|
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: 995.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 3 YMIGVDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMRESKVNkDDIKFVSFSAQMH 82
Cdd:TIGR01314 1 YMIGVDIGTTSTKAVLFEENGKIVAKSSIGYPLYTPASGMAEENPEEIFEAVLVTIREVSINLEDE-DEILFVSFSTQMH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 83 SLIAMDQQHQRLTNNITWADNRAAKYATVINEVHDGNAIYQRTGTPIHPMSPLAKIFWMKHEWQDVFQRTAKFADIKTYI 162
Cdd:TIGR01314 80 SLIAFDENWQPLTRLITWADNRAVKYAEQIKESKNGFDIYRRTGTPIHPMAPLSKIIWLEAEHPDIYQKAAKYLEIKGYI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 163 FYHLFDTYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTTYVMKGMKERYATLMGLNKDTPFVIGASDGV 242
Cdd:TIGR01314 160 FQRLFGTYKIDYSTASATGMFNLFELDWDKEALELTGIKESQLPKLVPTTEIEENLPHEYAKKMGIQSSTPFVIGASDGV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 243 LSNLGVNSVGKGEVAVTIGTSGAIRTVIDKPRTDYKGRIFCYVLTEDHYVIGGPVNNGGVVLRWLRDELLASEVETAKRL 322
Cdd:TIGR01314 240 LSNLGVNAIKKGEAAVTIGTSGAIRTVIDKPKTDEKGRIFCYALTKEHWVIGGPVNNGGDVLRWARDEIFDSEIETATRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 323 GVDPYDVLTQIAKRVKPGADGLIFHPYLAGERAPLWNANARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIEVMN 402
Cdd:TIGR01314 320 GIDPYDVLTEIAARVSPGADGLLFHPYLAGERAPLWNANARGSFFGLTYSHKKEHMIRAALEGVIYNLYTVALALVEVMG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 403 ETPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYESSCLGACVLGLKAVGDIEDFSIVSSMVGATNNHTPIEENVTVY 482
Cdd:TIGR01314 400 DPLNMIQATGGFASSEVWRQMMSDIFEQEIVVPESYESSCLGACILGLKALGLIEDFSEVSTMVGTTETHTPIEKNFEIY 479
|
490 500
....*....|....*....|....*.
gi 446799407 483 QEIVSIFINLSRSLTENYEQIADFQR 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: 688.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 3 YMIGVDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMreSKVNKDDIKFVSFSAQMH 82
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVL--AKLGGGEVDAIGFSSAMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 83 SLIAMDQQHQRLTNNITWADNRAAKYATVINEVHDGNAIYQRTGTPIHPMSPLAKIFWMKHEWQDVFQRTAKFADIKTYI 162
Cdd:cd07770 79 SLLGVDEDGEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAAKFVSIKEYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 163 FYHLFDTYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTTYVMKGMKERYATLMGLNKDTPFVIGASDGV 242
Cdd:cd07770 159 LYRLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAERLGLLAGTPVVLGASDGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 243 LSNLGVNSVGKGEVAVTIGTSGAIRTVIDKPRTDYKGRIFCYVLTEDHYVIGGPVNNGGVVLRWLRDELlasevetakRL 322
Cdd:cd07770 239 LANLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPGRLWCYRLDENRWLVGGAINNGGNVLDWLRDTL---------LL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 323 GVDPYDVLTQIAKRVKPGADGLIFHPYLAGERAPLWNANARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIEVMN 402
Cdd:cd07770 310 SGDDYEELDKLAEAVPPGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEALEELAG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 403 EtPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYESSCLGACVLGLKAVGDIEDFSiVSSMVGATNNHTPIEENVTVY 482
Cdd:cd07770 390 P-VKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSLE-ADELVKIGKVVEPDPENHAIY 467
|
490
....*....|
gi 446799407 483 QEIVSIFINL 492
Cdd:cd07770 468 AELYERFKKL 477
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
2-502 |
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: 574.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 2 KYMIGVDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMRESKVNKDDIKFVSFSAQM 81
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 82 HSLIAMDQQHQRLTNNITWADNRAAKYATVINEVHDGNAIYQRTGTPIHPMSPLAKIFWMKHEWQDVFQRTAKFADIKTY 161
Cdd:COG1070 81 HGLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAKVLLPKDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 162 IFYHLFDTYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTTYVMKGMKERYATLMGLNKDTPFVIGASDG 241
Cdd:COG1070 161 LRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAAETGLPAGTPVVAGAGDN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 242 VLSNLGVNSVGKGEVAVTIGTSGAIRTVIDKPRTDYKGRI--FCYVLtEDHYVIGGPVNNGGVVLRWLRDELLASEveta 319
Cdd:COG1070 241 AAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVhtFCHAV-PGRWLPMGATNNGGSALRWFRDLFADGE---- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 320 krlgVDPYDVLTQIAKRVKPGADGLIFHPYLAGERAPLWNANARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIE 399
Cdd:COG1070 316 ----LDDYEELNALAAEVPPGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEALEE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 400 vMNETPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYESSCLGACVLGLKAVGDIEDF-SIVSSMVGATNNHTPIEEN 478
Cdd:COG1070 392 -AGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLeEAAAAMVRVGETIEPDPEN 470
|
490 500
....*....|....*....|....
gi 446799407 479 VTVYQEIVSIFINLSRSLTENYEQ 502
Cdd:COG1070 471 VAAYDELYERYRELYPALKPLFER 494
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
3-489 |
7.29e-154 |
|
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: 447.74 E-value: 7.29e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 3 YMIGVDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMRESKVNKDDIKFVSFSAQMH 82
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 83 SLIAMDQQHQRLTNNITWADNRAAKYATVINEVHDGNAIYQR-TGTPIHPMSPLAKIFWMKHEWQDVFQRTAKFADIKTY 161
Cdd:cd07805 81 GVVPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLgGGNPPSGKDPLAKILWLKENEPEIYAKTHKFLDAKDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 162 IFYHLFDTYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTTYVMKGMKERYATLMGLNKDTPFVIGASDG 241
Cdd:cd07805 161 LNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAAAELGLPAGTPVVGGGGDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 242 VLSNLGVNSVGKGEVAVTIGTSGAIRTVIDKPRTDYKGRIFCYV-LTEDHYVIGGPVNNGGVVLRWLRDELLASEvetak 320
Cdd:cd07805 241 AAAALGAGAVEEGDAHIYLGTSGWVAAHVPKPKTDPDHGIFTLAsADPGRYLLAAEQETAGGALEWARDNLGGDE----- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 321 RLGVDPYDVLTQIAKRVKPGADGLIFHPYLAGERAPLWNANARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVyLALIEV 400
Cdd:cd07805 316 DLGADDYELLDELAAEAPPGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWL-LEALEK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 401 MNETPKMIKATGGFAKSEVWRQMMSDIFDTELVVPE-SYESSCLGACVLGLKAVGDIEDFSIVSSMVGATNNHTPIEENV 479
Cdd:cd07805 395 LTRKIDELRLVGGGARSDLWCQILADVLGRPVEVPEnPQEAGALGAALLAAVGLGLLKSFDEAKALVKVEKVFEPDPENR 474
|
490
....*....|
gi 446799407 480 TVYQEIVSIF 489
Cdd:cd07805 475 ARYDRLYEVF 484
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
3-493 |
3.10e-150 |
|
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: 438.51 E-value: 3.10e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 3 YMIGVDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMRESKVNKDDIKFVSFSAQMH 82
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 83 SLIAMDQQHQRLTNNITWADNRAAKYATVINEvHDGNAIYQRTGTPIHPMSPLAKIFWMK-HEwQDVFQRTAKFADIKTY 161
Cdd:cd07808 81 GLVLLDKNGRPLRPAILWNDQRSAAECEELEA-RLGDEILIITGNPPLPGFTLPKLLWLKeNE-PEIFARIRKILLPKDY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 162 IFYHLFDTYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTTYVMKGMKERYATLMGLNKDTPFVIGASDG 241
Cdd:cd07808 159 LRYRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAAEELGLPEGTPVVAGAGDN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 242 VLSNLGVNSVGKGEVAVTIGTSGAIRTVIDKPRTDYKGRI--FCYVLTEDHYVIGGpVNNGGVVLRWLRDELLASEveta 319
Cdd:cd07808 239 AAAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLhtFPHAVPGKWYAMGV-TLSAGLSLRWLRDLFGPDR---- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 320 krlgvDPYDVLTQIAKRVKPGADGLIFHPYLAGERAPLWNANARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIE 399
Cdd:cd07808 314 -----ESFDELDAEAAKVPPGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVLKE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 400 vMNETPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYESSCLGACVLGLKAVGDIEDF-SIVSSMVGATNNHTPIEEN 478
Cdd:cd07808 389 -LGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLeEAAAACIKIEKTIEPDPER 467
|
490
....*....|....*
gi 446799407 479 VTVYQEIVSIFINLS 493
Cdd:cd07808 468 HEAYDELYARYRELY 482
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
3-482 |
7.97e-133 |
|
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: 392.27 E-value: 7.97e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 3 YMIGVDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMRESKVNKDDIKFVSFSAQMH 82
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 83 SLIAMDQQHQRLTNNITWADNRAAKYATVinevhdgnaiyqrtgtpihpmsplakifwmkhewQDvfqrtakfadiktYI 162
Cdd:cd07779 81 TFVPVDEDGRPLRPAISWQDKRTAKFLTV----------------------------------QD-------------YL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 163 FYHLFDTYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTTYVMKGMKERYATLMGLNKDTPFVIGASDGV 242
Cdd:cd07779 114 LYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAAEETGLPEGTPVVAGGGDQQ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 243 LSNLGVNSVGKGEVAVTIGTSGAIRTVIDKPRTDYKGRIFCYV-LTEDHYVIGGPVNNGGVVLRWLRDELLASEVEtAKR 321
Cdd:cd07779 194 CAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPsAVPGKWVLEGSINTGGSAVRWFRDEFGQDEVA-EKE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 322 LGVDPYDVLTQIAKRVKPGADGLIFHPYLAGERAPLWNANARGSFFGLTLSHKKEHMIRAALEGVLYNLYTvYLALIEVM 401
Cdd:cd07779 273 LGVSPYELLNEEAAKSPPGSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELRD-NLEAMEKA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 402 NETPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYESSCLGACVLGLKAVGDIEDF-SIVSSMVGATNNHTPIEENVT 480
Cdd:cd07779 352 GVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFeEAVKAMVRVTDTFEPDPENVA 431
|
..
gi 446799407 481 VY 482
Cdd:cd07779 432 IY 433
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
3-449 |
8.60e-131 |
|
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: 385.38 E-value: 8.60e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 3 YMIGVDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMRESKVNKDDIKFVSFSAQMH 82
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 83 SLIAMDQQHQRLTNNITWADNRAakyatvinevhdgnaiyqrtgtpihpmsplakifwmkhewqdvfqrtaKFADIKTYI 162
Cdd:cd00366 81 GVVLVDADGNPLRPAIIWLDRRA------------------------------------------------KFLQPNDYI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 163 FYHLFDTYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTTYVMKGMKERYATLMGLNKDTPFVIGASDGV 242
Cdd:cd00366 113 VFRLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGGDTA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 243 LSNLGVNSVGKGEVAVTIGTSGAIRTVIDKPRtDYKGRIFC-YVLTEDHYVIGGPVNNGGVVLRWLRDELLASEVETAKR 321
Cdd:cd00366 193 AAALGAGVVEPGDAVDSTGTSSVLSVCTDEPV-PPDPRLLNrCHVVPGLWLLEGAINTGGASLRWFRDEFGEEEDSDAEY 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 322 LGvdpydvLTQIAKRVKPGADGLIFHPYLAGERAPLWNANARGSFFGLTLSHKKEHMIRAALEGVLYNLYTvYLALIEVM 401
Cdd:cd00366 272 EG------LDELAAEVPPGSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRD-NLEILEEL 344
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 446799407 402 NETPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYESSCLGACVLG 449
Cdd:cd00366 345 GVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
3-454 |
6.14e-130 |
|
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Rhodospirillum rubrum xylulose kinase (RrXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466806 [Multi-domain] Cd Length: 451 Bit Score: 385.34 E-value: 6.14e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 3 YMIGVDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMRESKVNKDDIKFVSFSAQMH 82
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 83 SLIAMDQQHQRLTNNITWADNRAAKYATVINEVHDGNAIYQRTGTPIHPMSPLAKIFWMKHEWQDVFQRTAKFADIKTYI 162
Cdd:cd07804 81 ALVPVDENGKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRKFLGAYDYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 163 FYHLFDTYIIDYSMASAT-GMFNLETLDWDVEALELLGISKEMLPELVPTTYVMKGMKERYATLMGLNKDTPFVIGASDG 241
Cdd:cd07804 161 VYKLTGEYVIDYSSAGNEgGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEAAEETGLAEGTPVVAGTVDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 242 VLSNLGVNSVGKGEVAVTIGTSGAIRTVIDKPRTDykGRIF-CYVLTEDHYVIGGPVNNGGVVLRWLRDELLASEVETAK 320
Cdd:cd07804 241 AASALSAGVVEPGDLLLMLGTAGDIGVVTDKLPTD--PRLWlDYHDIPGTYVLNGGMATSGSLLRWFRDEFAGEEVEAEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 321 RLGVDPYDVLTQIAKRVKPGADGLIFHPYLAGERAPLWNANARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVylalIEV 400
Cdd:cd07804 319 SGGDSAYDLLDEEAEKIPPGSDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYGLRHH----LEV 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 446799407 401 MNE---TPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYESSCLGACVLGLKAVG 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 |
1.17e-120 |
|
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: 361.52 E-value: 1.17e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 3 YMIGVDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMreSKVNKDDIKFVSFSAQMH 82
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAA--AQAGPDPIAAISVSSQGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 83 SLIAMDQQHQRLTNNITWADNRAAKYATVINEVHDGNAIYQRTGTPIHPMSPLAKIFWMKHEWQDVFQRTAKFADIKTYI 162
Cdd:cd07773 79 SGVPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAKWLSVADYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 163 FYHLFDTYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTTYVMKGMKERYATLMGLNKDTPFVIGASDGV 242
Cdd:cd07773 159 AYRLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEELGLPAGTPVVVGGHDHL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 243 LSNLGVNSVGKGEVAVTIGTSGAIRTVIDKPRTD----YKGRIFCYVLTEDHYVIGGPVnNGGVVLRWLRDELLASEVET 318
Cdd:cd07773 239 CAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLDemlaEGGLSYGHHVPGGYYYLAGSL-PGGALLEWFRDLFGGDESDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 319 AKRlgvdpydvlTQIAKRVKPGADGLIFHPYLAGERAPLWNANARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVyLALI 398
Cdd:cd07773 318 AAA---------DELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLN-LEAL 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446799407 399 EVMNETPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYESSCLGACVLGLKAVG 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 |
1.71e-110 |
|
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: 336.59 E-value: 1.71e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 5 IGVDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMRESKVNKDDIKFVSFSAQMHSL 84
Cdd:TIGR01312 1 LGIDLGTSGVKALLVDEQGEVIASGSAPHTVISPHPGWSEQDPEDWWDATEEAIKELLEQASEMGQDIKGIGISGQMHGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 85 IAMDQQHQRLTNNITWADNRAAKYATVINEVHDGNAIYQRTGTPIHPMSPLAKIFWMKHEWQDVFQRTAKFADIKTYIFY 164
Cdd:TIGR01312 81 VLLDANGEVLRPAILWNDTRTAQECEELEAELGDERVLEITGNLALPGFTAPKLLWVRKHEPEVFARIAKVMLPKDYLRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 165 HLFDTYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTTYVMKGMKERYATLMGLNKDTPFVIGASDGVLS 244
Cdd:TIGR01312 161 RLTGEYVTEYSDASGTGWFDVAKRAWSKELLDALDLPESQLPELIESSEKAGTVRPEVAARLGLSAGVPVAAGGGDNAAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 245 NLGVNSVGKGEVAVTIGTSGAIRTVIDKPRTDYKGRI--FCYVLTEDHYVIGgPVNNGGVVLRWLRDELLASEVETakrl 322
Cdd:TIGR01312 241 AIGTGTVDPGDAMMSLGTSGVVYAVTDKPLPDPAGAVhgFCHALPGGWLPMG-VTLSATSSLEWFRELFGKEDVEA---- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 323 gvdpydvLTQIAKRVKPGADGLIFHPYLAGERAPLWNANARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIEVMN 402
Cdd:TIGR01312 316 -------LNELAEQSPPGAEGVTFLPYLNGERTPHLDPQARGSFIGLTHNTTRADLTRAVLEGVTFALRDSLDILREAGG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 403 ETPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYESSCLGACVLGLKAVGDIEDFSIVSSMVGATNNHT-PIEENVTV 481
Cdd:TIGR01312 389 IPIQSIRLIGGGAKSPAWRQMLADIFGTPVDVPEGEEGPALGAAILAAWALGEKDLAALCSEAVVKQTESVlPIAENVEA 468
|
....*...
gi 446799407 482 YQEIVSIF 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 |
1.14e-105 |
|
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: 322.96 E-value: 1.14e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 3 YMIGVDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMRESKVNKDDIKFVSFSAQMH 82
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 83 SLIAMDQQHQRLTNNITWADNRAAKYATVINEVHDGNAIYQRTGTPIHPMSPLAKIFWMKHEWQDVFQRTAKFADIKTYI 162
Cdd:cd07802 81 GLYLVDKDGKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRIRTVLFCKDWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 163 FYHLFDTYIIDYSMASaTGMFNLETLDWDVEALELLGIS--KEMLPELVPTTYVMKGMKERYATLMGLNKDTPFVIGASD 240
Cdd:cd07802 161 RYRLTGEISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVTAEAAALTGLPEGTPVAAGAFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 241 GVLSNLGVNSVGKGEVAVTIGTSGAIRTVIDKPRTDYKGRIFCYVLTEDHYVIGGPVNNGGVVLRWLRDELLASEvetaK 320
Cdd:cd07802 240 VVASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDSVGSNSLHADPGLYLIVEASPTSASNLDWFLDTLLGEE----K 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 321 RLGVDPYDVLTQIAKRVKPGADGLIFHPYLAGERAplwNANARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIEv 400
Cdd:cd07802 316 EAGGSDYDELDELIAAVPPGSSGVIFLPYLYGSGA---NPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLV- 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 446799407 401 mNETPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYESSCLGACVLGLKAVG 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 |
3.90e-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: 290.28 E-value: 3.90e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 5 IGVDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMRESKVNkdDIKFVSFSAQMHSL 84
Cdd:cd07783 3 LGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPR--RVVAIAVDGTSGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 85 IAMDQQHQRLTNNITWADNRAAKYATVINEVhdGNAIYQRTGTPIHPMSPLAKIFWMKHEWQDVFQRTAKFADIKTYIFY 164
Cdd:cd07783 81 VLVDREGEPLRPAIMYNDARAVAEAEELAEA--AGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFLHQADWLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 165 HLFDTYII-DYSMASATGmFNLETLDWDVEALELLGISKEMLPELVPTTYVMKGMKERYATLMGLNKDTPFVIGASDGVL 243
Cdd:cd07783 159 RLTGDRGVtDYNNALKLG-YDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLPAGTPVVAGTTDSIA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 244 SNLGVNSVGKGEVAVTIGTSGAIRTVIDKPRTDYKGRIFCYVLTEDHYVIGGPVNNGGVVLRWLrdellasevetakrLG 323
Cdd:cd07783 238 AFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGVYSHRHGDGYWLVGGASNTGGAVLRWF--------------FS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 324 VDPYDVLTQIAKRvkPGADGLIFHPY-LAGERAPLWNANARGSFfgLTLSHKKEHMIRAALEGVLYNLYTVYLALIEVMN 402
Cdd:cd07783 304 DDELAELSAQADP--PGPSGLIYYPLpLRGERFPFWDPDARGFL--LPRPHDRAEFLRALLEGIAFIERLGYERLEELGA 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 446799407 403 ETPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESyESSCLGACVLGLKAV 453
Cdd:cd07783 380 PPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEE-EEAALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
3-454 |
1.32e-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: 1.32e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 3 YMIGVDIGTTSTKSVLYD-ENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMRESKVNKDDIKFVSFSAQM 81
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 82 HSLIAMDQQHQRLTNNITWADNRAAKYATVINEVHDGNAIYQrTGTPIHPMSPLAKIFWMKHEWQDVFQRTAKF---ADi 158
Cdd:cd07809 81 HGLVALDADGKVLRPAKLWCDTRTAPEAEELTEALGGKKCLL-VGLNIPARFTASKLLWLKENEPEHYARIAKIllpHD- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 159 ktYIFYHLFDTYIIDYSMASATGMFNLETLDWDVEALELLGIS---KEMLPELVPTTYVMKGMKERYATLMGLNKDTPFV 235
Cdd:cd07809 159 --YLNWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAIDPSrdlRDLLPEVLPAGEVAGRLTPEGAEELGLPAGIPVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 236 IGASDGVLSNLGVNSVGKGEVAVTIGTSGAIRTVIDKPRTDYKGRI--FCYVLteDHYViggPVNNG-GVVLRWLRdell 312
Cdd:cd07809 237 PGEGDNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSDPHGRVatFCDST--GGML---PLINTtNCLTAWTE---- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 313 asevETAKRLGVDpYDVLTQIAKRVKPGADGLIFHPYLAGERAPLWnANARGSFFGLTLS-HKKEHMIRAALEGVLYNLY 391
Cdd:cd07809 308 ----LFRELLGVS-YEELDELAAQAPPGAGGLLLLPFLNGERTPNL-PHGRASLVGLTLSnFTRANLARAALEGATFGLR 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446799407 392 tvY-LALIEVMNETPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYESSCLGACVLGLKAVG 454
Cdd:cd07809 382 --YgLDILRELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
3-454 |
2.16e-83 |
|
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: 265.64 E-value: 2.16e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 3 YMIGVDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMRESKVNKDDIKFVSFSAQMH 82
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 83 SLIAMDQQHQRLTNNITWADNRAAKYATVINEVHDGNAIYQRTGTPIHPMSPLAKIFWMKHEWQDVFQRTAKFADIKTYI 162
Cdd:cd24121 81 GTWLVDEDGRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKENEPERLERARTALHCKDWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 163 FYHLFDTYIIDYSMASATgMFNLETLDWDVEALELLGIS--KEMLPELVPTTYVMKGMKERYATLMGLNKDTPFVIGASD 240
Cdd:cd24121 161 FYKLTGEIATDPSDASLT-FLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAAAATGLPAGTPVVLGPFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 241 GVLSNLGVNSVGKGEVAVTIGTSGAIRTVIDKPRTDYK--GRIFCYVLtEDHYVIGGPVNNGGVVLRWLRDELLASEVET 318
Cdd:cd24121 240 VVATALGSGAIEPGDACSILGTTGVHEVVVDEPDLEPEgvGYTICLGV-PGRWLRAMANMAGTPNLDWFLRELGEVLKEG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 319 AKRLGVDPYDVLTQIAKRVKPGADGLIFHPYL--AGERAPLWNANARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYla 396
Cdd:cd24121 319 AEPAGSDLFQDLEELAASSPPGAEGVLYHPYLspAGERAPFVNPNARAQFTGLSLEHTRADLLRAVYEGVALAMRDCY-- 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446799407 397 liEVMNETPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYESSCLGACVLGLKAVG 454
Cdd:cd24121 397 --EHMGEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
3-247 |
1.52e-80 |
|
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: 251.49 E-value: 1.52e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 3 YMIGVDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMRESKVNKDDIKFVSFSAQMH 82
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 83 SLIAMDQQHQRLTNNITWADNRAAKYATVINEVHDGNAIYQRTGTPIHPMSPLAKIFWMKHEWQDVFQRTAKFADIKTYI 162
Cdd:pfam00370 81 GTVLLDKNDKPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIHDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 163 FYHLFDTYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTTYVMKGMKERYATLMGLNKDTPFVIGASDGV 242
Cdd:pfam00370 161 RWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGGDQQ 240
|
....*
gi 446799407 243 LSNLG 247
Cdd:pfam00370 241 AAAFG 245
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
3-496 |
2.51e-76 |
|
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: 248.99 E-value: 2.51e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 3 YMIGVDIGTTSTKSVLYD-ENGTFIMKHQIGYDLH--TPNVDVSEENPDELFDAVLMTIKYVMRESKVNKDDIKFVSFSA 79
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGyiPPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 80 QMHSLIAMDQQHQRLTNNITWADNRAAKYATVINEVHD--GNAIYQRTGTPIHPMSPLAKIFWMKHEWQDVFQRTAKFAD 157
Cdd:cd07781 81 TSSTVVPVDEDGNPLAPAILWMDHRAQEEAAEINETAHpaLEYYLAYYGGVYSSEWMWPKALWLKRNAPEVYDAAYTIVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 158 IKTYIFYHLFDTYIIDYSMASATGMFNLETLDWDVE-----ALELLGISKEMLPELVPTTYVMKGMKERYATLMGLNKDT 232
Cdd:cd07781 161 ACDWINARLTGRWVRSRCAAGHKWMYNEWGGGPPREflaalDPGLLKLREKLPGEVVPVGEPAGTLTAEAAERLGLPAGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 233 PFVIGASDGVLSNLGVNSVGKGEVAVTIGTSGAIRTVIDKPrTDYKGriFCYV----LTEDHYVI-GGPVNNGGVvLRWL 307
Cdd:cd07781 241 PVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTCHLMVSPKP-VDIPG--ICGPvpdaVVPGLYGLeAGQSAVGDI-FAWF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 308 RDELlaseVETAKRLGVDPYDVLTQIAKRVKPGADGLIFHPYLAGERAPLWNANARGSFFGLTLSHKKEHMIRAALEGVL 387
Cdd:cd07781 317 VRLF----VPPAEERGDSIYALLSEEAAKLPPGESGLVALDWFNGNRTPLVDPRLRGAIVGLTLGTTPAHIYRALLEATA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 388 YNLytvyLALIEVMNE---TPKMIKATGGFA-KSEVWRQMMSDIFDTELVVPESYESSCLGACVLGLKAVGDIEDF-SIV 462
Cdd:cd07781 393 FGT----RAIIERFEEagvPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVAAGVYADIeEAA 468
|
490 500 510
....*....|....*....|....*....|....
gi 446799407 463 SSMVGATNNHTPIEENVTVYQEIVSIFINLSRSL 496
Cdd:cd07781 469 DAMVRVDRVYEPDPENHAVYEELYALYKELYDAL 502
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
3-454 |
1.41e-75 |
|
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: 245.21 E-value: 1.41e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 3 YMIGVDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNV--DVSEENPDELFDAVLMTIKYVMRESKVNKDDIKFVSFSAQ 80
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDypDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 81 MHSLIAMDQQHQRL--TNNItwaDNRAAKYATVINEVHdGNAIYQRTGTPIHPMSPLAKIFWMKHEWQDVFQRTAKFADI 158
Cdd:cd07798 81 REGIVFLDKDGRELyaGPNI---DARGVEEAAEIDDEF-GEEIYTTTGHWPTELFPAARLLWFKENRPEIFERIATVLSI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 159 KTYIFYHLFDTYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTTYVMKGMKERYATLMGLNKDTPFVIGA 238
Cdd:cd07798 157 SDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAARELGLPEGTPVVVGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 239 SDGVLSNLGVNSVGKGEVAVTIGTSGAIRTVIDKPRTDYKGRIF--CYVLtEDHYVI---GGPVnngGVVLRWLRDELLA 313
Cdd:cd07798 237 ADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWtgCHLV-PGKWVLesnAGVT---GLNYQWLKELLYG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 314 SevetakrlGVDPYDVLTQIAKRVKPGADGLI--FHPYLAGERAplwNANARGSFFGLTLSH----KKEHMIRAALEGVL 387
Cdd:cd07798 313 D--------PEDSYEVLEEEASEIPPGANGVLafLGPQIFDARL---SGLKNGGFLFPTPLSaselTRGDFARAILENIA 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446799407 388 YNLYTVYLALIEVMNETPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYESSCLGACVLGLKAVG 454
Cdd:cd07798 382 FAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
3-454 |
5.45e-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: 226.58 E-value: 5.45e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 3 YMIGVDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMRESKVNKDDIKFVSFSAQMH 82
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 83 SLIAMDQQHQR-LTNNITWADNRAAKYATVINEVHDGNAIYQRTGTPIHPMSPLAKIFWMKHEWQDVFQRTAK----FAD 157
Cdd:cd07769 81 TTVVWDKKTGKpLYNAIVWQDRRTADICEELKAKGLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAERgellFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 158 IKTYIFYHL--FDTYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTTYVMkgmkeRYATLMGLNKDTPF- 234
Cdd:cd07769 161 IDTWLIWKLtgGKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVF-----GYTDPEGLGAGIPIa 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 235 -VIGASDGVLsnLGVNSVGKGEVAVTIGT-------SGairtviDKPRTDYKGRI--FCYVLTED-HYVIGGPVNNGGVV 303
Cdd:cd07769 236 gILGDQQAAL--FGQGCFEPGMAKNTYGTgcfllmnTG------EKPVPSKNGLLttIAWQIGGKvTYALEGSIFIAGAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 304 LRWLRDELL----ASEVETakrlgvdpydvltqIAKRVkPGADGLIFHPYLAGERAPLWNANARGSFFGLTLSHKKEHMI 379
Cdd:cd07769 308 IQWLRDNLGliedAAETEE--------------LARSV-EDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIV 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446799407 380 RAALEGVLYNLYTVYLALIEVMNETPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYESSCLGACVLGLKAVG 454
Cdd:cd07769 373 RAALESIAYQTRDVLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVG 447
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
3-485 |
6.17e-64 |
|
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: 216.04 E-value: 6.17e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 3 YMIGVDIGTTSTKSVLYDENGTFIMKHQIGYdLHTPNVDV-------SEENPDELFDavlmTIKYVMRESKVNKDDIKFV 75
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREW-RHKEVPDVpgsmdfdTEKNWKLICE----CIREALKKAGIAPKSIAAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 76 SFSAQMHSLIAMDQQHQRLtnnitWA----DNRAAKYATVINEVHDG--NAIYQRTG-TPihPMSPLAKIFWMKHEWQDV 148
Cdd:cd07775 76 STTSMREGIVLYDNEGEEI-----WAcanvDARAAEEVSELKELYNTleEEVYRISGqTF--ALGAIPRLLWLKNNRPEI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 149 FQRTAKFADIKTYIFYHLFDTYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTTYVMKGMKERYATLMGL 228
Cdd:cd07775 149 YRKAAKITMLSDWIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEAAEETGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 229 NKDTPFVIGASDGVLSNLGVNSVGKGEVAVTIGTSGAIRTVIDKPRTDYKG--RIFCYVLtEDHYVIGGPVNNGGVVLRW 306
Cdd:cd07775 229 KEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMniRVNCHVI-PDMWQAEGISFFPGLVMRW 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 307 LRDELLASEVETAKRLGVDPYDVLTQIAKRVKPGADGL--IF----------HPylagerAPlwnanargSFFGLTLSHK 374
Cdd:cd07775 308 FRDAFCAEEKEIAERLGIDAYDLLEEMAKDVPPGSYGImpIFsdvmnyknwrHA------AP--------SFLNLDIDPE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 375 KehmiraalegvlYNLYTVYLALIE----VMNETPKMIKA-----------TGGFAKSEVWRQMMSDIFDTELVVPESYE 439
Cdd:cd07775 374 K------------CNKATFFRAIMEnaaiVSAGNLERIAEfsgifpdslvfAGGASKGKLWCQILADVLGLPVKVPVVKE 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 446799407 440 SSCLGACVLGLKAVG---DIEDFsiVSSMVGATNNHTPIEENVTVYQEI 485
Cdd:cd07775 442 ATALGAAIAAGVGAGiysSLEEA--VESLVKWEREYLPNPENHEVYQDL 488
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
1-478 |
7.77e-63 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 213.30 E-value: 7.77e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 1 MKYMIGVDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMR--ESKVNKDDIKFVSFS 78
Cdd:PTZ00294 1 MKYIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKklREKGPSFKIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 79 AQMHSLIAMDQQHQR-LTNNITWADNRAAKYATVINEVHDG-NAIYQRTGTPIHPMSPLAKIFWM--KHEW--QDVFQRT 152
Cdd:PTZ00294 81 NQRETVVAWDKVTGKpLYNAIVWLDTRTYDIVNELTKKYGGsNFFQKITGLPISTYFSAFKIRWMleNVPAvkDAVKEGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 153 AKFADIKTYIFYHL--FDTYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTTyvmkgmkERYATLM---- 226
Cdd:PTZ00294 161 LLFGTIDTWLIWNLtgGKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSS-------ENFGTISgeav 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 227 GLNKDTPfvIGAS--DGVLSNLGVNSVGKGEVAVTIGTSGAIRTVI-DKPRTDYKGRI--FCYVLTEDH---YVIGGPVN 298
Cdd:PTZ00294 234 PLLEGVP--ITGCigDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTgTEIVFSKHGLLttVCYQLGPNGptvYALEGSIA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 299 NGGVVLRWLRDEL----LASEVEtakrlgvdpydvltQIAKRVKpGADGLIFHPYLAGERAPLWNANARGSFFGLTLSHK 374
Cdd:PTZ00294 312 VAGAGVEWLRDNMglisHPSEIE--------------KLARSVK-DTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 375 KEHMIRAALEGVLYNLYTVYLALIEVMNETPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYESSCLGACV---LGLK 451
Cdd:PTZ00294 377 RAHIVRAALEAIALQTNDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALlagLAVG 456
|
490 500
....*....|....*....|....*..
gi 446799407 452 AVGDIEDFSIVSSMVGATNNHTPIEEN 478
Cdd:PTZ00294 457 VWKSLEEVKKLIRRSNSTFSPQMSAEE 483
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
1-460 |
1.23e-58 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 201.83 E-value: 1.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 1 MKYMIGVDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPN---VdvsEENPDELFDAVLMTIKYVMRESKVNKDDIKFVSF 77
Cdd:COG0554 2 KKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQpgwV---EHDPEEIWESVLAVIREALAKAGISAEDIAAIGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 78 SAQMHSLIAMDqqhqR-----LTNNITWADNRAAKYATVINEVHDGNAIYQRTGTPIHPMSPLAKIFWMKHEWQDVFQRT 152
Cdd:COG0554 79 TNQRETTVVWD----RktgkpLYNAIVWQDRRTADICEELKADGLEDLIREKTGLVLDPYFSATKIKWILDNVPGARERA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 153 AK----FADIKTYIFYHLfdT----YIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTTYVMkGmkerYAT 224
Cdd:COG0554 155 EAgellFGTIDSWLIWKL--TggkvHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVF-G----ETD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 225 LMGLNKDTPF--VIGASDGVLsnlgvnsVG-----KGEVAVTIGTSGAIRTVI-DKPRTDYKGrifcyVLT--------E 288
Cdd:COG0554 228 PDLFGAEIPIagIAGDQQAAL-------FGqacfePGMAKNTYGTGCFLLMNTgDEPVRSKNG-----LLTtiawglggK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 289 DHYVIGGPVNNGGVVLRWLRDEL----LASEVETakrlgvdpydvltqIAKRVKPgADGLIFHPYLAGERAPLWNANARG 364
Cdd:COG0554 296 VTYALEGSIFVAGAAVQWLRDGLglidSAAESEA--------------LARSVED-NGGVYFVPAFTGLGAPYWDPDARG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 365 SFFGLTLSHKKEHMIRAALEGVLYNLYtvylALIEVMNE----TPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYES 440
Cdd:COG0554 361 AIFGLTRGTTRAHIARAALESIAYQTR----DVLDAMEAdsgiPLKELRVDGGASANDLLMQFQADILGVPVERPKVTET 436
|
490 500
....*....|....*....|...
gi 446799407 441 SCLGACVLGLKAVG---DIEDFS 460
Cdd:COG0554 437 TALGAAYLAGLAVGfwkSLEELA 459
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
3-460 |
3.55e-57 |
|
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: 198.17 E-value: 3.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 3 YMIGVDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMRESKVNKDDIKFVSFSAQMH 82
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 83 SLIAMDQQ-HQRLTNNITWADNRAAKYATVINE------VHDGNAIYQR-TGTPIH---------PMSPLAKIFWMKHEW 145
Cdd:cd07793 81 TFLTWDKKtGKPLHNFITWQDLRAAELCESWNRslllkaLRGGSKFLHFlTRNKRFlaasvlkfsTAHVSIRLLWILQNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 146 QDVFQRTAK----FADIKTYIFYHL--FDTYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTtyvmkgmk 219
Cdd:cd07793 161 PELKEAAEKgellFGTIDTWLLWKLtgGKVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDT-------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 220 eryATLMGLNKdtPFVIGAS--------DGVLSNLGVNSVGKGEVAVTIGTSgairTVID-----KPRTDYKGrifCYVL 286
Cdd:cd07793 233 ---SGDFGSTD--PSIFGAEipitavvaDQQAALFGECCFDKGDVKITMGTG----TFIDintgsKPHASVKG---LYPL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 287 T------EDHYVIGGPVNNGGVVLRWLRDELLASEVEtakrlgvdpydVLTQIAKRVkPGADGLIFHPYLAGERAPLWNA 360
Cdd:cd07793 301 VgwkiggEITYLAEGNASDTGTVIDWAKSIGLFDDPS-----------ETEDIAESV-EDTNGVYFVPAFSGLQAPYNDP 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 361 NARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIEVMNETPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYES 440
Cdd:cd07793 369 TACAGFIGLTPSTTKAHLVRAILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEM 448
|
490 500
....*....|....*....|....
gi 446799407 441 SCLGACVL-GLkAVG---DIEDFS 460
Cdd:cd07793 449 SALGAAFLaGL-ASGiwkSKEELK 471
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
5-446 |
2.51e-52 |
|
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: 183.58 E-value: 2.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 5 IGVDIGTTSTKSVLYD-ENGTFI--MKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMRESKvnkDDIKFVSFSAQM 81
Cdd:cd07777 3 LGIDIGTTSIKAALLDlESGRILesVSRPTPAPISSDDPGRSEQDPEKILEAVRNLIDELPREYL---SDVTGIGITGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 82 HSLIAMDQQHQRLTNNITWADNRAakyatviNEVHDGNAIY------QRTGTPIHPMSPLAKIFWMKHEwQDVFQRTAKF 155
Cdd:cd07777 80 HGIVLWDEDGNPVSPLITWQDQRC-------SEEFLGGLSTygeellPKSGMRLKPGYGLATLFWLLRN-GPLPSKADRA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 156 ADIKTYIFYHLFDTY--IIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTTyvmkgmkERYATL-MGLNKDT 232
Cdd:cd07777 152 GTIGDYIVARLTGLPkpVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSG-------EIVGTLsSALPKGI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 233 P-FV-IG---ASdgVLSNLgvnSVGKGEVAVTIGTSGAIRTVIDKPRTDYKGRIFCYVltEDHYVIGGPVNNGGVVLRWL 307
Cdd:cd07777 225 PvYVaLGdnqAS--VLGSG---LNEENDAVLNIGTGAQLSFLTPKFELSGSVEIRPFF--DGRYLLVAASLPGGRALAVL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 308 RDELlaseVETAKRLGVDP-----YDVLTQIAkrVKPGADGLIFHPYLAGERaplWNANARGSFFGLTLSH-KKEHMIRA 381
Cdd:cd07777 298 VDFL----REWLRELGGSLsddeiWEKLDELA--ESEESSDLSVDPTFFGER---HDPEGRGSITNIGESNfTLGNLFRA 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446799407 382 ALEGVLYNLYTVYLALIEVMNETPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYESSCLGAC 446
Cdd:cd07777 369 LCRGIAENLHEMLPRLDLDLSGIERIVGSGGALRKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAA 433
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
3-458 |
9.41e-52 |
|
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: 183.08 E-value: 9.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 3 YMIGVDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMRESKVNKDDIKFVSFSAQMH 82
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 83 SLIAMDQQHQR-LTNNITWADNRAAKYATVINEVHDGNAIYQRTGTPIHPMSPLAKIFWMKHEWQDVFQRTAK----FAD 157
Cdd:cd07786 81 TTVVWDRETGKpVYNAIVWQDRRTADICEELKAEGHEEMIREKTGLVLDPYFSATKIRWILDNVPGARERAERgelaFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 158 IKTYIFYHLFD--TYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTTYVMkgmkeRYATLMGLNKDTPF- 234
Cdd:cd07786 161 IDSWLIWKLTGgkVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVF-----GYTDPDLLGAEIPIa 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 235 -VIGASDGVLsnLGVNSVGKGEVAVTIGTSGAIRTVI-DKPRTDYKGrifcyVLT--------EDHYVIGGPVNNGGVVL 304
Cdd:cd07786 236 gIAGDQQAAL--FGQACFEPGMAKNTYGTGCFMLMNTgEKPVRSKNG-----LLTtiawqlggKVTYALEGSIFIAGAAV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 305 RWLRDELL----ASEVETakrlgvdpydvltqIAKRVkPGADGLIFHPYLAGERAPLWNANARGSFFGLTLSHKKEHMIR 380
Cdd:cd07786 309 QWLRDGLGliesAAETEA--------------LARSV-PDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIAR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 381 AALEGVLYNLYTVYLALIEVMNETPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYESSCLGACVL-GLkAVG---DI 456
Cdd:cd07786 374 AALESIAYQTRDLLEAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLaGL-AVGlwkSL 452
|
..
gi 446799407 457 ED 458
Cdd:cd07786 453 DE 454
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
5-496 |
1.96e-51 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 182.47 E-value: 1.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 5 IGVDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMRESKVNkdDIKFVSFSAQMHSL 84
Cdd:PRK15027 3 IGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQ--DVKALGIAGQMHGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 85 IAMDQQHQRLTNNITWADNRAAKYATVINE-VHDGNAIyqrTGTPIHPMSPLAKIFWMKHEWQDVFQRTAKFADIKTYIF 163
Cdd:PRK15027 81 TLLDAQQRVLRPAILWNDGRCAQECALLEArVPQSRVI---TGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 164 YHLFDTYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTTYVMKGMKERYATLMGLnKDTPFVIGASDGVL 243
Cdd:PRK15027 158 LRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAKAWGM-ATVPVVAGGGDNAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 244 SNLGVNSVGKGEVAVTIGTSGAIRTVID----KPRTDYKGriFCYVLTEdhyviggpvnnggvvlRW-LRDELL--ASEV 316
Cdd:PRK15027 237 GAVGVGMVDANQAMLSLGTSGVYFAVSEgflsKPESAVHS--FCHALPQ----------------RWhLMSVMLsaASCL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 317 ETAKRL-GVDPYDVLTQIAKRVKPGADGLIFHPYLAGERAPLWNANARGSFFGLTLSHKKEHMIRAALEGVLYNLYTvYL 395
Cdd:PRK15027 299 DWAAKLtGLSNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALAD-GM 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 396 ALIEVMNETPKMIKATGGFAKSEVWRQMMSDIFDTELvvpeSYESS-----CLGACVLGLKAVGDIEDFSIVSSMVGATN 470
Cdd:PRK15027 378 DVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQL----DYRTGgdvgpALGAARLAQIAANPEKSLIELLPQLPLEQ 453
|
490 500
....*....|....*....|....*.
gi 446799407 471 NHTPIEENVTVYQEIVSIFINLSRSL 496
Cdd:PRK15027 454 SHLPDAQRYAAYQPRRETFRRLYQQL 479
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
7-454 |
2.68e-49 |
|
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: 176.95 E-value: 2.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 7 VDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYV---MRESKVNKDDIKFVSFSAQMHS 83
Cdd:cd07792 6 IDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAvekLKALGISPSDIKAIGITNQRET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 84 LIAMDQQH-QRLTNNITWADNRAAKyaTV---INEVHDG-NAIYQRTGTPIHPMSPLAKIFWMK--HEW--QDVFQRTAK 154
Cdd:cd07792 86 TVVWDKSTgKPLYNAIVWLDTRTSD--TVeelSAKTPGGkDHFRKKTGLPISTYFSAVKLRWLLdnVPEvkKAVDDGRLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 155 FADIKTYIFYHL-----FDTYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTTyvmkgmkERYatlmGLN 229
Cdd:cd07792 164 FGTVDSWLIWNLtggknGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSS-------EVY----GKI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 230 KDTPFV-IGASdGVLSNLGVNSVG-----KGEVAVTIGT----------------SGAIRTVidkprtdykgrifCYVLT 287
Cdd:cd07792 233 ASGPLAgVPIS-GCLGDQQAALVGqgcfkPGEAKNTYGTgcfllyntgeepvfskHGLLTTV-------------AYKLG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 288 ED---HYVIGGPVNNGGVVLRWLRDELL----ASEVETakrlgvdpydvltqIAKRVkPGADGLIFHPYLAGERAPLWNA 360
Cdd:cd07792 299 PDappVYALEGSIAIAGAAVQWLRDNLGiissASEVET--------------LAASV-PDTGGVYFVPAFSGLFAPYWRP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 361 NARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIEVMNETPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYES 440
Cdd:cd07792 364 DARGTIVGLTQFTTKAHIARAALEAVCFQTREILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVET 443
|
490
....*....|....
gi 446799407 441 SCLGACVLGLKAVG 454
Cdd:cd07792 444 TALGAAIAAGLAVG 457
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
1-485 |
6.78e-47 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 170.96 E-value: 6.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 1 MKYMIGVDIGTTSTKSVLYDENGTFIMKHQIGY-DLHTPNVDVSEEnpdelFDA------VLMTIKYVMRESKVNKDDIK 73
Cdd:PRK10939 2 MSYLMALDAGTGSIRAVIFDLNGNQIAVGQAEWrHLAVPDVPGSME-----FDLeknwqlACQCIRQALQKAGIPASDIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 74 FVSFSAQMHSLIAMDQQHQRLtnnitWA----DNRAAKYATVINEVHDG--NAIYQRTGTPIhPMSPLAKIFWMKHEWQD 147
Cdd:PRK10939 77 AVSATSMREGIVLYDRNGTEI-----WAcanvDARASREVSELKELHNNfeEEVYRCSGQTL-ALGALPRLLWLAHHRPD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 148 VFQRTAKFADIKTYIFYHLFDTYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTTYVMKGMKERYATLMG 227
Cdd:PRK10939 151 IYRQAHTITMISDWIAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAKAAAETG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 228 LNKDTPFVIGASDGVLSNLGVNSVGKGEVAVTIGTSGAIRTVIDKPRTDYKG--RIFCYVLTedhyviggPVNNG----- 300
Cdd:PRK10939 231 LRAGTPVVMGGGDVQLGCLGLGVVRPGQTAVLGGTFWQQVVNLPAPVTDPNMniRINPHVIP--------GMVQAesisf 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 301 --GVVLRWLRDELLASEVETAKRLGVDPYDVLTQIAKRVKPGADGLI------------FHPylagerAPlwnanargSF 366
Cdd:PRK10939 303 ftGLTMRWFRDAFCAEEKLLAERLGIDAYSLLEEMASRVPVGSHGIIpifsdvmrfkswYHA------AP--------SF 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 367 FGLTL----SHKKEhMIRAALEgvlyNLYTVY---LALIEVM-NETPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESY 438
Cdd:PRK10939 369 INLSIdpekCNKAT-LFRALEE----NAAIVSacnLQQIAAFsGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVK 443
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 446799407 439 ESSCLGACVLGLKAVGDIEDFS-IVSSMVGATNNHTPIEENVTVYQEI 485
Cdd:PRK10939 444 EATALGCAIAAGVGAGIYSSLAeTGERLVRWERTFEPNPENHELYQEA 491
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
2-459 |
1.59e-46 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 169.23 E-value: 1.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 2 KYMIGVDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMRESKVNKDDIKFVSFSAQM 81
Cdd:PRK00047 5 KYILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGITNQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 82 HSLIAMDQQHQR-LTNNITWADNRAAKYATVINEVHDGNAIYQRTGTPIHPMSPLAKIFWMKHEWQDVFQRTAK----FA 156
Cdd:PRK00047 85 ETTVVWDKETGRpIYNAIVWQDRRTADICEELKRDGYEDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKgellFG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 157 DIKTYIFYHLFD--TYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTTyvmkgmkERYATlmgLNKDTPF 234
Cdd:PRK00047 165 TIDTWLVWKLTGgkVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSS-------EVYGK---TNPYGFF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 235 viGAS---DGVLSN-----LGVNSVGKGEVAVTIGT-------SGairtviDKPRTDYKGrifcyVLTEDHYVIGGPVN- 298
Cdd:PRK00047 235 --GGEvpiAGIAGDqqaalFGQLCFEPGMAKNTYGTgcfmlmnTG------EKAVKSENG-----LLTTIAWGIDGKVVy 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 299 -------NGGVVLRWLRDELL----ASEVETAkrlgvdpydvltqiAKRVKpGADGLIFHPYLAGERAPLWNANARGSFF 367
Cdd:PRK00047 302 alegsifVAGSAIQWLRDGLKiisdASDSEAL--------------ARKVE-DNDGVYVVPAFTGLGAPYWDSDARGAIF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 368 GLTLSHKKEHMIRAALEGVLYNLYTVYLALIEVMNETPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYESSCLGACV 447
Cdd:PRK00047 367 GLTRGTTKEHIIRATLESIAYQTRDVLDAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAY 446
|
490
....*....|....*.
gi 446799407 448 L-GLkAVG---DIEDF 459
Cdd:PRK00047 447 LaGL-AVGfwkDLDEL 461
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
7-454 |
2.75e-38 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 146.77 E-value: 2.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 7 VDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMRESKVNK----DDIKFVSFSAQMH 82
Cdd:PLN02295 5 IDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGhnvdSGLKAIGITNQRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 83 SLIAMDQQHQR-LTNNITWADNRAAKYATVI-NEVHDGNAIY-QRTGTPIHPMSPLAKIFWMKHE----WQDVFQRTAKF 155
Cdd:PLN02295 85 TTVAWSKSTGRpLYNAIVWMDSRTSSICRRLeKELSGGRKHFvETCGLPISTYFSATKLLWLLENvdavKEAVKSGDALF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 156 ADIKTYIFYHL-----FDTYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTTyvmkgmkERYATlmgLNK 230
Cdd:PLN02295 165 GTIDSWLIWNLtggasGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNS-------EVIGT---IAK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 231 DTPFVIGASDGVLSNLGVNSVG----KGEVAVTIGTsGA--IRTVIDKPRTDYKGRI--FCYVLTED---HYVIGGPVNN 299
Cdd:PLN02295 235 GWPLAGVPIAGCLGDQHAAMLGqrcrPGEAKSTYGT-GCfiLLNTGEEVVPSKHGLLttVAYKLGPDaptNYALEGSVAI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 300 GGVVLRWLRDEL----LASEVETakrlgvdpydvltqIAKRVkPGADGLIFHPYLAGERAPLWNANARGSFFGLTLSHKK 375
Cdd:PLN02295 314 AGAAVQWLRDNLgiikSASEIEA--------------LAATV-DDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 376 EHMIRAALEGVLYNLYTVYLALI-----EVMNETPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYESSCLGACVLGL 450
Cdd:PLN02295 379 AHIARAVLESMCFQVKDVLDAMRkdageEKSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAG 458
|
....
gi 446799407 451 KAVG 454
Cdd:PLN02295 459 LAVG 462
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
3-500 |
1.46e-32 |
|
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466788 [Multi-domain] Cd Length: 522 Bit Score: 130.44 E-value: 1.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 3 YMIGVDIGTTSTKSVLYD-ENGTFIMKHQIGY-DLHTPNVDVSEENPDELFDAVLMTIKYVMRESKVNKDDIKFVSFSAQ 80
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDlYAGLEMAQEPVPYyQDSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 81 MhSLIAMDQQHQRLT---------NNITWADNRAAKYATVINEVHDgNAIYQRTGTPIHPMSPLAKIFWMKHEWQDVFQR 151
Cdd:cd07768 81 C-SLAIFDREGTPLMalipypnedNVIFWMDHSAVNEAQWINMQCP-QQLLDYLGGKISPEMGVPKLKYFLDEYSHLRDK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 152 TAKFADIKTYIFYHLfdTYIIDYSMASATGMFNL--ETLDWDVEALELLGISKE------MLPELVPTTYVMKGMKERYA 223
Cdd:cd07768 159 HFHIFDLHDYIAYEL--TRLYEWNICGLLGKENLdgEESGWSSSFFKNIDPRLEhltttkNLPSNVPIGTTSGVALPEMA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 224 TLMGLNKDTPFVIGASDGVLSNLGVNSVG-KGEVAVTIGTSGAirtvidkprtdykgriFCYVLTEDHYVIG--GPVNNG 300
Cdd:cd07768 237 EKMGLHPGTAVVVSCIDAHASWFAVASPHlETSLFMIAGTSSC----------------HMYGTTISDRIPGvwGPFDTI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 301 ---------------GVVLRWL-RDELLASEVETAKRLGVDPYDVLTQIAKRVKP---GADGLIFHPYLAGERAPLWNAN 361
Cdd:cd07768 301 idpdysvyeagqsatGKLIEHLfESHPCARKFDEALKKGADIYQVLEQTIRQIEKnngLSIHILTLDMFFGNRSEFADPR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 362 ARGSFFGLTLSHKKEhmiraalegvlyNLYTVYLALIEVMNETPKMI--------------KATGGFAKSEVWRQMMSDI 427
Cdd:cd07768 381 LKGSFIGESLDTSML------------NLTYKYIAILEALAFGTRLIidtfqnegihikelRASGGQAKNERLLQLIALV 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446799407 428 FDTELVVPESYESSCLGACVLGLKAVGdieDFSIVSSMVGATNNHTPIEENVT-VYQEIVSIFINLSRSLTENY 500
Cdd:cd07768 449 TNVAIIKPKENMMGILGAAVLAKVAAG---KKQLADSITEADISNDRKSETFEpLAYRLGADYILLYKLLCVKY 519
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
256-452 |
1.84e-31 |
|
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: 120.12 E-value: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 256 VAVTIGTSGAIRTVIDKPRTDYKGRI--FCYVLTEDHYVIGGPVNNGGVVLRWLRDELLASEVETAKRlGVDPYDVLTQI 333
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSVHGVWgpYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRDAG-NVESLAELAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 334 AKRVKPGadGLIFHPYLAGERAPLWNANARGSFFGLTLSHKKEHMIRAALEGVLYNLYtvylALIEVMNETPKM----IK 409
Cdd:pfam02782 80 AAVAPAG--GLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLR----QILEALTKQEGHpidtIH 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446799407 410 ATGGFAKSEVWRQMMSDIFDTELVVPESYESSCLGACVLGLKA 452
Cdd:pfam02782 154 VSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
3-459 |
1.76e-30 |
|
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: 124.57 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 3 YMIGVDIGTTSTKSVLYDENGTFIMKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMRESKVNKDDIKFVSFSAQMh 82
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFDATC- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 83 SLIAMDQQHQRLT---------NNITWADNRAAKYATVINevhdgnaiyqRTGtpiHP--------MSP---LAKIFWMK 142
Cdd:cd07782 80 SLVVLDAEGKPVSvspsgdderNVILWMDHRAVEEAERIN----------ATG---HEvlkyvggkISPemePPKLLWLK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 143 HEWQDVFQRTAKFADIKTYIFYHLFD-------------TYIIDysMASATGmfnletldWDVEALELLGiskemLPELV 209
Cdd:cd07782 147 ENLPETWAKAGHFFDLPDFLTWKATGsltrslcslvckwTYLAH--EGSEGG--------WDDDFFKEIG-----LEDLV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 210 -------------PTTYVMKGMKERYATLMGLNKDTPF---VIGASDGVLSNLGVNSVGKGEVAVTI--------GTSGA 265
Cdd:cd07782 212 ednfakigsvvlpPGEPVGGGLTAEAAKELGLPEGTPVgvsLIDAHAGGLGTLGADVGGLPCEADPLtrrlalicGTSSC 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 266 IRTVIDKPRT------DYKGRIFC-YVLTEdhyviGGPVNNGGvvlrwLRDELLASEV------ETAKRLGVDPYDVLT- 331
Cdd:cd07782 292 HMAVSPEPVFvpgvwgPYYSAMLPgLWLNE-----GGQSATGA-----LLDHIIETHPaypelkEEAKAAGKSIYEYLNe 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 332 ---QIAKRVKPGADGLI----FHPYLAGERAPLWNANARGSFFGLTLSHKKEHMIraalegVLYnLYTV-YLAL-----I 398
Cdd:cd07782 362 rleQLAEEKGLPLAYLTrdlhVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLA------LLY-LATLqALAYgtrhiI 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446799407 399 EVMNE---TPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYESSCLGACVLGLKAVGDIEDF 459
Cdd:cd07782 435 EAMNAaghKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSL 498
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
1-458 |
9.67e-28 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 115.90 E-value: 9.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 1 MKYMIGVDIGTTSTKSVLYDENGTFIMKHqigydlHTPN-VDVSEENPDEL---FDAVLMTIKYVMRE--SKVNKDDIKF 74
Cdd:PRK10331 1 QDVILVLDCGATNVRAIAVDRQGKIVARA------STPNaSDIAAENSDWHqwsLDAILQRFADCCRQinSELTECHIRG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 75 VSFSAQMHSLIAMDQQHQRLTNNITWADNRAAKYATVINEVHDGNAIYQRTGTPIHPMSPLAKIFWMKHEWQDVFQRTAK 154
Cdd:PRK10331 75 ITVTTFGVDGALVDKQGNLLYPIISWKCPRTAAVMENIERYISAQQLQQISGVGAFSFNTLYKLVWLKENHPQLLEQAHA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 155 FADIKTYIFYHLFDTYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVPTTYVMKGMKERYATLMGLNK---- 230
Cdd:PRK10331 155 WLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPSAAALLGLPVgipv 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 231 -----DTPFVIGASdGVLSNLGVNSVGKGEVAVtigtsgaIRTVIDKPR--TDYKGrifcyvLTEDHYVIGGPVNNG--- 300
Cdd:PRK10331 235 isaghDTQFALFGS-GAGQNQPVLSSGTWEILM-------VRSAQVDTSllSQYAG------STCELDSQSGLYNPGmqw 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 301 --GVVLRWLRDELLASEvetakrlgvDPYDVLTQIAKRVKPGADGLIFHPYLAGeraplwnaNARGSFFGLTLSHKKEHM 378
Cdd:PRK10331 301 laSGVLEWVRKLFWTAE---------TPYQTMIEEARAIPPGADGVKMQCDLLA--------CQNAGWQGVTLNTTRGHF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 379 IRAALEGVLYNLYTVYLALIEVMNETPKMIKATGGFAKSEVWRQMMSDIFDTELVVPESYESSCLGACVLGLKAVGDIED 458
Cdd:PRK10331 364 YRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSS 443
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
3-485 |
3.31e-20 |
|
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: 93.78 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 3 YMIGVDIGTTSTKSVLYDENGTFIMKHQIGYD-----LHTPNVDVSEENPDELFDAVLMTIKYV------MRESKVNKDD 71
Cdd:cd07776 1 LYLGLDLSTQSLKAVVIDSDLKVVAEESVNFDsdlpeYGTKGGVHRDGDGGEVTSPVLMWVEALdlllekLKAAGFDFSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 72 IKFVSFSAQMH----------SLIAMDQQHQRLTNNI----------TWADNRAAKYATVINE-VHDGNAIYQRTGTPIH 130
Cdd:cd07776 81 VKAISGSGQQHgsvywskgaeSALANLDPSKSLAEQLegafsvpdspIWMDSSTTKQCRELEKaVGGPEALAKLTGSRAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 131 ---PMSPLAKIFwmkHEWQDVFQRTAKfadiktyIfyHLFDTYI----------IDYSMASATGMFNLETLDWDVEALEL 197
Cdd:cd07776 161 erfTGPQIAKIA---QTDPEAYENTER-------I--SLVSSFLaslllgryapIDESDGSGMNLMDIRSRKWSPELLDA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 198 LGIS--KEMLPELVPTTYVMKG----MKERYatlmGLNKDTPFVIGASDGVLSNLGVNsVGKGEVAVTIGTSGAIRTVID 271
Cdd:cd07776 229 ATAPdlKEKLGELVPSSTVAGGissyFVERY----GFSPDCLVVAFTGDNPASLAGLG-LEPGDVAVSLGTSDTVFLVLD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 272 KPRTDYKGRIFCYVLTEDHYVIGGPVNNGGVVLRWLRDellasevetakRLGVDPYDVLTQIAKRVKPGADGLIFHPYLA 351
Cdd:cd07776 304 EPKPGPEGHVFANPVDPGSYMAMLCYKNGSLARERVRD-----------RYAGGSWEKFNELLESTPPGNNGNLGLYFDE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 352 GERAPLWNANARGsFFGLTLSHKK---EHMIRAALEGVLYNLYtVYLALIEvMNETPKMIKATGGFAKSEVWRQMMSDIF 428
Cdd:cd07776 373 PEITPPVPGGGRR-FFGDDGVDAFfdpAVEVRAVVESQFLSMR-LHAERLG-SDIPPTRILATGGASANKAILQVLADVF 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446799407 429 DTELVVPESYESSCLGACVLGLKAVGDIEDFSIVSSMVGATNNH-----TPIEENVTVYQEI 485
Cdd:cd07776 450 GAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVVFSAEEpklvaEPDPEAAEVYDKL 511
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
1-484 |
4.45e-18 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 87.21 E-value: 4.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 1 MKYMIGVDIGTTSTKSVLYD-ENGTFIMKH-------QIGYDLHTPNvDVSEENPDELFDAVLMTIKYVMRESKVNKDDI 72
Cdd:PRK04123 2 MAYVIGLDFGTDSVRALLVDcATGEELATAvveyphwVKGRYLDLPP-NQALQHPLDYIESLEAAIPAVLKEAGVDPAAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 73 KFVSFSAQMHSLIAMDQQHQRLTNNITWADN-----------RAAKYATVINEV-HD-GNAIYQR-TGTPIHPMSPLAKI 138
Cdd:PRK04123 81 VGIGVDFTGSTPAPVDADGTPLALLPEFAENphamvklwkdhTAQEEAEEINRLaHErGEADLSRyIGGIYSSEWFWAKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 139 FWMKHEWQDVFQRTAKFADIKTYIFYHLFDTYI---IDYSMASA--TGMFN-----------LETLDWDVEAlellGISK 202
Cdd:PRK04123 161 LHVLREDPAVYEAAASWVEACDWVVALLTGTTDpqdIVRSRCAAghKALWHeswgglpsadfFDALDPLLAR----GLRD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 203 EMLPELVPTTYVMKGMKERYATLMGLNKDTPFVIGASDGVLSNLGVNsVGKGEVAVTIGTSGAIRTVIDKPRTdYKGrif 282
Cdd:PRK04123 237 KLFTETWTAGEPAGTLTAEWAQRLGLPEGVAVSVGAFDAHMGAVGAG-AEPGTLVKVMGTSTCDILLADKQRA-VPG--- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 283 cyvltedhyvIGGPVNNG---------------GVVLRWLRDELL-ASEVETAKRLGVDPYDVLTQIAKRVKPGADGLIF 346
Cdd:PRK04123 312 ----------ICGQVDGSivpgligyeagqsavGDIFAWFARLLVpPEYKDEAEARGKQLLELLTEAAAKQPPGEHGLVA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 347 HPYLAGERAPLWNANARGSFFGLTLSHKKEHMIRAALEGvlynlyTVY--LALIEVMNETPKMIK---ATGGFA-KSEVW 420
Cdd:PRK04123 382 LDWFNGRRTPLADQRLKGVITGLTLGTDAPDIYRALIEA------TAFgtRAIMECFEDQGVPVEeviAAGGIArKNPVL 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446799407 421 RQMMSDIFDTELVVPESYESSCLGACVLGLKAVG---DIEDFSIV-SSMVGATnnHTPIEENVTVYQE 484
Cdd:PRK04123 456 MQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGaypDIPEAQQAmASPVEKT--YQPDPENVARYEQ 521
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
3-210 |
2.19e-15 |
|
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: 78.34 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 3 YMIGVDIGTTSTKSVL--YDEnGTFIMKhqigyDLHT-PNVDVSEENP-----DELFDAVLMTIKyvmresKVNKDDIKF 74
Cdd:cd07771 1 NYLAVDLGASSGRVILgsLDG-GKLELE-----EIHRfPNRPVEINGHlywdiDRLFDEIKEGLK------KAAEQGGDI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 75 VSFS----AQMHSLIamDQQHQRLTNNITWADNRAAKYATVINEVHDGNAIYQRTGTPIHPMSPLAKIFWMKHEWQDVFQ 150
Cdd:cd07771 69 DSIGidtwGVDFGLL--DKNGELLGNPVHYRDPRTEGMMEELFEKISKEELYERTGIQFQPINTLYQLYALKKEGPELLE 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 151 RTAKFADIKTYIFYHLFDTYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLPELVP 210
Cdd:cd07771 147 RADKLLMLPDLLNYLLTGEKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVP 206
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-79 |
7.44e-07 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 51.05 E-value: 7.44e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446799407 1 MKYMIGVDIGTTSTKSVLYDENGTFIMKHQIGYDlhtpnvdvSEENPDELFDAVLMTIKYVMRESKVNKDDIKFVSFSA 79
Cdd:COG1940 4 AGYVIGIDIGGTKIKAALVDLDGEVLARERIPTP--------AGAGPEAVLEAIAELIEELLAEAGISRGRILGIGIGV 74
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
85-206 |
1.02e-06 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 51.26 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 85 IAMDQQHQRLTNNITWADNRA-AKYATVINEVhDGNAIYQRTGTPIHPMSPLAKIFWMKHEWQDVFQRTAKFADIKTYIF 163
Cdd:PRK10640 69 VLLDKQGQRVGLPVSYRDSRTdGVMAQAQQQL-GKRDIYRRSGIQFLPFNTLYQLRALTEQQPELIAQVAHALLIPDYFS 147
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446799407 164 YHLFDTYIIDYSMASATGMFNLETLDWDVEALELLGISKEMLP 206
Cdd:PRK10640 148 YRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGAPKAWFG 190
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
5-202 |
2.57e-04 |
|
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: 43.55 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 5 IGVDIGTTSTKSVLYDENGTFI--MKHQIGYDLHTPNVDVSEENPDELFDAVLMTIKYVMRESKVNKddIKFVSFSAQMh 82
Cdd:cd07778 3 IGIDVGSTSVRIGIFDYHGTLLatSERPISYKQDPKDLWFVTQSSTEIWKAIKTALKELIEELSDYI--VSGIGVSATC- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 83 SLIAMDQQ--------------HQRLTNNIT-WADNRAAKYATVINEVHDGNAIYQRTGTPIHPMSpLAKIFWMKHEWQD 147
Cdd:cd07778 80 SMVVMQRDsdtsylvpynviheKSNPDQDIIfWMDHRASEETQWLNNILPDDILDYLGGGFIPEMA-IPKLKYLIDLIKE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 148 VFQRTAKFADIKTYIFYHL----FDTYIIDYSMASATGMFNLETLD-WDVEALELLGISK 202
Cdd:cd07778 159 DTFKKLEVFDLHDWISYMLatnlGHSNIVPVNAPPSIGIGIDGSLKgWSKDFYSKLKIST 218
|
|
| YjiL |
COG1924 |
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ... |
1-75 |
4.23e-04 |
|
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport and metabolism];
Pssm-ID: 441527 [Multi-domain] Cd Length: 264 Bit Score: 42.01 E-value: 4.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446799407 1 MKYMIGVDIGTTSTKSVLYDENGTFIMKHqigYDLHTPNvdvSEENPDELFDAVLmtikyvmRESKVNKDDIKFV 75
Cdd:COG1924 2 GMIYLGIDIGSTTTKAVLLDEDGEILASA---YLPTGGD---PLEAAKEALKELL-------EEAGLKREDIAGV 63
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
7-448 |
8.27e-04 |
|
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: 41.86 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 7 VDIGTTSTKSVLYDENGtfimkhQIGYDLHTPNVDVSE-----ENPDELFDAVLMTIKYVMRESKVnkDDIKFVSFSAqm 81
Cdd:cd07772 5 FDIGKTNKKLLLFDENG------EVLAERSTPNPEIEEdgypcEDVEAIWEWLLDSLAELAKRHRI--DAINFTTHGA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 82 hSLIAMDQQHQRLTN--NITWA---DNRAAkyatvINEVHDGnaiYQRTGTPIHP-MSPLAK-IFWMKHEWQDVFQRTAK 154
Cdd:cd07772 75 -TFALLDENGELALPvyDYEKPipdEINEA-----YYAERGP---FEETGSPPLPgGLNLGKqLYWLKREKPELFARAKT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 155 FADIKTYIFYHLFDTYIIDYSMASA-TGMFNLETLDW-DVeaLELLGISKEMLPeLVPTTYVMKGMKERYATLMGLNKDT 232
Cdd:cd07772 146 ILPLPQYWAWRLTGKAASEITSLGChTDLWDFEKNEYsSL--VKKEGWDKLFPP-LRKAWEVLGPLRPDLARRTGLPKDI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 233 PFVIGASDgvlSNLGV----NSVGKGEVAVTIGT-------SGAIRTVIDKPRTDykgrIFCYVLtedhyVIGGPvnngg 301
Cdd:cd07772 223 PVGCGIHD---SNAALlpylAAGKEPFTLLSTGTwciamnpGNDLPLTELDLARD----CLYNLD-----VFGRP----- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446799407 302 vvlrwlrdellaseVETAKRLGVDPYDVLTQIAKRVKPGADGLIFHP-YLAGERAPLWNANARGSFFGLTLSHKKEHMIR 380
Cdd:cd07772 286 --------------VKTARFMGGREYERLVERIAKSFPQLPSLADLAkLLARGTFALPSFAPGGGPFPGSGGRGVLSAFP 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446799407 381 AALEgvLYNLYTVYLAL-----IEVMNETPKMIKATGGFAKSEVWRQMMSDIF-DTELVVPESYESSCLGACVL 448
Cdd:cd07772 352 SAEE--AYALAILYLALmtdyaLDLLGSGVGRIIVEGGFAKNPVFLRLLAALRpDQPVYLSDDSEGTALGAALL 423
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
5-70 |
6.87e-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: 38.21 E-value: 6.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446799407 5 IGVDIGTTSTKSVLYDENGTFIMKHQIgydlHTPnvdvSEENPDELFDAVLMTIKYVMRESKVNKD 70
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERV----PTP----AEEGPEAVLDRIAELIEELLAEAGVRER 58
|
|
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