|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
1-456 |
0e+00 |
|
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: 808.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 1 MWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLREiCWDKAGHFFDLPDFLSWKATGVTARSLCSLVC 80
Cdd:cd07782 105 LWMDHRAVEEAERINATGHEVLKYVGGKISPEMEPPKLLWLKENLPE-TWAKAGHFFDLPDFLTWKATGSLTRSLCSLVC 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 81 KWTYSA----EKGWDDSFWKMIGLEDFVADNYSKIGNQVLPPGASLGNGLTPEAARDLGLLPGIAVAASLIDAHAGGLGV 156
Cdd:cd07782 184 KWTYLAhegsEGGWDDDFFKEIGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAKELGLPEGTPVGVSLIDAHAGGLGT 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 157 IGADVrgHGLICEGQPVTSRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAF 236
Cdd:cd07782 264 LGADV--GGLPCEADPLTRRLALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGLWLNEGGQSATGALLDHIIETHPAY 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 237 PELQVKATARCQSIYAYLNSHLDLIKKAQ--PVGFLTVDLHVWPDFHGNRSPLADLTLKGMrttgylyipalaalhspss 314
Cdd:cd07782 342 PELKEEAKAAGKSIYEYLNERLEQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADPTLRGM------------------- 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 315 llspqVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEV 394
Cdd:cd07782 403 -----ISGLTLDTSLDDLALLYLATLQALAYGTRHIIEAMNAAGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEP 477
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034559822 395 ESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKLVEHQKEY 456
Cdd:cd07782 478 EAVLLGAAILGAVASGDFPSLWDAMAAMSGPGKVVEPNEELKKYHDRKYEVFLKMYEDQREY 539
|
|
| 5C_CHO_kinase |
TIGR01315 |
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ... |
1-456 |
0e+00 |
|
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of carbohydrate kinases. This subfamily is closely related to a set of ribulose kinases, and many members are designated ribitol kinase. However, the member from Klebsiella pneumoniae, from a ribitol catabolism operon, accepts D-ribulose and to a lesser extent D-arabinitol and ribitol (and JW Lengeler, personal communication); its annotation in GenBank as ribitol kinase is imprecise and may have affected public annotation of related proteins.
Pssm-ID: 273552 [Multi-domain] Cd Length: 541 Bit Score: 537.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 1 MWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVC 80
Cdd:TIGR01315 105 LWMDHRALAEAEKINATNHNLLRYVGGKMSVEMEIPKVLWLKNNMPPE-LFARCKFFDLTDFLTWRATGKEIRSFCSVVC 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 81 KWTY----SAEKGWDDSFWKMIGLEDFVADNYSKIGNQVLPPGASLGNGLTPEAARDLGLLPGIAVAASLIDAHAGGLGV 156
Cdd:TIGR01315 184 KWGFvpvdGSNKGWQEDFYETIGLGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQELGLPAGTAVGSGLIDAHAGWIGT 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 157 IGADVRGHGLICEGQpvtSRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAF 236
Cdd:TIGR01315 264 VGAKVAENGDVSQAF---TRLAAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGYWLAEGGQSAAGELMDHMLETHVAY 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 237 PELQVKATARCQSIYAYLNSHLdLIKKAQP----VGFLTVDLHVWPDFHGNRSPLADLTLKGMrttgylyipalaalhsp 312
Cdd:TIGR01315 341 DETVKEAEAAGKNIYDYLNEHL-KEMAAKTnapsISYLVRHFHVYPDLWGNRSPIADPNMRGV----------------- 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 313 ssllspqVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQ 392
Cdd:TIGR01315 403 -------IIGLSMDRSKDGLALLYYATMEFIAYGTRQIVEAMNTAGHTIKSIFMSGGQCQNPLLMQLIADACDMPVLIPY 475
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034559822 393 EVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQ-DKKYYDKKYQVFLKLVEHQKEY 456
Cdd:TIGR01315 476 VNEAVLHGAAMLGAKAAGTTESLWDAMDRMSKPGKTVWPRGDpAKKLHDRKYEIFLQLARTQQEY 540
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
1-456 |
1.46e-167 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 482.31 E-value: 1.46e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 1 MWLDHRAVSQVNRINE----TKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLC 76
Cdd:COG1069 117 LWKDHTAQEEAERINElakaRGEDYLRYVGGIISSEWFWPKILHLLREDPEV-YEAADSFVELCDWITWQLTGSLKRSRC 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 77 SLVCKWTYSA-EKGW-DDSFWKMIGLE-DFVADnysKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGG 153
Cdd:COG1069 196 TAGHKALWHAhEGGYpSEEFFAALDPLlDGLAD---RLGTEIYPLGEPAGT-LTAEWAARLGLPPGTAVAVGAIDAHAGA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 154 LGVIGadvrghglICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGH 233
Cdd:COG1069 272 VGAGG--------VEPGT-----LVKVMGTSTCHMLVSPEERFVPGICGQVDGSIVPGMWGYEAGQSAVGDIFAWFVRLL 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 234 AAFPELQVKATARCQSIYAYLNshldliKKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMrttgylyipalaalhsps 313
Cdd:COG1069 339 VPPLEYEKEAEERGISLHPLLT------EEAAKLPPGESGLHALDWFNGNRSPLADQRLKGV------------------ 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 314 sllspqVTGLKLSQDLDDlaiLYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHADITGMPVVLSQ 392
Cdd:COG1069 395 ------ILGLTLGTDAED---IYRALVEATAFGTRAIIERFEEEGVPIDEIIACGGIAtKNPLVMQIYADVTGRPIKVAA 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034559822 393 EVESVLVGAAVLGACASGDFASVQEAMAKMSKV-GKVVFPRLQDKKYYDKKYQVFLKLVEHQKEY 456
Cdd:COG1069 466 SEQACALGAAMFAAVAAGAYPDVEEAMAAMGSGfDKVYTPDPENVAVYDALYAEYLQLHDYFGRG 530
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
1-446 |
4.23e-121 |
|
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: 363.48 E-value: 4.23e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 1 MWLDHRAVSQVNRINETKHSVLQ-YVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLV 79
Cdd:cd07768 107 FWMDHSAVNEAQWINMQCPQQLLdYLGGKISPEMGVPKLKYFLDEYSHL-RDKHFHIFDLHDYIAYELTRLYEWNICGLL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 80 CKWTYSA-EKGWDDSFWKMIGLEDfVADNYSKIGNQVLPPGASLGNGLtPEAARDLGLLPGIAVAASLIDAHAGGLGVIG 158
Cdd:cd07768 186 GKENLDGeESGWSSSFFKNIDPRL-EHLTTTKNLPSNVPIGTTSGVAL-PEMAEKMGLHPGTAVVVSCIDAHASWFAVAS 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 159 ADVRGhglicegqpvtsRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPE 238
Cdd:cd07768 264 PHLET------------SLFMIAGTSSCHMYGTTISDRIPGVWGPFDTIIDPDYSVYEAGQSATGKLIEHLFESHPCARK 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 239 LqVKATARCQSIYAYLNshlDLIKKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllsp 318
Cdd:cd07768 332 F-DEALKKGADIYQVLE---QTIRQIEKNNGLSIHILTLDMFFGNRSEFADPRLKGS----------------------- 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 319 qVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVL 398
Cdd:cd07768 385 -FIGESLDTSMLNLTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGI 463
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1034559822 399 VGAAVLGACASGDFA---SVQEAMAKMSKVGKVVFPRLQD-KKYYDKKYQVF 446
Cdd:cd07768 464 LGAAVLAKVAAGKKQladSITEADISNDRKSETFEPLAYRlGADYILLYKLL 515
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
1-449 |
5.77e-116 |
|
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: 349.53 E-value: 5.77e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 1 MWLDHRAVSQVNRINETKHSV----LQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLC 76
Cdd:cd07781 100 LWMDHRAQEEAAEINETAHPAleyyLAYYGGVYSSEWMWPKALWLKRNAPEV-YDAAYTIVEACDWINARLTGRWVRSRC 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 77 SLVCKWTYSAEKG-WDDSFWKMIGLEDfvADNYSKIGNQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLG 155
Cdd:cd07781 179 AAGHKWMYNEWGGgPPREFLAALDPGL--LKLREKLPGEVVPVGEPAG-TLTAEAAERLGLPAGIPVAQGGIDAHMGAIG 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 156 VigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIdhmvqghAA 235
Cdd:cd07781 256 A--------GVVEPGT-----LALIMGTSTCHLMVSPKPVDIPGICGPVPDAVVPGLYGLEAGQSAVGDIF-------AW 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 236 FPELQVKATA-RCQSIYAYLNshlDLIKKAQPV--GFLTVDlhvWpdFHGNRSPLADLTLKGMrttgylyipalaalhsp 312
Cdd:cd07781 316 FVRLFVPPAEeRGDSIYALLS---EEAAKLPPGesGLVALD---W--FNGNRTPLVDPRLRGA----------------- 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 313 ssllspqVTGLKLSQDLddlAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHADITGMPVVLS 391
Cdd:cd07781 371 -------IVGLTLGTTP---AHIYRALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVP 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034559822 392 QEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKL 449
Cdd:cd07781 441 KSDQAPALGAAILAAVAAGVYADIEEAADAMVRVDRVYEPDPENHAVYEELYALYKEL 498
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
2-460 |
1.67e-69 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 230.50 E-value: 1.67e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 2 WLDHRAVSQVNRINETKHS-----VLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTA---- 72
Cdd:PRK04123 119 WKDHTAQEEAEEINRLAHErgeadLSRYIGGIYSSEWFWAKILHVLREDPAV-YEAAASWVEACDWVVALLTGTTDpqdi 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 73 -RSLCSLVCKWTYSAEKG--WDDSFWKMI--GLEDFVADnysKIGNQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLI 147
Cdd:PRK04123 198 vRSRCAAGHKALWHESWGglPSADFFDALdpLLARGLRD---KLFTETWTAGEPAG-TLTAEWAQRLGLPEGVAVSVGAF 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 148 DAHAGglgVIGADVRGHGLicegqpvtsrLAVIcGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLID 227
Cdd:PRK04123 274 DAHMG---AVGAGAEPGTL----------VKVM-GTSTCDILLADKQRAVPGICGQVDGSIVPGLIGYEAGQSAVGDIFA 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 228 HMVQgHAAFPELQVKATARCQSIYAYLNshldliKKA--QPVG---FLTVDlhvWpdFHGNRSPLADLTLKGMrttgyly 302
Cdd:PRK04123 340 WFAR-LLVPPEYKDEAEARGKQLLELLT------EAAakQPPGehgLVALD---W--FNGRRTPLADQRLKGV------- 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 303 ipalaalhspssllspqVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHA 381
Cdd:PRK04123 401 -----------------ITGLTLGTDAPDI---YRALIEATAFGTRAIMECFEDQGVPVEEVIAAGGIArKNPVLMQIYA 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 382 DITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKM-SKVGKVVFPRLQDKKYYDKKYQVFLKLVE-HQKEYLAI 459
Cdd:PRK04123 461 DVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEAQQAMaSPVEKTYQPDPENVARYEQLYQEYKQLHDyFGRGGNAV 540
|
.
gi 1034559822 460 M 460
Cdd:PRK04123 541 M 541
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
1-455 |
1.36e-65 |
|
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: 218.93 E-value: 1.36e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 1 MWLDHRAVSQVNRINET--KHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATG--VTARSLC 76
Cdd:COG1070 98 LWNDTRAAAEAAELREElgEEALYEITGNPLHPGFTAPKLLWLKENEPEI-FARIAKVLLPKDYLRYRLTGefVTDYSDA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 77 SlvckWT--YSAEKG-WDDSFWKMIGL-EDFVAdnyskignQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAG 152
Cdd:COG1070 177 S----GTglLDVRTRdWSDELLEALGIdRELLP--------ELVPPGEVAG-TLTAEAAAETGLPAGTPVVAGAGDNAAA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 153 GLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQg 232
Cdd:COG1070 244 ALGA--------GAVEPGD-----AAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAVPGRWLPMGATNNGGSALRWFRD- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 233 haafpelqvKATARCQSIYAYLNshlDLIKKAqPVG-----FLtvdlhvwPDFHGNRSPLADLTLKGMrttgylyipala 307
Cdd:COG1070 310 ---------LFADGELDDYEELN---ALAAEV-PPGadgllFL-------PYLSGERTPHWDPNARGA------------ 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 308 alhspssllspqVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMP 387
Cdd:COG1070 358 ------------FFGLTLSHTRAHL---ARAVLEGVAFALRDGLEALEEAGVKIDRIRATGGGARSPLWRQILADVLGRP 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034559822 388 VVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKLVEHQKE 455
Cdd:COG1070 423 VEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMVRVGETIEPDPENVAAYDELYERYRELYPALKP 490
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
177-408 |
2.97e-55 |
|
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: 182.52 E-value: 2.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 177 LAVICGTSSCHMGISKDP-IFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQvkATARCQSIYAYLN 255
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPvLSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELR--DAGNVESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 256 SHLDLikkaqpvgfLTVDLHVWPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLddlAIL 335
Cdd:pfam02782 79 LAAVA---------PAGGLLFYPDFSGNRAPGADPGARGS------------------------ITGLSSPTTL---AHL 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034559822 336 YLATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACA 408
Cdd:pfam02782 123 YRAILESLALQLRQILEALTKqEGHPIDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
1-409 |
2.27e-52 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466797 [Multi-domain] Cd Length: 544 Bit Score: 184.92 E-value: 2.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 1 MWLDHRAVSQVNRINE-TKHSVLQYVGGVMSVEMQAPKLLWLKENLREICWDKAgHFFDLPDFLSWKatgvtarsLCSLV 79
Cdd:cd07778 111 FWMDHRASEETQWLNNiLPDDILDYLGGGFIPEMAIPKLKYLIDLIKEDTFKKL-EVFDLHDWISYM--------LATNL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 80 CKW--TYSAE------------KGWDDSFWKMIGLEDFVAD--NYSKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVA 143
Cdd:cd07778 182 GHSniVPVNAppsigigidgslKGWSKDFYSKLKISTKVCNvgNTFKEAPPLPYAGIPIGK-VNVILASYLGIDKSTVVG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 144 ASLIDAHAGGLGVIgadvrghgliCEGQPVTSRLAVICGTSSCHMGISKDPI--FVPGVWGPyFSAMVPGFWLNEGGQSV 221
Cdd:cd07778 261 HGCIDCYAGWFSTF----------AAAKTLDTTLFMVAGTSTCFLYATSSSQvgPIPGIWGP-FDQLLKNYSVYEGGQSA 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 222 TGKLIDHMVQGHAAFPELQVKATarcqSIYAYLNSHLDLI--KKAQPVGFLTVDLHVWPDFHGNRSPLADltlkgmrttg 299
Cdd:cd07778 330 TGKLIEKLFNSHPAIIELLKSDA----NFFETVEEKIDKYerLLGQSIHYLTRHMFFYGDYLGNRTPYND---------- 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 300 ylyipalaalhspssllsPQVTG--LKLSQD--LDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPL 375
Cdd:cd07778 396 ------------------PNMSGsfIGESTDssLTDLVLKYILILEFLAFQTKLIIDNFQKEKIIIQKVVISGSQAKNAR 457
|
410 420 430
....*....|....*....|....*....|....*..
gi 1034559822 376 FVQMHADITGMPVV---LSQEVESVLVGAAVLGACAS 409
Cdd:cd07778 458 LLQLLSTVLSKIHIivpLSDSKYAVVKGAALLGKAAF 494
|
|
| L-ribulokinase |
TIGR01234 |
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely ... |
1-457 |
6.95e-52 |
|
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely related protein subfamily outside the scope of this model includes ribitol kinase from E. coli. [Energy metabolism, Sugars]
Pssm-ID: 130301 [Multi-domain] Cd Length: 536 Bit Score: 183.20 E-value: 6.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 1 MWLDHRAVSQVNRINETKHS----VLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLC 76
Cdd:TIGR01234 121 LWKHHAAQEEADRINRLAHApgevDLSRYGGIISSEWFWAKILQITEEDPAI-YQAADRWIELADWIVAQLSGDIRRGRC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 77 SLVCKWTYSAEKGW-DDSFWKMI--GLEDFVADNYSK-IGNQVLPPGAslgngLTPEAARDLGLLPGIAVAASLIDAHag 152
Cdd:TIGR01234 200 TAGYKALWHESWGYpSASFFDELnpILNRHLPDKLFTdIWTAGEPAGT-----LTPEWAQRTGLPEGVVVAVGNFDAH-- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 153 gLGVIGADVrghgliceGQPvtSRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQg 232
Cdd:TIGR01234 273 -VGAVAAGI--------AQP--GALVKIMGTSTCHVLIGDKQRAVPGMCGVVDGGIVPGFIGYEAGQSAVGDIFAWFGK- 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 233 HAAFPELQVKATARCQSiyayLNSHLDLIKKAQPV---GFLTVDlhvWpdFHGNRSPLADLTLKGMrttgylyipalaal 309
Cdd:TIGR01234 341 VCVPPELKTEANASQKQ----LHEALSEAAAKQPSgehGLVALD---W--FNGNRSPLVDQRLKGV-------------- 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 310 hspssllspqVTGLKLSQDLDDlaiLYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHADITGMPV 388
Cdd:TIGR01234 398 ----------ITGLTLATDAPL---LYRALIEATAFGTRMIMETFTDSGVPVEELMAAGGIArKNPVIMQIYADVTNRPL 464
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 389 VLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVF-PRLQDKKYYDKKYQVFLKLVEHQKEYL 457
Cdd:TIGR01234 465 QIVASDQAPALGAAIFAAVAAGVYADIPSAQAKMGSAVEKTLtPCSENAQRYEQLYARYQELAMSFGQYN 534
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
1-447 |
7.43e-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: 168.47 E-value: 7.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 1 MWLDHRAVSQVNRINET---KHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCS 77
Cdd:cd07805 97 IWSDTRAAEEAEEIAGGlggIEGYRLGGGNPPSGKDPLAKILWLKENEPEI-YAKTHKFLDAKDYLNFRLTGRAATDPST 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 78 LVCKWTYSAEKG-WDDSFWKMIGLEDfvadnySKIgNQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGV 156
Cdd:cd07805 176 ASTTGLMDLRKRrWSEELLRAAGIDP------DKL-PELVPSTEVVG-ELTPEAAAELGLPAGTPVVGGGGDAAAAALGA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 157 iGADVRGHGLICegqpvtsrlaviCGTSS---CHmgiSKDPIFVPGvwGPYFS--AMVPGFWLNEGGQSVTGKLIDHMVQ 231
Cdd:cd07805 248 -GAVEEGDAHIY------------LGTSGwvaAH---VPKPKTDPD--HGIFTlaSADPGRYLLAAEQETAGGALEWARD 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 232 gHAAFPELQVKatarcqSIYAYLNshlDLIKKAQP----VGFLtvdlhvwPDFHGNRSPLADLTLKGMrttgylYIpala 307
Cdd:cd07805 310 -NLGGDEDLGA------DDYELLD---ELAAEAPPgsngLLFL-------PWLNGERSPVEDPNARGA------FI---- 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 308 alhspssllspqvtGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMP 387
Cdd:cd07805 363 --------------GLSLEHTRADLA---RAVLEGVAFNLRWLLEALEKLTRKIDELRLVGGGARSDLWCQILADVLGRP 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034559822 388 V-VLSQEVESVLVGAAVLGACASGDFASVQEAmAKMSKVGKVVFPRLQDKKYYDKKYQVFL 447
Cdd:cd07805 426 VeVPENPQEAGALGAALLAAVGLGLLKSFDEA-KALVKVEKVFEPDPENRARYDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
48-439 |
1.96e-46 |
|
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: 166.15 E-value: 1.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 48 ICW-DK-AGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEdfvADNYSKIgnqvLPPGASLGN 124
Cdd:cd07779 96 ISWqDKrTAKFLTVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRdWSDDLLDAFGID---RDKLPEL----VPPGTVIGT 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 125 gLTPEAARDLGLLPGIAVAASlidAHAGGLGVIGADVRGHGLICegqpvtsrlaVICGTSSCHMGISKDPIFVPGVWGPY 204
Cdd:cd07779 169 -LTKEAAEETGLPEGTPVVAG---GGDQQCAALGAGVLEPGTAS----------LSLGTAAVVIAVSDKPVEDPERRIPC 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 205 FSAMVPGFWLNEGGQSVTGKLIDHMVQghaAFPELQVKATARCQSIYAYLNSHLDLIkkaqPVGFLtvDLHVWPDFHGNR 284
Cdd:cd07779 235 NPSAVPGKWVLEGSINTGGSAVRWFRD---EFGQDEVAEKELGVSPYELLNEEAAKS----PPGSD--GLLFLPYLAGAG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 285 SPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTL 364
Cdd:cd07779 306 TPYWNPEARGA------------------------FIGLTLSHTRAHL---ARAILEGIAFELRDNLEAMEKAGVPIEEI 358
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034559822 365 FLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYY 439
Cdd:cd07779 359 RVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAMVRVTDTFEPDPENVAIY 433
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
1-449 |
2.62e-44 |
|
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: 161.55 E-value: 2.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 1 MWLDHRAVSQVNRINET-KHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFdLP-DFLSWKATGVTAR----- 73
Cdd:cd07808 97 LWNDQRSAAECEELEARlGDEILIITGNPPLPGFTLPKLLWLKENEPEI-FARIRKIL-LPkDYLRYRLTGELATdpsda 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 74 --SLCslvckwtYSAEKG-WDDSFWKMIGLEdfvadnyskigNQVLPP---GASLGNGLTPEAARDLGLLPGIAVAASLI 147
Cdd:cd07808 175 sgTLL-------FDVEKReWSEELLEALGLD-----------PSILPPiveSTEIVGTLTPEAAEELGLPEGTPVVAGAG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 148 DAHAGGLGVigadvrghGLICEGQPV----TSrlAVICGTSSCHMGISKDPIF-----VPGVW---GPYFSAmvpGF--- 212
Cdd:cd07808 237 DNAAAALGA--------GVVEPGDALislgTS--GVVFAPTDKPVPDPKGRLHtfphaVPGKWyamGVTLSA---GLslr 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 213 WLNE--GGQSVTGKLIDHMVQGHAAfpelqvkatarcqsiyaylnshldlikKAQPVGFLtvdlhvwPDFHGNRSPLADL 290
Cdd:cd07808 304 WLRDlfGPDRESFDELDAEAAKVPP---------------------------GSEGLLFL-------PYLSGERTPYWDP 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 291 TLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGL 370
Cdd:cd07808 350 NARGS------------------------FFGLSLSHTRAHLA---RAVLEGVAFSLRDSLEVLKELGIKVKEIRLIGGG 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034559822 371 SKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKL 449
Cdd:cd07808 403 AKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACIKIEKTIEPDPERHEAYDELYARYREL 481
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
1-410 |
1.04e-35 |
|
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: 137.33 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 1 MWLDHRAVSQVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLcSL 78
Cdd:cd07773 95 VWFDPRGKEEAEELAEriGAEELYRITGLPPSPMYSLAKLLWLREHEPEI-FAKAAKWLSVADYIAYRLTGEPVTDY-SL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 79 VCKWTY--SAEKGWDDSFWKMIGLEdfvADNYSkignQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGV 156
Cdd:cd07773 173 ASRTMLfdIRKRTWSEELLEAAGID---ASLLP----ELVPSGTVIGT-VTPEAAEELGLPAGTPVVVGGHDHLCAALGA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 157 igadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFS---AMVPGFWLNEGGQSvTGKLIDHMVQGH 233
Cdd:cd07773 245 --------GVIEPGD-----VLDSTGTAEALLAVVDEPPLDEMLAEGGLSyghHVPGGYYYLAGSLP-GGALLEWFRDLF 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 234 AAFPELQVKATARCQSIYAylnshldlikKAQPVGFLtvdlhvwPDFHGNRSPLADLTLKGMrttgylyipalaalhsps 313
Cdd:cd07773 311 GGDESDLAAADELAEAAPP----------GPTGLLFL-------PHLSGSGTPDFDPDARGA------------------ 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 314 sllspqVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQE 393
Cdd:cd07773 356 ------FLGLTLGTTRADL---LRAILEGLAFELRLNLEALEKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEV 426
|
410
....*....|....*..
gi 1034559822 394 VESVLVGAAVLGACASG 410
Cdd:cd07773 427 PEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
1-410 |
1.20e-35 |
|
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: 137.27 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 1 MWLDHRAVSQVNRINETKHS--VLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATG--VTARSLC 76
Cdd:cd07804 97 LYGDRRATEEIEWLNENIGEdrIFEITGNPLDSQSVGPKLLWIKRNEPEV-FKKTRKFLGAYDYIVYKLTGeyVIDYSSA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 77 SLvckwtYS-----AEKGWDDSFWKMIGLEdfvadnySKIGNQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHA 151
Cdd:cd07804 176 GN-----EGglfdiRKRTWDEELLEALGID-------PDLLPELVPSTEIVG-EVTKEAAEETGLAEGTPVVAGTVDAAA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 152 GGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFSamVPGFWLNEGGQSVTGKLIDHMVQ 231
Cdd:cd07804 243 SALSA--------GVVEPGD-----LLLMLGTAGDIGVVTDKLPTDPRLWLDYHD--IPGTYVLNGGMATSGSLLRWFRD 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 232 GHAafPELQVKATARCQSIYAYLNshldliKKAQ--PVGfltVD-LHVWPDFHGNRSPLADLTLKGMrttgylyipalaa 308
Cdd:cd07804 308 EFA--GEEVEAEKSGGDSAYDLLD------EEAEkiPPG---SDgLIVLPYFMGERTPIWDPDARGV------------- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 309 lhspssllspqVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPV 388
Cdd:cd07804 364 -----------IFGLTLSHTRAHL---YRALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQ 429
|
410 420
....*....|....*....|..
gi 1034559822 389 VLSQEVESVLVGAAVLGACASG 410
Cdd:cd07804 430 EYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
1-406 |
1.28e-34 |
|
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: 133.89 E-value: 1.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 1 MWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVC 80
Cdd:cd07783 95 MYNDARAVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEV-LAKTAKFLHQADWLAGRLTGDRGVTDYNNAL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 81 KWTYSAEKG-WDDSFWKMIGLEdfvadnySKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGViga 159
Cdd:cd07783 174 KLGYDPETGrWPSWLLALLGIP-------PDLLPRVVAPGTVIGT-LTAEAAEELGLPAGTPVVAGTTDSIAAFLAS--- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 160 dvrghGLICEGQPVTSrlaviCGTSSCHMGISKDPIFVPGVwGPYFSAMVPGFWLNEGGQSVTGKLIDHmvqghaAFPEL 239
Cdd:cd07783 243 -----GAVRPGDAVTS-----LGTTLVLKLLSDKRVPDPGG-GVYSHRHGDGYWLVGGASNTGGAVLRW------FFSDD 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 240 QVKAtarcqsiyaylnshldLIKKAQPVGflTVDLHVWP-DFHGNRSPLADltlkgmrttgylyipalaalhspssllsP 318
Cdd:cd07783 306 ELAE----------------LSAQADPPG--PSGLIYYPlPLRGERFPFWD----------------------------P 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 319 QVTGLKLSQDLDDlAILYLATVQAIALGTRFIIEAMEAAGHS-ISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESV 397
Cdd:cd07783 340 DARGFLLPRPHDR-AEFLRALLEGIAFIERLGYERLEELGAPpVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEAA 418
|
....*....
gi 1034559822 398 LvGAAVLGA 406
Cdd:cd07783 419 L-GAALLAA 426
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
1-410 |
1.79e-33 |
|
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: 131.13 E-value: 1.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 1 MWLDHRAVSQVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVtarslcsL 78
Cdd:cd07802 97 LSNDSRAADIVDRWEEdgTLEKVYPLTGQPLWPGQPVALLRWLKENEPER-YDRIRTVLFCKDWIRYRLTGE-------I 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 79 VCKWT-YSA------EKGWDDSFWKMIGLEDFvadnYSKIGnQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHA 151
Cdd:cd07802 169 STDYTdAGSslldldTGEYDDELLDLLGIEEL----KDKLP-PLVPSTEIAG-RVTAEAAALTGLPEGTPVAAGAFDVVA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 152 GGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGpYFSAMVPGFWLNEGGQSVTGKLIDHMVQ 231
Cdd:cd07802 243 SALGA--------GAVDEGQ-----LCVILGTWSINEVVTDEPVVPDSVGS-NSLHADPGLYLIVEASPTSASNLDWFLD 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 232 ghaafpELQVKATARCQSIYAYLNshlDLIKKAQPVgfltvdlhvwpdfhgnrspladltlkgmrTTGYLYIPALAAlhs 311
Cdd:cd07802 309 ------TLLGEEKEAGGSDYDELD---ELIAAVPPG-----------------------------SSGVIFLPYLYG--- 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 312 psSLLSPQVT----GLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEAAGHsISTLFLCGGLSKNPLFVQMHADITGMP 387
Cdd:cd07802 348 --SGANPNARggffGLTAWHTRAHLL---RAVYEGIAFSHRDHLERLLVARK-PETIRLTGGGARSPVWAQIFADVLGLP 421
|
410 420
....*....|....*....|...
gi 1034559822 388 VVLSQEVESVLVGAAVLGACASG 410
Cdd:cd07802 422 VEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
51-405 |
6.58e-33 |
|
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: 128.45 E-value: 6.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 51 DKAGHFFDLPDFLSWKATGVTA--RSLCSLVCKWTYsAEKGWDDSFWKMIGL-EDFVADnyskignqVLPPGASLGnGLT 127
Cdd:cd00366 100 DRRAKFLQPNDYIVFRLTGEFAidYSNASGTGLYDI-KTGDWSEELLDALGIpREKLPP--------IVESGEVVG-RVT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 128 PEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVtsrlaVICGTSSCHMGISKDPIFVPGVWGPYFSA 207
Cdd:cd00366 170 PEAAEETGLPAGTPVVAGGGDTAAAALGA--------GVVEPGDAV-----DSTGTSSVLSVCTDEPVPPDPRLLNRCHV 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 208 mVPGFWLNEGGQSVTGKLIDHMVQghaafpelqvkATARCQSIYAYLNSHLDLIKKAQP----VGFLtvdlhvwPDFHGN 283
Cdd:cd00366 237 -VPGLWLLEGAINTGGASLRWFRD-----------EFGEEEDSDAEYEGLDELAAEVPPgsdgLIFL-------PYLSGE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 284 RSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSIST 363
Cdd:cd00366 298 RSPIWDPAARGV------------------------FFGLTLSHTRAHL---IRAVLEGVAYALRDNLEILEELGVKIKE 350
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1034559822 364 LFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLG 405
Cdd:cd00366 351 IRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
2-450 |
1.45e-31 |
|
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: 126.13 E-value: 1.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 2 WLDHRAVSQVNRI--NETKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATG--VTARSLCS 77
Cdd:cd07770 96 WADTRAAEEAERLrkEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPEL-FAKAAKFVSIKEYLLYRLTGelVTDYSTAS 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 78 lvckWT---YSAEKGWDDSFWKMIGLEdfvADNYSKIgnqvLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDahaGGL 154
Cdd:cd07770 175 ----GTgllNIHTLDWDEEALELLGID---EEQLPEL----VDPTEVLP-GLKPEFAERLGLLAGTPVVLGASD---GAL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 155 GVIGAdvrghGLICEGqpvtsRLAVICGTSschmG----ISKDPIFVP--GVWgPYFSAmvPGFWL-----NEGGqSVTG 223
Cdd:cd07770 240 ANLGS-----GALDPG-----RAALTVGTS----GairvVSDRPVLDPpgRLW-CYRLD--ENRWLvggaiNNGG-NVLD 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 224 KLIDHMVQGHAAFPELQVKATArcqsiyAYLNSHlDLIkkaqpvgFLtvdlhvwPDFHGNRSPLADLTLKGMrttgylyi 303
Cdd:cd07770 302 WLRDTLLLSGDDYEELDKLAEA------VPPGSH-GLI-------FL-------PYLAGERAPGWNPDARGA-------- 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 304 palaalhspssllspqVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADI 383
Cdd:cd07770 353 ----------------FFGLTLNHTRADI---LRAVLEGVAFNLKSIYEALEELAGPVKEIRASGGFLRSPLWLQILADV 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034559822 384 TGMPVVLSQEVESVLVGAAVLGACASGDFASVQEamAKMSKVGKVVFPRLQDKKYYDKKYQVFLKLV 450
Cdd:cd07770 414 LGRPVLVPEEEEASALGAALLALEALGLISSLEA--DELVKIGKVVEPDPENHAIYAELYERFKKLY 478
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
4-410 |
3.68e-25 |
|
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: 107.31 E-value: 3.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 4 DHRAVSQVNRINETKHSVLQYVGGVMSVEMQAP-KLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVtarslcsLVCKW 82
Cdd:cd07798 101 DARGVEEAAEIDDEFGEEIYTTTGHWPTELFPAaRLLWFKENRPEI-FERIATVLSISDWIGYRLTGE-------LVSEP 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 83 TYSAEKG--------WDDSFWKMIGLEDfvadnysKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGL 154
Cdd:cd07798 173 SQASETQlfdikkreWSQELLEALGLPP-------EILPEIVPSGTVLGT-VSEEAARELGLPEGTPVVVGGADTQCALL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 155 GVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVP--GVW-GPYfsaMVPGFWLNEGGQSVTGKLIDHMVQ 231
Cdd:cd07798 245 GS--------GAIEPGD-----IGIVAGTTTPVQMVTDEPIIDPerRLWtGCH---LVPGKWVLESNAGVTGLNYQWLKE 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 232 GHAAFPELQvkatarcqsiYAYLNSHLDLIKKAQP--VGFLTvdlhvwpdfhgnrSPLADLTLKGMRTTGYLYipalaal 309
Cdd:cd07798 309 LLYGDPEDS----------YEVLEEEASEIPPGANgvLAFLG-------------PQIFDARLSGLKNGGFLF------- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 310 hspSSLLSPQVTGLKlsqdldDLAIlylATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPV 388
Cdd:cd07798 359 ---PTPLSASELTRG------DFAR---AILENIAFAIRANLEQLEEvSGREIPYIILCGGGSRSALLCQILADVLGKPV 426
|
410 420
....*....|....*....|..
gi 1034559822 389 VLSQEVESVLVGAAVLGACASG 410
Cdd:cd07798 427 LVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
1-410 |
2.66e-22 |
|
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: 98.78 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 1 MWLDHRAVSQVNRINET-KHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAgHFFDLP-DFLSWKATG--VTARSLC 76
Cdd:cd07809 98 LWCDTRTAPEAEELTEAlGGKKCLLVGLNIPARFTASKLLWLKENEPEH-YARI-AKILLPhDYLNWKLTGekVTGLGDA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 77 SLVckwtysaekGWDDSF-----WKMIGLEDFVADNYSKIGnQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHA 151
Cdd:cd07809 176 SGT---------FPIDPRtrdydAELLAAIDPSRDLRDLLP-EVLPAGEVAG-RLTPEGAEELGLPAGIPVAPGEGDNMT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 152 GGLGVigadvrghGLICEGQPVTSrlaviCGTSSCHMGISKDPIFVPgvwgpyfSAMVPGF--------WLNEG---GQS 220
Cdd:cd07809 245 GALGT--------GVVNPGTVAVS-----LGTSGTAYGVSDKPVSDP-------HGRVATFcdstggmlPLINTtncLTA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 221 VTGKLIDHMVQGHAAFPELQVKATARCQSI--YAYLNshldlikkaqpvgfltvdlhvwpdfhgnrspladltlkGMRTT 298
Cdd:cd07809 305 WTELFRELLGVSYEELDELAAQAPPGAGGLllLPFLN--------------------------------------GERTP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 299 GYlyipalaalhspssllsPQVTGLKLSQDLDD--LAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLF 376
Cdd:cd07809 347 NL-----------------PHGRASLVGLTLSNftRANLARAALEGATFGLRYGLDILRELGVEIDEIRLIGGGSKSPVW 409
|
410 420 430
....*....|....*....|....*....|....
gi 1034559822 377 VQMHADITGMPVVLSQEVESVLVGAAVLGACASG 410
Cdd:cd07809 410 RQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
4-444 |
1.58e-21 |
|
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466794 [Multi-domain] Cd Length: 492 Bit Score: 97.02 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 4 DHRAVSQVNRINETKHSVLQ--YVGGVMSVEMQA-PKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTAR--SLCSL 78
Cdd:cd07775 101 DARAAEEVSELKELYNTLEEevYRISGQTFALGAiPRLLWLKNNRPEI-YRKAAKITMLSDWIAYKLSGELAVepSNGST 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 79 VCKWTySAEKGWDDSFWKMIGLEDFvadnyskIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVig 158
Cdd:cd07775 180 TGLFD-LKTRDWDPEILEMAGLKAD-------ILPPVVESGTVIGK-VTKEAAEETGLKEGTPVVVGGGDVQLGCLGL-- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 159 advrghGLICEGQpvtsrlAVICGTSSCHMGI-SKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQghAAFP 237
Cdd:cd07775 249 ------GVVRPGQ------TAVLGGSFWQQEVnTAAPVTDPAMNIRVNCHVIPDMWQAEGISFFPGLVMRWFRD--AFCA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 238 ELQVKATARCQSIYAYLNshldliKKAQ--PVGfltvdlhvwpdFHGNRSPLADLtlkgMRTTGYlYIPAlaalhspssl 315
Cdd:cd07775 315 EEKEIAERLGIDAYDLLE------EMAKdvPPG-----------SYGIMPIFSDV----MNYKNW-RHAA---------- 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 316 lsPQVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAA-GHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEV 394
Cdd:cd07775 363 --PSFLNLDIDPEKCNKATFFRAIMENAAIVSAGNLERIAEFsGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVK 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1034559822 395 ESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQ 444
Cdd:cd07775 441 EATALGAAIAAGVGAGIYSSLEEAVESLVKWEREYLPNPENHEVYQDLYE 490
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
1-410 |
3.88e-18 |
|
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: 86.52 E-value: 3.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 1 MWLDHRAVSQVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLREICwDKAGHFFDLPDFLSWKATGVTA--RSLC 76
Cdd:cd24121 97 LWLDGRAADIVERWQAdgIAEAVFEITGTGLFPGSQAAQLAWLKENEPERL-ERARTALHCKDWLFYKLTGEIAtdPSDA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 77 SLVCkwtYSAEKG-WDDSFWKMIGLEDFVAdnyskignqVLPP-GASLGNG--LTPEAARDLGLLPGIAVAASLIDAHAG 152
Cdd:cd24121 176 SLTF---LDFRTRqYDDEVLDLLGLEELRH---------LLPPiRPGTEVIgpLTPEAAAATGLPAGTPVVLGPFDVVAT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 153 GLGViGADVRGHGLicegqpvtsrlaVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLneggqsvtgklidHMVQG 232
Cdd:cd24121 244 ALGS-GAIEPGDAC------------SILGTTGVHEVVVDEPDLEPEGVGYTICLGVPGRWL-------------RAMAN 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 233 HAAFPELQvkatarcqsiYAylnshLDLIKKAQPVGFLTVDLHVWPDFHG--NRSPLAdltlkgmrTTGYLYIPALaalh 310
Cdd:cd24121 298 MAGTPNLD----------WF-----LRELGEVLKEGAEPAGSDLFQDLEElaASSPPG--------AEGVLYHPYL---- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 311 SPSSLLSP--------QVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMeaaGHSISTLFLCGGLSKNPLFVQMHAD 382
Cdd:cd24121 351 SPAGERAPfvnpnaraQFTGLSLEHTRADLL---RAVYEGVALAMRDCYEHM---GEDPGELRLSGGGARSDTWCQILAD 424
|
410 420
....*....|....*....|....*...
gi 1034559822 383 ITGMPVVLSQEVESVLVGAAVLGACASG 410
Cdd:cd24121 425 ALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
338-451 |
1.46e-15 |
|
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: 78.66 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 338 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGdFASVQ 416
Cdd:cd07769 374 AALESIAYQTRDVLEAMEKdSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVG-FWKDL 452
|
90 100 110
....*....|....*....|....*....|....*
gi 1034559822 417 EAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 451
Cdd:cd07769 453 DELASLWQVDKRFEPSMDEEE-RERLYRGWKKAVE 486
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
338-451 |
1.82e-15 |
|
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: 78.33 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 338 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 416
Cdd:cd07792 384 AALEAVCFQTREILDAMNKdSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLD 463
|
90 100 110
....*....|....*....|....*....|....*
gi 1034559822 417 EAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 451
Cdd:cd07792 464 ELKSLNEGGRTVFEPQISEEE-RERRYKRWKKAVE 497
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
338-451 |
2.42e-15 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 78.18 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 338 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 416
Cdd:COG0554 377 AALESIAYQTRDVLDAMEAdSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLE 456
|
90 100 110
....*....|....*....|....*....|....*
gi 1034559822 417 EaMAKMSKVGKVVFPRLqDKKYYDKKYQVFLKLVE 451
Cdd:COG0554 457 E-LAALWKVDRRFEPQM-DEEERERLYAGWKKAVE 489
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
338-438 |
1.47e-14 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 75.78 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 338 ATVQAIALGTRFIIEAME-AAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 416
Cdd:PTZ00294 383 AALEAIALQTNDVIESMEkDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLE 462
|
90 100
....*....|....*....|..
gi 1034559822 417 EAMAKMSKVGKVVFPRLQDKKY 438
Cdd:PTZ00294 463 EVKKLIRRSNSTFSPQMSAEER 484
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
338-451 |
1.49e-14 |
|
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: 75.61 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 338 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 416
Cdd:cd07786 374 AALESIAYQTRDLLEAMEAdSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLD 453
|
90 100 110
....*....|....*....|....*....|....*
gi 1034559822 417 EAmAKMSKVGKVVFPRLqDKKYYDKKYQVFLKLVE 451
Cdd:cd07786 454 EL-AKLWQVDRRFEPSM-SEEEREALYAGWKKAVK 486
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
338-452 |
4.28e-12 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 67.93 E-value: 4.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 338 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 416
Cdd:PRK00047 380 ATLESIAYQTRDVLDAMQAdSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLD 459
|
90 100 110
....*....|....*....|....*....|....*.
gi 1034559822 417 EaMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVEH 452
Cdd:PRK00047 460 E-LKEQWKIDRRFEPQMDEEE-REKLYAGWKKAVKR 493
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
297-451 |
5.32e-11 |
|
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: 64.51 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 297 TTGYLYIPALAALHSP--SSLLSPQVTGLKLSQDLDDLAIlylATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKN 373
Cdd:cd07793 349 TNGVYFVPAFSGLQAPynDPTACAGFIGLTPSTTKAHLVR---AILESIAFRVKQLLETMEKeTSIKISSIRVDGGVSNN 425
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034559822 374 PLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVqEAMAKMSKVGKVVFPRlQDKKYYDKKYQVFLKLVE 451
Cdd:cd07793 426 DFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSK-EELKKLRKIEKIFEPK-MDNEKREELYKNWKKAVK 501
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
37-438 |
7.57e-09 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 57.73 E-value: 7.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 37 KLLWLKENLREIcWDKAGHFFDLPDFLSWKATGV--TARSLCSlVCKWTYSAEKGWDDSFWKMIGLEdfvadnyskigNQ 114
Cdd:PRK10331 137 KLVWLKENHPQL-LEQAHAWLFISSLINHRLTGEftTDITMAG-TSQMLDIQQRDFSPEILQATGLS-----------RR 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 115 VLPP----GASLGNgLTPEAARDLGLLPGIAVAASlidAHAGGLGVIGAdvrGHGLiceGQPV----------------- 173
Cdd:PRK10331 204 LFPRlveaGEQIGT-LQPSAAALLGLPVGIPVISA---GHDTQFALFGS---GAGQ---NQPVlssgtweilmvrsaqvd 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 174 TSRLAVICGtSSCHMGiSKDPIFVPGVWgpyfsamvpgfWLNEGGQSVTGKLI-------DHMVQGHAAFPelqvkatAR 246
Cdd:PRK10331 274 TSLLSQYAG-STCELD-SQSGLYNPGMQ-----------WLASGVLEWVRKLFwtaetpyQTMIEEARAIP-------PG 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 247 CQSIYayLNSHLDLIKKAQPVGfltVDLHvwpdfhgnrspladltlkgmRTTGYLYIPALAALhspssllspqvtGLKLS 326
Cdd:PRK10331 334 ADGVK--MQCDLLACQNAGWQG---VTLN--------------------TTRGHFYRAALEGL------------TAQLK 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 327 QDLDDLailylatvqaialgtrfiieamEAAGH-SISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLG 405
Cdd:PRK10331 377 RNLQVL----------------------EKIGHfKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFG 434
|
410 420 430
....*....|....*....|....*....|...
gi 1034559822 406 ACASGDFASVQEAMAKMSKVGKVVFPRLQDKKY 438
Cdd:PRK10331 435 WYGVGEFSSPEQARAQMKYQYRYFYPQTEPEFI 467
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
4-452 |
1.35e-08 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 56.94 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 4 DHRAVSQVNRINETkHSVLQYvgGVMSVEMQA------PKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTA----- 72
Cdd:PRK10939 104 DARASREVSELKEL-HNNFEE--EVYRCSGQTlalgalPRLLWLAHHRPDI-YRQAHTITMISDWIAYMLSGELAvdpsn 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 73 ---RSLCSLVckwtysaEKGWDDSFWKMIGLEDfvadnysKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDA 149
Cdd:PRK10939 180 agtTGLLDLV-------TRDWDPALLEMAGLRA-------DILPPVKETGTVLGH-VTAKAAAETGLRAGTPVVMGGGDV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 150 HAGGLGVigadvrghGLICEGQpvtsrLAVICGT------------SSCHMGISKDPifvpgvwgpyfsAMVPGFWLNEG 217
Cdd:PRK10939 245 QLGCLGL--------GVVRPGQ-----TAVLGGTfwqqvvnlpapvTDPNMNIRINP------------HVIPGMVQAES 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 218 GQSVTGkLIdhMVQGHAAF-PELQVKATARCQSIYAYLNshldliKKAQ--PVGfltvDLHVWPDFHGnrspladltlkG 294
Cdd:PRK10939 300 ISFFTG-LT--MRWFRDAFcAEEKLLAERLGIDAYSLLE------EMASrvPVG----SHGIIPIFSD-----------V 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 295 MRTtGYLYipalaalHSPSSLLSpqvtgLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKN 373
Cdd:PRK10939 356 MRF-KSWY-------HAAPSFIN-----LSIDPEKCNKATLFRALEENAAIVSACNLQQIAAfSGVFPSSLVFAGGGSKG 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 374 PLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKK-------YQVF 446
Cdd:PRK10939 423 KLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSLAETGERLVRWERTFEPNPENHELYQEAkekwqavYADQ 502
|
....*.
gi 1034559822 447 LKLVEH 452
Cdd:PRK10939 503 LGLVDH 508
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
343-418 |
3.01e-08 |
|
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: 55.61 E-value: 3.01e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034559822 343 IALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSqEVESVLVGAAVLGACASGDFASVQEA 418
Cdd:cd07771 378 LALKYAKTIEELEElTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAG-PVEATAIGNLLVQLIALGEIKSLEEG 453
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
1-449 |
6.68e-08 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 54.59 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 1 MWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLREICWDKAGHFfdLP-DFLSWKATGVTARSLCSLV 79
Cdd:PRK15027 95 LWNDGRCAQECALLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVL--LPkDYLRLRMTGEFASDMSDAA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 80 -CKWTYSAEKGWDDSfwkMIGLEDFVADNYSkignqVLPPGASLGNGLTPEAARDLGlLPGIAVAASLIDAHAGGLGVig 158
Cdd:PRK15027 173 gTMWLDVAKRDWSDV---MLQACHLSRDQMP-----ALYEGSEITGALLPEVAKAWG-MATVPVVAGGGDNAAGAVGV-- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 159 advrghGLICEGQPVTSrlaviCGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWlneggqsvtgKLIDHMVQGhAAFPE 238
Cdd:PRK15027 242 ------GMVDANQAMLS-----LGTSGVYFAVSEGFLSKPESAVHSFCHALPQRW----------HLMSVMLSA-ASCLD 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 239 LQVKATARcQSIYAYLNSHLDLIKKAQPVGFLtvdlhvwPDFHGNRSPLADLTLKGMrttgylyIPALAALHSPSSLLSP 318
Cdd:PRK15027 300 WAAKLTGL-SNVPALIAAAQQADESAEPVWFL-------PYLSGERTPHNNPQAKGV-------FFGLTHQHGPNELARA 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 319 QVTGLKLsqdlddlailylatvqAIALGtrfiIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQ--EVES 396
Cdd:PRK15027 365 VLEGVGY----------------ALADG----MDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTggDVGP 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1034559822 397 VLvGAAVLGACASGDFASVQEAMAKMSkVGKVVFPRLQDKKYYDKKYQVFLKL 449
Cdd:PRK15027 425 AL-GAARLAQIAANPEKSLIELLPQLP-LEQSHLPDAQRYAAYQPRRETFRRL 475
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
338-451 |
1.95e-07 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 53.16 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 338 ATVQAIALGTRFIIEAM------EAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGD 411
Cdd:PLN02295 384 AVLESMCFQVKDVLDAMrkdageEKSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGL 463
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1034559822 412 FASVQEAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 451
Cdd:PLN02295 464 WTEEEIFASEKWKNTTTFRPKLDEEE-RAKRYASWCKAVE 502
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
2-155 |
1.23e-06 |
|
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: 49.64 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 2 WLDHRAVSQVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVtarslcsLV 79
Cdd:pfam00370 98 WKDRRTAEIVENLKEegNNQKLYEITGLPIWPGFTLSKLRWIKENEPEV-FEKIHKFLTIHDYLRWRLTGV-------FV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 80 CKWTYSAEKG--------WDDSFWKMIGLEdfvadnyskigNQVLPP----GASLGNgLTPEAARDLGLLPGIAVAASLI 147
Cdd:pfam00370 170 TDHTNASRSMmfnihkldWDPELLAALGIP-----------RDHLPPlvesSEIYGE-LNPELAAMWGLDEGVPVVGGGG 237
|
....*...
gi 1034559822 148 DAHAGGLG 155
Cdd:pfam00370 238 DQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
38-404 |
3.73e-06 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466792 [Multi-domain] Cd Length: 424 Bit Score: 49.18 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 38 LLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVC--------KWTYS---AEKGWDDSFWKMigledfvad 106
Cdd:cd07772 129 LYWLKREKPEL-FARAKTILPLPQYWAWRLTGKAASEITSLGChtdlwdfeKNEYSslvKKEGWDKLFPPL--------- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 107 nyskignqvLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAgglgvigadvrghglicegqpvtSRLAvicgtssc 186
Cdd:cd07772 199 ---------RKAWEVLGP-LRPDLARRTGLPKDIPVGCGIHDSNA-----------------------ALLP-------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 187 HMGISKDPiFV---PGVWgpyFSAMVPGF-----WLNEG-----GQSVTGKLIdhmvqGHAAFP-----ELQVKataRCQ 248
Cdd:cd07772 238 YLAAGKEP-FTllsTGTW---CIAMNPGNdlpltELDLArdclyNLDVFGRPV-----KTARFMggreyERLVE---RIA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 249 SIYAYLNSHLDLIKkaqpvgFLTVDLHVWPDFHGNRSPladltlkgmrttgylyIPALAALHSPSSLLSPqvtglklsQD 328
Cdd:cd07772 306 KSFPQLPSLADLAK------LLARGTFALPSFAPGGGP----------------FPGSGGRGVLSAFPSA--------EE 355
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034559822 329 LDDLAILYLATVQAIALgtrfiieamEAAGHSISTLFLCGGLSKNPLFVQMHADI-TGMPVVLSQEVESVLVGAAVL 404
Cdd:cd07772 356 AYALAILYLALMTDYAL---------DLLGSGVGRIIVEGGFAKNPVFLRLLAALrPDQPVYLSDDSEGTALGAALL 423
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
335-402 |
1.16e-04 |
|
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: 44.52 E-value: 1.16e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034559822 335 LYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGG-LSKNPLFVQMHADITGMPVVLSQEVESVLVGAA 402
Cdd:cd07777 365 LFRALCRGIAENLHEMLPRLDLDLSGIERIVGSGGaLRKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAA 433
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
358-441 |
1.60e-03 |
|
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466795 [Multi-domain] Cd Length: 514 Bit Score: 41.00 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559822 358 GHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKV----GKVVFPRL 433
Cdd:cd07776 423 DIPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVVFSaeepKLVAEPDP 502
|
....*...
gi 1034559822 434 QDKKYYDK 441
Cdd:cd07776 503 EAAEVYDK 510
|
|
| |
