|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
1-455 |
0e+00 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466802 [Multi-domain] Cd Length: 499 Bit Score: 820.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 1 MAIVNTVNECITGACKKLVAVGGKVEEIITIGITNQRESTVVWDRNSGQPLVNAIIWLDNRTTSTVEELLETIPNNArni 80
Cdd:cd07792 47 MEILESVYECIEEAVEKLKALGISPSDIKAIGITNQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELSAKTPGGK--- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 81 NYLRPLCGLPLSPYFSGVKLRWLRDNVPVVSQAMEKGTAMFGTIDTWLMYNLTGGKDCGVHKTDVTNASRTMLMNIETLQ 160
Cdd:cd07792 124 DHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDDGRLLFGTVDSWLIWNLTGGKNGGVHVTDVTNASRTMLMNLRTLQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 161 WDANLLKFFGLPKTILPEICSSSEFYGSIAQGVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTGPSIV 240
Cdd:cd07792 204 WDPELCEFFGIPMSILPEIRSSSEVYGKIASGPLAGVPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 241 HSTHGLLTTVGYQLGRKAVPFYALEGSVSIAGAAFNWLRDNMNLIQNSGQIETMASTVDNSLDVYFVPAFNGLYAPYWNQ 320
Cdd:cd07792 284 FSKHGLLTTVAYKLGPDAPPVYALEGSIAIAGAAVQWLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRP 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 321 DARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAET 400
Cdd:cd07792 364 DARGTIVGLTQFTTKAHIARAALEAVCFQTREILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVET 443
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 24654573 401 TALGAAMAAYKAVENRYQMEAP-LSKSGPREAIKPSISATDRNLRYQKWKMAIDRS 455
Cdd:cd07792 444 TALGAAIAAGLAVGVWKSLDELkSLNEGGRTVFEPQISEEERERRYKRWKKAVERS 499
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
1-458 |
0e+00 |
|
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of carbohydrate kinases. [Energy metabolism, Other]
Pssm-ID: 273549 [Multi-domain] Cd Length: 493 Bit Score: 730.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 1 MAIVNTVNECITGACKKLvavGGKVEEIITIGITNQRESTVVWDRNSGQPLVNAIIWLDNRTTSTVEELLETIPnnarnI 80
Cdd:TIGR01311 47 MEIWESVLSCIAEALAKA---GIKPDDIAAIGITNQRETTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGY-----G 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 81 NYLRPLCGLPLSPYFSGVKLRWLRDNVPVVSQAMEKGTAMFGTIDTWLMYNLTGGKdcgVHKTDVTNASRTMLMNIETLQ 160
Cdd:TIGR01311 119 EFIREKTGLPLDPYFSATKLRWLLDNVPGVREAAERGELLFGTIDTWLIWNLTGGK---VHVTDVTNASRTMLFNIHTLD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 161 WDANLLKFFGLPKTILPEICSSSEFYGSIAQG-VLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTGPSI 239
Cdd:TIGR01311 196 WDDELLELFGIPREILPEVRSSSEVYGYTDPGlLGAEIPITGVLGDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 240 VHSTHGLLTTVGYQLGRKAvPFYALEGSVSIAGAAFNWLRDNMNLIQNSGQIETMASTVDNSLDVYFVPAFNGLYAPYWN 319
Cdd:TIGR01311 276 VISKHGLLTTVAYQLGGKK-PVYALEGSVFVAGAAVQWLRDNLKLIKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWD 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 320 QDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAE 399
Cdd:TIGR01311 355 PDARGAIFGLTRGTTKAHIARAALEAIAFQTRDVLEAMEKDAGVEITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTE 434
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 400 TTALGAAMAAYKAVE-NRYQMEAPLSKSGPReAIKPSISATDRNLRYQKWKMAIDRSLNW 458
Cdd:TIGR01311 435 TTALGAAYAAGLAVGyWKSLEEIEALWRVEK-TFEPEMDEEEREARYAGWKEAVKRSLGW 493
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
1-459 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 655.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 1 MAIVNTVNECITGAckkLVAVGGKVEEIITIGITNQRESTVVWDRNSGQPLVNAIIWLDNRTTSTVEELletipNNARNI 80
Cdd:COG0554 49 EEIWESVLAVIREA---LAKAGISAEDIAAIGITNQRETTVVWDRKTGKPLYNAIVWQDRRTADICEEL-----KADGLE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 81 NYLRPLCGLPLSPYFSGVKLRWLRDNVPVVSQAMEKGTAMFGTIDTWLMYNLTGGKdcgVHKTDVTNASRTMLMNIETLQ 160
Cdd:COG0554 121 DLIREKTGLVLDPYFSATKIKWILDNVPGARERAEAGELLFGTIDSWLIWKLTGGK---VHVTDVTNASRTMLFNIHTLD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 161 WDANLLKFFGLPKTILPEICSSSEFYGSIAQGVL-QGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTGPSI 239
Cdd:COG0554 198 WDDELLELFGIPRSMLPEVRPSSEVFGETDPDLFgAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEP 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 240 VHSTHGLLTTVGYQLGRKAVpfYALEGSVSIAGAAFNWLRDNMNLIQNSGQIETMASTVDNSLDVYFVPAFNGLYAPYWN 319
Cdd:COG0554 278 VRSKNGLLTTIAWGLGGKVT--YALEGSIFVAGAAVQWLRDGLGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWD 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 320 QDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAE 399
Cdd:COG0554 356 PDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTE 435
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 400 TTALGAAMAAYKAVENRYQMEAPLSKSGPREAIKPSISATDRNLRYQKWKMAIDRSLNWE 459
Cdd:COG0554 436 TTALGAAYLAGLAVGFWKSLEELAALWKVDRRFEPQMDEEERERLYAGWKKAVERTLGWA 495
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
1-452 |
0e+00 |
|
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466789 [Multi-domain] Cd Length: 486 Bit Score: 632.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 1 MAIVNTVNECITGAckkLVAVGGKVEEIITIGITNQRESTVVWDRNSGQPLVNAIIWLDNRTTSTVEELletipNNARNI 80
Cdd:cd07769 46 EEIWENTLEVIREA---LAKAGISASDIAAIGITNQRETTVVWDKKTGKPLYNAIVWQDRRTADICEEL-----KAKGLE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 81 NYLRPLCGLPLSPYFSGVKLRWLRDNVPVVSQAMEKGTAMFGTIDTWLMYNLTGGKdcgVHKTDVTNASRTMLMNIETLQ 160
Cdd:cd07769 118 ERIREKTGLPLDPYFSATKIKWILDNVPGARERAERGELLFGTIDTWLIWKLTGGK---VHVTDVTNASRTMLFNIHTLE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 161 WDANLLKFFGLPKTILPEICSSSEFYGSI-AQGVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTGPSI 239
Cdd:cd07769 195 WDDELLELFGIPRSMLPEVRPSSEVFGYTdPEGLGAGIPIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 240 VHSTHGLLTTVGYQLGRKAVpfYALEGSVSIAGAAFNWLRDNMNLIQNSGQIETMASTVDNSLDVYFVPAFNGLYAPYWN 319
Cdd:cd07769 275 VPSKNGLLTTIAWQIGGKVT--YALEGSIFIAGAAIQWLRDNLGLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 320 QDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAE 399
Cdd:cd07769 353 PDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAE 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 24654573 400 TTALGAAMAAYKAVENrYQMEAPLSKSGPREAI-KPSISATDRNLRYQKWKMAI 452
Cdd:cd07769 433 TTALGAAYLAGLAVGF-WKDLDELASLWQVDKRfEPSMDEEERERLYRGWKKAV 485
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
1-459 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 619.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 1 MAIVNTVNECITGACKKLVAVGGKVEeIITIGITNQRESTVVWDRNSGQPLVNAIIWLDNRTTSTVEELLETIPNNarni 80
Cdd:PTZ00294 48 EEILRNVYKCMNEAIKKLREKGPSFK-IKAIGITNQRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKYGGS---- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 81 NYLRPLCGLPLSPYFSGVKLRWLRDNVPVVSQAMEKGTAMFGTIDTWLMYNLTGGKdcgVHKTDVTNASRTMLMNIETLQ 160
Cdd:PTZ00294 123 NFFQKITGLPISTYFSAFKIRWMLENVPAVKDAVKEGTLLFGTIDTWLIWNLTGGK---SHVTDVTNASRTFLMNIKTLK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 161 WDANLLKFFGLPKTILPEICSSSEFYGSI---AQGVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTGP 237
Cdd:PTZ00294 200 WDEELLNKFGIPKETLPEIKSSSENFGTIsgeAVPLLEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGT 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 238 SIVHSTHGLLTTVGYQLGRKAVPFYALEGSVSIAGAAFNWLRDNMNLIQNSGQIETMASTVDNSLDVYFVPAFNGLYAPY 317
Cdd:PTZ00294 280 EIVFSKHGLLTTVCYQLGPNGPTVYALEGSIAVAGAGVEWLRDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPY 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 318 WNQDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKI 397
Cdd:PTZ00294 360 WRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEM 439
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24654573 398 AETTALGAAMAA------YKAVEnryqmEAPLSKSGPREAIKPSISATDRNLRYQKWKMAIDRSLNWE 459
Cdd:PTZ00294 440 AETTALGAALLAglavgvWKSLE-----EVKKLIRRSNSTFSPQMSAEERKAIYKEWNKAVERSLKWA 502
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
1-458 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 603.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 1 MAIVNTVNECITGACKKLVAVGGKVEEII-TIGITNQRESTVVWDRNSGQPLVNAIIWLDNRTTSTVEELLETIPNNARN 79
Cdd:PLN02295 46 MEILESVLTCIAKALEKAAAKGHNVDSGLkAIGITNQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKELSGGRKH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 80 inyLRPLCGLPLSPYFSGVKLRWLRDNVPVVSQAMEKGTAMFGTIDTWLMYNLTGGKDCGVHKTDVTNASRTMLMNIETL 159
Cdd:PLN02295 126 ---FVETCGLPISTYFSATKLLWLLENVDAVKEAVKSGDALFGTIDSWLIWNLTGGASGGVHVTDVTNASRTMLMNLKTL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 160 QWDANLLKFFGLPKTILPEICSSSEFYGSIAQGV-LQGIGITSVLGDQQAALVGQQClAKGQAKATYGTGCFLLYNTGPS 238
Cdd:PLN02295 203 DWDKPTLEALGIPAEILPKIVSNSEVIGTIAKGWpLAGVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEE 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 239 IVHSTHGLLTTVGYQLGRKAVPFYALEGSVSIAGAAFNWLRDNMNLIQNSGQIETMASTVDNSLDVYFVPAFNGLYAPYW 318
Cdd:PLN02295 282 VVPSKHGLLTTVAYKLGPDAPTNYALEGSVAIAGAAVQWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRW 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 319 NQDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMHKDCKIP-----LAKLMVDGGMTVNNLFLQLQSDLVGIQVL 393
Cdd:PLN02295 362 RDDARGVCVGITRFTNKAHIARAVLESMCFQVKDVLDAMRKDAGEEkshkgLFLLRVDGGATANNLLMQIQADLLGSPVV 441
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24654573 394 RAKIAETTALGAAMAAYKAVeNRYQMEAPLSKSGPREAIK--PSISATDRNLRYQKWKMAIDRSLNW 458
Cdd:PLN02295 442 RPADIETTALGAAYAAGLAV-GLWTEEEIFASEKWKNTTTfrPKLDEEERAKRYASWCKAVERSFDL 507
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
1-453 |
0e+00 |
|
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases
Pssm-ID: 198361 [Multi-domain] Cd Length: 486 Bit Score: 597.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 1 MAIVNTVNECITGACKKlvaVGGKVEEIITIGITNQRESTVVWDRNSGQPLVNAIIWLDNRTTSTVEELLEtipnnARNI 80
Cdd:cd07786 46 EEIWESQLAVAREALAK---AGIRASDIAAIGITNQRETTVVWDRETGKPVYNAIVWQDRRTADICEELKA-----EGHE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 81 NYLRPLCGLPLSPYFSGVKLRWLRDNVPVVSQAMEKGTAMFGTIDTWLMYNLTGGKdcgVHKTDVTNASRTMLMNIETLQ 160
Cdd:cd07786 118 EMIREKTGLVLDPYFSATKIRWILDNVPGARERAERGELAFGTIDSWLIWKLTGGK---VHATDVTNASRTMLFNIHTLE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 161 WDANLLKFFGLPKTILPEICSSSEFYGSIAQGVL-QGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTGPSI 239
Cdd:cd07786 195 WDDELLELFGIPASMLPEVKPSSEVFGYTDPDLLgAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 240 VHSTHGLLTTVGYQLGRKAVpfYALEGSVSIAGAAFNWLRDNMNLIQNSGQIETMASTVDNSLDVYFVPAFNGLYAPYWN 319
Cdd:cd07786 275 VRSKNGLLTTIAWQLGGKVT--YALEGSIFIAGAAVQWLRDGLGLIESAAETEALARSVPDNGGVYFVPAFTGLGAPYWD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 320 QDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAE 399
Cdd:cd07786 353 PDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTE 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24654573 400 TTALGAAMAA---------YKAVENRYQMEaplsksgprEAIKPSISATDRNLRYQKWKMAID 453
Cdd:cd07786 433 TTALGAAYLAglavglwksLDELAKLWQVD---------RRFEPSMSEEEREALYAGWKKAVK 486
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
1-459 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 596.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 1 MAIVNTVNECITGAckkLVAVGGKVEEIITIGITNQRESTVVWDRNSGQPLVNAIIWLDNRTTSTVEELLEtipnnARNI 80
Cdd:PRK00047 51 NEIWASQLSVIAEA---LAKAGISPDQIAAIGITNQRETTVVWDKETGRPIYNAIVWQDRRTADICEELKR-----DGYE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 81 NYLRPLCGLPLSPYFSGVKLRWLRDNVPVVSQAMEKGTAMFGTIDTWLMYNLTGGKdcgVHKTDVTNASRTMLMNIETLQ 160
Cdd:PRK00047 123 DYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGELLFGTIDTWLVWKLTGGK---VHVTDYTNASRTMLFNIHTLD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 161 WDANLLKFFGLPKTILPEICSSSEFYGSIAQG--VLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTGPS 238
Cdd:PRK00047 200 WDDELLELLDIPRSMLPEVRPSSEVYGKTNPYgfFGGEVPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 239 IVHSTHGLLTTVGYQLGRKAVpfYALEGSVSIAGAAFNWLRDNMNLIQNSGQIETMASTVDNSLDVYFVPAFNGLYAPYW 318
Cdd:PRK00047 280 AVKSENGLLTTIAWGIDGKVV--YALEGSIFVAGSAIQWLRDGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYW 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 319 NQDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIA 398
Cdd:PRK00047 358 DSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVA 437
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24654573 399 ETTALGAAMAAYKAV---ENRYQMEaplSKSGPREAIKPSISATDRNLRYQKWKMAIDRSLNWE 459
Cdd:PRK00047 438 ETTALGAAYLAGLAVgfwKDLDELK---EQWKIDRRFEPQMDEEEREKLYAGWKKAVKRTLAWA 498
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
2-452 |
1.18e-135 |
|
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: 400.40 E-value: 1.18e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 2 AIVNTVNECITGAckklvavGGKVEEIITIGITNQRESTVVWDRNSGQPLVNAIIWLDNRTTSTVEELletipNNARNIN 81
Cdd:cd07793 51 QFVKVIKEALKNA-------GLTPEDIAAIGISTQRNTFLTWDKKTGKPLHNFITWQDLRAAELCESW-----NRSLLLK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 82 YLRPLCG----------------LPLSPYFSGVKLRWLRDNVPVVSQAMEKGTAMFGTIDTWLMYNLTGGKdcgVHKTDV 145
Cdd:cd07793 119 ALRGGSKflhfltrnkrflaasvLKFSTAHVSIRLLWILQNNPELKEAAEKGELLFGTIDTWLLWKLTGGK---VHATDY 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 146 TNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSSSEFYGSIAQGVLQG-IGITSVLGDQQAALVGQQCLAKGQAKAT 224
Cdd:cd07793 196 SNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFGSTDPSIFGAeIPITAVVADQQAALFGECCFDKGDVKIT 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 225 YGTGCFLLYNTGPSIVHSTHGLLTTVGYQLGRKAVpfYALEGSVSIAGAAFNWLRDnMNLIQNSGQIETMASTVDNSLDV 304
Cdd:cd07793 276 MGTGTFIDINTGSKPHASVKGLYPLVGWKIGGEIT--YLAEGNASDTGTVIDWAKS-IGLFDDPSETEDIAESVEDTNGV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 305 YFVPAFNGLYAPYWNQDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQ 384
Cdd:cd07793 353 YFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLI 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24654573 385 SDLVGIQVLRAKIAETTALGAAMAAYKAVENRYQMEApLSKSGPREAI-KPSISATDRNLRYQKWKMAI 452
Cdd:cd07793 433 ADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEE-LKKLRKIEKIfEPKMDNEKREELYKNWKKAV 500
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
9-409 |
3.85e-83 |
|
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: 265.16 E-value: 3.85e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 9 ECITGACKKLVA-VGGKVEEIITIGITNQRESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETIPNNArninyLRPLC 87
Cdd:COG1070 51 EAVVEAIRELLAkAGVDPEEIAAIGVSGQMHGLVLLDAD-GEPLRPAILWNDTRAAAEAAELREELGEEA-----LYEIT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 88 GLPLSPYFSGVKLRWLRDNVP-VVSQamekgTAMFGTIDTWLMYNLTGgkdcgVHKTDVTNASRTMLMNIETLQWDANLL 166
Cdd:COG1070 125 GNPLHPGFTAPKLLWLKENEPeIFAR-----IAKVLLPKDYLRYRLTG-----EFVTDYSDASGTGLLDVRTRDWSDELL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 167 KFFGLPKTILPEICSSSEFYG----SIAQ--GVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTgPSIV 240
Cdd:COG1070 195 EALGIDRELLPELVPPGEVAGtltaEAAAetGLPAGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVS-DKPL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 241 HSTHGLLTTVGYQLGRKavpfYALEGSVSIAGAAFNWLRDNMNLIQNS--GQIETMASTVD-NSLDVYFVPAFNGLYAPY 317
Cdd:COG1070 274 PDPEGRVHTFCHAVPGR----WLPMGATNNGGSALRWFRDLFADGELDdyEELNALAAEVPpGADGLLFLPYLSGERTPH 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 318 WNQDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMhKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKI 397
Cdd:COG1070 350 WDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEAL-EEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEA 428
|
410
....*....|..
gi 24654573 398 AETTALGAAMAA 409
Cdd:COG1070 429 EEGGALGAALLA 440
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
9-413 |
4.42e-77 |
|
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: 247.43 E-value: 4.42e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 9 ECITGACKKLVA-VGGKVEEIITIGITNQRESTVVWDRNsGQPLVNAIIWLDNRTtstveelletipnnarninylrplc 87
Cdd:cd07779 50 DALCEALKEAVAkAGVDPEDIAAIGLTSQRSTFVPVDED-GRPLRPAISWQDKRT------------------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 88 glplspyfsgvklrwlrdnvpvvsqamekgtAMFGTIDTWLMYNLTGgkdcgVHKTDVTNASRTMLMNIETLQWDANLLK 167
Cdd:cd07779 104 -------------------------------AKFLTVQDYLLYRLTG-----EFVTDTTSASRTGLPDIRTRDWSDDLLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 168 FFGLPKTILPEICSSSEFYGSI----AQ--GVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTGPSIVH 241
Cdd:cd07779 148 AFGIDRDKLPELVPPGTVIGTLtkeaAEetGLPEGTPVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVED 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 242 STHGLLTTVGyqlgrkAVPF-YALEGSVSIAGAAFNWLRDNM--NLIQNSGQ-------IETMASTVDN-SLDVYFVPAF 310
Cdd:cd07779 228 PERRIPCNPS------AVPGkWVLEGSINTGGSAVRWFRDEFgqDEVAEKELgvspyelLNEEAAKSPPgSDGLLFLPYL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 311 NGLYAPYWNQDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMhKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGI 390
Cdd:cd07779 302 AGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELRDNLEAM-EKAGVPIEEIRVSGGGSKSDLWNQIIADVFGR 380
|
410 420
....*....|....*....|...
gi 24654573 391 QVLRAKIAETTALGAAMAAYKAV 413
Cdd:cd07779 381 PVERPETSEATALGAAILAAVGA 403
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
2-413 |
6.95e-74 |
|
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: 239.41 E-value: 6.95e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 2 AIVNTVNECITGACKKLvavggKVEEIITIGITNQRESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETIPNNArnin 81
Cdd:cd07773 47 ELWEAVKEAIREAAAQA-----GPDPIAAISVSSQGESGVPVDRD-GEPLGPAIVWFDPRGKEEAEELAERIGAEE---- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 82 yLRPLCGLPLSPYFSGVKLRWLRDNVPVVSQAMEKgtamFGTIDTWLMYNLTGgkdcgVHKTDVTNASRTMLMNIETLQW 161
Cdd:cd07773 117 -LYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAK----WLSVADYIAYRLTG-----EPVTDYSLASRTMLFDIRKRTW 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 162 DANLLKFFGLPKTILPEICSSSEFYGSIAQGVLQGIGITS----VLG--DQQAALVGQQCLAKGQAkaTYGTG---CFLL 232
Cdd:cd07773 187 SEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEELGLPAgtpvVVGghDHLCAALGAGVIEPGDV--LDSTGtaeALLA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 233 YNTGPSIVHSTHGLLTTVGYQLGRKavpFYALEGSVSiAGAAFNWLRDNM--NLIQNSGQIETMASTVDNSLDVYFVPAF 310
Cdd:cd07773 265 VVDEPPLDEMLAEGGLSYGHHVPGG---YYYLAGSLP-GGALLEWFRDLFggDESDLAAADELAEAAPPGPTGLLFLPHL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 311 NGLYAPYWNQDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMhKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGI 390
Cdd:cd07773 341 SGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEAL-EKAGIPIDEIRAVGGGARSPLWLQLKADILGR 419
|
410 420
....*....|....*....|...
gi 24654573 391 QVLRAKIAETTALGAAMAAYKAV 413
Cdd:cd07773 420 PIEVPEVPEATALGAALLAGVGA 442
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
2-409 |
4.42e-69 |
|
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: 225.14 E-value: 4.42e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 2 AIVNTVNECITGAckklvavGGKVEEIITIGITNQRESTVVWDRNsGQPLVNAIIWLDNRttstveelletipnnarnin 81
Cdd:cd00366 51 AVVEAIREVLAKA-------GIDPSDIAAIGISGQMPGVVLVDAD-GNPLRPAIIWLDRR-------------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 82 ylrplcglplspyfsgvklrwlrdnvpvvsqamekgtAMFGTIDTWLMYNLTGgkdcgVHKTDVTNASRTMLMNIETLQW 161
Cdd:cd00366 103 -------------------------------------AKFLQPNDYIVFRLTG-----EFAIDYSNASGTGLYDIKTGDW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 162 DANLLKFFGLPKTILPEICSSSEFYGSIAQ------GVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNT 235
Cdd:cd00366 141 SEELLDALGIPREKLPPIVESGEVVGRVTPeaaeetGLPAGTPVVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 236 gPSIVHSTHGLLTTVGYQLGRkavpfYALEGSVSIAGAAFNWLRDN----MNLIQNSGQIETMASTVD-NSLDVYFVPAF 310
Cdd:cd00366 221 -DEPVPPDPRLLNRCHVVPGL-----WLLEGAINTGGASLRWFRDEfgeeEDSDAEYEGLDELAAEVPpGSDGLIFLPYL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 311 NGLYAPYWNQDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMhKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGI 390
Cdd:cd00366 295 SGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEIL-EELGVKIKEIRVTGGGAKSRLWNQIKADVLGV 373
|
410
....*....|....*....
gi 24654573 391 QVLRAKIAETTALGAAMAA 409
Cdd:cd00366 374 PVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
14-410 |
1.77e-67 |
|
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: 223.57 E-value: 1.77e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 14 ACKKLVA-VGGKVEEIITIGITNQRESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETIPNNARNINYLRPLCGLPLS 92
Cdd:cd07808 55 ALRELLAkAGISPSDIAAIGLTGQMHGLVLLDKN-GRPLRPAILWNDQRSAAECEELEARLGDEILIITGNPPLPGFTLP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 93 pyfsgvKLRWLRDNVPvvsQAMEKgtamfgtIDTWLM------YNLTGgkdcgVHKTDVTNASRTMLMNIETLQWDANLL 166
Cdd:cd07808 134 ------KLLWLKENEP---EIFAR-------IRKILLpkdylrYRLTG-----ELATDPSDASGTLLFDVEKREWSEELL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 167 KFFGLPKTILPEICSSSEFYGSIAQGVLQGIGI---TSVL---GDQQAALVGQQCLAKGQAKATYGTGCFLLYNTgPSIV 240
Cdd:cd07808 193 EALGLDPSILPPIVESTEIVGTLTPEAAEELGLpegTPVVagaGDNAAAALGAGVVEPGDALISLGTSGVVFAPT-DKPV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 241 HSTHGLLTTVGYqlgrkAVP--FYALeGSVSIAGAAFNWLRDNMNLIQNS-GQIETMASTVDNSLD-VYFVPAFNGLYAP 316
Cdd:cd07808 272 PDPKGRLHTFPH-----AVPgkWYAM-GVTLSAGLSLRWLRDLFGPDRESfDELDAEAAKVPPGSEgLLFLPYLSGERTP 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 317 YWNQDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMhKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAK 396
Cdd:cd07808 346 YWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVL-KELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPA 424
|
410
....*....|....
gi 24654573 397 IAETTALGAAMAAY 410
Cdd:cd07808 425 EEEGSAYGAALLAA 438
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
2-448 |
6.06e-60 |
|
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: 203.94 E-value: 6.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 2 AIVNTVNECITGACKKLvavggKVEEIITIGITNQRESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETipNNARNIn 81
Cdd:cd07770 47 EILEAVLEALKEVLAKL-----GGGEVDAIGFSSAMHSLLGVDED-GEPLTPVITWADTRAAEEAERLRKE--GDGSEL- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 82 YLRPLCglPLSPYFSGVKLRWLRDNVPVVSQAmekgTAMFGTIDTWLMYNLTGgkdcgVHKTDVTNASRTMLMNIETLQW 161
Cdd:cd07770 118 YRRTGC--PIHPMYPLAKLLWLKEERPELFAK----AAKFVSIKEYLLYRLTG-----ELVTDYSTASGTGLLNIHTLDW 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 162 DANLLKFFGLPKTILPEICSSSEFYGSIAQGVLQGIGITS----VLG--DQQAALVGQQCLAKGQAKATYGTGCFLLYNT 235
Cdd:cd07770 187 DEEALELLGIDEEQLPELVDPTEVLPGLKPEFAERLGLLAgtpvVLGasDGALANLGSGALDPGRAALTVGTSGAIRVVS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 236 GPSIVHSTHGLLTtvgYQLGRKavpFYALEGSVSIAGAAFNWLRDNMNLIQNS-GQIETMASTVDN-SLDVYFVPAFNGL 313
Cdd:cd07770 267 DRPVLDPPGRLWC---YRLDEN---RWLVGGAINNGGNVLDWLRDTLLLSGDDyEELDKLAEAVPPgSHGLIFLPYLAGE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 314 YAPYWNQDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMhKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVL 393
Cdd:cd07770 341 RAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEAL-EELAGPVKEIRASGGFLRSPLWLQILADVLGRPVL 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 24654573 394 RAKIAETTALGAAMAAYKAVeNRYQMEAPLSKSGPREAIKPSISATDrnlRYQKW 448
Cdd:cd07770 420 VPEEEEASALGAALLALEAL-GLISSLEADELVKIGKVVEPDPENHA---IYAEL 470
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
1-212 |
2.52e-57 |
|
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: 189.86 E-value: 2.52e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 1 MAIVNTVNECITGACKKLvavGGKVEEIITIGITNQRESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETIpnnarNI 80
Cdd:pfam00370 46 DEIWQAVAQCIAKTLSQL---GISLKQIKGIGISNQGHGTVLLDKN-DKPLYNAILWKDRRTAEIVENLKEEG-----NN 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 81 NYLRPLCGLPLSPYFSGVKLRWLRDNVPVVSQAMEKgtamFGTIDTWLMYNLTGgkdcgVHKTDVTNASRTMLMNIETLQ 160
Cdd:pfam00370 117 QKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHK----FLTIHDYLRWRLTG-----VFVTDHTNASRSMMFNIHKLD 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24654573 161 WDANLLKFFGLPKTILPEICSSSEFYG----SIAQ--GVLQGIGITSVLGDQQAALVG 212
Cdd:pfam00370 188 WDPELLAALGIPRDHLPPLVESSEIYGelnpELAAmwGLDEGVPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
11-413 |
4.70e-57 |
|
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: 196.20 E-value: 4.70e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 11 ITGACKKLVA-VGGKVEEIITIGITNQRESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETIPNnarnINYLRPLCGL 89
Cdd:cd07805 52 VCRATRALLEkSGIDPSDIAAIAFSGQMQGVVPVDKD-GNPLRNAIIWSDTRAAEEAEEIAGGLGG----IEGYRLGGGN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 90 PLSPYFSGVKLRWLRDNVPvvsQAMEKGTAMFGTIDtWLMYNLTGgkdcgVHKTDVTNASRTMLMNIETLQWDANLLKFF 169
Cdd:cd07805 127 PPSGKDPLAKILWLKENEP---EIYAKTHKFLDAKD-YLNFRLTG-----RAATDPSTASTTGLMDLRKRRWSEELLRAA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 170 GLPKTILPEICSSSEFYGSIAQGVLQGIGI---TSVL---GDQQAALVGQQCLAKGQAKATYGTGCFLLYNTGPSIVHST 243
Cdd:cd07805 198 GIDPDKLPELVPSTEVVGELTPEAAAELGLpagTPVVgggGDAAAAALGAGAVEEGDAHIYLGTSGWVAAHVPKPKTDPD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 244 HGLLTTVGyqlgrkAVP-FYALEGSVSIAGAAFNWLRDNMNLIQNSGQ-----IETMASTVD-NSLDVYFVPAFNGLYAP 316
Cdd:cd07805 278 HGIFTLAS------ADPgRYLLAAEQETAGGALEWARDNLGGDEDLGAddyelLDELAAEAPpGSNGLLFLPWLNGERSP 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 317 YWNQDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMHKDCKiPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAK 396
Cdd:cd07805 352 VEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVPE 430
|
410
....*....|....*...
gi 24654573 397 IA-ETTALGAAMAAYKAV 413
Cdd:cd07805 431 NPqEAGALGAALLAAVGL 448
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
15-413 |
3.73e-53 |
|
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: 185.04 E-value: 3.73e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 15 CKKLVAVGG-KVEEIITIGITNQRESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETIPNNArninyLRPLCGLPLSP 93
Cdd:cd07804 56 IRELLAKAGiSPKEIAAIGVSGLVPALVPVDEN-GKPLRPAILYGDRRATEEIEWLNENIGEDR-----IFEITGNPLDS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 94 YFSGVKLRWLRDNVPVVSqameKGTAMFGTIDTWLMYNLTGgkdcgVHKTDVTNASRTM-LMNIETLQWDANLLKFFGLP 172
Cdd:cd07804 130 QSVGPKLLWIKRNEPEVF----KKTRKFLGAYDYIVYKLTG-----EYVIDYSSAGNEGgLFDIRKRTWDEELLEALGID 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 173 KTILPEICSSSEFYGSI------AQGVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGT-GCFLLYNTGPsivHSTHG 245
Cdd:cd07804 201 PDLLPELVPSTEIVGEVtkeaaeETGLAEGTPVVAGTVDAAASALSAGVVEPGDLLLMLGTaGDIGVVTDKL---PTDPR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 246 LLTTVGYQLGRkavpfYALEGSVSIAGAAFNWLRDNMNLIQNSGQIETMASTVDnSLD------------VYFVPAFNGL 313
Cdd:cd07804 278 LWLDYHDIPGT-----YVLNGGMATSGSLLRWFRDEFAGEEVEAEKSGGDSAYD-LLDeeaekippgsdgLIVLPYFMGE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 314 YAPYWNQDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMHKDCkIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVL 393
Cdd:cd07804 352 RTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYGLRHHLEVIREAG-LPIKRLVAVGGGAKSPLWRQIVADVTGVPQE 430
|
410 420
....*....|....*....|
gi 24654573 394 RAKIAETTALGAAMAAYKAV 413
Cdd:cd07804 431 YVKDTVGASLGDAFLAGVGV 450
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
221-412 |
6.24e-52 |
|
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: 174.05 E-value: 6.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 221 AKATYGTGCFLLYnTGPSIVHSTHGLLTTVGYQLGRkavPFYALEGSVSIAGAAFNWLRDNMNL---IQNSGQIETMAST 297
Cdd:pfam02782 1 LAISAGTSSFVLV-ETPEPVLSVHGVWGPYTNEMLP---GYWGLEGGQSAAGSLLAWLLQFHGLreeLRDAGNVESLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 298 VDNSLD-----VYFVPAFNGLYAPYWNQDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMHKDCKIPLAKLMVDG 372
Cdd:pfam02782 77 AALAAVapaggLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24654573 373 GMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKA 412
Cdd:pfam02782 157 GGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
9-413 |
1.07e-46 |
|
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: 167.73 E-value: 1.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 9 ECITGACKKLvavGGKVEEIITIGITNQRESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETIPNNArninyLRPLCG 88
Cdd:cd07802 54 EAIRELLEKS---GVDPSDIAGVGVTGHGNGLYLVDKD-GKPVRNAILSNDSRAADIVDRWEEDGTLEK-----VYPLTG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 89 LPLSPYFSGVKLRWLRDNVP-VVSQAmekGTAMFGTiDtWLMYNLTGgkdcgVHKTDVTNASrTMLMNIETLQWDANLLK 167
Cdd:cd07802 125 QPLWPGQPVALLRWLKENEPeRYDRI---RTVLFCK-D-WIRYRLTG-----EISTDYTDAG-SSLLDLDTGEYDDELLD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 168 FFGLP--KTILPEICSSSEFYGSI------AQGVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTgcfllynTGPSI 239
Cdd:cd07802 194 LLGIEelKDKLPPLVPSTEIAGRVtaeaaaLTGLPEGTPVAAGAFDVVASALGAGAVDEGQLCVILGT-------WSINE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 240 VHSTHGLLTTVGYQLGRKAVP--FYALEGSVSIAGAaFNWLRDN-MNLIQNSGQI------ETMASTVDNSLDVYFVPaF 310
Cdd:cd07802 267 VVTDEPVVPDSVGSNSLHADPglYLIVEASPTSASN-LDWFLDTlLGEEKEAGGSdydeldELIAAVPPGSSGVIFLP-Y 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 311 ngLYAPYWNQDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMHKDCKIPLAKLMvdGGMTVNNLFLQLQSDLVGI 390
Cdd:cd07802 345 --LYGSGANPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLVARKPETIRLT--GGGARSPVWAQIFADVLGL 420
|
410 420
....*....|....*....|...
gi 24654573 391 QVLRAKIAETTALGAAMAAYKAV 413
Cdd:cd07802 421 PVEVPDGEELGALGAAICAAVAA 443
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
11-409 |
1.02e-42 |
|
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: 157.00 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 11 ITGACKKLVAVGGKV-EEIITIGITNQRESTVVWDRNSgqplvNAIIWLDNRTTSTVEELLEtIPNNARNINYLRPlcGL 89
Cdd:cd07798 54 ICEAIREALKKAGISpEDISAVSSTSQREGIVFLDKDG-----RELYAGPNIDARGVEEAAE-IDDEFGEEIYTTT--GH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 90 PLSPYFSGVKLRWLRDNVPvvsQAMEKgTAMFGTIDTWLMYNLtggkdCGVHKTDVTNASRTMLMNIETLQWDANLLKFF 169
Cdd:cd07798 126 WPTELFPAARLLWFKENRP---EIFER-IATVLSISDWIGYRL-----TGELVSEPSQASETQLFDIKKREWSQELLEAL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 170 GLPKTILPEICSSSEFYGSIAQGVLQGIGITS----VLG--DQQAALVGQQCLAKGQAKATYGTgcfllynTGPsIVHST 243
Cdd:cd07798 197 GLPPEILPEIVPSGTVLGTVSEEAARELGLPEgtpvVVGgaDTQCALLGSGAIEPGDIGIVAGT-------TTP-VQMVT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 244 HGLLTTVGYQL--GRKAVP-FYALEGSVSIAGAAFNWLRDNMNLIQNS--GQIETMASTVD-NSLDVYfvpAFNGLYAPy 317
Cdd:cd07798 269 DEPIIDPERRLwtGCHLVPgKWVLESNAGVTGLNYQWLKELLYGDPEDsyEVLEEEASEIPpGANGVL---AFLGPQIF- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 318 wNQDARGVICGL--------SEETTSEHIVRATLEAVCFQVRDILDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVG 389
Cdd:cd07798 345 -DARLSGLKNGGflfptplsASELTRGDFARAILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLG 423
|
410 420
....*....|....*....|
gi 24654573 390 IQVLRAKIAETTALGAAMAA 409
Cdd:cd07798 424 KPVLVPEGREASALGAAICA 443
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
11-409 |
1.05e-37 |
|
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: 142.75 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 11 ITGACKKLVAvGGKVEEIITIGITNQRESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETIPnnarninYLRPLCGLP 90
Cdd:cd07783 52 LRSLLRELPA-ELRPRRVVAIAVDGTSGTLVLVDRE-GEPLRPAIMYNDARAVAEAEELAEAAG-------AVAPRTGLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 91 LSPYFSGVKLRWLRDNVP--------VVSQAmekgtamfgtidTWLMYNLTGgkDCGVhkTDVTNASRTMLmNIETLQWD 162
Cdd:cd07783 123 VSPSSSLAKLLWLKRHEPevlaktakFLHQA------------DWLAGRLTG--DRGV--TDYNNALKLGY-DPETGRWP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 163 ANLLKFFGLPKTILPEICSSSEFYGSIAQGVLQGIGITS----VLG--DQQAALVGQQCLAKGQAKATYGTG-CFLLYNT 235
Cdd:cd07783 186 SWLLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLPAgtpvVAGttDSIAAFLASGAVRPGDAVTSLGTTlVLKLLSD 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 236 GPsIVHSTHGLlttvgYQLgRKAVPFYALEGSVSIAGAAFNWLRDNMNLIQNSGQIETMASTvdnSLDVYfvP-AFNGLY 314
Cdd:cd07783 266 KR-VPDPGGGV-----YSH-RHGDGYWLVGGASNTGGAVLRWFFSDDELAELSAQADPPGPS---GLIYY--PlPLRGER 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 315 APYWNQDARGVIcgLSEETTSEHIVRATLEAVCFQVRDILDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLR 394
Cdd:cd07783 334 FPFWDPDARGFL--LPRPHDRAEFLRALLEGIAFIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVI 411
|
410
....*....|....*
gi 24654573 395 AKIaETTALGAAMAA 409
Cdd:cd07783 412 AEE-EEAALGAALLA 425
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
3-409 |
6.94e-35 |
|
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: 135.04 E-value: 6.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 3 IVNTVNECITGACKKLVAvggkveEIITIGITNQRESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETIPNNarniny 82
Cdd:cd07777 51 ILEAVRNLIDELPREYLS------DVTGIGITGQMHGIVLWDED-GNPVSPLITWQDQRCSEEFLGGLSTYGEE------ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 83 LRPLCGLPLSPYFSGVKLRWLRDNVPVVSQAmekgtAMFGTIDTWLMYNLTGGKDcgvHKTDVTNASRTMLMNIETLQWD 162
Cdd:cd07777 118 LLPKSGMRLKPGYGLATLFWLLRNGPLPSKA-----DRAGTIGDYIVARLTGLPK---PVMHPTNAASWGLFDLETGTWN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 163 ANLLKFFGLPKTILPEICSSSEFYGSIAQGVLQGIGITSVLGDQQAALVGqqCLAKGQAKA--TYGTGCFLlyntgpSIV 240
Cdd:cd07777 190 KDLLEALGLPVILLPEIVPSGEIVGTLSSALPKGIPVYVALGDNQASVLG--SGLNEENDAvlNIGTGAQL------SFL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 241 hsTHGLLTTVGYQLgrkaVPFYalEGSV-----SI-AGAAFNWL----RDNMNLI---QNSGQI-ETMASTVDNSL--DV 304
Cdd:cd07777 262 --TPKFELSGSVEI----RPFF--DGRYllvaaSLpGGRALAVLvdflREWLRELggsLSDDEIwEKLDELAESEEssDL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 305 YFVPAFNGlyaPYWNQDARGVICGLSEETTS-EHIVRATLEAVCFQVRDILDSMHKDcKIPLAKLMVDGGMTVNNLFLQL 383
Cdd:cd07777 334 SVDPTFFG---ERHDPEGRGSITNIGESNFTlGNLFRALCRGIAENLHEMLPRLDLD-LSGIERIVGSGGALRKNPVLRR 409
|
410 420
....*....|....*....|....*..
gi 24654573 384 Q-SDLVGIQVLRAKIAETTALGAAMAA 409
Cdd:cd07777 410 IiEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
20-409 |
1.09e-32 |
|
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: 129.21 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 20 AVGGKVEEIITIGITNQRESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETIPNNARNINYLRPLCGlplspyFSGVK 99
Cdd:cd07809 63 DAGAELRDVAAIGISGQMHGLVALDAD-GKVLRPAKLWCDTRTAPEAEELTEALGGKKCLLVGLNIPAR------FTASK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 100 LRWLRDNVPvvsQAMEKgTAMFGTIDTWLMYNLTGGKdcgvhKTDVTNASRTMLMNIETLQWDANLLKFFGLPKT---IL 176
Cdd:cd07809 136 LLWLKENEP---EHYAR-IAKILLPHDYLNWKLTGEK-----VTGLGDASGTFPIDPRTRDYDAELLAAIDPSRDlrdLL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 177 PEICSSSEFYGSIAQ------GVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGT-GCFLLYNTGPsiVHSTHGLLTT 249
Cdd:cd07809 207 PEVLPAGEVAGRLTPegaeelGLPAGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTsGTAYGVSDKP--VSDPHGRVAT 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 250 -----VGYqlgrkaVPfyalegSVSIAGAAFNWLRDNMNLIQNS-GQIETMASTVD-NSLDVYFVPAFNGLYAPYWnQDA 322
Cdd:cd07809 285 fcdstGGM------LP------LINTTNCLTAWTELFRELLGVSyEELDELAAQAPpGAGGLLLLPFLNGERTPNL-PHG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 323 RGVICGLSEE-TTSEHIVRATLEAVCFQVRDILDSMHKDCkIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETT 401
Cdd:cd07809 352 RASLVGLTLSnFTRANLARAALEGATFGLRYGLDILRELG-VEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGG 430
|
....*...
gi 24654573 402 ALGAAMAA 409
Cdd:cd07809 431 ALGAALQA 438
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
2-409 |
5.44e-29 |
|
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: 118.50 E-value: 5.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 2 AIVNTVNECItgacKKLVA-VGGKVEEIITIGITNQRESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETiPNNARNI 80
Cdd:cd24121 47 ETWQAVVATI----REVVAkLDVLPDRVAAIGVTGQGDGTWLVDED-GRPVRDAILWLDGRAADIVERWQAD-GIAEAVF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 81 NYlrplCGLPLSPYFSGVKLRWLRDNVPvvsQAMEKGTAMFGTIDtWLMYNLTggkdcGVHKTDVTNASRTMLmNIETLQ 160
Cdd:cd24121 121 EI----TGTGLFPGSQAAQLAWLKENEP---ERLERARTALHCKD-WLFYKLT-----GEIATDPSDASLTFL-DFRTRQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 161 WDANLLKFFGLP--KTILPEICSSSE------FYGSIAQGVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLL 232
Cdd:cd24121 187 YDDEVLDLLGLEelRHLLPPIRPGTEvigpltPEAAAATGLPAGTPVVLGPFDVVATALGSGAIEPGDACSILGTTGVHE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 233 ----------YNTGPSIVHSTHGLLTtvgyqlgrKAVPfyALEGSVSI--------AGAAFNWLRDNMNLIQNsgqIETM 294
Cdd:cd24121 267 vvvdepdlepEGVGYTICLGVPGRWL--------RAMA--NMAGTPNLdwflrelgEVLKEGAEPAGSDLFQD---LEEL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 295 ASTVD-NSLDVYFVP--AFNGLYAPYWNQDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMhkdcKIPLAKLMVD 371
Cdd:cd24121 334 AASSPpGAEGVLYHPylSPAGERAPFVNPNARAQFTGLSLEHTRADLLRAVYEGVALAMRDCYEHM----GEDPGELRLS 409
|
410 420 430
....*....|....*....|....*....|....*...
gi 24654573 372 GGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAA 409
Cdd:cd24121 410 GGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNA 447
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
9-412 |
7.65e-27 |
|
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: 113.02 E-value: 7.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 9 ECITGACKKLVAVGGKV-EEIITIGI--TnqrESTVVWDRNSGQPLVNAIIWLDNRTTSTVEELLETI-PNNARNINYlr 84
Cdd:cd07781 53 EALEEAVRGALAEAGVDpEDVVGIGVdtT---SSTVVPVDEDGNPLAPAILWMDHRAQEEAAEINETAhPALEYYLAY-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 85 plCGLPLSP--YFSgvKLRWLRDNVPVVSQA----MEKGtamfgtiDtWLMYNLTGgkdcgVHKTDVTNAS-RTMLMNIE 157
Cdd:cd07781 128 --YGGVYSSewMWP--KALWLKRNAPEVYDAaytiVEAC-------D-WINARLTG-----RWVRSRCAAGhKWMYNEWG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 158 TLqWDANLLK-----FFGLPKTILPEICSSSEFYGSI----AQ--GVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYG 226
Cdd:cd07781 191 GG-PPREFLAaldpgLLKLREKLPGEVVPVGEPAGTLtaeaAErlGLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 227 T-GCFLLynTGPSIVHsTHGLLTTV------GYqlgrkavpfYALEGSVSIAGAAFNWLRDNMNLIQNSGQIET------ 293
Cdd:cd07781 270 TsTCHLM--VSPKPVD-IPGICGPVpdavvpGL---------YGLEAGQSAVGDIFAWFVRLFVPPAEERGDSIyallse 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 294 MASTVDN------SLDvyfvpAFNGLYAPYWNQDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMhKDCKIPLAK 367
Cdd:cd07781 338 EAAKLPPgesglvALD-----WFNGNRTPLVDPRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERF-EEAGVPVNR 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 24654573 368 LMVDGGMTVNN-LFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKA 412
Cdd:cd07781 412 VVACGGIAEKNpLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVA 457
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
25-447 |
4.80e-22 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 98.50 E-value: 4.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 25 VEEIITIGITNQRESTVVWDRNSgQPLVNAIIWLDNRTTSTVEELLETIPNNarninylRPLCGLPLSPYFSGVKLRWLR 104
Cdd:PRK15027 65 LQDVKALGIAGQMHGATLLDAQQ-RVLRPAILWNDGRCAQECALLEARVPQS-------RVITGNLMMPGFTAPKLLWVQ 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 105 DNVPVVSQAMEKgtaMFGTIDtWLMYNLTGgkdcgVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSSSE 184
Cdd:PRK15027 137 RHEPEIFRQIDK---VLLPKD-YLRLRMTG-----EFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 185 FYGSIAQGVLQGIGITSVL-----GDQQAALVGQQCLAKGQAKATYGT-GCFLLYNTG-----PSIVHS-THGLLttvgy 252
Cdd:PRK15027 208 ITGALLPEVAKAWGMATVPvvaggGDNAAGAVGVGMVDANQAMLSLGTsGVYFAVSEGflskpESAVHSfCHALP----- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 253 qlGRkavpfYALEGSVSIAGAAFNWLRDNMNLIQNSGQIETMASTVDNSLDVYFVPAFNGLYAPYWNQDARGVICGLSEE 332
Cdd:PRK15027 283 --QR-----WHLMSVMLSAASCLDWAAKLTGLSNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQ 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 333 TTSEHIVRATLEAVCFQVRDILDSMHkDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQV-LRAKIAETTALGAAMAAYK 411
Cdd:PRK15027 356 HGPNELARAVLEGVGYALADGMDVVH-ACGIKPQSVTLIGGGARSEYWRQMLADISGQQLdYRTGGDVGPALGAARLAQI 434
|
410 420 430
....*....|....*....|....*....|....*..
gi 24654573 412 AVENryqmEAPLSKSGPREAIKPS-ISATDRNLRYQK 447
Cdd:PRK15027 435 AANP----EKSLIELLPQLPLEQShLPDAQRYAAYQP 467
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
99-413 |
6.84e-22 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 98.18 E-value: 6.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 99 KLRWLRDNVPVVSQAMEKgtamFGTIDTWLMYNLTGgkdcgVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPE 178
Cdd:PRK10331 137 KLVWLKENHPQLLEQAHA----WLFISSLINHRLTG-----EFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 179 ICSSSEFYG----SIAQ--GVLQGIGITSVLGDQQAALVGQQClAKGQAKATYGTGCFLLYNTG---PSIVHSTHGLLTT 249
Cdd:PRK10331 208 LVEAGEQIGtlqpSAAAllGLPVGIPVISAGHDTQFALFGSGA-GQNQPVLSSGTWEILMVRSAqvdTSLLSQYAGSTCE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 250 VGYQLGrkavpFYAlEGSVSIAGAAFNWLRdnmNLIQNSGQI-ETM---ASTVDNSLD-VYFVPAFNGLyapywnqdARG 324
Cdd:PRK10331 287 LDSQSG-----LYN-PGMQWLASGVLEWVR---KLFWTAETPyQTMieeARAIPPGADgVKMQCDLLAC--------QNA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 325 VICGLSEETTSEHIVRATLEAVCFQVRDILDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALG 404
Cdd:PRK10331 350 GWQGVTLNTTRGHFYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAG 429
|
....*....
gi 24654573 405 AAMAAYKAV 413
Cdd:PRK10331 430 AAMFGWYGV 438
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
9-413 |
8.50e-21 |
|
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: 94.71 E-value: 8.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 9 ECITGACKKlvaVGGKVEEIITIGITNQRESTVVWDRNsGQPlvnaiIW----LDNRTTSTVEELLETIPNNARNInYLR 84
Cdd:cd07775 56 ECIREALKK---AGIAPKSIAAISTTSMREGIVLYDNE-GEE-----IWacanVDARAAEEVSELKELYNTLEEEV-YRI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 85 -----PLCGLPlspyfsgvKLRWLRDNVPVVSQAmekgTAMFGTIDTWLMYNLTGgkdcgVHKTDVTNASRTMLMNIETL 159
Cdd:cd07775 126 sgqtfALGAIP--------RLLWLKNNRPEIYRK----AAKITMLSDWIAYKLSG-----ELAVEPSNGSTTGLFDLKTR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 160 QWDANLLKFFGLPKTILPEICSSSEFYGSIAQ------GVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLY 233
Cdd:cd07775 189 DWDPEILEMAGLKADILPPVVESGTVIGKVTKeaaeetGLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 234 NTGPSIVHSTHGLLTTVGyqlGRKAVPFYalEGSVSIAGAAFNWLRDNM-----NLIQNSGQ-----IETMASTvdnsld 303
Cdd:cd07775 269 NTAAPVTDPAMNIRVNCH---VIPDMWQA--EGISFFPGLVMRWFRDAFcaeekEIAERLGIdaydlLEEMAKD------ 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 304 vyfVPAfnglyapywnqDARGVICGLS----------------------EETTSEHIVRATLEAVCFQVRDILDSMHKDC 361
Cdd:cd07775 338 ---VPP-----------GSYGIMPIFSdvmnyknwrhaapsflnldidpEKCNKATFFRAIMENAAIVSAGNLERIAEFS 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 24654573 362 KIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKAV 413
Cdd:cd07775 404 GIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGA 455
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
259-413 |
1.29e-16 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 82.09 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 259 VP-FYALEGSVSIAGAAFNWLRDNMNLiqnSGQIETMASTVDNSL----------------DVYFVPAFNGLYAPYWNQD 321
Cdd:COG1069 314 VPgMWGYEAGQSAVGDIFAWFVRLLVP---PLEYEKEAEERGISLhpllteeaaklppgesGLHALDWFNGNRSPLADQR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 322 ARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMhKDCKIPLAKLMVDGG-MTVNNLFLQLQSDLVGIQVLRAKIAET 400
Cdd:COG1069 391 LKGVILGLTLGTDAEDIYRALVEATAFGTRAIIERF-EEEGVPIDEIIACGGiATKNPLVMQIYADVTGRPIKVAASEQA 469
|
170
....*....|...
gi 24654573 401 TALGAAMAAykAV 413
Cdd:COG1069 470 CALGAAMFA--AV 480
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
291-435 |
3.43e-16 |
|
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.
Pssm-ID: 466800 [Multi-domain] Cd Length: 540 Bit Score: 81.04 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 291 IETMASTVDNSL-----DVYFVPAFNGLYAPYWNQDARGVICGLSEETTSEHIVR---ATLEAVCFQVRDILDSMHKdCK 362
Cdd:cd07782 363 LEQLAEEKGLPLayltrDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHIIEAMNA-AG 441
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24654573 363 IPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKAVENRYQM-EAPLSKSGPREAIKPS 435
Cdd:cd07782 442 HKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLwDAMAAMSGPGKVVEPN 515
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
3-434 |
3.63e-14 |
|
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: 74.58 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 3 IVNTVNECITGACKKlvaVGGKVEEIITIGItNQRESTVVWDRNsGQPLV---------NAIIWLDNRTTSTVEELLETI 73
Cdd:cd07768 50 IIKALQKCVQKLNIR---EGVDAYEVKGCGV-DATCSLAIFDRE-GTPLMalipypnedNVIFWMDHSAVNEAQWINMQC 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 74 PNNarninyLRPLCGLPLSPYFSGVKLRWLRDNVPVVSQAmekgTAMFGTIDTWLMYNLTggkdcgvhktdvtnasRTML 153
Cdd:cd07768 125 PQQ------LLDYLGGKISPEMGVPKLKYFLDEYSHLRDK----HFHIFDLHDYIAYELT----------------RLYE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 154 MNIETLQWDANLLKFFGLPktilpeicsSSEFYGSIAQGVLQG-----------IGITSVLGDQQAA----LVGQQCLAK 218
Cdd:cd07768 179 WNICGLLGKENLDGEESGW---------SSSFFKNIDPRLEHLtttknlpsnvpIGTTSGVALPEMAekmgLHPGTAVVV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 219 GQAKATYGTGCFLLYNTGPSIV-----HSTHGLLTTVGYQLGRKAVPFYAL--------EGSVSIAGAAFNWLRDN---- 281
Cdd:cd07768 250 SCIDAHASWFAVASPHLETSLFmiagtSSCHMYGTTISDRIPGVWGPFDTIidpdysvyEAGQSATGKLIEHLFEShpca 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 282 --MNLIQNSGQ---------IETMASTVDNSLDVYFVPAFNGLYAPYWNQDARGVICGLSEETTSE---HIVRATLEAVC 347
Cdd:cd07768 330 rkFDEALKKGAdiyqvleqtIRQIEKNNGLSIHILTLDMFFGNRSEFADPRLKGSFIGESLDTSMLnltYKYIAILEALA 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 348 FQVRDILDSMHKDcKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKAVENRYQM----EAPL 423
Cdd:cd07768 410 FGTRLIIDTFQNE-GIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAAVLAKVAAGKKQLAdsitEADI 488
|
490
....*....|.
gi 24654573 424 SKSGPREAIKP 434
Cdd:cd07768 489 SNDRKSETFEP 499
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
8-408 |
7.10e-13 |
|
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: 70.25 E-value: 7.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 8 NECITGackkLVAVGGKVEEIITIGITnqresTvvW-------DRNsGQPLVNAIIWLDNRTTSTVEELLETIPNNarni 80
Cdd:cd07771 52 DEIKEG----LKKAAEQGGDIDSIGID-----T--WgvdfgllDKN-GELLGNPVHYRDPRTEGMMEELFEKISKE---- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 81 nYLRPLCGLPLSPYFSGVKLRWLRDNVPvvsqamekgtAMFGTIDTWLM------YNLTGGKdcgvhKTDVTNASRTMLM 154
Cdd:cd07771 116 -ELYERTGIQFQPINTLYQLYALKKEGP----------ELLERADKLLMlpdllnYLLTGEK-----VAEYTIASTTQLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 155 NIETLQWDANLLKFFGLPKTILPEICSSSEFYGSI-----AQGVLQGIGITSVLG-DQQAALVGQQCLAKGQAkatY--- 225
Cdd:cd07771 180 DPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLkpevaEELGLKGIPVIAVAShDTASAVAAVPAEDEDAA---Fiss 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 226 GT----GCFLlynTGPsivhsthgLLTTVGYQLGrkavpfYALEGSV--------SIAG------AAFNWLRDNMNLiqN 287
Cdd:cd07771 257 GTwsliGVEL---DEP--------VITEEAFEAG------FTNEGGAdgtirllkNITGlwllqeCRREWEEEGKDY--S 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 288 SGQIETMASTVDnSLDVYFVPAFNGLYAPywnQDARGVICGLSEET------TSEHIVRATLEAVCFQVRDILDSMHKDC 361
Cdd:cd07771 318 YDELVALAEEAP-PFGAFIDPDDPRFLNP---GDMPEAIRAYCRETgqpvpeSPGEIARCIYESLALKYAKTIEELEELT 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 24654573 362 KIPLAKL-MVDGGmtVNNLFL-QLQSDLVGIQVlRAKIAETTALGAAMA 408
Cdd:cd07771 394 GKRIDRIhIVGGG--SRNALLcQLTADATGLPV-IAGPVEATAIGNLLV 439
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
26-409 |
3.71e-12 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 68.11 E-value: 3.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 26 EEIITIGITNQRESTVVWDRNsGQPlvnaiIW----LDNRTTSTVEELLETIPNNARNInYLR-----PLCGLPlspyfs 96
Cdd:PRK10939 73 SDIAAVSATSMREGIVLYDRN-GTE-----IWacanVDARASREVSELKELHNNFEEEV-YRCsgqtlALGALP------ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 97 gvKLRWLRDNVPVVSQAMEKGTaMfgtIDTWLMYNLtggkdCGVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTIL 176
Cdd:PRK10939 140 --RLLWLAHHRPDIYRQAHTIT-M---ISDWIAYML-----SGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADIL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 177 PEICSSSEFYGSIAQ------GVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTGPSIVHSTHGLlttv 250
Cdd:PRK10939 209 PPVKETGTVLGHVTAkaaaetGLRAGTPVVMGGGDVQLGCLGLGVVRPGQTAVLGGTFWQQVVNLPAPVTDPNMNI---- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 251 gyqlgrkAVPFYALEGSV---SIA---GAAFNWLRDNM-----NLIQNSGQ-----IETMASTVD-NSLDVyfVPAF-NG 312
Cdd:PRK10939 285 -------RINPHVIPGMVqaeSISfftGLTMRWFRDAFcaeekLLAERLGIdayslLEEMASRVPvGSHGI--IPIFsDV 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 313 LYAPYWNQDARGVIcGLS---EETTSEHIVRATLEAVCFQVRDILDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVG 389
Cdd:PRK10939 356 MRFKSWYHAAPSFI-NLSidpEKCNKATLFRALEENAAIVSACNLQQIAAFSGVFPSSLVFAGGGSKGKLWSQILADVTG 434
|
410 420
....*....|....*....|
gi 24654573 390 IQVLRAKIAETTALGAAMAA 409
Cdd:PRK10939 435 LPVKVPVVKEATALGCAIAA 454
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
310-449 |
2.33e-10 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 62.56 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 310 FNGLYAPYWNQDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMHkDCKIPLAKLMVDGGMTVNNLFL-QLQSDLV 388
Cdd:PRK04123 385 FNGRRTPLADQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFE-DQGVPVEEVIAAGGIARKNPVLmQIYADVL 463
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24654573 389 G--IQVLRAKiaETTALGAAM----AA--YKAVEnryqmEAPLS-KSGPREAIKPSISATDR-NLRYQKWK 449
Cdd:PRK04123 464 NrpIQVVASD--QCPALGAAIfaavAAgaYPDIP-----EAQQAmASPVEKTYQPDPENVARyEQLYQEYK 527
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
135-441 |
3.06e-07 |
|
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: 52.56 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 135 GKDCGVhktDVTNASRTMLMNIETLQWDANLLKFFGLP--KTILPEICSSSEFYGSIAQGVLQGIGITS---VL---GDQ 206
Cdd:cd07776 198 GRYAPI---DESDGSGMNLMDIRSRKWSPELLDAATAPdlKEKLGELVPSSTVAGGISSYFVERYGFSPdclVVaftGDN 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 207 QAALVGQqCLAKGQAKATYGT-GCFLLYNTGPSIVHSTHglltTVGYQLGRKAvpFYAL----EGSvsiagAAFNWLRDN 281
Cdd:cd07776 275 PASLAGL-GLEPGDVAVSLGTsDTVFLVLDEPKPGPEGH----VFANPVDPGS--YMAMlcykNGS-----LARERVRDR 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 282 MNLiqnsGQIET----MASTV---DNSLDVYF-----VPafNGLYAPYWNQDARGVIcglsEETTSEHIVRATLEAVCFQ 349
Cdd:cd07776 343 YAG----GSWEKfnelLESTPpgnNGNLGLYFdepeiTP--PVPGGGRRFFGDDGVD----AFFDPAVEVRAVVESQFLS 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 350 VRdiLDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKAVENR-----YQMEAPLS 424
Cdd:cd07776 413 MR--LHAERLGSDIPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAgsgdfSPEFVVFS 490
|
330
....*....|....*..
gi 24654573 425 KSGPREAIKPSISATDR 441
Cdd:cd07776 491 AEEPKLVAEPDPEAAEV 507
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
28-173 |
7.49e-07 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 51.26 E-value: 7.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 28 IITIGITNQRESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETIpnnARNINYLRplCGLPLSPYFSGVKLRWLRDNV 107
Cdd:PRK10640 56 IDSIGIDTWGVDYVLLDKQ-GQRVGLPVSYRDSRTDGVMAQAQQQL---GKRDIYRR--SGIQFLPFNTLYQLRALTEQQ 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24654573 108 P-VVSQAmekgtAMFGTIDTWLMYNLTGGKDCgvhktDVTNASRTMLMNIETLQWDANLLKFFGLPK 173
Cdd:PRK10640 130 PeLIAQV-----AHALLIPDYFSYRLTGKMNW-----EYTNATTTQLVNINSDDWDESLLAWSGAPK 186
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
323-409 |
9.13e-05 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466792 [Multi-domain] Cd Length: 424 Bit Score: 44.56 E-value: 9.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 323 RGVICGLSEETTSEHIVRATLEAVCFQvRDILDSMHKDCKiplaKLMVDGGMTVNNLFLQ-LQSDLVGIQVLRAKIAETT 401
Cdd:cd07772 342 GGRGVLSAFPSAEEAYALAILYLALMT-DYALDLLGSGVG----RIIVEGGFAKNPVFLRlLAALRPDQPVYLSDDSEGT 416
|
....*...
gi 24654573 402 ALGAAMAA 409
Cdd:cd07772 417 ALGAALLA 424
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
316-452 |
2.58e-03 |
|
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: 40.08 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654573 316 PYWNQDARGVICGLSEETTSEHIVR---ATLEAVCFQVRDILDSMHKDCkIPLAKLMVDGGMTVNNLFLQLQS---DLVG 389
Cdd:cd07778 392 PYNDPNMSGSFIGESTDSSLTDLVLkyiLILEFLAFQTKLIIDNFQKEK-IIIQKVVISGSQAKNARLLQLLStvlSKIH 470
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24654573 390 IQVLRAKIAETTALGAAMAAYKAVENRYQMEAPLSKSGPREAIKPSISATDRNLRYQKWKMAI 452
Cdd:cd07778 471 IIVPLSDSKYAVVKGAALLGKAAFLHNQSIEERLISLKNEDQISICASASIVKLVSDETKLAI 533
|
|
| |
