322
Cdd:cd07771 249 EDAAFISSGTWSLIGVELDEP-----------VITEEAF-EAGFTNEGGAdgtirLLKnitglWLLQECRR---EWEEEG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 323 GVDSYDVLTKIANNVKPgaDGLIFHPylageraplwnADARgsFF----------------GLTLSHKKEHMIRAALEGV 386
Cdd:cd07771 314 KDYSYDELVALAEEAPP--FGAFIDP-----------DDPR--FLnpgdmpeairaycretGQPVPESPGEIARCIYESL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 387 LYNLYTVYLALIEVMNETPKTIKATGGFAKSEVWRQMMADIfdTDLIV---PEsyESSCLGACVLGMKALGEIDDFSIIE 463
Cdd:cd07771 379 ALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADA--TGLPViagPV--EATAIGNLLVQLIALGEIKSLEEGR 454
|
....*.
gi 499621649 464 DMVGTT 469
Cdd:cd07771 455 ELVRNS 460
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
7-448 |
9.82e-10 |
|
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: 60.74 E-value: 9.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 7 VDIGTTSTKSVLYDEKGQFIMKhnigypLHTPNVEVSE-----ENPDELFDAVLMTIKYIMREADIAKedlklISFSAQM 81
Cdd:cd07772 5 FDIGKTNKKLLLFDENGEVLAE------RSTPNPEIEEdgypcEDVEAIWEWLLDSLAELAKRHRIDA-----INFTTHG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 82 HSLIAMDASHQRLT-----ENLTWADNRASRYAEAiktkhnGDaiYQRTGTPIHPMSpLS---KIFWMKHEQQEIFNQTA 153
Cdd:cd07772 74 ATFALLDENGELALpvydyEKPIPDEINEAYYAER------GP--FEETGSPPLPGG-LNlgkQLYWLKREKPELFARAK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 154 TFADIKTYIFYQLFETFVIDQ-SMASSTGMLNLESLEWDKEALsLLGItESQLPEIVPTTHILKGMKRRYAALMGIDENT 232
Cdd:cd07772 145 TILPLPQYWAWRLTGKAASEItSLGCHTDLWDFEKNEYSSLVK-KEGW-DKLFPPLRKAWEVLGPLRPDLARRTGLPKDI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 233 PVVVGASDgvlSNLGV----NAFKKGEVAVTIGT-------SGAIRTVIDKPRTDykgrIFCYVLtedhyVIGGPvnngg 301
Cdd:cd07772 223 PVGCGIHD---SNAALlpylAAGKEPFTLLSTGTwciamnpGNDLPLTELDLARD----CLYNLD-----VFGRP----- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 302 vvlrwlrdellaseVETAKRLGVDSYDVLTKIANNVKPGADGLIFHP-YLAGERAPLWNADARGSFFGLTLSHKKEHMIR 380
Cdd:cd07772 286 --------------VKTARFMGGREYERLVERIAKSFPQLPSLADLAkLLARGTFALPSFAPGGGPFPGSGGRGVLSAFP 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499621649 381 AALEgvLYNLYTVYLAL-----IEVMNETPKTIKATGGFAKSEVWRQMMADIFDTDLIVPESYES-SCLGACVL 448
Cdd:cd07772 352 SAEE--AYALAILYLALmtdyaLDLLGSGVGRIIVEGGFAKNPVFLRLLAALRPDQPVYLSDDSEgTALGAALL 423
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-79 |
1.37e-06 |
|
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: 50.28 E-value: 1.37e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499621649 1 MKYMIGVDIGTTSTKSVLYDEKGQFIMKHNIGYPlhtpnvevSEENPDELFDAVLMTIKYIMREADIAKEDLKLISFSA 79
Cdd:COG1940 4 AGYVIGIDIGGTKIKAALVDLDGEVLARERIPTP--------AGAGPEAVLEAIAELIEELLAEAGISRGRILGIGIGV 74
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
85-206 |
1.47e-06 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 50.49 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 85 IAMDASHQRLTENLTWADNRASRYAEAIKTKHNGDAIYQRTGTPIHPMSPLSKIFWMKHEQQEIFNQTATFADIKTYIFY 164
Cdd:PRK10640 69 VLLDKQGQRVGLPVSYRDSRTDGVMAQAQQQLGKRDIYRRSGIQFLPFNTLYQLRALTEQQPELIAQVAHALLIPDYFSY 148
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 499621649 165 QLFETFVIDQSMASSTGMLNLESLEWDKEALSLLGITESQLP 206
Cdd:PRK10640 149 RLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGAPKAWFG 190
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
5-500 |
7.59e-05 |
|
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: 45.47 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 5 IGVDIGTTSTKSVLYDEKGQFI--MKHNIGYPLHTPNVEVSEENPDELFDAvlmtIKYIMREADIAKED--LKLISFSAQ 80
Cdd:cd07778 3 IGIDVGSTSVRIGIFDYHGTLLatSERPISYKQDPKDLWFVTQSSTEIWKA----IKTALKELIEELSDyiVSGIGVSAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 81 MhSLIAM----DASH----------QRLTENLT-WADNRASRYAEAIKTKHNGDAIYQRTGTPIHPMSpLSKIFWMKHEQ 145
Cdd:cd07778 79 C-SMVVMqrdsDTSYlvpynvihekSNPDQDIIfWMDHRASEETQWLNNILPDDILDYLGGGFIPEMA-IPKLKYLIDLI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 146 QEIFNQTATFADIKTYIFYQLFETFVIDQSMAS----STGMLNLESLE-WDKEALSLLGIteSQLPEIVPTTHILKG--- 217
Cdd:cd07778 157 KEDTFKKLEVFDLHDWISYMLATNLGHSNIVPVnappSIGIGIDGSLKgWSKDFYSKLKI--STKVCNVGNTFKEAPplp 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 218 --------MKRRYAALMGIDENTPVVVGASDGVLSNLGVNAFKK---GEVAVTIGTSGAIRTVIDKPRTDYKGRI---FC 283
Cdd:cd07778 235 yagipigkVNVILASYLGIDKSTVVGHGCIDCYAGWFSTFAAAKtldTTLFMVAGTSTCFLYATSSSQVGPIPGIwgpFD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 284 YVLTEDHYVIGGPVNNGGvvlrwLRDELLASEVETAKRLGVDS------YDVLTKIANNVKPGADGLIFHPYL----AGE 353
Cdd:cd07778 315 QLLKNYSVYEGGQSATGK-----LIEKLFNSHPAIIELLKSDAnffetvEEKIDKYERLLGQSIHYLTRHMFFygdyLGN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 354 RAPLWNADARGSFFGLTLSHKKEHMIraalegVLYNLYTVYLA-----LIEVMNETPKTIKA---TGGFAKSEVWRQMMA 425
Cdd:cd07778 390 RTPYNDPNMSGSFIGESTDSSLTDLV------LKYILILEFLAfqtklIIDNFQKEKIIIQKvviSGSQAKNARLLQLLS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499621649 426 DIFDTDLIV---PESYESSCLGACVLGMKAlgeiddfSIIEDMVGTTNKHHPNEDNVR-----TYQQLISIFINLSRSLE 497
Cdd:cd07778 464 TVLSKIHIIvplSDSKYAVVKGAALLGKAA-------FLHNQSIEERLISLKNEDQISicasaSIVKLVSDETKLAIILR 536
|
...
gi 499621649 498 ARY 500
Cdd:cd07778 537 AKY 539
|
|
| YjiL |
COG1924 |
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ... |
1-75 |
1.28e-03 |
|
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport and metabolism];
Pssm-ID: 441527 [Multi-domain] Cd Length: 264 Bit Score: 40.86 E-value: 1.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499621649 1 MKYMIGVDIGTTSTKSVLYDEKGQFIMKHNIGyplhtpnvevSEENPDElfdAVLMTIKYIMREADIAKEDLKLI 75
Cdd:COG1924 2 GMIYLGIDIGSTTTKAVLLDEDGEILASAYLP----------TGGDPLE---AAKEALKELLEEAGLKREDIAGV 63
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
3-69 |
1.84e-03 |
|
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and similar proteins; This subfamily includes a group of uncharacterized proteins similar to N-acetylglucosamine kinase (Tm1224; EC 2.7.1.59) from Thermotoga maritima, which belongs to kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Tm1224 lacks the cysteine-rich zinc-binding motif, which presents in other family members.
Pssm-ID: 466909 [Multi-domain] Cd Length: 305 Bit Score: 40.26 E-value: 1.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499621649 3 YMIGVDIGTTSTKSVLYDEKGQFIMKHNigYPLHtpnvevSEENPDELFDAVLMTIKYIMREADIAK 69
Cdd:cd24059 2 YVIGVEIGRDLLSAVLCDLSGNILAREK--YPLD------EKENPEEVLEKLYELIDRLLEKENIKS 60
|
|
| ASKHA_NBD_BcrAD_BadFG-like |
cd24002 |
nucleotide-binding domain (NBD) of the BcrAD/BadFG-like ATPase family; The BcrAD/BadFG-like ... |
5-73 |
2.48e-03 |
|
nucleotide-binding domain (NBD) of the BcrAD/BadFG-like ATPase family; The BcrAD/BadFG-like ATPase 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, Methanocaldococcus jannaschii protein MJ0800, and Aquifex aeolicus hypothetical protein O66634, are also includes in this family. The members of the O66634-like group contain two copies of the BcrAD/BadFG-like region suggesting that they may structurally dimerize. The BcrAD/BadFG-like ATPase 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: 466852 [Multi-domain] Cd Length: 255 Bit Score: 39.72 E-value: 2.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499621649 5 IGVDIGTTSTKSVLYDEKGQfimkhnigypLHTPNVEVSEENPDELFDAVLMTIKYIMREADIAKEDLK 73
Cdd:cd24002 2 LGLDIGSTTSKAVLLDEGKN----------IVATEYERSGTGTSGPIEAVKKTLEKFLLEKGVKEEDIA 60
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
5-70 |
2.87e-03 |
|
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family corresponds to a group of proteins including sugar kinases, transcriptional repressors, and yet uncharacterized open reading frames. ROK family sugar kinases phosphorylate a range of structurally distinct hexoses including the key carbon source D-glucose, various glucose epimers, and several acetylated hexosamines. The sugar kinases include N-acetyl-D-glucosamine kinase (NAGK; EC 2.7.1.59), polyphosphate glucokinase (PPGK; EC 2.7.1.63/EC 2.7.1.2), glucokinase (GLK; EC 2.7.1.2), fructokinase (FRK; EC 2.7.1.4), hexokinase (HK; EC 2.7.1.1), D-allose kinase (AlsK; EC 2.7.1.55), bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE; EC 3.2.1.183/EC 2.7.1.60), N-acetylmannosamine kinase (NanK; EC 2.7.1.60), beta-glucoside kinase (BglK; EC 2.7.1.85), and N-acetylglucosamine kinase (EC 2.7.1.59). The family also contains the repressor proteins, such as N-acetylglucosamine repressor (NagC), xylose repressor (XylR), cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and protein Mlc. ROK kinases harbor a conserved N-terminal ATP binding motif of sequence DxGxT, while ROK repressors possess a N-terminal extension that contains a canonical helix-turn-helix DNA binding motif. The ROK family proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466849 [Multi-domain] Cd Length: 239 Bit Score: 39.37 E-value: 2.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499621649 5 IGVDIGTTSTKSVLYDEKGQFIMKHNIGYPlhtpnvevSEENPDELFDAVLMTIKYIMREADIAKE 70
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTP--------AEEGPEAVLDRIAELIEELLAEAGVRER 58
|
|
| BcrAD_BadFG |
pfam01869 |
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ... |
5-77 |
3.78e-03 |
|
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: 39.26 E-value: 3.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499621649 5 IGVDIGTTSTKSVLYDEKGQFIMKhniGYPLHTPNVEVSEENP-DELFDAvlmtIKYIMREADIAKEDLKLISF 77
Cdd:pfam01869 1 LGIDGGSTKTKAVLMDDDGEVLGR---AIAGSANFESVGVEAAeRNLKDA----ITEALEEAGLKLDDIEYMFL 67
|
|
| ASKHA_NBD_BcrAD_BadFG_HgdC_HadI |
cd24036 |
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and ... |
5-75 |
5.23e-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: 38.67 E-value: 5.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499621649 5 IGVDIGTTSTKSVLYDEKGQFIMKHNI--GYplhtpnvevseeNPDELFDAVLmtiKYIMREADIAKEDLKLI 75
Cdd:cd24036 2 AGIDVGSTTTKAVILDDKGKILGKAVIrtGT------------DPEKTAERAL---EEALEEAGLSREDIEYI 59
|
|
| |
