|
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; ... |
11-510 |
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: 950.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 11 PLVGAVVQGTNSTRFLVFNpKTAELVGSHQVELTQEYPKEGWVEEDPKEILQSVYECIAKTCEKLTEANIDTSKIKAIGV 90
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFD-STGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLKALGISPSDIKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 91 SNQRETTVVWDKFTGEPLYNAVVWLDLRTQSTVESLNKKIPGNSNFVKSKTGLPLSTYFSAVKLRWMLDNLRPIQKAVEE 170
Cdd:cd07792 80 TNQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELSAKTPGGKDHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 171 DRALFGTIDSWLIWCMTGGVNGGIHCTDVTNASRTMLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGQMTSGALEG 250
Cdd:cd07792 160 GRLLFGTVDSWLIWNLTGGKNGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIASGPLAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 251 VPISGCLGDQSAALVGQMCFQEGQAKNTYGTGCFLLCNTGQKCVFSEHGLLTTVAYKLGKNKPAFYALEGSVAIAGAVIR 330
Cdd:cd07792 240 VPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAYKLGPDAPPVYALEGSIAIAGAAVQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 331 WLRDNFELITSSGEVEDLAREVGTAYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREIVDA 410
Cdd:cd07792 320 WLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREILDA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 411 MNRDCGIPLSHLRVDGRMTNNKILMQLQADILHIPVVKSVMPETTALGAAMAAGAAEGIDVWSIEPEDLSSMLMERYEPQ 490
Cdd:cd07792 400 MNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSLNEGGRTVFEPQ 479
|
490 500
....*....|....*....|
gi 51854223 491 IQATESEIRFSTWKRAVMKS 510
Cdd:cd07792 480 ISEEERERRYKRWKKAVERS 499
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
11-513 |
0e+00 |
|
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of carbohydrate kinases. [Energy metabolism, Other]
Pssm-ID: 273549 [Multi-domain] Cd Length: 493 Bit Score: 781.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 11 PLVGAVVQGTNSTRFLVFNpKTAELVGSHQVELTQEYPKEGWVEEDPKEILQSVYECIAKTCEKlteANIDTSKIKAIGV 90
Cdd:TIGR01311 1 PYILAIDQGTTSSRAIVFD-KDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAK---AGIKPDDIAAIGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 91 SNQRETTVVWDKFTGEPLYNAVVWLDLRTQSTVESLNKKIPGNsnFVKSKTGLPLSTYFSAVKLRWMLDNLRPIQKAVEE 170
Cdd:TIGR01311 77 TNQRETTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYGE--FIREKTGLPLDPYFSATKLRWLLDNVPGVREAAER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 171 DRALFGTIDSWLIWCMTGGvngGIHCTDVTNASRTMLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGQMTSGAL-E 249
Cdd:TIGR01311 155 GELLFGTIDTWLIWNLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYTDPGLLgA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 250 GVPISGCLGDQSAALVGQMCFQEGQAKNTYGTGCFLLCNTGQKCVFSEHGLLTTVAYKLGKNKPAfYALEGSVAIAGAVI 329
Cdd:TIGR01311 232 EIPITGVLGDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKKPV-YALEGSVFVAGAAV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 330 RWLRDNFELITSSGEVEDLAREVGTAYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREIVD 409
Cdd:TIGR01311 311 QWLRDNLKLIKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTRDVLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 410 AMNRDCGIPLSHLRVDGRMTNNKILMQLQADILHIPVVKSVMPETTALGAAMAAGAAEGIDVWSIEPEDLSSmLMERYEP 489
Cdd:TIGR01311 391 AMEKDAGVEITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWR-VEKTFEP 469
|
490 500
....*....|....*....|....
gi 51854223 490 QIQATESEIRFSTWKRAVMKSMGW 513
Cdd:TIGR01311 470 EMDEEEREARYAGWKEAVKRSLGW 493
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
13-514 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 729.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 13 VGAVVQGTNSTRFLVFNPKtAELVGSHQVELTQEYPKEGWVEEDPKEILQSVYECIAKTcekLTEANIDTSKIKAIGVSN 92
Cdd:COG0554 5 ILAIDQGTTSTRAILFDRD-GNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREA---LAKAGISAEDIAAIGITN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 93 QRETTVVWDKFTGEPLYNAVVWLDLRTQSTVESLNKKipGNSNFVKSKTGLPLSTYFSAVKLRWMLDNLRPIQKAVEEDR 172
Cdd:COG0554 81 QRETTVVWDRKTGKPLYNAIVWQDRRTADICEELKAD--GLEDLIREKTGLVLDPYFSATKIKWILDNVPGARERAEAGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 173 ALFGTIDSWLIWCMTGGvngGIHCTDVTNASRTMLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGQMTSGAL-EGV 251
Cdd:COG0554 159 LLFGTIDSWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDPDLFgAEI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 252 PISGCLGDQSAALVGQMCFQEGQAKNTYGTGCFLLCNTGQKCVFSEHGLLTTVAYKLGkNKPAfYALEGSVAIAGAVIRW 331
Cdd:COG0554 236 PIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLG-GKVT-YALEGSIFVAGAAVQW 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 332 LRDNFELITSSGEVEDLAREVGTAYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREIVDAM 411
Cdd:COG0554 314 LRDGLGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 412 NRDCGIPLSHLRVDGRMTNNKILMQLQADILHIPVVKSVMPETTalgaamaagaaegIDVWSiEPEDLSSM--LMERYEP 489
Cdd:COG0554 394 EADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTalgaay--laglaVGFWK-SLEELAALwkVDRRFEP 470
|
490 500
....*....|....*....|....*
gi 51854223 490 QIQATESEIRFSTWKRAVMKSMGWV 514
Cdd:COG0554 471 QMDEEERERLYAGWKKAVERTLGWA 495
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
13-507 |
0e+00 |
|
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466789 [Multi-domain] Cd Length: 486 Bit Score: 727.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 13 VGAVVQGTNSTRFLVFNPKtAELVGSHQVELTQEYPKEGWVEEDPKEILQSVYECIAKTcekLTEANIDTSKIKAIGVSN 92
Cdd:cd07769 2 ILAIDQGTTSTRAILFDED-GNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREA---LAKAGISASDIAAIGITN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 93 QRETTVVWDKFTGEPLYNAVVWLDLRTQSTVESLNKKipGNSNFVKSKTGLPLSTYFSAVKLRWMLDNLRPIQKAVEEDR 172
Cdd:cd07769 78 QRETTVVWDKKTGKPLYNAIVWQDRRTADICEELKAK--GLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAERGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 173 ALFGTIDSWLIWCMTGGvngGIHCTDVTNASRTMLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGQM-TSGALEGV 251
Cdd:cd07769 156 LLFGTIDTWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTdPEGLGAGI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 252 PISGCLGDQSAALVGQMCFQEGQAKNTYGTGCFLLCNTGQKCVFSEHGLLTTVAYKLGKnkPAFYALEGSVAIAGAVIRW 331
Cdd:cd07769 233 PIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQIGG--KVTYALEGSIFIAGAAIQW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 332 LRDNFELITSSGEVEDLAREVGTAYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREIVDAM 411
Cdd:cd07769 311 LRDNLGLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLEAM 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 412 NRDCGIPLSHLRVDGRMTNNKILMQLQADILHIPVVKSVMPETTalgaamaagaaeGIDVWSiEPEDLSSMLME--RYEP 489
Cdd:cd07769 391 EKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTalgaa--ylaglAVGFWK-DLDELASLWQVdkRFEP 467
|
490
....*....|....*...
gi 51854223 490 QIQATESEIRFSTWKRAV 507
Cdd:cd07769 468 SMDEEERERLYRGWKKAV 485
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
11-514 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 692.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 11 PLVGAVVQGTNSTRFLVFNPKtAELVGSHQVELTQEYPKEGWVEEDPKEILQSVYECIAKTCEKLTEANIDTsKIKAIGV 90
Cdd:PTZ00294 2 KYIGSIDQGTTSTRFIIFDEK-GNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKGPSF-KIKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 91 SNQRETTVVWDKFTGEPLYNAVVWLDLRTQSTVESLNKKIpGNSNFVKSKTGLPLSTYFSAVKLRWMLDNLRPIQKAVEE 170
Cdd:PTZ00294 80 TNQRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKY-GGSNFFQKITGLPISTYFSAFKIRWMLENVPAVKDAVKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 171 DRALFGTIDSWLIWCMTGGvngGIHCTDVTNASRTMLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGQMTS---GA 247
Cdd:PTZ00294 159 GTLLFGTIDTWLIWNLTGG---KSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTISGeavPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 248 LEGVPISGCLGDQSAALVGQMCFQEGQAKNTYGTGCFLLCNTGQKCVFSEHGLLTTVAYKLGKNKPAFYALEGSVAIAGA 327
Cdd:PTZ00294 236 LEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYQLGPNGPTVYALEGSIAVAGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 328 VIRWLRDNFELITSSGEVEDLAREVGTAYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREI 407
Cdd:PTZ00294 316 GVEWLRDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 408 VDAMNRDCGIPLSHLRVDGRMTNNKILMQLQADILHIPVVKSVMPETTalGAAMAAGAAEGIDVW-SIEP-EDLSSMLME 485
Cdd:PTZ00294 396 IESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETT--ALGAALLAGLAVGVWkSLEEvKKLIRRSNS 473
|
490 500
....*....|....*....|....*....
gi 51854223 486 RYEPQIQATESEIRFSTWKRAVMKSMGWV 514
Cdd:PTZ00294 474 TFSPQMSAEERKAIYKEWNKAVERSLKWA 502
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
13-514 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 679.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 13 VGAVVQGTNSTRFLVFNpKTAELVGSHQVELTQEYPKEGWVEEDPKEILQSVYECIAktcEKLTEANIDTSKIKAIGVSN 92
Cdd:PRK00047 7 ILALDQGTTSSRAIIFD-HDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIA---EALAKAGISPDQIAAIGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 93 QRETTVVWDKFTGEPLYNAVVWLDLRTQSTVESLNKKipGNSNFVKSKTGLPLSTYFSAVKLRWMLDNLRPIQKAVEEDR 172
Cdd:PRK00047 83 QRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRD--GYEDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 173 ALFGTIDSWLIWCMTGGvngGIHCTDVTNASRTMLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGQMTSG--ALEG 250
Cdd:PRK00047 161 LLFGTIDTWLVWKLTGG---KVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYgfFGGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 251 VPISGCLGDQSAALVGQMCFQEGQAKNTYGTGCFLLCNTGQKCVFSEHGLLTTVAYKLGkNKPAfYALEGSVAIAGAVIR 330
Cdd:PRK00047 238 VPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGID-GKVV-YALEGSIFVAGSAIQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 331 WLRDNFELITSSGEVEDLAREVGTAYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREIVDA 410
Cdd:PRK00047 316 WLRDGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 411 MNRDCGIPLSHLRVDGRMTNNKILMQLQADILHIPVVKSVMPETTalGAAMAAGAAEGIDVWSiEPEDLSSM--LMERYE 488
Cdd:PRK00047 396 MQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETT--ALGAAYLAGLAVGFWK-DLDELKEQwkIDRRFE 472
|
490 500
....*....|....*....|....*.
gi 51854223 489 PQIQATESEIRFSTWKRAVMKSMGWV 514
Cdd:PRK00047 473 PQMDEEEREKLYAGWKKAVKRTLAWA 498
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
12-514 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 674.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 12 LVGAVVQGTNSTRFLVFnPKTAELVGSHQVELTQEYPKEGWVEEDPKEILQSVYECIAKTCEKLTEANID-TSKIKAIGV 90
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIY-DRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGHNvDSGLKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 91 SNQRETTVVWDKFTGEPLYNAVVWLDLRTQSTVESLNKKIPGNSNFVKSKTGLPLSTYFSAVKLRWMLDNLRPIQKAVEE 170
Cdd:PLN02295 80 TNQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKELSGGRKHFVETCGLPISTYFSATKLLWLLENVDAVKEAVKS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 171 DRALFGTIDSWLIWCMTGGVNGGIHCTDVTNASRTMLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGQMTSG-ALE 249
Cdd:PLN02295 160 GDALFGTIDSWLIWNLTGGASGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIAKGwPLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 250 GVPISGCLGDQSAALVGQMCfQEGQAKNTYGTGCFLLCNTGQKCVFSEHGLLTTVAYKLGKNKPAFYALEGSVAIAGAVI 329
Cdd:PLN02295 240 GVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYKLGPDAPTNYALEGSVAIAGAAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 330 RWLRDNFELITSSGEVEDLAREVGTAYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREIVD 409
Cdd:PLN02295 319 QWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQVKDVLD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 410 AMNRDCGIPLSH-----LRVDGRMTNNKILMQLQADILHIPVVKSVMPETTalGAAMAAGAAEGIDVWSiEPEDLSSMLM 484
Cdd:PLN02295 399 AMRKDAGEEKSHkglflLRVDGGATANNLLMQIQADLLGSPVVRPADIETT--ALGAAYAAGLAVGLWT-EEEIFASEKW 475
|
490 500 510
....*....|....*....|....*....|...
gi 51854223 485 E---RYEPQIQATESEIRFSTWKRAVMKSMGWV 514
Cdd:PLN02295 476 KnttTFRPKLDEEERAKRYASWCKAVERSFDLA 508
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
18-507 |
0e+00 |
|
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases
Pssm-ID: 198361 [Multi-domain] Cd Length: 486 Bit Score: 669.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 18 QGTNSTRFLVFNPKtAELVGSHQVELTQEYPKEGWVEEDPKEILQSVYECIAktcEKLTEANIDTSKIKAIGVSNQRETT 97
Cdd:cd07786 7 QGTTSSRAILFDHD-GNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAR---EALAKAGIRASDIAAIGITNQRETT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 98 VVWDKFTGEPLYNAVVWLDLRTQSTVESLNKKipGNSNFVKSKTGLPLSTYFSAVKLRWMLDNLRPIQKAVEEDRALFGT 177
Cdd:cd07786 83 VVWDRETGKPVYNAIVWQDRRTADICEELKAE--GHEEMIREKTGLVLDPYFSATKIRWILDNVPGARERAERGELAFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 178 IDSWLIWCMTGGvngGIHCTDVTNASRTMLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGqMTSGAL--EGVPISG 255
Cdd:cd07786 161 IDSWLIWKLTGG---KVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFG-YTDPDLlgAEIPIAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 256 CLGDQSAALVGQMCFQEGQAKNTYGTGCFLLCNTGQKCVFSEHGLLTTVAYKLGkNKPAfYALEGSVAIAGAVIRWLRDN 335
Cdd:cd07786 237 IAGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLG-GKVT-YALEGSIFIAGAAVQWLRDG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 336 FELITSSGEVEDLAREVGTAYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREIVDAMNRDC 415
Cdd:cd07786 315 LGLIESAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEADS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 416 GIPLSHLRVDGRMTNNKILMQLQADILHIPVVKSVMPETTalGAAMAAGAAEGIDVWSiEPEDLSSM--LMERYEPQIQA 493
Cdd:cd07786 395 GIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETT--ALGAAYLAGLAVGLWK-SLDELAKLwqVDRRFEPSMSE 471
|
490
....*....|....
gi 51854223 494 TESEIRFSTWKRAV 507
Cdd:cd07786 472 EEREALYAGWKKAV 485
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
19-507 |
2.91e-144 |
|
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: 425.44 E-value: 2.91e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 19 GTNSTRFLVFNpKTAELVGSHQVELTQEYPKEGWVEEDPKEILQSVYECIaktCEKLTEANIDTSKIKAIGVSNQRETTV 98
Cdd:cd07793 8 GTTNIRCHIFD-KKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVI---KEALKNAGLTPEDIAAIGISTQRNTFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 99 VWDKFTGEPLYNAVVWLDLRTQSTVESLNKK-----IPGNSNFVKSKTGLP---------LSTYFSAVKLRWMLDNLRPI 164
Cdd:cd07793 84 TWDKKTGKPLHNFITWQDLRAAELCESWNRSlllkaLRGGSKFLHFLTRNKrflaasvlkFSTAHVSIRLLWILQNNPEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 165 QKAVEEDRALFGTIDSWLIWCMTGGvngGIHCTDVTNASRTMLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGqMT 244
Cdd:cd07793 164 KEAAEKGELLFGTIDTWLLWKLTGG---KVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFG-ST 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 245 SGALEG--VPISGCLGDQSAALVGQMCFQEGQAKNTYGTGCFLLCNTGQKCVFSEHGLLTTVAYKLGKNKpaFYALEGSV 322
Cdd:cd07793 240 DPSIFGaeIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGGEI--TYLAEGNA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 323 AIAGAVIRWLRDnFELITSSGEVEDLAREVGTAYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCF 402
Cdd:cd07793 318 SDTGTVIDWAKS-IGLFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIAF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 403 QTREIVDAMNRDCGIPLSHLRVDGRMTNNKILMQLQADILHIPVVKSVMPETTalGAAMAAGAAEGIDVWSiEPEDLSSM 482
Cdd:cd07793 397 RVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMS--ALGAAFLAGLASGIWK-SKEELKKL 473
|
490 500
....*....|....*....|....*..
gi 51854223 483 --LMERYEPQIQATESEIRFSTWKRAV 507
Cdd:cd07793 474 rkIEKIFEPKMDNEKREELYKNWKKAV 500
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
12-266 |
3.84e-100 |
|
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: 302.72 E-value: 3.84e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 12 LVGAVVQGTNSTRFLVFNpKTAELVGSHQVELTQEYPKEGWVEEDPKEILQSVYECIAKTCeklTEANIDTSKIKAIGVS 91
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFN-EQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTL---SQLGISLKQIKGIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 92 NQRETTVVWDKfTGEPLYNAVVWLDLRTQSTVESLNKkiPGNSNFVKSKTGLPLSTYFSAVKLRWMLDNLRPIQKAVEed 171
Cdd:pfam00370 77 NQGHGTVLLDK-NDKPLYNAILWKDRRTAEIVENLKE--EGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIH-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 172 raLFGTIDSWLIWCMTGgvnggIHCTDVTNASRTMLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGQMTS------ 245
Cdd:pfam00370 152 --KFLTIHDYLRWRLTG-----VFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPelaamw 224
|
250 260
....*....|....*....|.
gi 51854223 246 GALEGVPISGCLGDQSAALVG 266
Cdd:pfam00370 225 GLDEGVPVVGGGGDQQAAAFG 245
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
19-455 |
1.93e-93 |
|
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: 294.43 E-value: 1.93e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 19 GTNSTRFLVFNPkTAELVGSHQVELTQEYPKEGWVEEDPKEILQSVYECIAKTcekLTEANIDTSKIKAIGVSNQRETTV 98
Cdd:COG1070 9 GTTSVKAVLFDA-DGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIREL---LAKAGVDPEEIAAIGVSGQMHGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 99 VWDKfTGEPLYNAVVWLDLRTQSTVESLNKKIPGNSNFvkSKTGLPLSTYFSAVKLRWMLDNlrpiQKAVEEDRALFGTI 178
Cdd:COG1070 85 LLDA-DGEPLRPAILWNDTRAAAEAAELREELGEEALY--EITGNPLHPGFTAPKLLWLKEN----EPEIFARIAKVLLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 179 DSWLIWCMTGgvnggIHCTDVTNASRTMLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGQMTS------GALEGVP 252
Cdd:COG1070 158 KDYLRYRLTG-----EFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAeaaaetGLPAGTP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 253 ISGCLGDQSAALVGQMCFQEGQAKNTYGTGCFLLCNTGQKcVFSEHGLLTTVAYKLgknkPAFYALEGSVAIAGAVIRWL 332
Cdd:COG1070 233 VVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKP-LPDPEGRVHTFCHAV----PGRWLPMGATNNGGSALRWF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 333 RDNFeLITSSGEVEDLAREVGT----AYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREIV 408
Cdd:COG1070 308 RDLF-ADGELDDYEELNALAAEvppgADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGL 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 51854223 409 DAMnRDCGIPLSHLRVDGRMTNNKILMQLQADILHIPVVKSVMPETT 455
Cdd:COG1070 387 EAL-EEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGG 432
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
19-455 |
1.06e-90 |
|
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: 284.07 E-value: 1.06e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 19 GTNSTRFLVFNPkTAELVGSHQVELTQEYPKEGWVEEDPKEILQSVYECIAktcEKLTEANIDTSKIKAIGVSNQRETTV 98
Cdd:cd00366 8 GTTSVKAALFDE-DGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIR---EVLAKAGIDPSDIAAIGISGQMPGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 99 VWDKfTGEPLYNAVVWLDLRtqstveslnkkipgnsnfvksktglplstyfsavklrwmldnlrpiqkaveedrALFGTI 178
Cdd:cd00366 84 LVDA-DGNPLRPAIIWLDRR------------------------------------------------------AKFLQP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 179 DSWLIWCMTGgvnggIHCTDVTNASRTMLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGQMTSGA------LEGVP 252
Cdd:cd00366 109 NDYIVFRLTG-----EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAaeetglPAGTP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 253 ISGCLGDQSAALVGQMCFQEGQAKNTYGTGCFLLCNTgQKCVFSEHGLLTTVAYKLGKnkpafYALEGSVAIAGAVIRWL 332
Cdd:cd00366 184 VVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCT-DEPVPPDPRLLNRCHVVPGL-----WLLEGAINTGGASLRWF 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 333 RDNFELITSS----GEVEDLAREVGT-AYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREI 407
Cdd:cd00366 258 RDEFGEEEDSdaeyEGLDELAAEVPPgSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDN 337
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 51854223 408 VDAMnRDCGIPLSHLRVDGRMTNNKILMQLQADILHIPVVKSVMPETT 455
Cdd:cd00366 338 LEIL-EELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGA 384
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
19-455 |
4.93e-88 |
|
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: 278.25 E-value: 4.93e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 19 GTNSTRFLVFNPkTAELVGSHQVELTQEYPKEGWVEEDPKEILQSVYECIAKTCEKlteANIDTSKIKAIGVSNQRETTV 98
Cdd:cd07779 8 GTTSTRAIIFDL-DGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAK---AGVDPEDIAAIGLTSQRSTFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 99 VWDKfTGEPLYNAVVWLDLRTqstveslnkkipgnsnfvksktglplstyfsavklrwmldnlrpiqkaveedrALFGTI 178
Cdd:cd07779 84 PVDE-DGRPLRPAISWQDKRT-----------------------------------------------------AKFLTV 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 179 DSWLIWCMTGGvnggiHCTDVTNASRTMLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGQMTS------GALEGVP 252
Cdd:cd07779 110 QDYLLYRLTGE-----FVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKeaaeetGLPEGTP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 253 ISGCLGDQSAALVGQMCFQEGQAKNTYGTGCFLLCNTgQKCVFSEHGLLTTVAYkLGKNKpafYALEGSVAIAGAVIRWL 332
Cdd:cd07779 185 VVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVS-DKPVEDPERRIPCNPS-AVPGK---WVLEGSINTGGSAVRWF 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 333 RDNF---ELITSSGEV---EDLAREVGT----AYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCF 402
Cdd:cd07779 260 RDEFgqdEVAEKELGVspyELLNEEAAKsppgSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAF 339
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 51854223 403 QTREIVDAMnRDCGIPLSHLRVDGRMTNNKILMQLQADILHIPVVKSVMPETT 455
Cdd:cd07779 340 ELRDNLEAM-EKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEAT 391
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
19-455 |
6.07e-80 |
|
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: 259.01 E-value: 6.07e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 19 GTNSTRFLVFNPKtAELVGSHQVELTQEYPKEGWVEEDPKEILQSVYECIAKTcekLTEANIDTSKIKAIGVSNQRETTV 98
Cdd:cd07808 8 GTSSVKAVLVDED-GRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALREL---LAKAGISPSDIAAIGLTGQMHGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 99 VWDKfTGEPLYNAVVWLDLRTQSTVESLNKKIPgnsNFVKSKTGLPLSTYFSAVKLRWMLDNLRPIQKAVeeDRALFGTi 178
Cdd:cd07808 84 LLDK-NGRPLRPAILWNDQRSAAECEELEARLG---DEILIITGNPPLPGFTLPKLLWLKENEPEIFARI--RKILLPK- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 179 DsWLIWCMTGgvnggIHCTDVTNASRTMLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGQMTSGA------LEGVP 252
Cdd:cd07808 157 D-YLRYRLTG-----ELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAaeelglPEGTP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 253 -ISGClGDQSAALVGQMCFQEGQAKNTYGTGCFLLCNTgQKCVFSEHGLLTTVAYKLGknkPAFYALeGSVAIAGAVIRW 331
Cdd:cd07808 231 vVAGA-GDNAAAALGAGVVEPGDALISLGTSGVVFAPT-DKPVPDPKGRLHTFPHAVP---GKWYAM-GVTLSAGLSLRW 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 332 LRDNF-ELITSSGEVEDLAREVG-TAYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREIVD 409
Cdd:cd07808 305 LRDLFgPDRESFDELDAEAAKVPpGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLE 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 51854223 410 AMnRDCGIPLSHLRVDGRMTNNKILMQLQADILHIPVVKSVMPETT 455
Cdd:cd07808 385 VL-KELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGS 429
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
19-455 |
5.51e-78 |
|
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: 252.51 E-value: 5.51e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 19 GTNSTRFLVFNPkTAELVGSHQVELTQEYPKEGWVEEDPKEILQSVYECIAKTCEKLteaniDTSKIKAIGVSNQRETTV 98
Cdd:cd07773 8 GTTNVKAVLFDE-DGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQA-----GPDPIAAISVSSQGESGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 99 VWDKfTGEPLYNAVVWLDLRTQSTVESLNKKIPGNSNFvkSKTGLPLSTYFSAVKLRWMLDNLRPIQKAVeeDRALfgTI 178
Cdd:cd07773 82 PVDR-DGEPLGPAIVWFDPRGKEEAEELAERIGAEELY--RITGLPPSPMYSLAKLLWLREHEPEIFAKA--AKWL--SV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 179 DSWLIWCMTGGvnggiHCTDVTNASRTMLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGQMTSGALE------GVP 252
Cdd:cd07773 155 ADYIAYRLTGE-----PVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEelglpaGTP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 253 IsgCLG--DQSAALVGQMCFQEGQAKNTYGTG-CFLLC-NTGQKCVFSEHGLLTTVAYKLGKnkpaFYALEGSVAiAGAV 328
Cdd:cd07773 230 V--VVGghDHLCAALGAGVIEPGDVLDSTGTAeALLAVvDEPPLDEMLAEGGLSYGHHVPGG----YYYLAGSLP-GGAL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 329 IRWLRDNF--ELITSSGEVEDLAREVGTAYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTRE 406
Cdd:cd07773 303 LEWFRDLFggDESDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRL 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 51854223 407 IVDAMnRDCGIPLSHLRVDGRMTNNKILMQLQADILHIPVVKSVMPETT 455
Cdd:cd07773 383 NLEAL-EKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEAT 430
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
19-447 |
6.40e-71 |
|
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: 234.34 E-value: 6.40e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 19 GTNSTRFLVFNPKtAELVGSHQVELTQEYPKEGWVEEDPKEILQSVYECIAKTCEKlteANIDTSKIKAIGVSNQRETTV 98
Cdd:cd07804 8 GTTGTKGVLVDED-GKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAK---AGISPKEIAAIGVSGLVPALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 99 VWDKFtGEPLYNAVVWLDLRTQSTVESLNKKIpgNSNFVKSKTGLPLSTYFSAVKLRWMLDNlRPiqkAVEEDRALFGTI 178
Cdd:cd07804 84 PVDEN-GKPLRPAILYGDRRATEEIEWLNENI--GEDRIFEITGNPLDSQSVGPKLLWIKRN-EP---EVFKKTRKFLGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 179 DSWLIWCMTGgvnggIHCTDVTNASRTM-LFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGQMTSGA------LEGV 251
Cdd:cd07804 157 YDYIVYKLTG-----EYVIDYSSAGNEGgLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEAaeetglAEGT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 252 PISGCLGDQSAALVGQMCFQEGQAKNTYGT-GCFLLCNtgqkcvfseHGLLTTVAYKLGKN-KPAFYALEGSVAIAGAVI 329
Cdd:cd07804 232 PVVAGTVDAAASALSAGVVEPGDLLLMLGTaGDIGVVT---------DKLPTDPRLWLDYHdIPGTYVLNGGMATSGSLL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 330 RWLRDNFelitSSGEVEDLAREVGTAY---------------GCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAF 394
Cdd:cd07804 303 RWFRDEF----AGEEVEAEKSGGDSAYdlldeeaekippgsdGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYR 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 51854223 395 AALEAVCFQTREIVDAMNRDcGIPLSHLRVDGRMTNNKILMQLQADILHIPVV 447
Cdd:cd07804 379 ALLEGVAYGLRHHLEVIREA-GLPIKRLVAVGGGAKSPLWRQIVADVTGVPQE 430
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
19-455 |
1.65e-68 |
|
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: 228.59 E-value: 1.65e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 19 GTNSTRFLVFNPKtAELVGSHQVELTQEYPKEGWVEEDPKEILQSVYECIAKTCEKLteaniDTSKIKAIGVSNQRETTV 98
Cdd:cd07770 8 GTTSTKAVLFDED-GRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKL-----GGGEVDAIGFSSAMHSLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 99 VWDKfTGEPLYNAVVWLDLRTQSTVESLnkKIPGNSNFVKSKTGLPLSTYFSAVKLRWMLDNLRPIQKAVeedrALFGTI 178
Cdd:cd07770 82 GVDE-DGEPLTPVITWADTRAAEEAERL--RKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKA----AKFVSI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 179 DSWLIWCMTGGvnggiHCTDVTNASRTMLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGQMTS------GALEGVP 252
Cdd:cd07770 155 KEYLLYRLTGE-----LVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPefaerlGLLAGTP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 253 ISGCLGDQSAALVGQMCFQEGQAKNTYGTgcfllcnTGQKCVFSEHGLLT----TVAYKLGKNkpaFYALEGSVAIAGAV 328
Cdd:cd07770 230 VVLGASDGALANLGSGALDPGRAALTVGT-------SGAIRVVSDRPVLDppgrLWCYRLDEN---RWLVGGAINNGGNV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 329 IRWLRDNFELITSS-GEVEDLAREVG-TAYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTRE 406
Cdd:cd07770 300 LDWLRDTLLLSGDDyEELDKLAEAVPpGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKS 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 51854223 407 IVDAMnRDCGIPLSHLRVDGRMTNNKILMQLQADILHIPVVKSVMPETT 455
Cdd:cd07770 380 IYEAL-EELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEAS 427
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
34-453 |
7.39e-64 |
|
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: 216.62 E-value: 7.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 34 ELVGSHQVELTQEYPKEGWVEEDPKEILQSVYECiakTCEKLTEANIDTSKIKAIGVSNQRETTVVWDKfTGEPLYNAVV 113
Cdd:cd07805 22 ELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRA---TRALLEKSGIDPSDIAAIAFSGQMQGVVPVDK-DGNPLRNAII 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 114 WLDLRTQSTVESLNKKIPGNSnFVKSKTGLPLSTYFSAVKLRWMLDNlRPiqKAVEEDRALFGTIDsWLIWCMTGGVngg 193
Cdd:cd07805 98 WSDTRAAEEAEEIAGGLGGIE-GYRLGGGNPPSGKDPLAKILWLKEN-EP--EIYAKTHKFLDAKD-YLNFRLTGRA--- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 194 ihCTDVTNASRTMLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGQMTSGA------LEGVPISGCLGDQSAALVGQ 267
Cdd:cd07805 170 --ATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAaaelglPAGTPVVGGGGDAAAAALGA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 268 MCFQEGQAkNTY-GTGCFLLCNTGQKCVFSEHGlLTTVAYKLgknkPAFYALEGSVAIAGAVIRWLRDNFELITSSG--- 343
Cdd:cd07805 248 GAVEEGDA-HIYlGTSGWVAAHVPKPKTDPDHG-IFTLASAD----PGRYLLAAEQETAGGALEWARDNLGGDEDLGadd 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 344 --EVEDLAREVGT-AYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREIVDAMNRDCGiPLS 420
Cdd:cd07805 322 yeLLDELAAEAPPgSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWLLEALEKLTR-KID 400
|
410 420 430
....*....|....*....|....*....|...
gi 51854223 421 HLRVDGRMTNNKILMQLQADILHIPVVKSVMPE 453
Cdd:cd07805 401 ELRLVGGGARSDLWCQILADVLGRPVEVPENPQ 433
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
19-458 |
2.70e-48 |
|
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: 173.51 E-value: 2.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 19 GTNSTRFLVFNPKTAElVGSHQVELTQEYPKEGWVEEDPKEILQSVYECIAKTCEKlteANIDTSKIKAIGVSNQRETTV 98
Cdd:cd07802 8 GTTNVKAVLFDLDGRE-IAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEK---SGVDPSDIAGVGVTGHGNGLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 99 VWDKfTGEPLYNAVVWLDLRTQSTVESLNKKipGNSNFVKSKTGLPLSTYFSAVKLRWMLDNlRP--IQKAveedRALFG 176
Cdd:cd07802 84 LVDK-DGKPVRNAILSNDSRAADIVDRWEED--GTLEKVYPLTGQPLWPGQPVALLRWLKEN-EPerYDRI----RTVLF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 177 TIDsWLIWCMTGgvnggIHCTDVTNASrTMLFNIHSLEWDKELCKFFEIP--MSILPNVRSSSEIYGQMTSGA------L 248
Cdd:cd07802 156 CKD-WIRYRLTG-----EISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVTAEAaaltglP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 249 EGVPISGCLGDQSAALVGQMCFQEGQAKNTYGTGCfllCNTG--QKCVFSEHGLLTTVAYKLGKnkpaFYALEGSVAIAG 326
Cdd:cd07802 229 EGTPVAAGAFDVVASALGAGAVDEGQLCVILGTWS---INEVvtDEPVVPDSVGSNSLHADPGL----YLIVEASPTSAS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 327 aVIRWLRDNF---ELITSSGEVEDLAREVGT----AYGCYFVPaFsgLYAPYWEPSARGIICGLTQFTNKCHIAFAALEA 399
Cdd:cd07802 302 -NLDWFLDTLlgeEKEAGGSDYDELDELIAAvppgSSGVIFLP-Y--LYGSGANPNARGGFFGLTAWHTRAHLLRAVYEG 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 51854223 400 VCFQTREIVDAMNRDCgiPLSHLRVDGRMTNNKILMQLQADILHIPVVKSVMPETTALG 458
Cdd:cd07802 378 IAFSHRDHLERLLVAR--KPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALG 434
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
275-458 |
6.33e-44 |
|
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: 154.40 E-value: 6.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 275 AKNTYGTGCFLLCNTGQKCVFsEHGLLTTVAYKLGknkPAFYALEGSVAIAGAVIRWLRDNFEL---ITSSGEVEDLA-- 349
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLS-VHGVWGPYTNEML---PGYWGLEGGQSAAGSLLAWLLQFHGLreeLRDAGNVESLAel 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 350 --REVGT-AYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREIVDAMNRDCGIPLSHLRVDG 426
Cdd:pfam02782 77 aaLAAVApAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSG 156
|
170 180 190
....*....|....*....|....*....|..
gi 51854223 427 RMTNNKILMQLQADILHIPVVKSVMPETTALG 458
Cdd:pfam02782 157 GGSRNPLLLQLLADALGLPVVVPGPDEATALG 188
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
19-454 |
2.66e-43 |
|
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: 159.70 E-value: 2.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 19 GTNSTRFLVFNPKtAELVGSHQVELTQEYPKEGWVEEDPKEILQSVYECIAKTCeklteANIDTSKIKAIGVSNQRETTV 98
Cdd:cd07783 8 GTSGVRAVVVDED-GTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELP-----AELRPRRVVAIAVDGTSGTLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 99 VWDKfTGEPLYNAVVWLDLRTQSTVESLNKKIPgnsnFVKSKTGLPLSTYFSAVKLRWMLDNLRPIQKAVeedrALFGTI 178
Cdd:cd07783 82 LVDR-EGEPLRPAIMYNDARAVAEAEELAEAAG----AVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKT----AKFLHQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 179 DSWLIWCMTGGVNggihCTDVTNASRTmLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGQMTS------GALEGVP 252
Cdd:cd07783 153 ADWLAGRLTGDRG----VTDYNNALKL-GYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAeaaeelGLPAGTP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 253 IsgCLG--DQSAALVGQMCFQEGQAKNTYGTG-CF-LLCntgQKCVFSEHGLLTTvaYKLGKNkpaFYALEGSVAIAGAV 328
Cdd:cd07783 228 V--VAGttDSIAAFLASGAVRPGDAVTSLGTTlVLkLLS---DKRVPDPGGGVYS--HRHGDG---YWLVGGASNTGGAV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 329 IRWLrdnfeliTSSGEVEDLAREVGTAY--GCYFVP-AFSGLYAPYWEPSARGIICGLTqfTNKCHIAFAALEAVCFQTR 405
Cdd:cd07783 298 LRWF-------FSDDELAELSAQADPPGpsGLIYYPlPLRGERFPFWDPDARGFLLPRP--HDRAEFLRALLEGIAFIER 368
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 51854223 406 EIVDAMNRDCGIPLSHLRVDGRMTNNKILMQLQADILHIPVVKSVMPET 454
Cdd:cd07783 369 LGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEA 417
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
19-455 |
8.34e-42 |
|
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to Bacillus subtilis sugar kinase YoaC. It is part of the yoaDCB operon and induced by sulfate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466804 [Multi-domain] Cd Length: 448 Bit Score: 155.84 E-value: 8.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 19 GTNSTRFLVFNPKTAELVGSHQvELTQEYPK--EGWVEEDPKEILQSVYECIAKTcekLTEANIDTSKIKAIGVSNQRET 96
Cdd:cd07798 8 GTGGGRCALVDSEGKIVAIAYR-EWEYYTDDdyPDAKEFDPEELWEKICEAIREA---LKKAGISPEDISAVSSTSQREG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 97 TVVWDKFtGEPLYnAVVWLDLRTQSTVESLNKKIPgnsNFVKSKTGLPLSTYFSAVKLRWmldnLRPIQKAVEEDRALFG 176
Cdd:cd07798 84 IVFLDKD-GRELY-AGPNIDARGVEEAAEIDDEFG---EEIYTTTGHWPTELFPAARLLW----FKENRPEIFERIATVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 177 TIDSWLIWCMTGGVnggihCTDVTNASRTMLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGQMTSGA------LEG 250
Cdd:cd07798 155 SISDWIGYRLTGEL-----VSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAarelglPEG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 251 VPISGCLGDQSAALVGQMCFQEGQAKNTYGTGCFLLCNTGqKCVFSEHGLLTTVAYkLGKNKpafYALEGSVAIAGAVIR 330
Cdd:cd07798 230 TPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTD-EPIIDPERRLWTGCH-LVPGK---WVLESNAGVTGLNYQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 331 WLRDNFeLITSSGEVEDLAREVGTA-YGCYFVPAFSGLYAPYwePSARGIICGLTQFT--------NKCHIAFAALEAVC 401
Cdd:cd07798 305 WLKELL-YGDPEDSYEVLEEEASEIpPGANGVLAFLGPQIFD--ARLSGLKNGGFLFPtplsaselTRGDFARAILENIA 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 51854223 402 FQTREIVDAMNRDCGIPLSHLRVDGRMTNNKILMQLQADILHIPVVKSVMPETT 455
Cdd:cd07798 382 FAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREAS 435
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
19-458 |
2.18e-32 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 129.21 E-value: 2.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 19 GTNSTRFLVFNPKTAELVGSHQVELTQEYPKEGWVEEDPKEILQSVYECIAKTcekLTEANIDTSKIKAIGVSNQRETTV 98
Cdd:cd07809 8 GTQSIKAVLIDAETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQL---LKDAGAELRDVAAIGISGQMHGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 99 VWDKfTGEPLYNAVVWLDLRTQSTVESLNKKIPGNsnfVKSKTGLPLSTYFSAVKLRWMLDNlrpiqkavEEDraLFGTI 178
Cdd:cd07809 85 ALDA-DGKVLRPAKLWCDTRTAPEAEELTEALGGK---KCLLVGLNIPARFTASKLLWLKEN--------EPE--HYARI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 179 DS------WLIWCMTGGvnggiHCTDVTNASRTMLFNIHSLEWDKELCKFFE---IPMSILPNVRSSSEIYGQMT-SGAL 248
Cdd:cd07809 151 AKillphdYLNWKLTGE-----KVTGLGDASGTFPIDPRTRDYDAELLAAIDpsrDLRDLLPEVLPAGEVAGRLTpEGAE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 249 E-----GVPISGCLGDQSAALVGQMCFQEGQAKNTYGT-GCflLCNTGQKCVFSEHGLLTTVAYKLGknkpafyALEGSV 322
Cdd:cd07809 226 ElglpaGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTsGT--AYGVSDKPVSDPHGRVATFCDSTG-------GMLPLI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 323 AIAGAVIRWLRDNFELITSS-GEVEDLAREV-GTAYGCYFVPAFSGLYAPYWePSARGIICGLTQF-TNKCHIAFAALEA 399
Cdd:cd07809 297 NTTNCLTAWTELFRELLGVSyEELDELAAQApPGAGGLLLLPFLNGERTPNL-PHGRASLVGLTLSnFTRANLARAALEG 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 51854223 400 VCFQTREIVDAMnRDCGIPLSHLRVDGRMTNNKILMQLQADILHIPVVKSVMPETTALG 458
Cdd:cd07809 376 ATFGLRYGLDIL-RELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALG 433
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
19-458 |
9.64e-29 |
|
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: 118.86 E-value: 9.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 19 GTNSTRFLVFNPKTAELVGSHQVE--LTQEYPKEGWVEEDPKEILQSVYECIAKTCEKLTeanidtSKIKAIGVSNQRET 96
Cdd:cd07777 8 GTTSIKAALLDLESGRILESVSRPtpAPISSDDPGRSEQDPEKILEAVRNLIDELPREYL------SDVTGIGITGQMHG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 97 TVVWDKfTGEPLYNAVVWLDLRtqSTVESLNKKIPGNSNFvKSKTGLPLSTYFSAVKLRWMLDNlrpiqKAVEEDRALFG 176
Cdd:cd07777 82 IVLWDE-DGNPVSPLITWQDQR--CSEEFLGGLSTYGEEL-LPKSGMRLKPGYGLATLFWLLRN-----GPLPSKADRAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 177 TIDSWLIWCMTGGvngGIHCTDVTNASRTMLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGQMTSGALEGVPISGC 256
Cdd:cd07777 153 TIGDYIVARLTGL---PKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLSSALPKGIPVYVA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 257 LGDQSAALVGQMCFQEGQAKNTYGTG---CFLLCNTGQKCV-----FSEHGLLTTVAyklgknkpafyALEGSVAIAgAV 328
Cdd:cd07777 230 LGDNQASVLGSGLNEENDAVLNIGTGaqlSFLTPKFELSGSveirpFFDGRYLLVAA-----------SLPGGRALA-VL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 329 IRWLRDNFELITSSGEVED----LAREVGTAYGC--YFVPAFSGlyaPYWEPSARGIICGLTQ--FTNKcHIAFAALEAV 400
Cdd:cd07777 298 VDFLREWLRELGGSLSDDEiwekLDELAESEESSdlSVDPTFFG---ERHDPEGRGSITNIGEsnFTLG-NLFRALCRGI 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51854223 401 CfqtREIVDAMNRDC--GIPLSHLRVDGRM-TNNKILMQLQADILHIPVVKSVMPETTALG 458
Cdd:cd07777 374 A---ENLHEMLPRLDldLSGIERIVGSGGAlRKNPVLRRIIEKRFGLPVVLSEGSEEAAVG 431
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
19-455 |
3.45e-27 |
|
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466799 [Multi-domain] Cd Length: 504 Bit Score: 114.94 E-value: 3.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 19 GTNSTRFLVFNPKTAELVGSHQVELTQEY--PKEGWVEEDPKEILQSVYECIAKTCEkltEANIDTSKIKAIGVSNQRET 96
Cdd:cd07781 8 GTQSVRAGLVDLADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALA---EAGVDPEDVVGIGVDTTSST 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 97 TVVWDKfTGEPLYNAVVWLDLRTQSTVESLNKKIPGNSNFVKSKTGLPLS--TYFSavKLRWMLDNlrpiqkaveeDRAL 174
Cdd:cd07781 85 VVPVDE-DGNPLAPAILWMDHRAQEEAAEINETAHPALEYYLAYYGGVYSseWMWP--KALWLKRN----------APEV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 175 FGTIDS------WLIWCMTGGVNGGIhCtdvtNASRTMLFNIHSLEWDKELCK-----FFEIPMSILPNVRSSSEIYGQM 243
Cdd:cd07781 152 YDAAYTiveacdWINARLTGRWVRSR-C----AAGHKWMYNEWGGGPPREFLAaldpgLLKLREKLPGEVVPVGEPAGTL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 244 TS------GALEGVPISGCLGDQSAALVGQMCFQEGQAKNTYGT-GCFLLcnTGQKCVFSEhGLLTTVAyklGKNKPAFY 316
Cdd:cd07781 227 TAeaaerlGLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTsTCHLM--VSPKPVDIP-GICGPVP---DAVVPGLY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 317 ALEGSVAIAGAVIRWLRDNF--ELITSSGEV----EDLAREVGTayGCyfvpafSGLYA---------PYWEPSARGIIC 381
Cdd:cd07781 301 GLEAGQSAVGDIFAWFVRLFvpPAEERGDSIyallSEEAAKLPP--GE------SGLVAldwfngnrtPLVDPRLRGAIV 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51854223 382 GLTQFTNKCHIAFAALEAVCFQTREIVDAMnRDCGIPLSHLRVDGRMT-NNKILMQLQADILHIPVVKSVMPETT 455
Cdd:cd07781 373 GLTLGTTPAHIYRALLEATAFGTRAIIERF-EEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAP 446
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
19-454 |
1.90e-24 |
|
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: 106.17 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 19 GTNSTRFLVFNPKTAELvGSHQVELTQEYPKEGWVEEDPKEILQSVYECIAKTCEKLTEAnidTSKIKAIGVSNQRETTV 98
Cdd:cd24121 8 GTSVVKAVAFDLDGREL-AVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVL---PDRVAAIGVTGQGDGTW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 99 VWDKfTGEPLYNAVVWLDLRTQSTVESLNKKipGNSNFVKSKTGLPLSTYFSAVKLRWMLDNlRPiqKAVEEDRALFGTI 178
Cdd:cd24121 84 LVDE-DGRPVRDAILWLDGRAADIVERWQAD--GIAEAVFEITGTGLFPGSQAAQLAWLKEN-EP--ERLERARTALHCK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 179 DsWLIWCMTGGVnggihCTDVTNASRTMlFNIHSLEWDKELCKFFEIP--MSILPNVRSSSEIYGQMTS------GALEG 250
Cdd:cd24121 158 D-WLFYKLTGEI-----ATDPSDASLTF-LDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPeaaaatGLPAG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 251 VPISGCLGDQSAALVGQMCFQEGQAKNTYGTGCFllcntGQKCVFSEHglltTVAYKLGKNKPafYALEGSV-----AIA 325
Cdd:cd24121 231 TPVVLGPFDVVATALGSGAIEPGDACSILGTTGV-----HEVVVDEPD----LEPEGVGYTIC--LGVPGRWlramaNMA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 326 G-AVIRWLRDNFELITSSG----------EVEDLAREV-----GTAYGCYFVPAfsGLYAPYWEPSARGIICGLTQFTNK 389
Cdd:cd24121 300 GtPNLDWFLRELGEVLKEGaepagsdlfqDLEELAASSppgaeGVLYHPYLSPA--GERAPFVNPNARAQFTGLSLEHTR 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51854223 390 CHIAFAALEAVCFQTREIVDAMnrdcGIPLSHLRVDGRMTNNKILMQLQADILHIPVVKSVMPET 454
Cdd:cd24121 378 ADLLRAVYEGVALAMRDCYEHM----GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEF 438
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
15-458 |
3.86e-24 |
|
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: 105.88 E-value: 3.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 15 AVVQGTNSTRFLVFNpKTAELVGSHQVELTQ-EYPK-EGWVEEDPKEILQSVYECIAKTCEKlteANIDTSKIKAIGVSN 92
Cdd:cd07775 4 ALDAGTGSGRAVIFD-LEGNQIAVAQREWRHkEVPDvPGSMDFDTEKNWKLICECIREALKK---AGIAPKSIAAISTTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 93 QRETTVVWDKfTGEPLYnAVVWLDLRTQSTVESLNKKIPGNSNFVKSKTGLPLStyFSAV-KLRWMLDNLRPIQKAVeed 171
Cdd:cd07775 80 MREGIVLYDN-EGEEIW-ACANVDARAAEEVSELKELYNTLEEEVYRISGQTFA--LGAIpRLLWLKNNRPEIYRKA--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 172 rALFGTIDSWLIWCMTGgvnggIHCTDVTNASRTMLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGQMT------S 245
Cdd:cd07775 153 -AKITMLSDWIAYKLSG-----ELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTkeaaeeT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 246 GALEGVPISGCLGDQSAALVGQMCFQEGQAKNTYGTGCFLLCNTGQKcVFSEHGLLTTVAYKLgknkPAFYALEGSVAIA 325
Cdd:cd07775 227 GLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAP-VTDPAMNIRVNCHVI----PDMWQAEGISFFP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 326 GAVIRWLRDNF---ELITSSGE-------VEDLAREVGTayGCY-FVPAFSGL--YApYWEPSARGIIcGLTQFTNKCHI 392
Cdd:cd07775 302 GLVMRWFRDAFcaeEKEIAERLgidaydlLEEMAKDVPP--GSYgIMPIFSDVmnYK-NWRHAAPSFL-NLDIDPEKCNK 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51854223 393 A--FAAL-EAVCFQTREIVDAMNRDCGIPLSHLRVDGRMTNNKILMQLQADILHIPVVKSVMPETTALG 458
Cdd:cd07775 378 AtfFRAImENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALG 446
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
56-456 |
1.14e-19 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 92.01 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 56 DPKEILQSVYECIAKTCEKLTEANIDTSKIKAIGVsnqrETTVVWDKftGEPLYNAVVWLDLRTQSTVESLNKKIPGNSN 135
Cdd:PRK10331 48 SLDAILQRFADCCRQINSELTECHIRGITVTTFGV----DGALVDKQ--GNLLYPIISWKCPRTAAVMENIERYISAQQL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 136 FVKSKTG-LPLSTYFsavKLRWMLDNlRP--IQKAveeDRALFgtIDSWLIWCMTGgvnggIHCTDVTNASRTMLFNIHS 212
Cdd:PRK10331 122 QQISGVGaFSFNTLY---KLVWLKEN-HPqlLEQA---HAWLF--ISSLINHRLTG-----EFTTDITMAGTSQMLDIQQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 213 LEWDKELCKFFEIPMSILPNVRSSSEIYGQMTSGALE------GVPISGCLGDQSAALVGQMCfQEGQAKNTYGTGCFLL 286
Cdd:PRK10331 188 RDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPSAAAllglpvGIPVISAGHDTQFALFGSGA-GQNQPVLSSGTWEILM 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 287 CNTGQ---KCVFSEHGLLTTVAYKLGKNKPAFYALegsvaiAGAVIRWLRdnfELITSSGEVEDL----AREVGT-AYGC 358
Cdd:PRK10331 267 VRSAQvdtSLLSQYAGSTCELDSQSGLYNPGMQWL------ASGVLEWVR---KLFWTAETPYQTmieeARAIPPgADGV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 359 YFVPAFSGlyapywepSARGIICGLTQFTNKCHIAFAALEAVCFQTREIVDAMNRDCGIPLSHLRVDGRMTNNKILMQLQ 438
Cdd:PRK10331 338 KMQCDLLA--------CQNAGWQGVTLNTTRGHFYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIK 409
|
410
....*....|....*...
gi 51854223 439 ADILHIPVVKSVMPETTA 456
Cdd:PRK10331 410 ANMLDIPIKVLDDAETTV 427
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
19-441 |
7.38e-19 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 89.64 E-value: 7.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 19 GTNSTRFLVFNPKtAELVGSHQVELTQEYPKEGWVEEDPKEILQSVYECIaktceKLTEANIDTSKIKAIGVSNQRETTV 98
Cdd:PRK15027 8 GTSGVKVILLNEQ-GEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAM-----KALGDQHSLQDVKALGIAGQMHGAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 99 VWDKfTGEPLYNAVVWLDLRTQSTVESLNKKIPGNsnfvKSKTGLPLSTYFSAVKLRWmldnlrpIQKaveEDRALFGTI 178
Cdd:PRK15027 82 LLDA-QQRVLRPAILWNDGRCAQECALLEARVPQS----RVITGNLMMPGFTAPKLLW-------VQR---HEPEIFRQI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 179 DS------WLIWCMTGGVnggihCTDVTNASRTMLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGQMTSGALE--- 249
Cdd:PRK15027 147 DKvllpkdYLRLRMTGEF-----ASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAKawg 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 250 --GVPISGCLGDQSAALVGQMCFQEGQAKNTYGTgcfllcnTGQKCVFSEhGLLT---TVAYKLGKNKPAFYALEGSVAI 324
Cdd:PRK15027 222 maTVPVVAGGGDNAAGAVGVGMVDANQAMLSLGT-------SGVYFAVSE-GFLSkpeSAVHSFCHALPQRWHLMSVMLS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 325 AGAVIRW------LRDNFELITSSGEVEDLAREVgtaygcYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALE 398
Cdd:PRK15027 294 AASCLDWaakltgLSNVPALIAAAQQADESAEPV------WFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLE 367
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 51854223 399 AVCFQTREIVDAMNrDCGIPLSHLRVDGRMTNNKILMQLQADI 441
Cdd:PRK15027 368 GVGYALADGMDVVH-ACGIKPQSVTLIGGGARSEYWRQMLADI 409
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
19-448 |
2.26e-16 |
|
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: 81.90 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 19 GTNSTRFLVFNPKTAELVGSHQVELTQ-EYPKEGWVEEDPKEILQSVYECIAKTcekLTEANIDTSKIKAIGVSN----- 92
Cdd:cd07768 8 GTSSARAGVYDLYAGLEMAQEPVPYYQdSSKKSWKFWQKSTEIIKALQKCVQKL---NIREGVDAYEVKGCGVDAtcsla 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 93 --QRETTVVWDKFTGEPLYNAVVWLDLRTQSTVESLNKKIPgnsnfvksKTGLP-----LSTYFSAVKLRWMLDNLRPIQ 165
Cdd:cd07768 85 ifDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWINMQCP--------QQLLDylggkISPEMGVPKLKYFLDEYSHLR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 166 KAVEEdraLFGTIDsWLIWCMTGGVNGGIhCTDVTNASrtmlFNIHSLEWDKELCKFFEIPMS------ILPNVRSSSEI 239
Cdd:cd07768 157 DKHFH---IFDLHD-YIAYELTRLYEWNI-CGLLGKEN----LDGEESGWSSSFFKNIDPRLEhltttkNLPSNVPIGTT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 240 YG----QMTS--GALEGVPISGCLGDQSAALVGQmcfqegqAKNTYGTGCFLLCNTGqkcvfSEHGLLTTVAYKLGKN-- 311
Cdd:cd07768 228 SGvalpEMAEkmGLHPGTAVVVSCIDAHASWFAV-------ASPHLETSLFMIAGTS-----SCHMYGTTISDRIPGVwg 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 312 ------KPAFYALEGSVAIAGAVIRWLRDN------FELITSSGE---------VEDLAREVGTAYGCYFVPAFSGLYAP 370
Cdd:cd07768 296 pfdtiiDPDYSVYEAGQSATGKLIEHLFEShpcarkFDEALKKGAdiyqvleqtIRQIEKNNGLSIHILTLDMFFGNRSE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 371 YWEPSARGIICGLTQFT---NKCHIAFAALEAVCFQTREIVDAMNRDcGIPLSHLRVDGRMTNNKILMQLQADILHIPVV 447
Cdd:cd07768 376 FADPRLKGSFIGESLDTsmlNLTYKYIAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKNERLLQLIALVTNVAII 454
|
.
gi 51854223 448 K 448
Cdd:cd07768 455 K 455
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
105-447 |
2.61e-15 |
|
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.
Pssm-ID: 466791 [Multi-domain] Cd Length: 460 Bit Score: 78.34 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 105 GEPLYNAVVWLDLRTQSTVESLNKKIPGNSNFvkSKTGLPLSTYFSAVKLRWMLDNLRPIQKavEEDRALFgtIDSWLIW 184
Cdd:cd07771 87 GELLGNPVHYRDPRTEGMMEELFEKISKEELY--ERTGIQFQPINTLYQLYALKKEGPELLE--RADKLLM--LPDLLNY 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 185 CMTGGVnggihCTDVTNASRTMLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGQMTS-----GALEGVP-ISGCLG 258
Cdd:cd07771 161 LLTGEK-----VAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPevaeeLGLKGIPvIAVASH 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 259 DQSAALVGQMCFQEGQAkntygtgcFLLCNT----GqkcVFSEHGLLTTVAYKLG-KNkpafyalEGSVA--------IA 325
Cdd:cd07771 236 DTASAVAAVPAEDEDAA--------FISSGTwsliG---VELDEPVITEEAFEAGfTN-------EGGADgtirllknIT 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 326 GaviRWL----RDNFELITSSGEVEDLAREVGTA--YGCYFVPAFSGLYAPywePSARGIICGLTQFTN------KCHIA 393
Cdd:cd07771 298 G---LWLlqecRREWEEEGKDYSYDELVALAEEAppFGAFIDPDDPRFLNP---GDMPEAIRAYCRETGqpvpesPGEIA 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 51854223 394 FAALEAVCFQTREIVDAMNRDCGIPLSHLRVDGRMTNNKILMQLQADILHIPVV 447
Cdd:cd07771 372 RCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPVI 425
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
19-447 |
1.12e-14 |
|
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: 76.80 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 19 GTNSTRFLVFNPkTAELVGSHQVELTQEYPKEGWVEEDPKEILQSVYECIAKTCEKlteANIDTSKIKAIGVsnqrETT- 97
Cdd:cd07782 8 GTGSARAGLFDL-DGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEG---AGVDPEQVKGIGF----DATc 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 98 --VVWDKfTGEPL---------YNAVVWLDLRTQSTVESLNKkipgnsnfvkskTGLPLSTYFSAV--------KLRWML 158
Cdd:cd07782 80 slVVLDA-EGKPVsvspsgddeRNVILWMDHRAVEEAERINA------------TGHEVLKYVGGKispemeppKLLWLK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 159 DNLRPiqkavEEDRA--LFGTIDsWLIWCMTGGVNGGIhCTDVtnASRTMLFNIHSLE-WDKELCKffEIPMSILpnvrs 235
Cdd:cd07782 147 ENLPE-----TWAKAghFFDLPD-FLTWKATGSLTRSL-CSLV--CKWTYLAHEGSEGgWDDDFFK--EIGLEDL----- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 236 SSEIYGQMTSGALE-GVPISGCLGDQSAAlvgQMCFQEGQAKNT-----Y----GT-GCFLLCNTGQKCVFSEHglLTTV 304
Cdd:cd07782 211 VEDNFAKIGSVVLPpGEPVGGGLTAEAAK---ELGLPEGTPVGVslidaHagglGTlGADVGGLPCEADPLTRR--LALI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 305 A------YKLGKNK---------------PAFYALEGSVAIAGAVIRWLRDN----FELITSSGE------------VED 347
Cdd:cd07782 286 CgtsschMAVSPEPvfvpgvwgpyysamlPGLWLNEGGQSATGALLDHIIEThpayPELKEEAKAagksiyeylnerLEQ 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 348 LAREVGTAYGC-----YFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIA---FAALEAVCFQTREIVDAMNRdCGIPL 419
Cdd:cd07782 366 LAEEKGLPLAYltrdlHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLAllyLATLQALAYGTRHIIEAMNA-AGHKI 444
|
490 500
....*....|....*....|....*...
gi 51854223 420 SHLRVDGRMTNNKILMQLQADILHIPVV 447
Cdd:cd07782 445 DTIFMCGGLSKNPLFVQLHADVTGCPVV 472
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
19-458 |
5.08e-13 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 71.30 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 19 GTNSTRFLVFNPKTAELVGSHQVELTQ----EY--PKEGWVEEDPKEILQSVYECIaktCEKLTEANIDTSKIKAIGVSN 92
Cdd:COG1069 10 GTDSVRAVVVDAADGEELASAVHPYPRwvigLYlpPPPDQARQHPLDYLEALEAAV---REALAQAGVDPADVVGIGVDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 93 QRETTVVWDK----------FTGEPLYNAVVWLDLRTQSTVESLNKkipgnsnfVKSKTGLPLSTY---------FSAvK 153
Cdd:COG1069 87 TGCTPVPVDAdgtplallpeFAENPHAMVILWKDHTAQEEAERINE--------LAKARGEDYLRYvggiissewFWP-K 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 154 LRWMLdnlrpiqkavEEDRALFGTIDS------WLIWCMTGGVNGGIhCTdvtnASRTMLFNIHSLEW-DKElckFFEip 226
Cdd:COG1069 158 ILHLL----------REDPEVYEAADSfvelcdWITWQLTGSLKRSR-CT----AGHKALWHAHEGGYpSEE---FFA-- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 227 mSILPNV-----RSSSEIY------GQMTS------GALEGVPISGCLGDQSAALVGQMCFQEGQ-AKNtYGT-GCFLLC 287
Cdd:COG1069 218 -ALDPLLdgladRLGTEIYplgepaGTLTAewaarlGLPPGTAVAVGAIDAHAGAVGAGGVEPGTlVKV-MGTsTCHMLV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 288 NTGQKC-------VFSehGLLttvayklgknkPAFYALEGSVAIAGAVIRWLRDNfelITSSGEVEDLAREVG------- 353
Cdd:COG1069 296 SPEERFvpgicgqVDG--SIV-----------PGMWGYEAGQSAVGDIFAWFVRL---LVPPLEYEKEAEERGislhpll 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 354 ---------TAYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREIVDAMNrDCGIPLSHLRV 424
Cdd:COG1069 360 teeaaklppGESGLHALDWFNGNRSPLADQRLKGVILGLTLGTDAEDIYRALVEATAFGTRAIIERFE-EEGVPIDEIIA 438
|
490 500 510
....*....|....*....|....*....|....*..
gi 51854223 425 -DGRMTNNKILMQLQADILHIP--VVKSvmPETTALG 458
Cdd:COG1069 439 cGGIATKNPLVMQIYADVTGRPikVAAS--EQACALG 473
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
15-258 |
2.90e-08 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 56.17 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 15 AVVQGTNSTRFLVFNPKTAELVGSHQVELTQEYPK-EGWVEEDPKEILQSVYECIAktcEKLTEANIDTSKIKAIGVSNQ 93
Cdd:PRK10939 7 ALDAGTGSIRAVIFDLNGNQIAVGQAEWRHLAVPDvPGSMEFDLEKNWQLACQCIR---QALQKAGIPASDIAAVSATSM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 94 RETTVVWDKfTGEPLYnAVVWLDLRTQSTVESLNKKIPGNSNFVKSKTGLPLStyFSAV-KLRWmLDNLRPiqkAVEEDR 172
Cdd:PRK10939 84 REGIVLYDR-NGTEIW-ACANVDARASREVSELKELHNNFEEEVYRCSGQTLA--LGALpRLLW-LAHHRP---DIYRQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 173 ALFGTIDSWLIWCMTGGVnggihCTDVTNASRTMLFNIHSLEWDKELCKFFEIPMSILPNVRSSSEIYGQMT------SG 246
Cdd:PRK10939 156 HTITMISDWIAYMLSGEL-----AVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTakaaaeTG 230
|
250 260
....*....|....*....|
gi 51854223 247 ALEGVPI--------SGCLG 258
Cdd:PRK10939 231 LRAGTPVvmgggdvqLGCLG 250
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
377-458 |
9.13e-04 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 42.14 E-value: 9.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51854223 377 RGIICGLTQFTNKCHIAFAALEAVCFQTREIVDAMnRDCGIPLSHLRVDGRM-TNNKILMQLQADILHIP--VVKSvmPE 453
Cdd:PRK04123 398 KGVITGLTLGTDAPDIYRALIEATAFGTRAIMECF-EDQGVPVEEVIAAGGIaRKNPVLMQIYADVLNRPiqVVAS--DQ 474
|
....*
gi 51854223 454 TTALG 458
Cdd:PRK04123 475 CPALG 479
|
|
| |
