|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
19-540 |
0e+00 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466802 [Multi-domain] Cd Length: 499 Bit Score: 540.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 19 SSThcRFLIYSTKnAEVLAYHELKLRQIVHQAGWMEYDPSEIWKNTQECIETAYKNLVILEINPRDIIAIGIVNQRGTSV 98
Cdd:cd07792 11 TST--RFIVFDST-GELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLKALGISPSDIKAIGITNQRETTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 99 LWNLETGQPLHNAIGWSDCRSTPILKTLLHNVRHNVDYVRYRSGLPLSSCFSALKIRWLMDHVPAVATAIEENKCLFGTL 178
Cdd:cd07792 88 VWDKSTGKPLYNAIVWLDTRTSDTVEELSAKTPGGKDHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDDGRLLFGTV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 179 DSWLLWNLTGGVEMGVHSTDITNAHYTSLMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYVLEGPLHGTPIAAMMG 258
Cdd:cd07792 168 DSWLIWNLTGGKNGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIASGPLAGVPISGCLG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 259 EQPASLLGQLCVKAGQNVCTLDDSCFVLLNTGREKLDSANGLITGIAHKLGEKAATNYTLEGAISNAGSTVTWLRDKLQI 338
Cdd:cd07792 248 DQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAYKLGPDAPPVYALEGSIAIAGAAVQWLRDNLGI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 339 nteINSNDNVVEslntfigensmissscsssmlnaecgLAAK---RSEITFVPAFHGMYAPYWRHDARGIILGLTSQTTA 415
Cdd:cd07792 328 ---ISSASEVET--------------------------LAASvpdTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 416 ENITQAAYEATGFQIFEVLQAFKRDtpnwdrsSMQPVLTF---GGDYAENLhLVQFIADIIGYMLERPQTTSPAGLGVMI 492
Cdd:cd07792 379 AHIARAALEAVCFQTREILDAMNKD-------SGIPLTSLrvdGGMTKNNL-LMQIQADILGIPVERPSMVETTALGAAI 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 386767767 493 TAGVTMKVVSLEHAVKMYT-PPTDVFSPTTTKNRRELLYKRWAYAVKKC 540
Cdd:cd07792 451 AAGLAVGVWKSLDELKSLNeGGRTVFEPQISEEERERRYKRWKKAVERS 499
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
21-543 |
2.25e-167 |
|
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of carbohydrate kinases. [Energy metabolism, Other]
Pssm-ID: 273549 [Multi-domain] Cd Length: 493 Bit Score: 485.59 E-value: 2.25e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 21 THCRFLIYsTKNAEVLAYHELKLRQIVHQAGWMEYDPSEIWKNTQECIETAYKNLVILeinPRDIIAIGIVNQRGTSVLW 100
Cdd:TIGR01311 11 TSSRAIVF-DKDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAGIK---PDDIAAIGITNQRETTVVW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 101 NLETGQPLHNAIGWSDCRSTPILKTLLHNVRhnVDYVRYRSGLPLSSCFSALKIRWLMDHVPAVATAIEENKCLFGTLDS 180
Cdd:TIGR01311 87 DKATGKPLYNAIVWQDRRTASICEELKAEGY--GEFIREKTGLPLDPYFSATKLRWLLDNVPGVREAAERGELLFGTIDT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 181 WLLWNLTGGvemGVHSTDITNAHYTSLMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYVLEG-PLHGTPIAAMMGE 259
Cdd:TIGR01311 165 WLIWNLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYTDPGlLGAEIPITGVLGD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 260 QPASLLGQLCVKAGQNVCTLDDSCFVLLNTGREKLDSANGLITGIAHKLGEKAATnYTLEGAISNAGSTVTWLRDKLQIn 339
Cdd:TIGR01311 242 QQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKKPV-YALEGSVFVAGAAVQWLRDNLKL- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 340 teINSNDNVvESLNTFIGENsmissscsssmlnaecglaakrSEITFVPAFHGMYAPYWRHDARGIILGLTSQTTAENIT 419
Cdd:TIGR01311 320 --IKHAAES-EALARSVEDN----------------------GGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 420 QAAYEATGFQIFEVLQAFKRDTPnwdrSSMQPVLTFGGDYAENLhLVQFIADIIGYMLERPQTTSPAGLGVMITAGVTMK 499
Cdd:TIGR01311 375 RAALEAIAFQTRDVLEAMEKDAG----VEITKLRVDGGMTNNNL-LMQFQADILGVPVVRPKVTETTALGAAYAAGLAVG 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 386767767 500 V-VSLEHAVKMYtPPTDVFSPTTTKNRRELLYKRWAYAVKKCLHW 543
Cdd:TIGR01311 450 YwKSLEEIEALW-RVEKTFEPEMDEEEREARYAGWKEAVKRSLGW 493
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
19-538 |
4.07e-165 |
|
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: 479.66 E-value: 4.07e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 19 SSTHCRFLIYStKNAEVLAYHELKLRQIVHQAGWMEYDPSEIWKNTQECIETAyknLVILEINPRDIIAIGIVNQRGTSV 98
Cdd:cd07769 8 GTTSTRAILFD-EDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREA---LAKAGISASDIAAIGITNQRETTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 99 LWNLETGQPLHNAIGWSDCRSTPILKTLlhNVRHNVDYVRYRSGLPLSSCFSALKIRWLMDHVPAVATAIEENKCLFGTL 178
Cdd:cd07769 84 VWDKKTGKPLYNAIVWQDRRTADICEEL--KAKGLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAERGELLFGTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 179 DSWLLWNLTGGvemGVHSTDITNAHYTSLMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYV-LEGPLHGTPIAAMM 257
Cdd:cd07769 162 DTWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTdPEGLGAGIPIAGIL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 258 GEQPASLLGQLCVKAGQNVCTLDDSCFVLLNTGREKLDSANGLITGIAHKLGEKaaTNYTLEGAISNAGSTVTWLRDKLQ 337
Cdd:cd07769 239 GDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQIGGK--VTYALEGSIFIAGAAIQWLRDNLG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 338 InteINSNDNvVESLntfigensmissscsssmlnaecglaAKRSE----ITFVPAFHGMYAPYWRHDARGIILGLTSQT 413
Cdd:cd07769 317 L---IEDAAE-TEEL--------------------------ARSVEdnggVYFVPAFSGLGAPYWDPDARGAIVGLTRGT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 414 TAENITQAAYEATGFQIFEVLQAFKRDTpnwdrSSMQPVLTFGGDYAENLHLVQFIADIIGYMLERPQ---TTSpagLGV 490
Cdd:cd07769 367 TKAHIVRAALESIAYQTRDVLEAMEKDS-----GIKLKELRVDGGATANNFLMQFQADILGVPVVRPKvaeTTA---LGA 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 386767767 491 MITAGVTMKVVSLEHAVKMYTPPTDVFSPTTTKNRRELLYKRWAYAVK 538
Cdd:cd07769 439 AYLAGLAVGFWKDLDELASLWQVDKRFEPSMDEEERERLYRGWKKAVE 486
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
19-543 |
1.77e-163 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 476.00 E-value: 1.77e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 19 SSTHCRFLIYsTKNAEVLAYHELKLRQIVHQAGWMEYDPSEIWKNTQECIETAYKNLVILEINpRDIIAIGIVNQRGTSV 98
Cdd:PTZ00294 10 GTTSTRFIIF-DEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKGPS-FKIKAIGITNQRETVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 99 LWNLETGQPLHNAIGWSDCRSTPILKTLLhNVRHNVDYVRYRSGLPLSSCFSALKIRWLMDHVPAVATAIEENKCLFGTL 178
Cdd:PTZ00294 88 AWDKVTGKPLYNAIVWLDTRTYDIVNELT-KKYGGSNFFQKITGLPISTYFSAFKIRWMLENVPAVKDAVKEGTLLFGTI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 179 DSWLLWNLTGGvemGVHSTDITNAHYTSLMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYV---LEGPLHGTPIAA 255
Cdd:PTZ00294 167 DTWLIWNLTGG---KSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTIsgeAVPLLEGVPITG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 256 MMGEQPASLLGQLCVKAGQNVCTLDDSCFVLLNTGREKLDSANGLITGIAHKLGEKAATNYTLEGAISNAGSTVTWLRDK 335
Cdd:PTZ00294 244 CIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYQLGPNGPTVYALEGSIAVAGAGVEWLRDN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 336 LQINTEINSNDNVVESLNTFIGensmissscsssmlnaecglaakrseITFVPAFHGMYAPYWRHDARGIILGLTSQTTA 415
Cdd:PTZ00294 324 MGLISHPSEIEKLARSVKDTGG--------------------------VVFVPAFSGLFAPYWRPDARGTIVGMTLKTTR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 416 ENITQAAYEATGFQIFEVLQAFKRDTPNwdrssMQPVLTFGGDYAENLHLVQFIADIIGYMLERPQTTSPAGLGVMITAG 495
Cdd:PTZ00294 378 AHIVRAALEAIALQTNDVIESMEKDAGI-----ELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAG 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 386767767 496 VTMKVV-SLEHAVKMYTPPTDVFSPTTTKNRRELLYKRWAYAVKKCLHW 543
Cdd:PTZ00294 453 LAVGVWkSLEEVKKLIRRSNSTFSPQMSAEERKAIYKEWNKAVERSLKW 501
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
19-543 |
2.14e-156 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 458.39 E-value: 2.14e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 19 SSThcRFLIYsTKNAEVLAYHELKLRQIVHQAGWMEYDPSEIWKNTQECIETAYKNLVILEIN-PRDIIAIGIVNQRGTS 97
Cdd:PLN02295 10 TST--RFIIY-DRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGHNvDSGLKAIGITNQRETT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 98 VLWNLETGQPLHNAIGWSDCRSTPILKTLLHNVRHNVDYVRYRSGLPLSSCFSALKIRWLMDHVPAVATAIEENKCLFGT 177
Cdd:PLN02295 87 VAWSKSTGRPLYNAIVWMDSRTSSICRRLEKELSGGRKHFVETCGLPISTYFSATKLLWLLENVDAVKEAVKSGDALFGT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 178 LDSWLLWNLTGGVEMGVHSTDITNAHYTSLMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYVLEG-PLHGTPIAAM 256
Cdd:PLN02295 167 IDSWLIWNLTGGASGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIAKGwPLAGVPIAGC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 257 MGEQPASLLGQLCvKAGQNVCTLDDSCFVLLNTGREKLDSANGLITGIAHKLGEKAATNYTLEGAISNAGSTVTWLRDKL 336
Cdd:PLN02295 247 LGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYKLGPDAPTNYALEGSVAIAGAAVQWLRDNL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 337 QInteINSNDNvVESLNTFIGENSMissscsssmlnaecglaakrseITFVPAFHGMYAPYWRHDARGIILGLTSQTTAE 416
Cdd:PLN02295 326 GI---IKSASE-IEALAATVDDTGG----------------------VYFVPAFSGLFAPRWRDDARGVCVGITRFTNKA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 417 NITQAAYEATGFQIFEVLQAFKRDTPNWDRSSMQPVLTF-GGDYAENLhLVQFIADIIGYMLERPQTTSPAGLGVMITAG 495
Cdd:PLN02295 380 HIARAVLESMCFQVKDVLDAMRKDAGEEKSHKGLFLLRVdGGATANNL-LMQIQADLLGSPVVRPADIETTALGAAYAAG 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 386767767 496 VTMKVVSLEHAVK--MYTPPTdVFSPTTTKNRRELLYKRWAYAVKKCLHW 543
Cdd:PLN02295 459 LAVGLWTEEEIFAseKWKNTT-TFRPKLDEEERAKRYASWCKAVERSFDL 507
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
21-545 |
1.93e-153 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 450.28 E-value: 1.93e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 21 THCRFLIYsTKNAEVLAYHELKLRQIVHQAGWMEYDPSEIWKNTQECIETAYKNLvilEINPRDIIAIGIVNQRGTSVLW 100
Cdd:COG0554 13 TSTRAILF-DRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKA---GISAEDIAAIGITNQRETTVVW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 101 NLETGQPLHNAIGWSDCRSTPI---LKTLLHNvrhnvDYVRYRSGLPLSSCFSALKIRWLMDHVPAVATAIEENKCLFGT 177
Cdd:COG0554 89 DRKTGKPLYNAIVWQDRRTADIceeLKADGLE-----DLIREKTGLVLDPYFSATKIKWILDNVPGARERAEAGELLFGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 178 LDSWLLWNLTGGvemGVHSTDITNAHYTSLMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYVLEGPL-HGTPIAAM 256
Cdd:COG0554 164 IDSWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDPDLFgAEIPIAGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 257 MGEQPASLLGQLCVKAGQNVCTLDDSCFVLLNTGREKLDSANGLITGIAHKLGEKaaTNYTLEGAISNAGSTVTWLRDKL 336
Cdd:COG0554 241 AGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGGK--VTYALEGSIFVAGAAVQWLRDGL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 337 QInteINSNDnVVESLntfigensmissscsssmlnaecglaAKRSEIT----FVPAFHGMYAPYWRHDARGIILGLTSQ 412
Cdd:COG0554 319 GL---IDSAA-ESEAL--------------------------ARSVEDNggvyFVPAFTGLGAPYWDPDARGAIFGLTRG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 413 TTAENITQAAYEATGFQIFEVLQAFKRDTPnwdrSSMQPVLTFGGDYAENLhLVQFIADIIGYMLERPQ---TTSpagLG 489
Cdd:COG0554 369 TTRAHIARAALESIAYQTRDVLDAMEADSG----IPLKELRVDGGASANDL-LMQFQADILGVPVERPKvteTTA---LG 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 386767767 490 VMITAGVTMKVVSLEHAVKMYTPPTDVFSPTTTKNRRELLYKRWAYAVKKCLHWNN 545
Cdd:COG0554 441 AAYLAGLAVGFWKSLEELAALWKVDRRFEPQMDEEERERLYAGWKKAVERTLGWAE 496
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
21-538 |
1.94e-145 |
|
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: 429.22 E-value: 1.94e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 21 THCRFLIYStKNAEVLAYHELKLRQIVHQAGWMEYDPSEIWKNTQECIETAYKNLvilEINPRDIIAIGIVNQRGTSVLW 100
Cdd:cd07786 10 TSSRAILFD-HDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKA---GIRASDIAAIGITNQRETTVVW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 101 NLETGQPLHNAIGWSDCRSTPI---LKTLLHNvrhnvDYVRYRSGLPLSSCFSALKIRWLMDHVPAVATAIEENKCLFGT 177
Cdd:cd07786 86 DRETGKPVYNAIVWQDRRTADIceeLKAEGHE-----EMIREKTGLVLDPYFSATKIRWILDNVPGARERAERGELAFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 178 LDSWLLWNLTGGvemGVHSTDITNAHYTSLMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYVLEGPL-HGTPIAAM 256
Cdd:cd07786 161 IDSWLIWKLTGG---KVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDPDLLgAEIPIAGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 257 MGEQPASLLGQLCVKAGQNVCTLDDSCFVLLNTGREKLDSANGLITGIAHKLGEKaaTNYTLEGAISNAGSTVTWLRDKL 336
Cdd:cd07786 238 AGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLGGK--VTYALEGSIFIAGAAVQWLRDGL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 337 QInteINSNdnvveslntfigensmissscsssmlnAECGLAAKRSE----ITFVPAFHGMYAPYWRHDARGIILGLTSQ 412
Cdd:cd07786 316 GL---IESA---------------------------AETEALARSVPdnggVYFVPAFTGLGAPYWDPDARGAIFGLTRG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 413 TTAENITQAAYEATGFQIFEVLQAFKRDTPnwdrSSMQpVLTFGGDYAENLHLVQFIADIIGYMLERPQTTSPAGLGVMI 492
Cdd:cd07786 366 TTRAHIARAALESIAYQTRDLLEAMEADSG----IPLK-ELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAY 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 386767767 493 TAGVTMKVVSLEHAVKMYTPPTDVFSPTTTKNRRELLYKRWAYAVK 538
Cdd:cd07786 441 LAGLAVGLWKSLDELAKLWQVDRRFEPSMSEEEREALYAGWKKAVK 486
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
21-543 |
2.15e-143 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 424.62 E-value: 2.15e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 21 THCRFLIYStKNAEVLAYHELKLRQIVHQAGWMEYDPSEIWKNTQECIETAyknLVILEINPRDIIAIGIVNQRGTSVLW 100
Cdd:PRK00047 15 TSSRAIIFD-HDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEA---LAKAGISPDQIAAIGITNQRETTVVW 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 101 NLETGQPLHNAIGWSDCRSTPILKTLLHNVRhnVDYVRYRSGLPLSSCFSALKIRWLMDHVPAVATAIEENKCLFGTLDS 180
Cdd:PRK00047 91 DKETGRPIYNAIVWQDRRTADICEELKRDGY--EDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGELLFGTIDT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 181 WLLWNLTGGvemGVHSTDITNAHYTSLMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYVLEGPLHGT--PIAAMMG 258
Cdd:PRK00047 169 WLVWKLTGG---KVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYGFFGGevPIAGIAG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 259 EQPASLLGQLCVKAGQNVCTLDDSCFVLLNTGREKLDSANGLITGIAHKLGEKAatNYTLEGAISNAGSTVTWLRDKLQI 338
Cdd:PRK00047 246 DQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGIDGKV--VYALEGSIFVAGSAIQWLRDGLKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 339 nteINSndnvveslntfigensmissscsssmlNAECGLAAKRSE----ITFVPAFHGMYAPYWRHDARGIILGLTSQTT 414
Cdd:PRK00047 324 ---ISD---------------------------ASDSEALARKVEdndgVYVVPAFTGLGAPYWDSDARGAIFGLTRGTT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 415 AENITQAAYEATGFQIFEVLQAFKRDtpnwdrSSMQ-PVLTFGGDYAENLHLVQFIADIIGYMLERPQTTSPAGLGVMIT 493
Cdd:PRK00047 374 KEHIIRATLESIAYQTRDVLDAMQAD------SGIRlKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYL 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 386767767 494 AGVTMKV-VSLEHAVKMYTPPTdVFSPTTTKNRRELLYKRWAYAVKKCLHW 543
Cdd:PRK00047 448 AGLAVGFwKDLDELKEQWKIDR-RFEPQMDEEEREKLYAGWKKAVKRTLAW 497
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
18-538 |
3.91e-104 |
|
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: 323.74 E-value: 3.91e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 18 VSSTHCRFLIYStKNAEVLAYHELKLRQIVHQAGWMEYDPSEIWKNTQECIETAYKNLvilEINPRDIIAIGIVNQRGTS 97
Cdd:cd07793 7 VGTTNIRCHIFD-KKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNA---GLTPEDIAAIGISTQRNTF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 98 VLWNLETGQPLHNAIGWSDCRSTPILK---------------TLLHNV-RHNvdyvRYRSG--LPLSSCFSALKIRWLMD 159
Cdd:cd07793 83 LTWDKKTGKPLHNFITWQDLRAAELCEswnrslllkalrggsKFLHFLtRNK----RFLAAsvLKFSTAHVSIRLLWILQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 160 HVPAVATAIEENKCLFGTLDSWLLWNLTGGvemGVHSTDITNAHYTSLMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEI 239
Cdd:cd07793 159 NNPELKEAAEKGELLFGTIDTWLLWKLTGG---KVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 240 FGYVLEGPL-HGTPIAAMMGEQPASLLGQLCVKAGQNVCTLDDSCFVLLNTGREKLDSANGLITGIAHKLGEKaaTNYTL 318
Cdd:cd07793 236 FGSTDPSIFgAEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGGE--ITYLA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 319 EGAISNAGSTVTWLRDKLQINTEINSNDnVVESLNTFIGensmissscsssmlnaecglaakrseITFVPAFHGMYAPYW 398
Cdd:cd07793 314 EGNASDTGTVIDWAKSIGLFDDPSETED-IAESVEDTNG--------------------------VYFVPAFSGLQAPYN 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 399 RHDARGIILGLTSQTTAENITQAAYEATGFQIFEVLQAFKRDTpnwdRSSMQPVLTFGGdYAENLHLVQFIADIIGYMLE 478
Cdd:cd07793 367 DPTACAGFIGLTPSTTKAHLVRAILESIAFRVKQLLETMEKET----SIKISSIRVDGG-VSNNDFILQLIADLLGKPVE 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 479 RPQTTSPAGLGVMITAGVTMKVVSLEHAVKMYTPPTDVFSPTTTKNRRELLYKRWAYAVK 538
Cdd:cd07793 442 RPKNTEMSALGAAFLAGLASGIWKSKEELKKLRKIEKIFEPKMDNEKREELYKNWKKAVK 501
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
18-533 |
4.91e-67 |
|
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: 226.25 E-value: 4.91e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 18 VSSTHCRFLIYSTkNAEVLAYHELKLRQIVHQAGWMEYDPSEIWKNTQECIETAYKNLvilEINPRDIIAIGIVNQRGTS 97
Cdd:COG1070 8 IGTTSVKAVLFDA-DGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKA---GVDPEEIAAIGVSGQMHGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 98 VLWNlETGQPLHNAIGWSDCRSTPILKTLLHnvRHNVDYVRYRSGLPLSSCFSALKIRWLMDHVPAVATAIEenkcLFGT 177
Cdd:COG1070 84 VLLD-ADGEPLRPAILWNDTRAAAEAAELRE--ELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIA----KVLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 178 LDSWLLWNLTGgvemgVHSTDITNAHYTSLMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYVLE------GPLHGT 251
Cdd:COG1070 157 PKDYLRYRLTG-----EFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAeaaaetGLPAGT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 252 PIAAMMGEQPASLLGQLCVKAGQNVCTLDDSCFVLLNTGREKLDsANGLITGIAHKLGEKaatnYTLEGAISNAGSTVTW 331
Cdd:COG1070 232 PVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPD-PEGRVHTFCHAVPGR----WLPMGATNNGGSALRW 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 332 LRDKLqinteinsNDNVVESLNTfigensmissscsssmLNAECGLAAKRSE-ITFVPAFHGMYAPYWRHDARGIILGLT 410
Cdd:COG1070 307 FRDLF--------ADGELDDYEE----------------LNALAAEVPPGADgLLFLPYLSGERTPHWDPNARGAFFGLT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 411 SQTTAENITQAAYEATGFQIFEVLQAFKRDTPNWDRssmqpvLTFGGDYAENLHLVQFIADIIGYMLERPQTTSPAGLGV 490
Cdd:COG1070 363 LSHTRAHLARAVLEGVAFALRDGLEALEEAGVKIDR------IRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGA 436
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 386767767 491 MITAGVTMKVV-SLEHAVKMYTPPTDVFSPTTTKNRR-ELLYKRW 533
Cdd:COG1070 437 ALLAAVGLGLYdDLEEAAAAMVRVGETIEPDPENVAAyDELYERY 481
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
32-494 |
2.37e-57 |
|
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: 197.40 E-value: 2.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 32 NAEVLAYHELKLRQIVHQAGWMEYDPSEIWKNTQECIETAYKNLvilEINPRDIIAIGIVNQRGTSVLWNlETGQPLHNA 111
Cdd:cd00366 20 DGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKA---GIDPSDIAAIGISGQMPGVVLVD-ADGNPLRPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 112 IGWSDCRSTpilktllhnvrhnvdyvryrsglplsscfsalkirwlmdhvpavataieenkclFGTLDSWLLWNLTGgve 191
Cdd:cd00366 96 IIWLDRRAK------------------------------------------------------FLQPNDYIVFRLTG--- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 192 mgVHSTDITNAHYTSLMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYVLE------GPLHGTPIAAMMGEQPASLL 265
Cdd:cd00366 119 --EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPeaaeetGLPAGTPVVAGGGDTAAAAL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 266 GQLCVKAGQNVCTLDDSCFVLLNTGREKldSANGLITGIAHKLGEKaatnYTLEGAISNAGSTVTWLRDklqintEINSN 345
Cdd:cd00366 197 GAGVVEPGDAVDSTGTSSVLSVCTDEPV--PPDPRLLNRCHVVPGL----WLLEGAINTGGASLRWFRD------EFGEE 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 346 DNVVESLntfigensmissscssSMLNAECGLAAKRSE-ITFVPAFHGMYAPYWRHDARGIILGLTSQTTAENITQAAYE 424
Cdd:cd00366 265 EDSDAEY----------------EGLDELAAEVPPGSDgLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLE 328
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 425 ATGFQIFEVLQAFKRDTpnWDRSSMqpVLTFGGdyAENLHLVQFIADIIGYMLERPQTTSPAGLGVMITA 494
Cdd:cd00366 329 GVAYALRDNLEILEELG--VKIKEI--RVTGGG--AKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
49-533 |
1.32e-54 |
|
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: 192.75 E-value: 1.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 49 QAGWMEYDPSEIWKNTQECIETAYKNLvilEINPRDIIAIGIVNQRGTSVLWNlETGQPLHNAIGWSDCRSTPILKTLLH 128
Cdd:cd07808 37 KPGWAEQDPEDWWQATKEALRELLAKA---GISPSDIAAIGLTGQMHGLVLLD-KNGRPLRPAILWNDQRSAAECEELEA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 129 NVRhnvDYVRYRSGLPLSSCFSALKIRWLMDHVPAVATAIEenKCLFGTlDsWLLWNLTGgvemgVHSTDITNAHYTSLM 208
Cdd:cd07808 113 RLG---DEILIITGNPPLPGFTLPKLLWLKENEPEIFARIR--KILLPK-D-YLRYRLTG-----ELATDPSDASGTLLF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 209 NVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYVLE------GPLHGTPIAAMMGEQPASLLGQLCVKAGQNVCTLDDS 282
Cdd:cd07808 181 DVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPeaaeelGLPEGTPVVAGAGDNAAAALGAGVVEPGDALISLGTS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 283 CFVLLNTGREKLDSANGLITgIAHKLGEKaatNYTLeGAISNAGSTVTWLRdklqinteinsnDNVVESLNTFigensmi 362
Cdd:cd07808 261 GVVFAPTDKPVPDPKGRLHT-FPHAVPGK---WYAM-GVTLSAGLSLRWLR------------DLFGPDRESF------- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 363 ssscssSMLNAEcglaAKRSEI-----TFVPAFHGMYAPYWRHDARGIILGLTSQTTAENITQAAYEATGFQIFEVLQAF 437
Cdd:cd07808 317 ------DELDAE----AAKVPPgseglLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 438 KRDTPNWDRssmqpvLTFGGDYAENLHLVQFIADIIGYMLERPQTTSPAGLGVMITAGVTMKV-VSLEHAVKMYTPPTDV 516
Cdd:cd07808 387 KELGIKVKE------IRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVfDDLEEAAAACIKIEKT 460
|
490 500
....*....|....*....|
gi 386767767 517 FSPttTKNRREL---LYKRW 533
Cdd:cd07808 461 IEP--DPERHEAydeLYARY 478
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
13-266 |
1.01e-53 |
|
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: 183.31 E-value: 1.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 13 IGVACvSSTHCRFLIYStKNAEVLAYHELKLRQIVHQAGWMEYDPSEIWKNTQECIEtayKNLVILEINPRDIIAIGIVN 92
Cdd:pfam00370 3 LGIDC-GTTSTKAILFN-EQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIA---KTLSQLGISLKQIKGIGISN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 93 QRGTSVLWNlETGQPLHNAIGWSDCRSTPILKTLLHNVrhNVDYVRYRSGLPLSSCFSALKIRWLMDHVPAVATAIEenk 172
Cdd:pfam00370 78 QGHGTVLLD-KNDKPLYNAILWKDRRTAEIVENLKEEG--NNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIH--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 173 cLFGTLDSWLLWNLTGgvemgVHSTDITNAHYTSLMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYV------LEG 246
Cdd:pfam00370 152 -KFLTIHDYLRWRLTG-----VFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELnpelaaMWG 225
|
250 260
....*....|....*....|
gi 386767767 247 PLHGTPIAAMMGEQPASLLG 266
Cdd:pfam00370 226 LDEGVPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
18-519 |
5.20e-52 |
|
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: 184.26 E-value: 5.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 18 VSSTHCRFLIYSTKNAEV-LAYHELKLRQIvhQAGWMEYDPSEIWKNTQECIETAYKNLvilEINPRDIIAIGIVNQRGT 96
Cdd:cd07779 7 VGTTSTRAIIFDLDGNIVaSGYREYPPYYP--EPGWVEQDPDDWWDALCEALKEAVAKA---GVDPEDIAAIGLTSQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 97 SVLWNlETGQPLHNAIGWSDCRstpilktllhnvrhnvdyVRYrsglplsscfsalkirwlmdhvpavataieenkclFG 176
Cdd:cd07779 82 FVPVD-EDGRPLRPAISWQDKR------------------TAK-----------------------------------FL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 177 TLDSWLLWNLTGgvemgVHSTDITNAHYTSLMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYVLE------GPLHG 250
Cdd:cd07779 108 TVQDYLLYRLTG-----EFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKeaaeetGLPEG 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 251 TPIAAMMGEQPASLLGQLCVKAGQNVCTLDDSCFVLLNTGREKLDSANGLITGIAHKLGekaatNYTLEGAISNAGSTVT 330
Cdd:cd07779 183 TPVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPG-----KWVLEGSINTGGSAVR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 331 WLRDKL-QINTEINSNDNVVESLntfigensmissscsssmLNAECGLAAKRSE-ITFVPAFHGMYAPYWRHDARGIILG 408
Cdd:cd07779 258 WFRDEFgQDEVAEKELGVSPYEL------------------LNEEAAKSPPGSDgLLFLPYLAGAGTPYWNPEARGAFIG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 409 LTSQTTAENITQAAYEATGFQIFEVLQAFKRDTPNWDRssmqpVLTFGGdyAENLHL-VQFIADIIGYMLERPQTTSPAG 487
Cdd:cd07779 320 LTLSHTRAHLARAILEGIAFELRDNLEAMEKAGVPIEE-----IRVSGG--GSKSDLwNQIIADVFGRPVERPETSEATA 392
|
490 500 510
....*....|....*....|....*....|...
gi 386767767 488 LGVMITAGVTMKV-VSLEHAVKMYTPPTDVFSP 519
Cdd:cd07779 393 LGAAILAAVGAGIyPDFEEAVKAMVRVTDTFEP 425
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
49-533 |
6.53e-47 |
|
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: 171.55 E-value: 6.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 49 QAGWMEYDPSEIW----KNTQECIETAyknlvilEINPRDIIAIGIVNQRGTSVLWNlETGQPLHNAIGWSDCRSTPILK 124
Cdd:cd07805 37 KPGWAEQDPEDWWdavcRATRALLEKS-------GIDPSDIAAIAFSGQMQGVVPVD-KDGNPLRNAIIWSDTRAAEEAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 125 TLLHnvRHNVDYVRYRSGLP-LSSCFSALKIRWLMDHVPAVAtaiEENKCLFGTLDsWLLWNLTGgvemgVHSTDITNAH 203
Cdd:cd07805 109 EIAG--GLGGIEGYRLGGGNpPSGKDPLAKILWLKENEPEIY---AKTHKFLDAKD-YLNFRLTG-----RAATDPSTAS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 204 YTSLMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYVLE------GPLHGTPIAAMMGEQPASLLGQLCVKAGQNVC 277
Cdd:cd07805 178 TTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPeaaaelGLPAGTPVVGGGGDAAAAALGAGAVEEGDAHI 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 278 TLDDSCFVLLNTGREKLDSANGLITgIAHKLGEKaatnYTLEGAISNAGSTVTWLRDKLQINTEINSNDnvveslntfig 357
Cdd:cd07805 258 YLGTSGWVAAHVPKPKTDPDHGIFT-LASADPGR----YLLAAEQETAGGALEWARDNLGGDEDLGADD----------- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 358 ensmissscsSSMLNAECGLAAKRSE-ITFVPAFHGMYAPYWRHDARGIILGLTSQTTAENITQAAYEATGFQIFEVLQA 436
Cdd:cd07805 322 ----------YELLDELAAEAPPGSNgLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWLLEA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 437 FKRDTPNWDRssmqpvLTFGGDYAENLHLVQFIADIIGYMLERPQTTSPAG-LGVMITAGVTMKVVSLEHAVKMYTPPTD 515
Cdd:cd07805 392 LEKLTRKIDE------LRLVGGGARSDLWCQILADVLGRPVEVPENPQEAGaLGAALLAAVGLGLLKSFDEAKALVKVEK 465
|
490
....*....|....*....
gi 386767767 516 VFSP-TTTKNRRELLYKRW 533
Cdd:cd07805 466 VFEPdPENRARYDRLYEVF 484
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
20-496 |
1.94e-46 |
|
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: 169.30 E-value: 1.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 20 STHCRFLIYStKNAEVLAYHELKLRQIVHQAGWMEYDPSEIWKNTQECIETAYKNLvileiNPRDIIAIGIvnqrgTS-- 97
Cdd:cd07773 9 TTNVKAVLFD-EDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQA-----GPDPIAAISV-----SSqg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 98 ---VLWNlETGQPLHNAIGWSDCRSTPILKTLLHnvRHNVDYVRYRSGLPLSSCFSALKIRWLMDHVPAVATAIEenKCL 174
Cdd:cd07773 78 esgVPVD-RDGEPLGPAIVWFDPRGKEEAEELAE--RIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAA--KWL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 175 fgTLDSWLLWNLTGgvemgVHSTDITNAHYTSLMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYVLE------GPL 248
Cdd:cd07773 153 --SVADYIAYRLTG-----EPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPeaaeelGLP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 249 HGTPIAAmmG--EQPASLLGQLCVKAGQNVctldDSC------FVLLNTGREKLDSANGLITGIAHKLGEKaatnYTLEG 320
Cdd:cd07773 226 AGTPVVV--GghDHLCAALGAGVIEPGDVL----DSTgtaealLAVVDEPPLDEMLAEGGLSYGHHVPGGY----YYLAG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 321 AISnAGSTVTWLRDKLQINTEinsndnvveslntfigensmisSSCSSSMLNAECglAAKRSEITFVPAFHGMYAPYWRH 400
Cdd:cd07773 296 SLP-GGALLEWFRDLFGGDES----------------------DLAAADELAEAA--PPGPTGLLFLPHLSGSGTPDFDP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 401 DARGIILGLTSQTTAENITQAAYEATGFQIFEVLQAFKRDTPNWDRssmqpVLTFGGDyAENLHLVQFIADIIGYMLERP 480
Cdd:cd07773 351 DARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEALEKAGIPIDE-----IRAVGGG-ARSPLWLQLKADILGRPIEVP 424
|
490
....*....|....*.
gi 386767767 481 QTTSPAGLGVMITAGV 496
Cdd:cd07773 425 EVPEATALGAALLAGV 440
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
276-498 |
1.23e-38 |
|
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: 140.92 E-value: 1.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 276 VCTLDDSCFVLLnTGREKLDSANGLITGIAhklGEKAATNYTLEGAISNAGSTVTWLRDKLQINTEINSNDNVvESLntf 355
Cdd:pfam02782 2 AISAGTSSFVLV-ETPEPVLSVHGVWGPYT---NEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRDAGNV-ESL--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 356 igensmissscsssMLNAECGLAAKRSEITFVPAFHGMYAPYWRHDARGIILGLTSQTTAENITQAAYEATGFQIFEVLQ 435
Cdd:pfam02782 74 --------------AELAALAAVAPAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILE 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386767767 436 AFKRDTpnwdRSSMQPVLTFGGdYAENLHLVQFIADIIGYMLERPQTTSPAGLGVMITAGVTM 498
Cdd:pfam02782 140 ALTKQE----GHPIDTIHVSGG-GSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVAA 197
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
18-533 |
2.27e-38 |
|
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: 147.70 E-value: 2.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 18 VSSTHCRFLIYSTKnAEVLAYHELKLRQIVHQAGWMEYDPSEIWKNTQECIETayknlVILEINPRDIIAIGIvnqrgTS 97
Cdd:cd07770 7 IGTTSTKAVLFDED-GRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKE-----VLAKLGGGEVDAIGF-----SS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 98 VLWNL----ETGQPLHNAIGWSDCRSTPILKTLLhnVRHNVDYVRYRSGLPLSSCFSALKIRWLMDHVPAVAtaieENKC 173
Cdd:cd07770 76 AMHSLlgvdEDGEPLTPVITWADTRAAEEAERLR--KEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELF----AKAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 174 LFGTLDSWLLWNLTGgvemgVHSTDITNAHYTSLMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYVLE------GP 247
Cdd:cd07770 150 KFVSIKEYLLYRLTG-----ELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPefaerlGL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 248 LHGTPIAAMMGEQPASLLGQLCVKAGQNVCTLDDSCFVLLNTGREKLDSANGLITgiaHKLGEKaatNYTLEGAISNAGS 327
Cdd:cd07770 225 LAGTPVVLGASDGALANLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPGRLWC---YRLDEN---RWLVGGAINNGGN 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 328 TVTWLRDKLqinteiNSNDNVVESLNTFIGEnsmissscsssmlnaecgLAAKRSEITFVPAFHGMYAPYWRHDARGIIL 407
Cdd:cd07770 299 VLDWLRDTL------LLSGDDYEELDKLAEA------------------VPPGSHGLIFLPYLAGERAPGWNPDARGAFF 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 408 GLTSQTTAENITQAAYEATGFQIFEVLQAFkrdtpnwdRSSMQPV--LTFGGDYAENLHLVQFIADIIGYMLERPQTTSP 485
Cdd:cd07770 355 GLTLNHTRADILRAVLEGVAFNLKSIYEAL--------EELAGPVkeIRASGGFLRSPLWLQILADVLGRPVLVPEEEEA 426
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 386767767 486 AGLGVMITAGVTMKVVSLEHAVKMyTPPTDVFSPTTTKNRR-ELLYKRW 533
Cdd:cd07770 427 SALGAALLALEALGLISSLEADEL-VKIGKVVEPDPENHAIyAELYERF 474
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
28-496 |
4.54e-36 |
|
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: 140.74 E-value: 4.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 28 YSTK------NAEVLAYHELKLRQIVHQAGWMEYDPSEIWKNTQECIETAYKNLvilEINPRDIIAIGIVNQRGTSVLWN 101
Cdd:cd07804 10 TGTKgvlvdeDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKA---GISPKEIAAIGVSGLVPALVPVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 102 lETGQPLHNAIGWSDCRSTPILKTLLHNVrhNVDYVRYRSGLPLSSCFSALKIRWLMDHVPAVATAIEenkcLFGTLDSW 181
Cdd:cd07804 87 -ENGKPLRPAILYGDRRATEEIEWLNENI--GEDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTR----KFLGAYDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 182 LLWNLTGgvemgVHSTDITNA-HYTSLMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYVLE------GPLHGTPIA 254
Cdd:cd07804 160 IVYKLTG-----EYVIDYSSAgNEGGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKeaaeetGLAEGTPVV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 255 AMMGEQPASLLGQLCVKAGQNVCTLDDSCFVLLNTgreklDSANGLIT--GIAHKLGEKaatnYTLEGAISNAGSTVTWL 332
Cdd:cd07804 235 AGTVDAAASALSAGVVEPGDLLLMLGTAGDIGVVT-----DKLPTDPRlwLDYHDIPGT----YVLNGGMATSGSLLRWF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 333 RDKL---QINTEINSNDNVVESLNTfigensmissscsssmlnaecgLAAK---RSE-ITFVPAFHGMYAPYWRHDARGI 405
Cdd:cd07804 306 RDEFageEVEAEKSGGDSAYDLLDE----------------------EAEKippGSDgLIVLPYFMGERTPIWDPDARGV 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 406 ILGLTSQTTAENITQAAYEATGFQIFEVLQAFKRDTPNWDRSsmqpVLTFGGdyAENLHLVQFIADIIGYMLERPQTTSP 485
Cdd:cd07804 364 IFGLTLSHTRAHLYRALLEGVAYGLRHHLEVIREAGLPIKRL----VAVGGG--AKSPLWRQIVADVTGVPQEYVKDTVG 437
|
490
....*....|.
gi 386767767 486 AGLGVMITAGV 496
Cdd:cd07804 438 ASLGDAFLAGV 448
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
35-496 |
3.83e-34 |
|
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: 134.99 E-value: 3.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 35 VLAYHELKLRQIVHQAGWMEYDPSEIWKNTQECIETAYKNlviLEINPRDIIAIGIVNQrGTSvLWNL-ETGQPLHNAIG 113
Cdd:cd07802 23 EIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEK---SGVDPSDIAGVGVTGH-GNG-LYLVdKDGKPVRNAIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 114 WSDCRSTPILKTLLHNVRHnvDYVRYRSGLPLSSCFSALKIRWLMDHVPAVATAIEenKCLFGTlDsWLLWNLTggvemG 193
Cdd:cd07802 98 SNDSRAADIVDRWEEDGTL--EKVYPLTGQPLWPGQPVALLRWLKENEPERYDRIR--TVLFCK-D-WIRYRLT-----G 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 194 VHSTDITNAHyTSLMNVSTEQWDPKLCQFFRLP--LNILPRIRSNSEIFGYVLE------GPLHGTPIAAMMGEQPASLL 265
Cdd:cd07802 167 EISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVTAeaaaltGLPEGTPVAAGAFDVVASAL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 266 GQLCVKAGQNVCTLDDSCfvlLNTG-REKLDSANGLITGIAHKLGEKaatnYTLEGAISNAGSTVTWLRDKLqINTEINS 344
Cdd:cd07802 246 GAGAVDEGQLCVILGTWS---INEVvTDEPVVPDSVGSNSLHADPGL----YLIVEASPTSASNLDWFLDTL-LGEEKEA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 345 NDNVVESLNTFIGEnsmissscsssmlnaecgLAAKRSEITFVPaFhgMYAPYWRHDARGIILGLTSQTTAENITQAAYE 424
Cdd:cd07802 318 GGSDYDELDELIAA------------------VPPGSSGVIFLP-Y--LYGSGANPNARGGFFGLTAWHTRAHLLRAVYE 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386767767 425 ATGFQIFEVLQAFKRDTPnwdrssMQPV-LTFGGdyAENLHLVQFIADIIGYMLERPQTTSPAGLGVMITAGV 496
Cdd:cd07802 377 GIAFSHRDHLERLLVARK------PETIrLTGGG--ARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAV 441
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
23-496 |
3.35e-26 |
|
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: 111.55 E-value: 3.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 23 CRFLIYsTKNAEVLAYHELKLRQIVHQAGWMEYDPSEIWKNTQECIETayknlVILEINPRDIIAIGIVNQRGTSVLWNl 102
Cdd:cd07783 12 VRAVVV-DEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRE-----LPAELRPRRVVAIAVDGTSGTLVLVD- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 103 ETGQPLHNAIGWSDCRSTPILKTLlhnvRHNVDYVRYRSGLPLSSCFSALKIRWLMDHVPAVATAIEenKCLFGTlDsWL 182
Cdd:cd07783 85 REGEPLRPAIMYNDARAVAEAEEL----AEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTA--KFLHQA-D-WL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 183 LWNLTGgvEMGVhsTDITNAHyTSLMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYVLE------GPLHGTPIAAM 256
Cdd:cd07783 157 AGRLTG--DRGV--TDYNNAL-KLGYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAeaaeelGLPAGTPVVAG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 257 MGEQPASLLGQLCVKAGQNVCTLDDS-CFVLLnTGREKLDSANGLITgiaHKLGEkaatNYTLEGAISNAG-STVTWLRD 334
Cdd:cd07783 232 TTDSIAAFLASGAVRPGDAVTSLGTTlVLKLL-SDKRVPDPGGGVYS---HRHGD----GYWLVGGASNTGgAVLRWFFS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 335 KLQINTeinsndnvveslntfigensmissscsssmLNAEcglAAKR--SEITFVP-AFHGMYAPYWRHDARGIILGLTs 411
Cdd:cd07783 304 DDELAE------------------------------LSAQ---ADPPgpSGLIYYPlPLRGERFPFWDPDARGFLLPRP- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 412 qTTAENITQAAYEATGF---QIFEVLQAFKRDTPNwdrssmqPVLTFGGdYAENLHLVQFIADIIGYMLERPQTTSPAgL 488
Cdd:cd07783 350 -HDRAEFLRALLEGIAFierLGYERLEELGAPPVE-------EVRTAGG-GARNDLWNQIRADVLGVPVVIAEEEEAA-L 419
|
....*...
gi 386767767 489 GVMITAGV 496
Cdd:cd07783 420 GAALLAAA 427
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
12-497 |
4.04e-26 |
|
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: 111.49 E-value: 4.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 12 LIGVACvSSTHCRFLIYSTKNAEVLA--YHELKLRQIvhQAGWMEYDPSEIWKNTQECIETAYKNLVileINPRDIIAIG 89
Cdd:cd07809 2 VLGIDL-GTQSIKAVLIDAETGRVVAsgSAPHENILI--DPGWAEQDPEDWWDALQAAFAQLLKDAG---AELRDVAAIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 90 IVNQ-RGTSVLwnLETGQPLHNAIGWSDCRSTPILKTLLHNVrhNVDYVRYRSGLPLSScFSALKIRWLMDHVPAVATAI 168
Cdd:cd07809 76 ISGQmHGLVAL--DADGKVLRPAKLWCDTRTAPEAEELTEAL--GGKKCLLVGLNIPAR-FTASKLLWLKENEPEHYARI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 169 eenkCLFGTLDSWLLWNLTGGvemgvHSTDITNAHYTSLMNVSTEQWDPKLCQFF---RLPLNILPRIRSNSEIFGYV-- 243
Cdd:cd07809 151 ----AKILLPHDYLNWKLTGE-----KVTGLGDASGTFPIDPRTRDYDAELLAAIdpsRDLRDLLPEVLPAGEVAGRLtp 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 244 ---LEGPLH-GTPIAAMMGEQPASLLGQLCVKAGQNVCTLDDSCFVLLNTGREKLDsANGLITGIAHklgekaatnytle 319
Cdd:cd07809 222 egaEELGLPaGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSD-PHGRVATFCD------------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 320 gaisnagSTVTWLrdkLQINTeINSNDNVVESLNTFIGensmisssCSSSMLNAECGLAAKRSE-ITFVPAFHGMYAPYW 398
Cdd:cd07809 288 -------STGGML---PLINT-TNCLTAWTELFRELLG--------VSYEELDELAAQAPPGAGgLLLLPFLNGERTPNL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 399 RHdARGIILGLT-SQTTAENITQAAYEAT------GFQIFEVLQAfkrdtpnwdrSSMQPVLTFGGdyAENLHLVQFIAD 471
Cdd:cd07809 349 PH-GRASLVGLTlSNFTRANLARAALEGAtfglryGLDILRELGV----------EIDEIRLIGGG--SKSPVWRQILAD 415
|
490 500
....*....|....*....|....*.
gi 386767767 472 IIGYMLERPQTTSPAGLGVMITAGVT 497
Cdd:cd07809 416 VFGVPVVVPETGEGGALGAALQAAWG 441
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
54-266 |
2.88e-23 |
|
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: 102.69 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 54 EYDPSEIWKNTQECIETayknlvILEINPRDIIAIGIVNQRGTSVLWNlETGQPLHNAIGWSDCR-STPILKTLLHNVRH 132
Cdd:cd07777 45 EQDPEKILEAVRNLIDE------LPREYLSDVTGIGITGQMHGIVLWD-EDGNPVSPLITWQDQRcSEEFLGGLSTYGEE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 133 nvdyVRYRSGLPLSSCFSALKIRWLMDHVPavataIEENKCLFGTLDSWLLWNLTGGVEmgvHSTDITNAHYTSLMNVST 212
Cdd:cd07777 118 ----LLPKSGMRLKPGYGLATLFWLLRNGP-----LPSKADRAGTIGDYIVARLTGLPK---PVMHPTNAASWGLFDLET 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 386767767 213 EQWDPKLCQFFRLPLNILPRIRSNSEIFGYVLEGPLHGTPIAAMMGEQPASLLG 266
Cdd:cd07777 186 GTWNKDLLEALGLPVILLPEIVPSGEIVGTLSSALPKGIPVYVALGDNQASVLG 239
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
19-496 |
4.12e-21 |
|
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: 96.52 E-value: 4.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 19 SSTHCrfLIYSTKNAEV-LAYHELKLRQIVHQAGWMEYDPSEIWKNTQECIETAYKNLvilEINPRDIIAIGIVNQRGTS 97
Cdd:cd07798 10 GGGRC--ALVDSEGKIVaIAYREWEYYTDDDYPDAKEFDPEELWEKICEAIREALKKA---GISPEDISAVSSTSQREGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 98 VLWNLEtGQPL-------HNAIGWSDCRSTPILKtllhnvrhnvdYVRYRSGLPLSSCFSALKIRWLMDHVPAVATAIEe 170
Cdd:cd07798 85 VFLDKD-GRELyagpnidARGVEEAAEIDDEFGE-----------EIYTTTGHWPTELFPAARLLWFKENRPEIFERIA- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 171 nkcLFGTLDSWLLWNLTGGVemgvhSTDITNAHYTSLMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYVLE----- 245
Cdd:cd07798 152 ---TVLSISDWIGYRLTGEL-----VSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEeaare 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 246 -GPLHGTPIAAMMGEQPASLLGQLCVKAGQNVCTLDDSCFVLLNTGREKLDSANGLITGiAHKLGEKaatnYTLEgaiSN 324
Cdd:cd07798 224 lGLPEGTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTG-CHLVPGK----WVLE---SN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 325 AGST---VTWLRDKLQinteiNSNDNVVESLNTFIGENSMissscsssmlnAECGlaakrseitfVPAFHGMYAPYwrHD 401
Cdd:cd07798 296 AGVTglnYQWLKELLY-----GDPEDSYEVLEEEASEIPP-----------GANG----------VLAFLGPQIFD--AR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 402 ARGIILGL--------TSQTTAENITQAAYEATGFQIFEVLQAFKRDTPnwdrSSMQPVLTFGGDYAENLhLVQFIADII 473
Cdd:cd07798 348 LSGLKNGGflfptplsASELTRGDFARAILENIAFAIRANLEQLEEVSG----REIPYIILCGGGSRSAL-LCQILADVL 422
|
490 500
....*....|....*....|...
gi 386767767 474 GYMLERPQTTSPAGLGVMITAGV 496
Cdd:cd07798 423 GKPVLVPEGREASALGAAICAAV 445
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
49-496 |
1.32e-16 |
|
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: 82.67 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 49 QAGWMEYDPSEIWKNTQECIETAyknLVILEINPRDIIAIGIVNQ-RGTsvlWNL-ETGQPLHNAIGWSDCRSTPILKTL 126
Cdd:cd24121 37 QPGWAEQDMNETWQAVVATIREV---VAKLDVLPDRVAAIGVTGQgDGT---WLVdEDGRPVRDAILWLDGRAADIVERW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 127 LHNVRhnVDYVRYRSGLPLSSCFSALKIRWLMDHVPAvatAIEENKCLFGTLDsWLLWNLTggvemGVHSTDITNAHYTS 206
Cdd:cd24121 111 QADGI--AEAVFEITGTGLFPGSQAAQLAWLKENEPE---RLERARTALHCKD-WLFYKLT-----GEIATDPSDASLTF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 207 LmNVSTEQWDPKLCQFFRLP--LNILPRIRSNSEIFGYVLE------GPLHGTPIAAMMGEQPASLLGqlcvkAGqnVCT 278
Cdd:cd24121 180 L-DFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPeaaaatGLPAGTPVVLGPFDVVATALG-----SG--AIE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 279 LDDSCFVLLNTG-REKLDSANGLitgiahklgEKAATNYTL----EG----AISNAGST--VTWLRDKLQINTEINSNDN 347
Cdd:cd24121 252 PGDACSILGTTGvHEVVVDEPDL---------EPEGVGYTIclgvPGrwlrAMANMAGTpnLDWFLRELGEVLKEGAEPA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 348 VVESLNTFigensmissscsssmlnaECGLAAKRseitfvPAFHG-MY----------APYWRHDARGIILGLTSQTTAE 416
Cdd:cd24121 323 GSDLFQDL------------------EELAASSP------PGAEGvLYhpylspagerAPFVNPNARAQFTGLSLEHTRA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 417 NITQAAYEATGFQIFEVLQAFKRDTPNWdrssmqpVLTFGGdyAENLHLVQFIADIIGYMLERPQTTSPAGLGVMITAGV 496
Cdd:cd24121 379 DLLRAVYEGVALAMRDCYEHMGEDPGEL-------RLSGGG--ARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAV 449
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
23-532 |
6.12e-15 |
|
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: 77.58 E-value: 6.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 23 CRFLIYSTKNAEVLAYH--ELKLRQIVHQAGWMEYDPSEIWkntqECIETAYKNLV-ILEINPRDIIAIGiVNQRGTSVL 99
Cdd:cd07781 12 VRAGLVDLADGEELASAvvPYPTGYIPPRPGWAEQNPADYW----EALEEAVRGALaEAGVDPEDVVGIG-VDTTSSTVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 100 WNLETGQPLHNAIGWSDCRSTP----ILKTLLHNVRHNVDYV--RYRSGLPLSscfsalKIRWLMDHVPAV----ATAIE 169
Cdd:cd07781 87 PVDEDGNPLAPAILWMDHRAQEeaaeINETAHPALEYYLAYYggVYSSEWMWP------KALWLKRNAPEVydaaYTIVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 170 EnkclfgtLDsWLLWNLTGGVemgVHStdITNAHYTSLMNVSTEQW--------DPKLcqfFRLPLNILPRIRSNSEIFG 241
Cdd:cd07781 161 A-------CD-WINARLTGRW---VRS--RCAAGHKWMYNEWGGGPpreflaalDPGL---LKLREKLPGEVVPVGEPAG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 242 YVLE------GPLHGTPIAAMMGEQPASLLGQLCVKAGQNVCTLDDSCFVLLNTGREKLDS------ANGLITGIahklg 309
Cdd:cd07781 225 TLTAeaaerlGLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTCHLMVSPKPVDIPgicgpvPDAVVPGL----- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 310 ekaatnYTLEGAISNAGSTVTWLRDKLQINTEiNSNDNVVESLNTF-----IGENsmissscsssmlnaecGLAAkrsei 384
Cdd:cd07781 300 ------YGLEAGQSAVGDIFAWFVRLFVPPAE-ERGDSIYALLSEEaaklpPGES----------------GLVA----- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 385 tfVPAFHGMYAPYWRHDARGIILGLTSQTTAENITQAAYEATGFQIFEVLQAFKRDTPNWDRssmqpVLTFGGDYAENLH 464
Cdd:cd07781 352 --LDWFNGNRTPLVDPRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERFEEAGVPVNR-----VVACGGIAEKNPL 424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 465 LVQFIADIIGYMLERPQTTSPAGLGVMITAGVTMKVV-SLEHAVKMYTPPTDVFSPTTTKNRR-ELLYKR 532
Cdd:cd07781 425 WMQIYADVLGRPIKVPKSDQAPALGAAILAAVAAGVYaDIEEAADAMVRVDRVYEPDPENHAVyEELYAL 494
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
51-274 |
4.63e-14 |
|
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: 74.68 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 51 GWMEYDPSEIWKNTQECIEtayKNLVILEINPRDIIAIGIVNQRGTSVLWNlETGQPL---HNAigwsDCRSTPILKTLL 127
Cdd:cd07775 41 GSMDFDTEKNWKLICECIR---EALKKAGIAPKSIAAISTTSMREGIVLYD-NEGEEIwacANV----DARAAEEVSELK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 128 HNVRHNVDYVRYRSGLPLSscFSAL-KIRWLMDHVPAVATAIeenkCLFGTLDSWLLWNLTGgvemgVHSTDITNAHYTS 206
Cdd:cd07775 113 ELYNTLEEEVYRISGQTFA--LGAIpRLLWLKNNRPEIYRKA----AKITMLSDWIAYKLSG-----ELAVEPSNGSTTG 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386767767 207 LMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYV------LEGPLHGTPIAAMMGEQPASLLGQLCVKAGQ 274
Cdd:cd07775 182 LFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVtkeaaeETGLKEGTPVVVGGGDVQLGCLGLGVVRPGQ 255
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
44-274 |
4.84e-13 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 71.58 E-value: 4.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 44 RQI-VHQAGW-----------MEYDPSEIWKNTQECIETAYKNLvilEINPRDIIAIGIVNQRGTSVLWNlETGQPLHnA 111
Cdd:PRK10939 25 NQIaVGQAEWrhlavpdvpgsMEFDLEKNWQLACQCIRQALQKA---GIPASDIAAVSATSMREGIVLYD-RNGTEIW-A 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 112 IGWSDCRSTPILKTL--LHNvrhNVDYVRYR-SGLPLSscFSAL-KIRWLMDHVPAvataIEENKCLFGTLDSWLLWNLT 187
Cdd:PRK10939 100 CANVDARASREVSELkeLHN---NFEEEVYRcSGQTLA--LGALpRLLWLAHHRPD----IYRQAHTITMISDWIAYMLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 188 GgvemgVHSTDITNAHYTSLMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYVLE------GPLHGTPIAAMMGEQP 261
Cdd:PRK10939 171 G-----ELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAkaaaetGLRAGTPVVMGGGDVQ 245
|
250
....*....|...
gi 386767767 262 ASLLGQLCVKAGQ 274
Cdd:PRK10939 246 LGCLGLGVVRPGQ 258
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
27-478 |
2.74e-11 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 66.14 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 27 IYSTKNAEVLAYHELKLRQIVHQAGWMEYDPSEIWKNTqeciETAYKNLVILEiNPRDIIAIGIVNQRGTSVLWNlETGQ 106
Cdd:PRK15027 15 ILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQAT----DRAMKALGDQH-SLQDVKALGIAGQMHGATLLD-AQQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 107 PLHNAIGWSDCRSTPILKTLlhnvRHNVDYVRYRSGLPLSSCFSALKIRWLMDHVPAVATAIEenKCLFGTldSWLLWNL 186
Cdd:PRK15027 89 VLRPAILWNDGRCAQECALL----EARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQID--KVLLPK--DYLRLRM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 187 TggvemGVHSTDITNAHYTSLMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYVLEGPLH-----GTPIAAMMGEQP 261
Cdd:PRK15027 161 T-----GEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAKawgmaTVPVVAGGGDNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 262 ASLLGQLCVKAGQNVCTLDDS--CFVLLNTGREKLDSAnglITGIAHKLGEKaatnYTLEGAISNAGSTVTW---LRDKL 336
Cdd:PRK15027 236 AGAVGVGMVDANQAMLSLGTSgvYFAVSEGFLSKPESA---VHSFCHALPQR----WHLMSVMLSAASCLDWaakLTGLS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 337 QINTEINSNDNVVESLNTfigensmissscsssmlnaecglaakrseITFVPAFHGMYAPYWRHDARGIILGLTSQTTAE 416
Cdd:PRK15027 309 NVPALIAAAQQADESAEP-----------------------------VWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPN 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386767767 417 NITQAAYEATGFQI---FEVLQAfkrdtpnwdrSSMQP-VLTFGGDYAENLHLVQFIADIIGYMLE 478
Cdd:PRK15027 360 ELARAVLEGVGYALadgMDVVHA----------CGIKPqSVTLIGGGARSEYWRQMLADISGQQLD 415
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
13-531 |
1.26e-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: 64.18 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 13 IGVAcVSSTHCRFLIYSTKNAEVLAYHELKLRQIVH-QAGWMEYDPSEIWKNTQECIETAYKNLvilEINPRDIIAIG-- 89
Cdd:cd07768 3 IGVD-VGTSSARAGVYDLYAGLEMAQEPVPYYQDSSkKSWKFWQKSTEIIKALQKCVQKLNIRE---GVDAYEVKGCGvd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 90 ------IVNQRGTSvLWNLETGQPLHNAIGWSDCRSTPILKTLlHNVRHNVDYVRYrsGLPLSSCFSALKIRWLMDHVPA 163
Cdd:cd07768 79 atcslaIFDREGTP-LMALIPYPNEDNVIFWMDHSAVNEAQWI-NMQCPQQLLDYL--GGKISPEMGVPKLKYFLDEYSH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 164 VATAIEEnkclFGTLDSWLLWNLTGGVEmgvhsTDITNAHYTSLMNVSTEQWDPklcQFFRlplNILPRIRSN--SEIFG 241
Cdd:cd07768 155 LRDKHFH----IFDLHDYIAYELTRLYE-----WNICGLLGKENLDGEESGWSS---SFFK---NIDPRLEHLttTKNLP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 242 YVL---EGPLHGTP-IAAMMGEQPASLLGQLCVKA-----GQNVCTLDDSCFVLLNTgreklDSANGLITGIAHKLGEKA 312
Cdd:cd07768 220 SNVpigTTSGVALPeMAEKMGLHPGTAVVVSCIDAhaswfAVASPHLETSLFMIAGT-----SSCHMYGTTISDRIPGVW 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 313 ATNYTL--------EGAISNAGSTVTWL-------RDKLQInteINSNDNVVESLNTFIGEnsmissscsssmLNAECGL 377
Cdd:cd07768 295 GPFDTIidpdysvyEAGQSATGKLIEHLfeshpcaRKFDEA---LKKGADIYQVLEQTIRQ------------IEKNNGL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 378 AakrSEITFVPAFHGMYAPYWRHDARGIILGLTSQTTAENITQ---AAYEATGFQIFEVLQAFKRDTPNWDRssmqpvLT 454
Cdd:cd07768 360 S---IHILTLDMFFGNRSEFADPRLKGSFIGESLDTSMLNLTYkyiAILEALAFGTRLIIDTFQNEGIHIKE------LR 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 455 FGGDYAENLHLVQFIADIIGYMLERPQTTSPAGLGVM----ITAGVTMKVVSLEHAVKMYTPPTDVFSPTTTK--NRREL 528
Cdd:cd07768 431 ASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAAvlakVAAGKKQLADSITEADISNDRKSETFEPLAYRlgADYIL 510
|
...
gi 386767767 529 LYK 531
Cdd:cd07768 511 LYK 513
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
52-258 |
3.71e-09 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 59.27 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 52 WMEYDPSEIWKNTQECIETayknlVILEINPRDIIAIGIVNQRGTSVLWNlETGQPLHNAIGWSDCRSTPILKTLLHNVr 131
Cdd:PRK10331 44 WHQWSLDAILQRFADCCRQ-----INSELTECHIRGITVTTFGVDGALVD-KQGNLLYPIISWKCPRTAAVMENIERYI- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767767 132 hNVDYVRYRSGLPLSScFSAL-KIRWLMDHVPAvataieenkcLFGTLDSWLL------WNLTGgvemgVHSTDITNAHY 204
Cdd:PRK10331 117 -SAQQLQQISGVGAFS-FNTLyKLVWLKENHPQ----------LLEQAHAWLFisslinHRLTG-----EFTTDITMAGT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 386767767 205 TSLMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYVLegplhgTPIAAMMG 258
Cdd:PRK10331 180 SQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQ------PSAAALLG 227
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
186-255 |
1.61e-05 |
|
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: 47.52 E-value: 1.61e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386767767 186 LTGgvEMGvhsTDITNAHYTSLMNVSTEQWDPKLCQFFRLPLNILPRIRSNSEIFGYVL-----EGPLHGTPIAA 255
Cdd:cd07771 162 LTG--EKV---AEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKpevaeELGLKGIPVIA 231
|
|
| |
