|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
3-467 |
2.50e-154 |
|
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: 447.37 E-value: 2.50e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 3 LLGIDLGTGSVKLVTIDADGVERAVASEPYPLSSPRPGWAEIAPETWWDALVRAAARLPA---DERAQVVAIGLSGQMHG 79
Cdd:cd07808 2 LLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAkagISPSDIAAIGLTGQMHG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 80 VVLMDAAARPVRPALLWPDTRASREAEAARWPDAP-------NPVAPGMAGPLLCWLAAHEPDTLRAARWAVQPKDWLRV 152
Cdd:cd07808 82 LVLLDKNGRPLRPAILWNDQRSAAECEELEARLGDeiliitgNPPLPGFTLPKLLWLKENEPEIFARIRKILLPKDYLRY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 153 ALGGEVAADPSDACATALASPD-GAWDRARIKALALPADRFAPVRASAARCGTLDARAAAALGLPAGVPLATGAGDTACA 231
Cdd:cd07808 162 RLTGELATDPSDASGTLLFDVEkREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAAEELGLPEGTPVVAGAGDNAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 232 ALGSGLVASGDALLTTGSGGQIVVLADALPP-ARRGLHRYRAAAGGGYYTMAAMQNVGLALEAVRGWLG--YPDWAAAYD 308
Cdd:cd07808 242 ALGAGVVEPGDALISLGTSGVVFAPTDKPVPdPKGRLHTFPHAVPGKWYAMGVTLSAGLSLRWLRDLFGpdRESFDELDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 309 DAFAQPP-SERLCFLPYLTGERSPWMNPDARGGWLGLALGDTRGAMMRAAFEGVAFALRAGLDAIRDANrdDPVASLRVA 387
Cdd:cd07808 322 EAAKVPPgSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVLKELG--IKVKEIRLI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 388 GGGSVDPRWRQLLADALGASLHALECPNAATRGAALLAGLAIGHWSESALPALAPAASPVA---APRDDRALAARHARFV 464
Cdd:cd07808 400 GGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACIKIEKTiepDPERHEAYDELYARYR 479
|
...
gi 2669191611 465 DLY 467
Cdd:cd07808 480 ELY 482
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
3-475 |
2.61e-127 |
|
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: 378.79 E-value: 2.61e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 3 LLGIDLGTGSVKLVTIDADGVERAVASEPYPLSSPRPGWAEIAPETWWDALVRAAARLPAD---ERAQVVAIGLSGQMHG 79
Cdd:COG1070 3 VLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKagvDPEEIAAIGVSGQMHG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 80 VVLMDAAARPVRPALLWPDTRASREAEA--ARWPDAP------NPVAPGMAGPLLCWLAAHEPDTLRAARWAVQPKDWLR 151
Cdd:COG1070 83 LVLLDADGEPLRPAILWNDTRAAAEAAElrEELGEEAlyeitgNPLHPGFTAPKLLWLKENEPEIFARIAKVLLPKDYLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 152 VALGGEVAADPSDACATALASP-DGAWDRARIKALALPADRFAPVRASAARCGTLDARAAAALGLPAGVPLATGAGDTAC 230
Cdd:COG1070 163 YRLTGEFVTDYSDASGTGLLDVrTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAAETGLPAGTPVVAGAGDNAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 231 AALGSGLVASGDALLTTGSGGQI-VVLADALPPARRGLHRYRAAAGGGYYTMAAMQNVGLALEAVRGWLGY---PDWAAA 306
Cdd:COG1070 243 AALGAGAVEPGDAAVSLGTSGVVfVVSDKPLPDPEGRVHTFCHAVPGRWLPMGATNNGGSALRWFRDLFADgelDDYEEL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 307 YDDAFAQPP-SERLCFLPYLTGERSPWMNPDARGGWLGLALGDTRGAMMRAAFEGVAFALRAGLDAIRDANRddPVASLR 385
Cdd:COG1070 323 NALAAEVPPgADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEALEEAGV--KIDRIR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 386 VAGGGSVDPRWRQLLADALGASLHALECPNAATRGAALLAGLAIGHWSESALPALAPAASPVAAPRDD---RALAARHAR 462
Cdd:COG1070 401 ATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMVRVGETIEPDPenvAAYDELYER 480
|
490
....*....|...
gi 2669191611 463 FVDLYARTDAWFA 475
Cdd:COG1070 481 YRELYPALKPLFE 493
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
3-433 |
8.88e-107 |
|
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: 326.01 E-value: 8.88e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 3 LLGIDLGTGSVKLVTIDADGVERAVASEPYPLSSPRPGWAEIAPETWWDALVRAAARLPA---DERAQVVAIGLSGQMHG 79
Cdd:cd07805 2 ILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEksgIDPSDIAAIAFSGQMQG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 80 VVLMDAAARPVRPALLWPDTRASREAE--AARWPDAP-------NPVAPGMAGPLLCWLAAHEPDTLRAARWAVQPKDWL 150
Cdd:cd07805 82 VVPVDKDGNPLRNAIIWSDTRAAEEAEeiAGGLGGIEgyrlgggNPPSGKDPLAKILWLKENEPEIYAKTHKFLDAKDYL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 151 RVALGGEVAADPSDACATALASP-DGAWDRARIKALALPADRFAPVRASAARCGTLDARAAAALGLPAGVPLATGAGDTA 229
Cdd:cd07805 162 NFRLTGRAATDPSTASTTGLMDLrKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAAAELGLPAGTPVVGGGGDAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 230 CAALGSGLVASGDALLTTGSGGQI-VVLADALPPARRGLHRYRAAAGGGYYTMAAMQNVGLALEAVRGWLGYPDWAAAYD 308
Cdd:cd07805 242 AAALGAGAVEEGDAHIYLGTSGWVaAHVPKPKTDPDHGIFTLASADPGRYLLAAEQETAGGALEWARDNLGGDEDLGADD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 309 DAF-------AQPPSERLCFLPYLTGERSPWMNPDARGGWLGLALGDTRGAMMRAAFEGVAFALRAGLDAIRDANRddPV 381
Cdd:cd07805 322 YELldelaaeAPPGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWLLEALEKLTR--KI 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2669191611 382 ASLRVAGGGSVDPRWRQLLADALGASLHALECP-NAATRGAALLAGLAIGHWS 433
Cdd:cd07805 400 DELRLVGGGARSDLWCQILADVLGRPVEVPENPqEAGALGAALLAAVGLGLLK 452
|
|
| XylB |
TIGR01312 |
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ... |
4-430 |
5.49e-104 |
|
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: 318.49 E-value: 5.49e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 4 LGIDLGTGSVKLVTIDADGVERAVASEPYPLSSPRPGWAEIAPETWWDALVRAAARLPAD---ERAQVVAIGLSGQMHGV 80
Cdd:TIGR01312 1 LGIDLGTSGVKALLVDEQGEVIASGSAPHTVISPHPGWSEQDPEDWWDATEEAIKELLEQaseMGQDIKGIGISGQMHGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 81 VLMDAAARPVRPALLWPDTRASREAE-------AARWPDAP-NPVAPGMAGPLLCWLAAHEPDTLRAARWAVQPKDWLRV 152
Cdd:TIGR01312 81 VLLDANGEVLRPAILWNDTRTAQECEeleaelgDERVLEITgNLALPGFTAPKLLWVRKHEPEVFARIAKVMLPKDYLRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 153 ALGGEVAADPSDACATA-LASPDGAWDRARIKALALPADRFAPVRASAARCGTLDARAAAALGLPAGVPLATGAGDTACA 231
Cdd:TIGR01312 161 RLTGEYVTEYSDASGTGwFDVAKRAWSKELLDALDLPESQLPELIESSEKAGTVRPEVAARLGLSAGVPVAAGGGDNAAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 232 ALGSGLVASGDALLTTGSGGQIVVLADALPPARRG-LHRYRAAAGGGYYTMAAMQNVGLALEAVRGWLGYPDWAAAYDDA 310
Cdd:TIGR01312 241 AIGTGTVDPGDAMMSLGTSGVVYAVTDKPLPDPAGaVHGFCHALPGGWLPMGVTLSATSSLEWFRELFGKEDVEALNELA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 311 -FAQPPSERLCFLPYLTGERSPWMNPDARGGWLGLALGDTRGAMMRAAFEGVAFALRAGLDAIRDANrDDPVASLRVAGG 389
Cdd:TIGR01312 321 eQSPPGAEGVTFLPYLNGERTPHLDPQARGSFIGLTHNTTRADLTRAVLEGVTFALRDSLDILREAG-GIPIQSIRLIGG 399
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2669191611 390 GSVDPRWRQLLADALGASLHALECPNAATRGAALLAGLAIG 430
Cdd:TIGR01312 400 GAKSPAWRQMLADIFGTPVDVPEGEEGPALGAAILAAWALG 440
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
3-425 |
5.01e-102 |
|
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: 310.65 E-value: 5.01e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 3 LLGIDLGTGSVKLVTIDADGVERAVASEPYPLSSPRPGWAEIAPETWWDALVRAAARLPA---DERAQVVAIGLSGQMHG 79
Cdd:cd00366 2 LLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAkagIDPSDIAAIGISGQMPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 80 VVLMDAAARPVRPALLWPDTRAsreaeaarwpdapnpvapgmagpllcwlaahepdtlraarWAVQPKDWLRVALGGEVA 159
Cdd:cd00366 82 VVLVDADGNPLRPAIIWLDRRA----------------------------------------KFLQPNDYIVFRLTGEFA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 160 ADPSDACATALASP-DGAWDRARIKALALPADRFAPVRASAARCGTLDARAAAALGLPAGVPLATGAGDTACAALGSGLV 238
Cdd:cd00366 122 IDYSNASGTGLYDIkTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGGDTAAAALGAGVV 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 239 ASGDALLTTGSGGQIVVLADALPPARRGLHRYRAAAGGGYYTMAAMQNVGLALEAVRGWLGYPDWAAAYDDAF------A 312
Cdd:cd00366 202 EPGDAVDSTGTSSVLSVCTDEPVPPDPRLLNRCHVVPGLWLLEGAINTGGASLRWFRDEFGEEEDSDAEYEGLdelaaeV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 313 QPPSERLCFLPYLTGERSPWMNPDARGGWLGLALGDTRGAMMRAAFEGVAFALRAGLDAIRDANRDdpVASLRVAGGGSV 392
Cdd:cd00366 282 PPGSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEILEELGVK--IKEIRVTGGGAK 359
|
410 420 430
....*....|....*....|....*....|...
gi 2669191611 393 DPRWRQLLADALGASLHALECPNAATRGAALLA 425
Cdd:cd00366 360 SRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
3-430 |
5.06e-93 |
|
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: 289.10 E-value: 5.06e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 3 LLGIDLGTGSVKLVTIDADGVERAVASEPYPLSSPRPGWAEIAPETWWDALVRAAARLPAD-ERAQVVAIGLSGQMHGVV 81
Cdd:cd07773 2 LLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQaGPDPIAAISVSSQGESGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 82 LMDAAARPVRPALLWPDTRASREAEA-ARWPDAP-------NPVAPGMAGPLLCWLAAHEPDTLRAARWAVQPKDWLRVA 153
Cdd:cd07773 82 PVDRDGEPLGPAIVWFDPRGKEEAEElAERIGAEelyritgLPPSPMYSLAKLLWLREHEPEIFAKAAKWLSVADYIAYR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 154 LGGEVAADPSDACATALAS-PDGAWDRARIKALALPADRFAPVRASAARCGTLDARAAAALGLPAGVPLATGAGDTACAA 232
Cdd:cd07773 162 LTGEPVTDYSLASRTMLFDiRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEELGLPAGTPVVVGGHDHLCAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 233 LGSGLVASGDALLTTGSGGQIVVLADALPPARRGLHR---YRAAAGGGYYTMAAMQNVGLALEAVRGWLGYPDWAAAYDD 309
Cdd:cd07773 242 LGAGVIEPGDVLDSTGTAEALLAVVDEPPLDEMLAEGglsYGHHVPGGYYYLAGSLPGGALLEWFRDLFGGDESDLAAAD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 310 AFAQ---PPSERLCFLPYLTGERSPWMNPDARGGWLGLALGDTRGAMMRAAFEGVAFALRAGLDAIRDANRddPVASLRV 386
Cdd:cd07773 322 ELAEaapPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEALEKAGI--PIDEIRA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2669191611 387 AGGGSVDPRWRQLLADALGASLHALECPNAATRGAALLAGLAIG 430
Cdd:cd07773 400 VGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
3-430 |
1.74e-92 |
|
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: 287.91 E-value: 1.74e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 3 LLGIDLGTGSVKLVTIDADGVERAVASEPYPLSSPRPGWAEIAPETWWDALVRAAARL---PADERAQVVAIGLSGQMHG 79
Cdd:cd07802 2 LLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELlekSGVDPSDIAGVGVTGHGNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 80 VVLMDAAARPVRPALLWPDTRASREAEaaRWPDAP----------NPVAPGMAGPLLCWLAAHEPDTLRAARWAVQPKDW 149
Cdd:cd07802 82 LYLVDKDGKPVRNAILSNDSRAADIVD--RWEEDGtlekvypltgQPLWPGQPVALLRWLKENEPERYDRIRTVLFCKDW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 150 LRVALGGEVAADPSDACATALASPDGAWDRARIKALALPA--DRFAPVRASAARCGTLDARAAAALGLPAGVPLATGAGD 227
Cdd:cd07802 160 IRYRLTGEISTDYTDAGSSLLDLDTGEYDDELLDLLGIEElkDKLPPLVPSTEIAGRVTAEAAALTGLPEGTPVAAGAFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 228 TACAALGSGLVASGDALLTTGSGGQIVVLADALPPARRGLHRYRAAAGGGYYTMAAMQNVGLALE-AVRGWLGYPDWAAA 306
Cdd:cd07802 240 VVASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDSVGSNSLHADPGLYLIVEASPTSASNLDwFLDTLLGEEKEAGG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 307 YDDAF------AQPP-SERLCFLPYLTGERspwMNPDARGGWLGLALGDTRGAMMRAAFEGVAFALRAGLDAIRDANRDD 379
Cdd:cd07802 320 SDYDEldeliaAVPPgSSGVIFLPYLYGSG---ANPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLVARKPE 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2669191611 380 PVaslRVAGGGSVDPRWRQLLADALGASLHALECPNAATRGAALLAGLAIG 430
Cdd:cd07802 397 TI---RLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
3-430 |
1.74e-85 |
|
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: 269.78 E-value: 1.74e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 3 LLGIDLGTGSVKLVTIDADGVERAVASEPYPLSSPRPGWAEIAPETWWDALVRAAARLPADER---AQVVAIGLSGQMHG 79
Cdd:cd07804 2 LLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGispKEIAAIGVSGLVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 80 VVLMDAAARPVRPALLWPDTRASREAEAAR---WPDA-----PNPVAPGMAGPLLCWLAAHEPDTLRAARWAVQPKDWLR 151
Cdd:cd07804 82 LVPVDENGKPLRPAILYGDRRATEEIEWLNeniGEDRifeitGNPLDSQSVGPKLLWIKRNEPEVFKKTRKFLGAYDYIV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 152 VALGGEVAADPSDACATALA--SPDGAWDRARIKALALPADRFAPVRASAARCGTLDARAAAALGLPAGVPLATGAGDTA 229
Cdd:cd07804 162 YKLTGEYVIDYSSAGNEGGLfdIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEAAEETGLAEGTPVVAGTVDAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 230 CAALGSGLVASGDALLTTGSGGQIVVLADALPPARRGLHRYrAAAGGGYYTMAAMQNVGLALEAVRGWLGYPDWAAAY-- 307
Cdd:cd07804 242 ASALSAGVVEPGDLLLMLGTAGDIGVVTDKLPTDPRLWLDY-HDIPGTYVLNGGMATSGSLLRWFRDEFAGEEVEAEKsg 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 308 -DDAFAQ--------PP-SERLCFLPYLTGERSPWMNPDARGGWLGLALGDTRGAMMRAAFEGVAFALRAGLDAIRDANr 377
Cdd:cd07804 321 gDSAYDLldeeaekiPPgSDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYGLRHHLEVIREAG- 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2669191611 378 dDPVASLRVAGGGSVDPRWRQLLADALGASLHALECPNAATRGAALLAGLAIG 430
Cdd:cd07804 400 -LPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
4-434 |
7.07e-85 |
|
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: 269.04 E-value: 7.07e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 4 LGIDLGTGSVKLVTIDADGVERAVASEPYPLSSPRPGWAEIAPETWWDALVRAAARLPAD-ERAQVVAIGLSGQMHGVVL 82
Cdd:cd07770 3 LGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKlGGGEVDAIGFSSAMHSLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 83 MDAAARPVRPALLWPDTRASREAEAARWPDAPN--------PVAPgMAgPL--LCWLAAHEPDTLRAARWAVQPKDWLRV 152
Cdd:cd07770 83 VDEDGEPLTPVITWADTRAAEEAERLRKEGDGSelyrrtgcPIHP-MY-PLakLLWLKEERPELFAKAAKFVSIKEYLLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 153 ALGGEVAADPSDACATAL-ASPDGAWDRARIKALALPADRFAPVRASAARCGTLDARAAAALGLPAGVPLATGAGDTACA 231
Cdd:cd07770 161 RLTGELVTDYSTASGTGLlNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAERLGLLAGTPVVLGASDGALA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 232 ALGSGLVASGDALLTTGSGGQI-VVLADALPPARRGLHRYRAAAG----GGyytmaAMQNVGLALEAVRGWLGYPDwaAA 306
Cdd:cd07770 241 NLGSGALDPGRAALTVGTSGAIrVVSDRPVLDPPGRLWCYRLDENrwlvGG-----AINNGGNVLDWLRDTLLLSG--DD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 307 YDDAFAQ-----PPSERLCFLPYLTGERSPWMNPDARGGWLGLALGDTRGAMMRAAFEGVAFALRAGLDAIRDANrdDPV 381
Cdd:cd07770 314 YEELDKLaeavpPGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEALEELA--GPV 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2669191611 382 ASLRVAGGGSVDPRWRQLLADALGASLHALECPNAATRGAALLAGLAIGHWSE 434
Cdd:cd07770 392 KEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISS 444
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
3-428 |
1.25e-79 |
|
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: 254.07 E-value: 1.25e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 3 LLGIDLGTGSVKLVTIDADGVERAVASEPYPLSSPRPGWAEIAPETWWDALVRAAARLPADER-AQVVAIGLSGQMHGVV 81
Cdd:cd07783 2 FLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRpRRVVAIAVDGTSGTLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 82 LMDAAARPVRPALLWPDTRASREAEAAR------WPDAPNPVAPGMAGPLLCWLAAHEPDTLRAARWAVQPKDWLRVAL- 154
Cdd:cd07783 82 LVDREGEPLRPAIMYNDARAVAEAEELAeaagavAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFLHQADWLAGRLt 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 155 GGEVAADPSDACATALASPDGAWDRARIKALALPADRFAPVRASAARCGTLDARAAAALGLPAGVPLATGAGDTACAALG 234
Cdd:cd07783 162 GDRGVTDYNNALKLGYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLPAGTPVVAGTTDSIAAFLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 235 SGLVASGDALLTTGSGGQIVVLAD-ALPPARRGLHRYRaaAGGGYYTMAAMQNVGLAleAVRgWLGYPDWAAAYDDAFAQ 313
Cdd:cd07783 242 SGAVRPGDAVTSLGTTLVLKLLSDkRVPDPGGGVYSHR--HGDGYWLVGGASNTGGA--VLR-WFFSDDELAELSAQADP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 314 PPSERLCFLPY-LTGERSPWMNPDARGGWLGlaLGDTRGAMMRAAFEGVAFALRAGLDAIRDANRdDPVASLRVAGGGSV 392
Cdd:cd07783 317 PGPSGLIYYPLpLRGERFPFWDPDARGFLLP--RPHDRAEFLRALLEGIAFIERLGYERLEELGA-PPVEEVRTAGGGAR 393
|
410 420 430
....*....|....*....|....*....|....*.
gi 2669191611 393 DPRWRQLLADALGASLHALECPNAATrGAALLAGLA 428
Cdd:cd07783 394 NDLWNQIRADVLGVPVVIAEEEEAAL-GAALLAAAG 428
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
3-430 |
1.04e-77 |
|
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: 249.39 E-value: 1.04e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 3 LLGIDLGTGSVKLVTIDA-DGVERAVASEPYPLSSPRPGWAEIAPETWWDALVRAAARLPAD---ERAQVVAIGLSGQMH 78
Cdd:cd07809 2 VLGIDLGTQSIKAVLIDAeTGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDagaELRDVAAIGISGQMH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 79 GVVLMDAAARPVRPALLWPDTRASREAEAA-------RWPDAPNPVAPGMAGPLLCWLAAHEPDTLRAARWAVQPKDWLR 151
Cdd:cd07809 82 GLVALDADGKVLRPAKLWCDTRTAPEAEELtealggkKCLLVGLNIPARFTASKLLWLKENEPEHYARIAKILLPHDYLN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 152 VALGGEVAADPSDACATALASPD-GAWDRARIKALAL---PADRFAPVRASAARCGTLDARAAAALGLPAGVPLATGAGD 227
Cdd:cd07809 162 WKLTGEKVTGLGDASGTFPIDPRtRDYDAELLAAIDPsrdLRDLLPEVLPAGEVAGRLTPEGAEELGLPAGIPVAPGEGD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 228 TACAALGSGLVASGDALLTTGSGGQIVVLADALPPARRGLHRYRAAAGGGYYTMAAMQNVG-LALEAVRGWLGyPDWAAA 306
Cdd:cd07809 242 NMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSDPHGRVATFCDSTGGMLPLINTTNCLtAWTELFRELLG-VSYEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 307 YDDAFAQPP-SERLCFLPYLTGERSPwMNPDARGGWLGLALGD-TRGAMMRAAFEGVAFALRAGLDAIRDANrdDPVASL 384
Cdd:cd07809 321 DELAAQAPPgAGGLLLLPFLNGERTP-NLPHGRASLVGLTLSNfTRANLARAALEGATFGLRYGLDILRELG--VEIDEI 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2669191611 385 RVAGGGSVDPRWRQLLADALGASLHALECPNAATRGAALLAGLAIG 430
Cdd:cd07809 398 RLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
3-430 |
4.59e-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: 4.59e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 3 LLGIDLGTGSVKLVTIDADGVERAVASEPYPLSSPRPGWAEIAPETWWDALVRAAARLPA---DERAQVVAIGLSGQMHG 79
Cdd:cd07779 2 ILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAkagVDPEDIAAIGLTSQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 80 VVLMDAAARPVRPALLWPDTRAsreaeaarwpdapnpvapgmagpllcwlaahepdtlraaRWAVQPKDWLRVALGGEVA 159
Cdd:cd07779 82 FVPVDEDGRPLRPAISWQDKRT---------------------------------------AKFLTVQDYLLYRLTGEFV 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 160 ADPSDACATALASP-DGAWDRARIKALALPADRFAPVRASAARCGTLDARAAAALGLPAGVPLATGAGDTACAALGSGLV 238
Cdd:cd07779 123 TDTTSASRTGLPDIrTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAAEETGLPEGTPVVAGGGDQQCAALGAGVL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 239 ASGDALLTTGSGGQIVVLADALPPARRGLHRYRAAAGGGYYTMAAMQNVGLAL-----------EAVRGWLGYPDWAAAY 307
Cdd:cd07779 203 EPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWVLEGSINTGGSAvrwfrdefgqdEVAEKELGVSPYELLN 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 308 DDAFAQPP-SERLCFLPYLTGERSPWMNPDARGGWLGLALGDTRGAMMRAAFEGVAFALRAGLDAIRDANRddPVASLRV 386
Cdd:cd07779 283 EEAAKSPPgSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELRDNLEAMEKAGV--PIEEIRV 360
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2669191611 387 AGGGSVDPRWRQLLADALGASLHALECPNAATRGAALLAGLAIG 430
Cdd:cd07779 361 SGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAG 404
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
3-430 |
1.80e-70 |
|
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: 230.97 E-value: 1.80e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 3 LLGIDLGTGSVKLVTIDADGVERAVASEPYPLSSPRPGWAEIAPETWWDALVRAAARLPA---DERAQVVAIGLSGQMHG 79
Cdd:cd24121 2 LIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAkldVLPDRVAAIGVTGQGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 80 VVLMDAAARPVRPALLWPDTRASREAEaaRWPDAP----------NPVAPGMAGPLLCWLAAHEPDTLRAARWAVQPKDW 149
Cdd:cd24121 82 TWLVDEDGRPVRDAILWLDGRAADIVE--RWQADGiaeavfeitgTGLFPGSQAAQLAWLKENEPERLERARTALHCKDW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 150 LRVALGGEVAADPSDACATALASPDGAWDRARIKALALPADR--FAPVRASAARCGTLDARAAAALGLPAGVPLATGAGD 227
Cdd:cd24121 160 LFYKLTGEIATDPSDASLTFLDFRTRQYDDEVLDLLGLEELRhlLPPIRPGTEVIGPLTPEAAAATGLPAGTPVVLGPFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 228 TACAALGSGLVASGDALLTTGSGGQIVVLADALPPARRGLHRYRAAAGGGYY-----TMAAMQN-------VGLALEAVR 295
Cdd:cd24121 240 VVATALGSGAIEPGDACSILGTTGVHEVVVDEPDLEPEGVGYTICLGVPGRWlramaNMAGTPNldwflreLGEVLKEGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 296 GWLGYPDWAAAYDDAFAQPP-SERLCFLPYL--TGERSPWMNPDARGGWLGLALGDTRGAMMRAAFEGVAFALRaglDAI 372
Cdd:cd24121 320 EPAGSDLFQDLEELAASSPPgAEGVLYHPYLspAGERAPFVNPNARAQFTGLSLEHTRADLLRAVYEGVALAMR---DCY 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2669191611 373 RDANRDdpVASLRVAGGGSVDPRWRQLLADALGASLHALECPNAATRGAALLAGLAIG 430
Cdd:cd24121 397 EHMGED--PGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
4-430 |
7.56e-61 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 206.36 E-value: 7.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 4 LGIDLGTGSVKLVTIDADGVERAVASEPYPLSSPRPGWAEIAPETWWDALVRAAARLPADERAQ-VVAIGLSGQMHGVVL 82
Cdd:PRK15027 3 IGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQdVKALGIAGQMHGATL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 83 MDAAARPVRPALLWPDTRASREAE--AARWPDAP----NPVAPGMAGPLLCWLAAHEPDTLRAARWAVQPKDWLRVALGG 156
Cdd:PRK15027 83 LDAQQRVLRPAILWNDGRCAQECAllEARVPQSRvitgNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRLRMTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 157 EVAADPSDACATA---LASPDgaWDRARIKALALPADRFAPVRASAARCGTLdARAAAALGLPAGVPLATGAGDTACAAL 233
Cdd:PRK15027 163 EFASDMSDAAGTMwldVAKRD--WSDVMLQACHLSRDQMPALYEGSEITGAL-LPEVAKAWGMATVPVVAGGGDNAAGAV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 234 GSGLVASGDALLTTGSGGQIVVLADA-LPPARRGLHRYRAAAGGGYYTMAAMQNVGLALEAVRGWLGYPDWAAAYDDA-F 311
Cdd:PRK15027 240 GVGMVDANQAMLSLGTSGVYFAVSEGfLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWAAKLTGLSNVPALIAAAqQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 312 AQPPSERLCFLPYLTGERSPWMNPDARGGWLGLALGDTRGAMMRAAFEGVAFALRAGLDAIRDANRDDpvASLRVAGGGS 391
Cdd:PRK15027 320 ADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKP--QSVTLIGGGA 397
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2669191611 392 VDPRWRQLLADALGASLHALECPNAA-TRGAALLAGLAIG 430
Cdd:PRK15027 398 RSEYWRQMLADISGQQLDYRTGGDVGpALGAARLAQIAAN 437
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
2-425 |
1.21e-51 |
|
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: 180.88 E-value: 1.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 2 RLLGIDLGTGSVKLVTIDADG---VERAVASEPYPLSSPRPGWAEIAPETWWDALVRAAARLPADERAQVVAIGLSGQMH 78
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLESgriLESVSRPTPAPISSDDPGRSEQDPEKILEAVRNLIDELPREYLSDVTGIGITGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 79 GVVLMDAAARPVRPALLWPDTRASREAEAARWPDAPN-------PVAPGMAGPLLCWLAAHEPDTLRAARwAVQPKDWLR 151
Cdd:cd07777 81 GIVLWDEDGNPVSPLITWQDQRCSEEFLGGLSTYGEEllpksgmRLKPGYGLATLFWLLRNGPLPSKADR-AGTIGDYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 152 VALGG--EVAADPSDACATALASPD-GAWDRARIKALALPADRFAPVRASAARCGTLdaraaaALGLPAGVPLATGAGDT 228
Cdd:cd07777 160 ARLTGlpKPVMHPTNAASWGLFDLEtGTWNKDLLEALGLPVILLPEIVPSGEIVGTL------SSALPKGIPVYVALGDN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 229 ACAALGSGLVASGDALLTTGSGGQIVVLADALPParRGLHRYRAAAGGGYYTMAAMQNVGLALEA----VRGWL----GY 300
Cdd:cd07777 234 QASVLGSGLNEENDAVLNIGTGAQLSFLTPKFEL--SGSVEIRPFFDGRYLLVAASLPGGRALAVlvdfLREWLrelgGS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 301 PDWAAAYD---DAFAQPPSERLCFLPYLTGERspwMNPDARGGWLGLALGD-TRGAMMRAAFEGVAFALRAGLDaiRDAN 376
Cdd:cd07777 312 LSDDEIWEkldELAESEESSDLSVDPTFFGER---HDPEGRGSITNIGESNfTLGNLFRALCRGIAENLHEMLP--RLDL 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2669191611 377 RDDPVASLRVAGGGSV-DPRWRQLLADALGASLHALECPNAATRGAALLA 425
Cdd:cd07777 387 DLSGIERIVGSGGALRkNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
4-234 |
3.81e-47 |
|
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: 163.28 E-value: 3.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 4 LGIDLGTGSVKLVTIDADGVERAVASEPYPLSSPRPGWAEIAPETWWDALVRAAA----RLPADERaQVVAIGLSGQMHG 79
Cdd:pfam00370 3 LGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAktlsQLGISLK-QIKGIGISNQGHG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 80 VVLMDAAARPVRPALLWPDTRASREAEAAR--------WPDAPNPVAPGMAGPLLCWLAAHEPDTLRAARWAVQPKDWLR 151
Cdd:pfam00370 82 TVLLDKNDKPLYNAILWKDRRTAEIVENLKeegnnqklYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIHDYLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 152 VALGGEVAADPSDACATALAS-PDGAWDRARIKALALPADRFAPVRASAARCGTLDARAAAALGLPAGVPLATGAGDTAC 230
Cdd:pfam00370 162 WRLTGVFVTDHTNASRSMMFNiHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGGDQQA 241
|
....
gi 2669191611 231 AALG 234
Cdd:pfam00370 242 AAFG 245
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
3-430 |
4.14e-46 |
|
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: 167.33 E-value: 4.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 3 LLGIDLGTGSVKLVTID-ADGVERAVASEPYPLS--SPRPGWAEIAPETWWDALVRAAARLPADE---RAQVVAIGLSGQ 76
Cdd:cd07781 2 VIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGyiPPRPGWAEQNPADYWEALEEAVRGALAEAgvdPEDVVGIGVDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 77 MHGVVLMDAAARPVRPALLWPDTRASREAEA-ARWPDAPNPVAPGMAG---------PLLCWLAAHEPDTLRAARWAVQP 146
Cdd:cd07781 82 SSTVVPVDEDGNPLAPAILWMDHRAQEEAAEiNETAHPALEYYLAYYGgvyssewmwPKALWLKRNAPEVYDAAYTIVEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 147 KDWLRVALGGEVAADPSDACATALASPDGA-WDRARIKALALPADR-----FAPVRASAARCGTLDARAAAALGLPAGVP 220
Cdd:cd07781 162 CDWINARLTGRWVRSRCAAGHKWMYNEWGGgPPREFLAALDPGLLKlreklPGEVVPVGEPAGTLTAEAAERLGLPAGIP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 221 LATGAGDTACAALGSGLVASGDALLTTGSGGQIVVLADALPPARRGLHRYRAAAGGGYYTMAAMQN-VGLALEAVRGWLG 299
Cdd:cd07781 242 VAQGGIDAHMGAIGAGVVEPGTLALIMGTSTCHLMVSPKPVDIPGICGPVPDAVVPGLYGLEAGQSaVGDIFAWFVRLFV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 300 YPDWAAAYDD-------AFAQPP-SERLCFLPYLTGERSPWMNPDARGGWLGLALGDTRGAMMRAAFEGVAFALRAGLDA 371
Cdd:cd07781 322 PPAEERGDSIyallseeAAKLPPgESGLVALDWFNGNRTPLVDPRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIER 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 372 IRDANRddPVASLRVAGGGSV-DPRWRQLLADALGASLHALECPNAATRGAALLAGLAIG 430
Cdd:cd07781 402 FEEAGV--PVNRVVACGGIAEkNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVAAG 459
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
3-430 |
2.19e-40 |
|
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: 150.45 E-value: 2.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 3 LLGIDLGTGSVKLVTIDADGVERAVASEPYPLSSP-RPGWA-EIAPETWWDALVRAAARL---PADERAQVVAIGLSGQM 77
Cdd:cd07798 2 YLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDdDYPDAkEFDPEELWEKICEAIREAlkkAGISPEDISAVSSTSQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 78 HGVVLMDAAARPV--------RpALLWPDTRASREAEA-----ARWPDAPNPVAPgmagplLCWLAAHEPDTLRAARWAV 144
Cdd:cd07798 82 EGIVFLDKDGRELyagpnidaR-GVEEAAEIDDEFGEEiytttGHWPTELFPAAR------LLWFKENRPEIFERIATVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 145 QPKDWLRVALGGEVAADPSDACATALAspD---GAWDRARIKALALPADRFAPVRASAARCGTLDARAAAALGLPAGVPL 221
Cdd:cd07798 155 SISDWIGYRLTGELVSEPSQASETQLF--DikkREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAARELGLPEGTPV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 222 ATGAGDTACAALGSGLVASGDALLTTGSGGQIV-VLADALP-PARR---GLHryraaAGGGYYTM---AAMqnVGLALEA 293
Cdd:cd07798 233 VVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQmVTDEPIIdPERRlwtGCH-----LVPGKWVLesnAGV--TGLNYQW 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 294 VRGWLgYPDWAAAYDDAFAQ----PPSERLCfLPYLTGER-SPWMNPDARGGWLGLALGD----TRGAMMRAAFEGVAFA 364
Cdd:cd07798 306 LKELL-YGDPEDSYEVLEEEaseiPPGANGV-LAFLGPQIfDARLSGLKNGGFLFPTPLSaselTRGDFARAILENIAFA 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2669191611 365 LRAGLDAIRDAnRDDPVASLRVAGGGSVDPRWRQLLADALGASLHALECPNAATRGAALLAGLAIG 430
Cdd:cd07798 384 IRANLEQLEEV-SGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
4-433 |
5.66e-36 |
|
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: 139.23 E-value: 5.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 4 LGIDLGTGSVKLVTIDADGVERAVASEPYPLSSPRPGWAEIAPETWWDALVR------AAARLPAderAQVVAIGLSGQM 77
Cdd:cd07793 3 LAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKvikealKNAGLTP---EDIAAIGISTQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 78 HGVVLMDA-AARPVRPALLWPDTRASREAEaaRWPDAP-----NPVA---------------------PGMAGPLLCWLA 130
Cdd:cd07793 80 NTFLTWDKkTGKPLHNFITWQDLRAAELCE--SWNRSLllkalRGGSkflhfltrnkrflaasvlkfsTAHVSIRLLWIL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 131 AHEPDTLRAARwavqpKD---------WLRVAL-GGEV-AADPSDACATALASP-DGAWDRARIKALALPADRFAPVRAS 198
Cdd:cd07793 158 QNNPELKEAAE-----KGellfgtidtWLLWKLtGGKVhATDYSNASATGLFDPfTLEWSPILLSLFGIPSSILPEVKDT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 199 AARCGTLDARAAAALglpagVPLATGAGDTACAALGSGLVASGDALLTTGSGGQI-VVLADALPPARRGLhrYRAAA--- 274
Cdd:cd07793 233 SGDFGSTDPSIFGAE-----IPITAVVADQQAALFGECCFDKGDVKITMGTGTFIdINTGSKPHASVKGL--YPLVGwki 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 275 GGGYYTMA--AMQNVGLALEAVRGWLGYPDWAAAYDDAFAQPPSERLCFLPYLTGERSPWMNPDARGGWLGLALGDTRGA 352
Cdd:cd07793 306 GGEITYLAegNASDTGTVIDWAKSIGLFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 353 MMRAAFEGVAFALRAGLDAIRDANRdDPVASLRVAGGGSVDPRWRQLLADALGASLHALECPNAATRGAALLAGLAIGHW 432
Cdd:cd07793 386 LVRAILESIAFRVKQLLETMEKETS-IKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIW 464
|
.
gi 2669191611 433 S 433
Cdd:cd07793 465 K 465
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
4-433 |
8.44e-31 |
|
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: 124.50 E-value: 8.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 4 LGIDLGTGSVKLVTIDADGVERAVASEPYPLSSPRPGWAEIAPETWWDALVRAAARLPAD---ERAQVVAIGLSGQMHGV 80
Cdd:cd07769 3 LAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKagiSASDIAAIGITNQRETT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 81 VLMDAA-ARPVRPALLWPDTRASREAEaaRWPDAPN----------PVAPGMAGPLLCWLAAHEPDTLRAA---RWAVQP 146
Cdd:cd07769 83 VVWDKKtGKPLYNAIVWQDRRTADICE--ELKAKGLeerirektglPLDPYFSATKIKWILDNVPGARERAergELLFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 147 KD-WLRVAL-GGEVAA-DPSDACATALASP-DGAWDRARIKALALPADRFAPVRASAARCGTLDARAAAALglpagVPLA 222
Cdd:cd07769 161 IDtWLIWKLtGGKVHVtDVTNASRTMLFNIhTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTDPEGLGAG-----IPIA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 223 TGAGDTACAALGSGLVASGDALLTTGSGGQIVV-LADALPPARRGL----------HRYRAAAGGGYYTmaamqnvGLAL 291
Cdd:cd07769 236 GILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMnTGEKPVPSKNGLlttiawqiggKVTYALEGSIFIA-------GAAI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 292 EAVRGWLGYPDWAAAYDD-AFAQPPSERLCFLPYLTGERSPWMNPDARGGWLGLALGDTRGAMMRAAFEGVAFALRAGLD 370
Cdd:cd07769 309 QWLRDNLGLIEDAAETEElARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLE 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2669191611 371 AI-RDANRddPVASLRVAGGGSVDPRWRQLLADALGASLHALECPNAATRGAALLAGLAIGHWS 433
Cdd:cd07769 389 AMeKDSGI--KLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWK 450
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
3-434 |
8.97e-28 |
|
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466794 [Multi-domain] Cd Length: 492 Bit Score: 115.89 E-value: 8.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 3 LLGIDLGTGSVKLVTIDADGVERAVASEPYP-LSSPR-PGWAEIAPETWWDALVRAAARLPAD---ERAQVVAIGLSGQM 77
Cdd:cd07775 2 LLALDAGTGSGRAVIFDLEGNQIAVAQREWRhKEVPDvPGSMDFDTEKNWKLICECIREALKKagiAPKSIAAISTTSMR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 78 HGVVLMDAAARPvrpalLWP----DTRASREAEAARwpDAPNPVAPGM-----------AGPLLCWLAAHEPDTLRAARW 142
Cdd:cd07775 82 EGIVLYDNEGEE-----IWAcanvDARAAEEVSELK--ELYNTLEEEVyrisgqtfalgAIPRLLWLKNNRPEIYRKAAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 143 AVQPKDWLRVALGGEVAADPSDACATAL-ASPDGAWDRARIKALALPADRFAPVRASAARCGTLDARAAAALGLPAGVPL 221
Cdd:cd07775 155 ITMLSDWIAYKLSGELAVEPSNGSTTGLfDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEAAEETGLKEGTPV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 222 ATGAGDTACAALGSGLVASGDALLTTGSGGQIVVLADALPPARRGLHRYRAAAGGGYYTMAAMQ-NVGLALEAVRgwlgy 300
Cdd:cd07775 235 VVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMNIRVNCHVIPDMWQAEGISfFPGLVMRWFR----- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 301 pdwaaaydDAFAQPPSE---RLCFLPY-LTGERSPWMNPDARG------------GW-------LGLALGD---TRGAMM 354
Cdd:cd07775 310 --------DAFCAEEKEiaeRLGIDAYdLLEEMAKDVPPGSYGimpifsdvmnykNWrhaapsfLNLDIDPekcNKATFF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 355 RAAFEGVAFALRAGLDAIRDANRDDPvASLRVAGGGSVDPRWRQLLADALGASLHALECPNAATRGAALLAGLAIGHWSE 434
Cdd:cd07775 382 RAIMENAAIVSAGNLERIAEFSGIFP-DSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAGIYSS 460
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
3-433 |
7.76e-27 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 112.85 E-value: 7.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 3 LLGIDLGTGSVKLVTIDADGVERAVASEPYPLSSPRPGWAEIAPETWWDALVRAAARLPAD---ERAQVVAIGLSGQMHG 79
Cdd:COG0554 5 ILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKagiSAEDIAAIGITNQRET 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 80 VVLMDAA-ARPVRPALLWPDTRASREAEA-ARWPDAPN-------PVAPGMAGPLLCWLAAHEPDtlraARWAVQPKD-- 148
Cdd:COG0554 85 TVVWDRKtGKPLYNAIVWQDRRTADICEElKADGLEDLirektglVLDPYFSATKIKWILDNVPG----ARERAEAGEll 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 149 ------WLRVAL-GGEV-AADPSDACATALASP-DGAWDRARIKALALPADRFAPVRASAARCGTLDARAAAALglpagV 219
Cdd:COG0554 161 fgtidsWLIWKLtGGKVhVTDVTNASRTMLFNIhTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDPDLFGAE-----I 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 220 PLATGAGD---------------------TACAAL---GSGLVASGDALLTT---GSGGQIVvladalpparrglhrYrA 272
Cdd:COG0554 236 PIAGIAGDqqaalfgqacfepgmakntygTGCFLLmntGDEPVRSKNGLLTTiawGLGGKVT---------------Y-A 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 273 AAGGGYYTMAAMQnvglaleavrgWLGypDWAAAYDDA-----FAQ--PPSERLCFLPYLTGERSPWMNPDARGGWLGLA 345
Cdd:COG0554 300 LEGSIFVAGAAVQ-----------WLR--DGLGLIDSAaeseaLARsvEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 346 LGDTRGAMMRAAFEGVAFALRAGLDAIR-DANRddPVASLRVAGGGSVDPRWRQLLADALGASLHALECPNAATRGAALL 424
Cdd:COG0554 367 RGTTRAHIARAALESIAYQTRDVLDAMEaDSGI--PLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYL 444
|
....*....
gi 2669191611 425 AGLAIGHWS 433
Cdd:COG0554 445 AGLAVGFWK 453
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
3-433 |
8.48e-27 |
|
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: 112.58 E-value: 8.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 3 LLGIDLGTGSVKLVTIDADGVERAVASEPYPLSSPRPGWAEIAPETWWDALVRAAARLPAD---ERAQVVAIGLSGQMHG 79
Cdd:cd07786 2 ILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKagiRASDIAAIGITNQRET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 80 VVLMDAAA-RPVRPALLWPDTRASREAE---AARWPDAPN-----PVAPGMAGPLLCWLAAHEPDtlraARWAVQPKD-- 148
Cdd:cd07786 82 TVVWDRETgKPVYNAIVWQDRRTADICEelkAEGHEEMIRektglVLDPYFSATKIRWILDNVPG----ARERAERGEla 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 149 ------WLRVAL-GGEV-AADPSDACATAL-ASPDGAWDRARIKALALPADRFAPVRASAARCGTLDARAAAALglpagV 219
Cdd:cd07786 158 fgtidsWLIWKLtGGKVhATDVTNASRTMLfNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDPDLLGAE-----I 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 220 PLATGAGDTACAALGSGLVASGDALLTTGSGGQIVV-LADALPPARRGLHRyraaagggyyTMAAMQN--VGLALE---- 292
Cdd:cd07786 233 PIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMnTGEKPVRSKNGLLT----------TIAWQLGgkVTYALEgsif 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 293 ---AVRGWLGypD-----WAAAYDDAFAQ--PPSERLCFLPYLTGERSPWMNPDARGGWLGLALGDTRGAMMRAAFEGVA 362
Cdd:cd07786 303 iagAAVQWLR--DglgliESAAETEALARsvPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIA 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2669191611 363 FALRAGLDAIR-DANRddPVASLRVAGGGSVDPRWRQLLADALGASLHALECPNAATRGAALLAGLAIGHWS 433
Cdd:cd07786 381 YQTRDLLEAMEaDSGI--PLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWK 450
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
3-434 |
1.77e-24 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 106.21 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 3 LLGIDLGTGSVKLVTIDADGVERAVASEPYPLSSPRPGWAEIAPETWWD----ALVRAAARL-PADERAQVVAIGLSGQM 77
Cdd:PTZ00294 4 IGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRnvykCMNEAIKKLrEKGPSFKIKAIGITNQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 78 HGVVLMDAA-ARPVRPALLWPDTRAsrEAEAARWPDAPN-----------PVAPGMAGPLLCWLAAHEPdtlrAARWAVQ 145
Cdd:PTZ00294 84 ETVVAWDKVtGKPLYNAIVWLDTRT--YDIVNELTKKYGgsnffqkitglPISTYFSAFKIRWMLENVP----AVKDAVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 146 PKD--------WLRVAL--GGEVAADPSDACATALASPDG-AWDRARIKALALPADRFAPVRASAARCGTLdarAAAALG 214
Cdd:PTZ00294 158 EGTllfgtidtWLIWNLtgGKSHVTDVTNASRTFLMNIKTlKWDEELLNKFGIPKETLPEIKSSSENFGTI---SGEAVP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 215 LPAGVPLATGAGDTACAALGSGLVASGDALLTTGSGGQIVV-LADALPPARRGL-----HRYRAAAGGGYYTMAAMQNVG 288
Cdd:PTZ00294 235 LLEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMnTGTEIVFSKHGLlttvcYQLGPNGPTVYALEGSIAVAG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 289 LALEAVRGWLG-YPDWAAAYDDAFAQPPSERLCFLPYLTGERSPWMNPDARGGWLGLALGDTRGAMMRAAFEGVAFALRA 367
Cdd:PTZ00294 315 AGVEWLRDNMGlISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTND 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2669191611 368 GLDA-IRDANRddPVASLRVAGGGSVDPRWRQLLADALGASLHALECPNAATRGAALLAGLAIGHWSE 434
Cdd:PTZ00294 395 VIESmEKDAGI--ELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKS 460
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
249-428 |
1.42e-22 |
|
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: 95.08 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 249 SGGQIVVLADALPPARRGLHRYRAAAGGGYYTM--------AAMQNVGLALEAVRGWL---GYPDWAAAYDDAfAQPPSE 317
Cdd:pfam02782 8 SSFVLVETPEPVLSVHGVWGPYTNEMLPGYWGLeggqsaagSLLAWLLQFHGLREELRdagNVESLAELAALA-AVAPAG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 318 RLCFLPYLTGERSPWMNPDARGGWLGLALGDTRGAMMRAAFEGVAFALRAGLDAIRDAnRDDPVASLRVAGGGSVDPRWR 397
Cdd:pfam02782 87 GLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQ-EGHPIDTIHVSGGGSRNPLLL 165
|
170 180 190
....*....|....*....|....*....|.
gi 2669191611 398 QLLADALGASLHALECPNAATRGAALLAGLA 428
Cdd:pfam02782 166 QLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
6-434 |
2.22e-21 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 96.69 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 6 IDLGTGSVKLVTIDADGVERAVASEPYPLSSPRPGWAEIAPETWWD----ALVRAAARLPADE---RAQVVAIGLSGQMH 78
Cdd:PLN02295 5 IDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILEsvltCIAKALEKAAAKGhnvDSGLKAIGITNQRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 79 GVVLMDAA-ARPVRPALLWPDTRASREAEA--ARWPDAPN--------PVAPGMAGPLLCWLAAHEPdtlrAARWAVQPK 147
Cdd:PLN02295 85 TTVAWSKStGRPLYNAIVWMDSRTSSICRRleKELSGGRKhfvetcglPISTYFSATKLLWLLENVD----AVKEAVKSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 148 D--------WLRVAL-----GGEVAADPSDACATALASPDG-AWDRARIKALALPADRFAPVRASAARCGTLDARAAAAL 213
Cdd:PLN02295 161 DalfgtidsWLIWNLtggasGGVHVTDVTNASRTMLMNLKTlDWDKPTLEALGIPAEILPKIVSNSEVIGTIAKGWPLAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 214 glpagVPLATGAGDTACAALGSgLVASGDALLTTGSG-------GQIVVladalpPARRGL-----HRYRAAAGGGYYTM 281
Cdd:PLN02295 241 -----VPIAGCLGDQHAAMLGQ-RCRPGEAKSTYGTGcfillntGEEVV------PSKHGLlttvaYKLGPDAPTNYALE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 282 AAMQNVGLALEAVRGWLGYPDWAAAYDDAFAQ-PPSERLCFLPYLTGERSPWMNPDARGGWLGLALGDTRGAMMRAAFEG 360
Cdd:PLN02295 309 GSVAIAGAAVQWLRDNLGIIKSASEIEALAATvDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLES 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2669191611 361 VAFALRAGLDAIR-DANRDDPV---ASLRVAGGGSVDPRWRQLLADALGASLHALECPNAATRGAALLAGLAIGHWSE 434
Cdd:PLN02295 389 MCFQVKDVLDAMRkDAGEEKSHkglFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTE 466
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
3-433 |
6.73e-21 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 95.46 E-value: 6.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 3 LLGIDLGTGSVKLVTIDADGVERAVASEPYP-LSSPR-PGWAEIAPETWWDALVR------AAARLPAderAQVVAIGLS 74
Cdd:PRK10939 5 LMALDAGTGSIRAVIFDLNGNQIAVGQAEWRhLAVPDvPGSMEFDLEKNWQLACQcirqalQKAGIPA---SDIAAVSAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 75 GQMHGVVLMDAAARPvrpalLWP----DTRASREAEA--ARWPDAPNPV--------APGmAGPLLCWLAAHEPDTLRAA 140
Cdd:PRK10939 82 SMREGIVLYDRNGTE-----IWAcanvDARASREVSElkELHNNFEEEVyrcsgqtlALG-ALPRLLWLAHHRPDIYRQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 141 RWAVQPKDWLRVALGGEVAADPSDACATALAS-PDGAWDRARIKALALPADRFAPVRASAARCGTLDARAAAALGLPAGV 219
Cdd:PRK10939 156 HTITMISDWIAYMLSGELAVDPSNAGTTGLLDlVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAKAAAETGLRAGT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 220 PLATGAGDTACAALGSGLVASGDALLTTGSGGQIVV--LADALPPARR---------GLHRYRAAAgggYYTMAAMQ--- 285
Cdd:PRK10939 236 PVVMGGGDVQLGCLGLGVVRPGQTAVLGGTFWQQVVnlPAPVTDPNMNirinphvipGMVQAESIS---FFTGLTMRwfr 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 286 ---NVGLALEAVRgwLGYPDWAAAYDDAFAQPP---------SERLCFlpyltgerSPWMNpdARGGWLGLALGD---TR 350
Cdd:PRK10939 313 dafCAEEKLLAER--LGIDAYSLLEEMASRVPVgshgiipifSDVMRF--------KSWYH--AAPSFINLSIDPekcNK 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 351 GAMMRAAFEGVAFALRAGLDAIRDANRDDPvASLRVAGGGSVDPRWRQLLADALGASLHALECPNAATRGAALLAGLAIG 430
Cdd:PRK10939 381 ATLFRALEENAAIVSACNLQQIAAFSGVFP-SSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGAG 459
|
...
gi 2669191611 431 HWS 433
Cdd:PRK10939 460 IYS 462
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
6-434 |
5.14e-19 |
|
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: 89.51 E-value: 5.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 6 IDLGTGSVKLVTIDADGVERAVASEPYPLSSPRPGWAEIAPETWWDALVR----AAARLPADER--AQVVAIGLSGQMHG 79
Cdd:cd07792 6 IDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYEcieeAVEKLKALGIspSDIKAIGITNQRET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 80 VVLMDAAA-RPVRPALLWPDTRASREAEA--ARWPDAPN--------PVAPGMAGPLLCWLAAHEPdtlrAARWAVQPKD 148
Cdd:cd07792 86 TVVWDKSTgKPLYNAIVWLDTRTSDTVEElsAKTPGGKDhfrkktglPISTYFSAVKLRWLLDNVP----EVKKAVDDGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 149 --------WLRVALGGEVAA-----DPSDACATALASPD-GAWDRARIKALALPADRFAPVRASAARCGTLDARAAAAlg 214
Cdd:cd07792 162 llfgtvdsWLIWNLTGGKNGgvhvtDVTNASRTMLMNLRtLQWDPELCEFFGIPMSILPEIRSSSEVYGKIASGPLAG-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 215 lpagVPLATGAGDTACAALGSGLVASGDALLTTGSG-------GQIVVladalpPARRGLHRYRAaagggyYTMAAMQNV 287
Cdd:cd07792 240 ----VPISGCLGDQQAALVGQGCFKPGEAKNTYGTGcfllyntGEEPV------FSKHGLLTTVA------YKLGPDAPP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 288 GLALE---AVRG----WL----GYPDWAAAYDDAFAQ-PPSERLCFLPYLTGERSPWMNPDARGGWLGLALGDTRGAMMR 355
Cdd:cd07792 304 VYALEgsiAIAGaavqWLrdnlGIISSASEVETLAASvPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIAR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 356 AAFEGVAFALRAGLDAI-RDAnrDDPVASLRVAGGGSVDPRWRQLLADALGASLHALECPNAATRGAALLAGLAIGHWSE 434
Cdd:cd07792 384 AALEAVCFQTREILDAMnKDS--GIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKS 461
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
4-433 |
4.51e-16 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 80.25 E-value: 4.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 4 LGIDLGTGSVKLVTIDADGVERAVASEPYPLSSPRPGWAEIAPETWWDALVRAAARLPAD---ERAQVVAIGLSGQMHGV 80
Cdd:PRK00047 8 LALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKagiSPDQIAAIGITNQRETT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 81 VLMD-AAARPVRPALLWPDTRASREAEAARWPDAPN--------PVAPGMAGPLLCWLAAHEPdtlrAARWAVQPKD--- 148
Cdd:PRK00047 88 VVWDkETGRPIYNAIVWQDRRTADICEELKRDGYEDyirektglVIDPYFSGTKIKWILDNVE----GARERAEKGEllf 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 149 -----WLRVAL-GGEV-AADPSDACATALAS-PDGAWDRARIKALALPADRFAPVRASAARCGTldarAAAALGLPAGVP 220
Cdd:PRK00047 164 gtidtWLVWKLtGGKVhVTDYTNASRTMLFNiHTLDWDDELLELLDIPRSMLPEVRPSSEVYGK----TNPYGFFGGEVP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 221 LATGAGDTACAALGSGLVASGDALLTTGSGGQIVV-LADALPPARRGLhryraaagggyYTMAAMQ---NVGLALE---A 293
Cdd:PRK00047 240 IAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMnTGEKAVKSENGL-----------LTTIAWGidgKVVYALEgsiF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 294 VRG----WLgyPD-----WAAAYDDAFAQ--PPSERLCFLPYLTGERSPWMNPDARGGWLGLALGDTRGAMMRAAFEGVA 362
Cdd:PRK00047 309 VAGsaiqWL--RDglkiiSDASDSEALARkvEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIA 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2669191611 363 FALRAGLDAI-RDANRDdpVASLRVAGGGSVDPRWRQLLADALGASLHALECPNAATRGAALLAGLAIGHWS 433
Cdd:PRK00047 387 YQTRDVLDAMqADSGIR--LKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWK 456
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
126-425 |
1.50e-14 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 75.45 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 126 LCWLAAHEPDTLRaarwavQPKDWLRVA------LGGEVAADPSDACATALAS-PDGAWDRARIKALALPADRFAPVRAS 198
Cdd:PRK10331 138 LVWLKENHPQLLE------QAHAWLFISslinhrLTGEFTTDITMAGTSQMLDiQQRDFSPEILQATGLSRRLFPRLVEA 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 199 AARCGTLDARAAAALGLPAGVPLATGAGDTACAALGSGlVASGDALLTTGSGGQIVVLADALPPARrgLHRYRAA----- 273
Cdd:PRK10331 212 GEQIGTLQPSAAALLGLPVGIPVISAGHDTQFALFGSG-AGQNQPVLSSGTWEILMVRSAQVDTSL--LSQYAGStceld 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 274 AGGGYYTmAAMQNVGLA-LEAVRGWLGYPD--WAAAYDDAFAQPPserlcflpyltGERSPWMNPD----ARGGWLGLAL 346
Cdd:PRK10331 289 SQSGLYN-PGMQWLASGvLEWVRKLFWTAEtpYQTMIEEARAIPP-----------GADGVKMQCDllacQNAGWQGVTL 356
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2669191611 347 GDTRGAMMRAAFEGVAFALRAGLDAIRDANRDDpVASLRVAGGGSVDPRWRQLLADALGASLHALECPNAATRGAALLA 425
Cdd:PRK10331 357 NTTRGHFYRAALEGLTAQLKRNLQVLEKIGHFK-ASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFG 434
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
4-430 |
6.19e-10 |
|
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: 61.49 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 4 LGIDLGTGSVKLVTID-ADGVERAVASEPY-PLSSPRPGWAEIAPETWWDAL---VRAAARLPADERAQVVAIGLSGQMH 78
Cdd:cd07768 3 IGVDVGTSSARAGVYDlYAGLEMAQEPVPYyQDSSKKSWKFWQKSTEIIKALqkcVQKLNIREGVDAYEVKGCGVDATCS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 79 GVVL--------MDAAARPVRPALLWPDTRASREAEA--ARWPDAPNP-----VAPGMAGPLLCWLAAHEPDTLRAARWA 143
Cdd:cd07768 83 LAIFdregtplmALIPYPNEDNVIFWMDHSAVNEAQWinMQCPQQLLDylggkISPEMGVPKLKYFLDEYSHLRDKHFHI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 144 VQPKDWLRVALGG-EVAADPSDACATALASPDGAWDRARIKAL--ALPADRFAPVRAS----AARCGTLDARAAAALGLP 216
Cdd:cd07768 163 FDLHDYIAYELTRlYEWNICGLLGKENLDGEESGWSSSFFKNIdpRLEHLTTTKNLPSnvpiGTTSGVALPEMAEKMGLH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 217 AGVPLATGAGDTACAALGSGlVASGDALLTTGSGGQIVVLADAlpparRGLHR-------YRAAAGGGYYTMAAMQNVGL 289
Cdd:cd07768 243 PGTAVVVSCIDAHASWFAVA-SPHLETSLFMIAGTSSCHMYGT-----TISDRipgvwgpFDTIIDPDYSVYEAGQSATG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 290 ALEA--VRGWLGYPDWAAAYDDA-------------FAQPP--SERLCFLPYLTGERSPWMNPDARGGWLGLALGDTRGA 352
Cdd:cd07768 317 KLIEhlFESHPCARKFDEALKKGadiyqvleqtirqIEKNNglSIHILTLDMFFGNRSEFADPRLKGSFIGESLDTSMLN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 353 M---MRAAFEGVAFALRAGLDAIRdaNRDDPVASLRVAGGGSVDPRWRQLLADALGASLHALECPNAATRGAALLAGLAI 429
Cdd:cd07768 397 LtykYIAILEALAFGTRLIIDTFQ--NEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAAVLAKVAA 474
|
.
gi 2669191611 430 G 430
Cdd:cd07768 475 G 475
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
2-405 |
3.30e-09 |
|
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: 58.69 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 2 RLLGIDLGTGSVK--LVTIDADGVERAV----ASEPYplssprpgwaEIAPETWWDAL-----VRAAARLPADERAQVVA 70
Cdd:cd07771 1 NYLAVDLGASSGRviLGSLDGGKLELEEihrfPNRPV----------EINGHLYWDIDrlfdeIKEGLKKAAEQGGDIDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 71 IGLSGqmHGV--VLMDAAARPVRPALLWPDTR--ASREAEAARWPDA------PNPVAPGMAGPLLCWLAAHEPDTL-RA 139
Cdd:cd07771 71 IGIDT--WGVdfGLLDKNGELLGNPVHYRDPRteGMMEELFEKISKEelyertGIQFQPINTLYQLYALKKEGPELLeRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 140 ARWAVQPkDWLRVALGGEVAADPSDACATALASPD-GAWDRARIKALALPADRFAPVRASAARCGTLDaRAAAALGLPAG 218
Cdd:cd07771 149 DKLLMLP-DLLNYLLTGEKVAEYTIASTTQLLDPRtKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLK-PEVAEELGLKG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 219 VPLATGAG-DTACAALGSGLVASGDALLTTGSGGQI-------VVLADALppaRRGLHRYRAAAGG--------GYYTma 282
Cdd:cd07771 227 IPVIAVAShDTASAVAAVPAEDEDAAFISSGTWSLIgveldepVITEEAF---EAGFTNEGGADGTirllknitGLWL-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 283 aMQNVGLALEAVRGWLGYPD-----WAAAYDDAFAQPPSERLcFLP---------YL--TGERSPwmnpdarggwlglal 346
Cdd:cd07771 302 -LQECRREWEEEGKDYSYDElvalaEEAPPFGAFIDPDDPRF-LNPgdmpeairaYCreTGQPVP--------------- 364
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2669191611 347 gDTRGAMMRAAFEGVAFALRAGLDAIRDANrDDPVASLRVAGGGSVDPRWRQLLADALG 405
Cdd:cd07771 365 -ESPGEIARCIYESLALKYAKTIEELEELT-GKRIDRIHIVGGGSRNALLCQLTADATG 421
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
224-433 |
1.89e-08 |
|
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: 56.41 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 224 GAGDTACAALGSGLvASGDALLTTGSGGQIVVLADALPPARRGlHRYRAAAG-GGYYTMAAMQNVGLALEAVRGWLGYPD 302
Cdd:cd07776 270 FTGDNPASLAGLGL-EPGDVAVSLGTSDTVFLVLDEPKPGPEG-HVFANPVDpGSYMAMLCYKNGSLARERVRDRYAGGS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 303 WAAAYD--DAFAQPPSERLCFlPYLTGERSP-WMNPDARGGWLGLALGDTRGAM-MRAAFEGVAFALRAgldAIRDANRD 378
Cdd:cd07776 348 WEKFNEllESTPPGNNGNLGL-YFDEPEITPpVPGGGRRFFGDDGVDAFFDPAVeVRAVVESQFLSMRL---HAERLGSD 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2669191611 379 DPVASLRVAGGGSVDPRWRQLLADALGASLHALECPNAATRGAALLAGLAIGHWS 433
Cdd:cd07776 424 IPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAG 478
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
321-431 |
5.95e-06 |
|
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: 48.69 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 321 FLPYLTGERSPWMNPDARGGWLGLALGDTRGAMMR---AAFEGVAFALRAGLDAIRDANRddPVASLRVAGGGSVDPRWR 397
Cdd:cd07782 383 VLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHIIEAMNAAGH--KIDTIFMCGGLSKNPLFV 460
|
90 100 110
....*....|....*....|....*....|....
gi 2669191611 398 QLLADALGASLHALECPNAATRGAALLAGLAIGH 431
Cdd:cd07782 461 QLHADVTGCPVVLPKEPEAVLLGAAILGAVASGD 494
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
6-249 |
1.15e-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: 47.64 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 6 IDLGTGSVKLVTIDADGVERAVASEPYPlSSPRPGWAEIAPETWWDALVRAAARLPAdeRAQVVAIGLSGqmHG--VVLM 83
Cdd:cd07772 5 FDIGKTNKKLLLFDENGEVLAERSTPNP-EIEEDGYPCEDVEAIWEWLLDSLAELAK--RHRIDAINFTT--HGatFALL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 84 DAAARPVRPAL--LWPDTRASREAEAARWPDAP---NPVAPGM--AGPLLCWLAAHEPDTLRAARWAV---QPKDWLrva 153
Cdd:cd07772 80 DENGELALPVYdyEKPIPDEINEAYYAERGPFEetgSPPLPGGlnLGKQLYWLKREKPELFARAKTILplpQYWAWR--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 154 LGGEVAADPSDA-CATALASPdGAWDRARIKALALPADRFAPVRASAARCGTLDARAAAALGLPAGVPLATGAGDTAcAA 232
Cdd:cd07772 157 LTGKAASEITSLgCHTDLWDF-EKNEYSSLVKKEGWDKLFPPLRKAWEVLGPLRPDLARRTGLPKDIPVGCGIHDSN-AA 234
|
250
....*....|....*....
gi 2669191611 233 LGSGLVASGD--ALLTTGS 249
Cdd:cd07772 235 LLPYLAAGKEpfTLLSTGT 253
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
93-475 |
1.11e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 45.01 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 93 ALLWPDTRASREAEAARWPDAPNPVAPGMAGPLLCWLAAHEPDTLRAARWAVQPKDWLRVALGGEVAADPSDACATALAS 172
Cdd:COG3903 550 ALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAAL 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 173 PDGAWDRARIKALALPADRFAPVRASAARCGTLDARAAAALGLPAGVPLATGAGDTACAALGSGLVASGDALLTTGSGGQ 252
Cdd:COG3903 630 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAA 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 253 IVVLADALPPARRGLHRYRAAAGGGYYTMAAMQNVGLALEAVRGWLGYPDWAAAYDDAFAQPPSERLCFLPYLTGERSPW 332
Cdd:COG3903 710 ALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAA 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 333 MNPDARGGWLGLALGDTRGAMMRAAFEGVAFALRAGLDAIRDANRDDPVASLRVAGGGSVDPRWRQLLADALGASLHALE 412
Cdd:COG3903 790 AAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAA 869
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2669191611 413 CPNAATRGAALLAGLAIGHWSESALPALAPAASPVAAPRDDRALAARHARFVDLYARTDAWFA 475
Cdd:COG3903 870 LAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAA 932
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
4-106 |
1.64e-04 |
|
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: 44.06 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 4 LGIDLGTGSVKLVTIDADGVERAVASEPYPLSSPRPGWAEIAPETWWDAL---VRAAARLPADERAQVVAIGLSGQMHGV 80
Cdd:cd07782 3 IGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVceaVKEVLEGAGVDPEQVKGIGFDATCSLV 82
|
90 100 110
....*....|....*....|....*....|....*
gi 2669191611 81 VLmDAAARPV---------RPALLWPDTRASREAE 106
Cdd:cd07782 83 VL-DAEGKPVsvspsgddeRNVILWMDHRAVEEAE 116
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
4-430 |
5.41e-04 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 42.53 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 4 LGIDLGTGSVKLVTIDA-DGVERAVASEPYPL------SSPRPGWAEIAPETWWDAL---VRAAARLPADERAQVVAIGL 73
Cdd:PRK04123 6 IGLDFGTDSVRALLVDCaTGEELATAVVEYPHwvkgryLDLPPNQALQHPLDYIESLeaaIPAVLKEAGVDPAAVVGIGV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 74 SGQMHGVVLMDAAARPV--RPAL---------LWPDTRASREAE-----AARWPDAPNPVAPG-------MAGPLLCWLA 130
Cdd:PRK04123 86 DFTGSTPAPVDADGTPLalLPEFaenphamvkLWKDHTAQEEAEeinrlAHERGEADLSRYIGgiyssewFWAKILHVLR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 131 aHEPDTLRAARWAVQPKDWLRVALGGEVaaDPSD----ACAT---AL--ASPDGAWDRARIKAL------ALPADRFAPV 195
Cdd:PRK04123 166 -EDPAVYEAAASWVEACDWVVALLTGTT--DPQDivrsRCAAghkALwhESWGGLPSADFFDALdpllarGLRDKLFTET 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 196 RASAARCGTLDARAAAALGLPAGVPLATGAGDTACAALGSGlVASGDALLTTGSGGQIVVLADALpparrglhryRAAAG 275
Cdd:PRK04123 243 WTAGEPAGTLTAEWAQRLGLPEGVAVSVGAFDAHMGAVGAG-AEPGTLVKVMGTSTCDILLADKQ----------RAVPG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 276 --G--------GYYTMAAMQN-VGLALEAVRGWLGYPDWAAAYDD------------AFAQPPSER-LCFLPYLTGERSP 331
Cdd:PRK04123 312 icGqvdgsivpGLIGYEAGQSaVGDIFAWFARLLVPPEYKDEAEArgkqllellteaAAKQPPGEHgLVALDWFNGRRTP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 332 WMNPDARGGWLGLALGDTRGAMMRAAFEGVAFALRAGLDAIRDAnrDDPVASLRVAGGGSV-DPRWRQLLADALGASLHA 410
Cdd:PRK04123 392 LADQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFEDQ--GVPVEEVIAAGGIARkNPVLMQIYADVLNRPIQV 469
|
490 500
....*....|....*....|
gi 2669191611 411 LECPNAATRGAALLAGLAIG 430
Cdd:PRK04123 470 VASDQCPALGAAIFAAVAAG 489
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
3-135 |
2.44e-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: 40.47 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2669191611 3 LLGIDLGTGSVKLVTIDADGVERAVASEPYP-LSSPRPGW--AEIAPETwWDALVRAAARLPADERA-QVVAIGLSGQMH 78
Cdd:cd07778 2 GIGIDVGSTSVRIGIFDYHGTLLATSERPISyKQDPKDLWfvTQSSTEI-WKAIKTALKELIEELSDyIVSGIGVSATCS 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2669191611 79 GVVL-MDAAA---RPVRPAL----------LWPDTRASREAE--AARWPDAPNP-----VAPGMAGPLLCWLAAHEPD 135
Cdd:cd07778 81 MVVMqRDSDTsylVPYNVIHeksnpdqdiiFWMDHRASEETQwlNNILPDDILDylgggFIPEMAIPKLKYLIDLIKE 158
|
|
| |
