|
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 ... |
11-544 |
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: 1002.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDATCS 88
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEgaGVDPEQVKGIGFDATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 89 LVVLDKQFHPLPVNQEGDSHRNVIMWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLREiCWDKAGHF 168
Cdd:cd07782 81 LVVLDAEGKPVSVSPSGDDERNVILWMDHRAVEEAERINATGHEVLKYVGGKISPEMEPPKLLWLKENLPE-TWAKAGHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 169 FDLPDFLSWKATGVTARSLCSLVCKWTYSA----EKGWDDSFWKMIGLEDFVADNYSKIGNQVLPPGASLGNGLTPEAAR 244
Cdd:cd07782 160 FDLPDFLTWKATGSLTRSLCSLVCKWTYLAhegsEGGWDDDFFKEIGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 245 DLGLLPGIAVAASLIDAHAGGLGVIGADVrgHGLICEGQPVTSRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGF 324
Cdd:cd07782 240 ELGLPEGTPVGVSLIDAHAGGLGTLGADV--GGLPCEADPLTRRLALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 325 WLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNSHLDLIKKAQ--PVGFLTVDLHVWPDFHGNRSPLADL 402
Cdd:cd07782 318 WLNEGGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNERLEQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 403 TLKGMVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEV 482
Cdd:cd07782 398 TLRGMISGLTLDTSLDDLALLYLATLQALAYGTRHIIEAMNAAGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEP 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164663828 483 ESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKLVEHQKEY 544
Cdd:cd07782 478 EAVLLGAAILGAVASGDFPSLWDAMAAMSGPGKVVEPNEELKKYHDRKYEVFLKMYEDQREY 539
|
|
| 5C_CHO_kinase |
TIGR01315 |
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ... |
11-544 |
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: 677.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVV--QGIDLNQIRGLGFDATCS 88
Cdd:TIGR01315 1 HYIGVDVGTGSARACIIDSTGDILALAAQNIKTWTPSSGLEGQSSVYIWQAICNCVKQVLaeSKVDPNSVKGIGFDATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 89 LVVLDKQFHPLPVNQEGDSHRNVIMWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHF 168
Cdd:TIGR01315 81 LVVLTHDGEPLPVSKNGGADQNIILWMDHRALAEAEKINATNHNLLRYVGGKMSVEMEIPKVLWLKNNMPPE-LFARCKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 169 FDLPDFLSWKATGVTARSLCSLVCKWTY----SAEKGWDDSFWKMIGLEDFVADNYSKIGNQVLPPGASLGNGLTPEAAR 244
Cdd:TIGR01315 160 FDLTDFLTWRATGKEIRSFCSVVCKWGFvpvdGSNKGWQEDFYETIGLGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 245 DLGLLPGIAVAASLIDAHAGGLGVIGADVRGHGLICEGQpvtSRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGF 324
Cdd:TIGR01315 240 ELGLPAGTAVGSGLIDAHAGWIGTVGAKVAENGDVSQAF---TRLAAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 325 WLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNSHLdLIKKAQP----VGFLTVDLHVWPDFHGNRSPLA 400
Cdd:TIGR01315 317 WLAEGGQSAAGELMDHMLETHVAYDETVKEAEAAGKNIYDYLNEHL-KEMAAKTnapsISYLVRHFHVYPDLWGNRSPIA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 401 DLTLKGMVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQ 480
Cdd:TIGR01315 396 DPNMRGVIIGLSMDRSKDGLALLYYATMEFIAYGTRQIVEAMNTAGHTIKSIFMSGGQCQNPLLMQLIADACDMPVLIPY 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164663828 481 EVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQ-DKKYYDKKYQVFLKLVEHQKEY 544
Cdd:TIGR01315 476 VNEAVLHGAAMLGAKAAGTTESLWDAMDRMSKPGKTVWPRGDpAKKLHDRKYEIFLQLARTQQEY 540
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
9-544 |
0e+00 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 601.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 9 ERYYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKNWEP---------QFnhhEQSSEDIWAACCVVTKKVVQ--GIDLN 76
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDaADGEELASAVHPYPRWVIglylppppdQA---RQHPLDYLEALEAAVREALAqaGVDPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 77 QIRGLGFDAT-CSLVVLDKQFHPLPVNQE--GDSHRNVIMWLDHRAVSQVNRINE----TKHSVLQYVGGVMSVEMQAPK 149
Cdd:COG1069 78 DVVGIGVDATgCTPVPVDADGTPLALLPEfaENPHAMVILWKDHTAQEEAERINElakaRGEDYLRYVGGIISSEWFWPK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 150 LLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGW-DDSFWKMIGLE-DFVADnysKIGNQ 226
Cdd:COG1069 158 ILHLLREDPEV-YEAADSFVELCDWITWQLTGSLKRSRCTAGHKALWHAhEGGYpSEEFFAALDPLlDGLAD---RLGTE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 227 VLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIGadvrghglICEGQpvtsrLAVICGTSSCHMGISKDP 306
Cdd:COG1069 234 IYPLGEPAGT-LTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGG--------VEPGT-----LVKVMGTSTCHMLVSPEE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 307 IFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNshldliKKAQPVGFLTVDL 386
Cdd:COG1069 300 RFVPGICGQVDGSIVPGMWGYEAGQSAVGDIFAWFVRLLVPPLEYEKEAEERGISLHPLLT------EEAAKLPPGESGL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 387 HVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDlaiLYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFV 465
Cdd:COG1069 374 HALDWFNGNRSPLADQRLKGVILGLTLGTDAED---IYRALVEATAFGTRAIIERFEEEGVPIDEIIACGGIAtKNPLVM 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 466 QMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKV-GKVVFPRLQDKKYYDKKYQVFLKLVEHQKEY 544
Cdd:COG1069 451 QIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMAAMGSGfDKVYTPDPENVAVYDALYAEYLQLHDYFGRG 530
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
11-537 |
5.83e-156 |
|
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: 455.93 E-value: 5.83e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALVDQS-GVLLAFADQPIKNWE-PQFNHHEQSSEDIWAACCVVTKKVV--QGIDLNQIRGLGFDAT 86
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDLYaGLEMAQEPVPYYQDSsKKSWKFWQKSTEIIKALQKCVQKLNirEGVDAYEVKGCGVDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 87 CSLVVLDKQFHPLPVNQEGDSHRNVIMWLDHRAVSQVNRINETKHSVLQ-YVGGVMSVEMQAPKLLWLKENLREIcWDKA 165
Cdd:cd07768 81 CSLAIFDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWINMQCPQQLLdYLGGKISPEMGVPKLKYFLDEYSHL-RDKH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 166 GHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGWDDSFWKMIGLEDfVADNYSKIGNQVLPPGASLGNGLtPEAAR 244
Cdd:cd07768 160 FHIFDLHDYIAYELTRLYEWNICGLLGKENLDGeESGWSSSFFKNIDPRL-EHLTTTKNLPSNVPIGTTSGVAL-PEMAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 245 DLGLLPGIAVAASLIDAHAGGLGVIGADVRGhglicegqpvtsRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGF 324
Cdd:cd07768 238 KMGLHPGTAVVVSCIDAHASWFAVASPHLET------------SLFMIAGTSSCHMYGTTISDRIPGVWGPFDTIIDPDY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 325 WLNEGGQSVTGKLIDHMVQGHAAFPELqVKATARCQSIYAYLNshlDLIKKAQPVGFLTVDLHVWPDFHGNRSPLADLTL 404
Cdd:cd07768 306 SVYEAGQSATGKLIEHLFESHPCARKF-DEALKKGADIYQVLE---QTIRQIEKNNGLSIHILTLDMFFGNRSEFADPRL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 405 KGMVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVES 484
Cdd:cd07768 382 KGSFIGESLDTSMLNLTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMM 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 164663828 485 VLVGAAVLGACASGDFA---SVQEAMAKMSKVGKVVFPRLQD-KKYYDKKYQVFLKL 537
Cdd:cd07768 462 GILGAAVLAKVAAGKKQladSITEADISNDRKSETFEPLAYRlGADYILLYKLLCVK 518
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
11-537 |
1.26e-152 |
|
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: 446.60 E-value: 1.26e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKNWE--PQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDA 85
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAeaGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 86 TCSLVVldkqfhplPVNQEGDSHRNVIMWLDHRAVSQVNRINETKHSV----LQYVGGVMSVEMQAPKLLWLKENLREIc 161
Cdd:cd07781 81 TSSTVV--------PVDEDGNPLAPAILWMDHRAQEEAAEINETAHPAleyyLAYYGGVYSSEWMWPKALWLKRNAPEV- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 162 WDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEDfvADNYSKIGNQVLPPGASLGnGLTP 240
Cdd:cd07781 152 YDAAYTIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGgPPREFLAALDPGL--LKLREKLPGEVVPVGEPAG-TLTA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 241 EAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFSAM 320
Cdd:cd07781 229 EAAERLGLPAGIPVAQGGIDAHMGAIGA--------GVVEPGT-----LALIMGTSTCHLMVSPKPVDIPGICGPVPDAV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 321 VPGFWLNEGGQSVTGKLIdhmvqghAAFPELQVKATA-RCQSIYAYLNshlDLIKKAQPV--GFLTVDlhvWpdFHGNRS 397
Cdd:cd07781 296 VPGLYGLEAGQSAVGDIF-------AWFVRLFVPPAEeRGDSIYALLS---EEAAKLPPGesGLVALD---W--FNGNRT 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 398 PLADLTLKGMVTGLKLSQDLddlAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHADITGMPV 476
Cdd:cd07781 361 PLVDPRLRGAIVGLTLGTTP---AHIYRALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPI 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164663828 477 VLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKL 537
Cdd:cd07781 438 KVPKSDQAPALGAAILAAVAAGVYADIEEAADAMVRVDRVYEPDPENHAVYEELYALYKEL 498
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
10-543 |
3.39e-103 |
|
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: 319.47 E-value: 3.39e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 10 RYYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDAT- 86
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAkaGVDPEEIAAIGVSGQm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 87 CSLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINET--KHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDK 164
Cdd:COG1070 81 HGLVLLDADGEPL---------RPAILWNDTRAAAEAAELREElgEEALYEITGNPLHPGFTAPKLLWLKENEPEI-FAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 165 AGHFFDLPDFLSWKATG--VTARSLCSlvckWT--YSAEKG-WDDSFWKMIGL-EDFVAdnyskignQVLPPGASLGnGL 238
Cdd:COG1070 151 IAKVLLPKDYLRYRLTGefVTDYSDAS----GTglLDVRTRdWSDELLEALGIdRELLP--------ELVPPGEVAG-TL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 239 TPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFS 318
Cdd:COG1070 218 TAEAAAETGLPAGTPVVAGAGDNAAAALGA--------GAVEPGD-----AAVSLGTSGVVFVVSDKPLPDPEGRVHTFC 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 319 AMVPGFWLNEGGQSVTGKLIDHMVQghaafpelqvKATARCQSIYAYLNshlDLIKKAqPVG-----FLtvdlhvwPDFH 393
Cdd:COG1070 285 HAVPGRWLPMGATNNGGSALRWFRD----------LFADGELDDYEELN---ALAAEV-PPGadgllFL-------PYLS 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 394 GNRSPLADLTLKGMVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITG 473
Cdd:COG1070 344 GERTPHWDPNARGAFFGLTLSHTRAHL---ARAVLEGVAFALRDGLEALEEAGVKIDRIRATGGGARSPLWRQILADVLG 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 474 MPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKLVEHQKE 543
Cdd:COG1070 421 RPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMVRVGETIEPDPENVAAYDELYERYRELYPALKP 490
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
9-548 |
4.29e-89 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 284.43 E-value: 4.29e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 9 ERYYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKNW---------EPQFNHHEQSSEDIWAAccvVTKKVVQ--GIDLN 76
Cdd:PRK04123 2 MAYVIGLDFGTDSVRALLVDcATGEELATAVVEYPHWvkgryldlpPNQALQHPLDYIESLEA---AIPAVLKeaGVDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 77 QIRGLGFDAT-CSLVVLDKQFHPLPVNQEGDSHRN--VIMWLDHRAVSQVNRINETKHS-----VLQYVGGVMSVEMQAP 148
Cdd:PRK04123 79 AVVGIGVDFTgSTPAPVDADGTPLALLPEFAENPHamVKLWKDHTAQEEAEEINRLAHErgeadLSRYIGGIYSSEWFWA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 149 KLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTA-----RSLCSLVCKWTYSAEKG--WDDSFWKMI--GLEDFVADn 219
Cdd:PRK04123 159 KILHVLREDPAV-YEAAASWVEACDWVVALLTGTTDpqdivRSRCAAGHKALWHESWGglPSADFFDALdpLLARGLRD- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 220 ysKIGNQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGglgVIGADVRGHGLicegqpvtsrLAVIcGTSSCH 299
Cdd:PRK04123 237 --KLFTETWTAGEPAG-TLTAEWAQRLGLPEGVAVSVGAFDAHMG---AVGAGAEPGTL----------VKVM-GTSTCD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 300 MGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQgHAAFPELQVKATARCQSIYAYLNshldliKKA--Q 377
Cdd:PRK04123 300 ILLADKQRAVPGICGQVDGSIVPGLIGYEAGQSAVGDIFAWFAR-LLVPPEYKDEAEARGKQLLELLT------EAAakQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 378 PVG---FLTVDlhvWpdFHGNRSPLADLTLKGMVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFL 454
Cdd:PRK04123 373 PPGehgLVALD---W--FNGRRTPLADQRLKGVITGLTLGTDAPDI---YRALIEATAFGTRAIMECFEDQGVPVEEVIA 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 455 CGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKM-SKVGKVVFPRLQDKKYYDKKYQ 532
Cdd:PRK04123 445 AGGIArKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEAQQAMaSPVEKTYQPDPENVARYEQLYQ 524
|
570
....*....|....*..
gi 164663828 533 VFLKLVE-HQKEYLAIM 548
Cdd:PRK04123 525 EYKQLHDyFGRGGNAVM 541
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
12-497 |
3.59e-83 |
|
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: 268.89 E-value: 3.59e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 12 YVGVDVGTGSVRAALVDQSGVLLAFADQPI--KNWEPQFNHHEQSSEDIWAACCVVTKKVVQGIDLNQIRGLGFDATCSL 89
Cdd:cd07778 2 GIGIDVGSTSVRIGIFDYHGTLLATSERPIsyKQDPKDLWFVTQSSTEIWKAIKTALKELIEELSDYIVSGIGVSATCSM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 90 VVLDKQ-----FHPLPVNQE-GDSHRNVIMWLDHRAVSQVNRINE-TKHSVLQYVGGVMSVEMQAPKLLWLKENLREICW 162
Cdd:cd07778 82 VVMQRDsdtsyLVPYNVIHEkSNPDQDIIFWMDHRASEETQWLNNiLPDDILDYLGGGFIPEMAIPKLKYLIDLIKEDTF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 163 DKAgHFFDLPDFLSWKatgvtarsLCSLVCKW--TYSAE------------KGWDDSFWKMIGLEDFVAD--NYSKIGNQ 226
Cdd:cd07778 162 KKL-EVFDLHDWISYM--------LATNLGHSniVPVNAppsigigidgslKGWSKDFYSKLKISTKVCNvgNTFKEAPP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 227 VLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIgadvrghgliCEGQPVTSRLAVICGTSSCHMGISKDP 306
Cdd:cd07778 233 LPYAGIPIGK-VNVILASYLGIDKSTVVGHGCIDCYAGWFSTF----------AAAKTLDTTLFMVAGTSTCFLYATSSS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 307 I--FVPGVWGPyFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATarcqSIYAYLNSHLDLI--KKAQPVGFL 382
Cdd:cd07778 302 QvgPIPGIWGP-FDQLLKNYSVYEGGQSATGKLIEKLFNSHPAIIELLKSDA----NFFETVEEKIDKYerLLGQSIHYL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 383 TVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNP 462
Cdd:cd07778 377 TRHMFFYGDYLGNRTPYNDPNMSGSFIGESTDSSLTDLVLKYILILEFLAFQTKLIIDNFQKEKIIIQKVVISGSQAKNA 456
|
490 500 510
....*....|....*....|....*....|....*...
gi 164663828 463 LFVQMHADITGMPVV---LSQEVESVLVGAAVLGACAS 497
Cdd:cd07778 457 RLLQLLSTVLSKIHIivpLSDSKYAVVKGAALLGKAAF 494
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
11-535 |
6.57e-81 |
|
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: 261.30 E-value: 6.57e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDAT-C 87
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEksGIDPSDIAAIAFSGQmQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 88 SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINET---KHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDK 164
Cdd:cd07805 81 GVVPVDKDGNPL---------RNAIIWSDTRAAEEAEEIAGGlggIEGYRLGGGNPPSGKDPLAKILWLKENEPEI-YAK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 165 AGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEDfvadnySKIgNQVLPPGASLGnGLTPEAA 243
Cdd:cd07805 151 THKFLDAKDYLNFRLTGRAATDPSTASTTGLMDLRKRrWSEELLRAAGIDP------DKL-PELVPSTEVVG-ELTPEAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 244 RDLGLLPGIAVAASLIDAHAGGLGViGADVRGHGLICegqpvtsrlaviCGTSS---CHmgiSKDPIFVPGvwGPYFS-- 318
Cdd:cd07805 223 AELGLPAGTPVVGGGGDAAAAALGA-GAVEEGDAHIY------------LGTSGwvaAH---VPKPKTDPD--HGIFTla 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 319 AMVPGFWLNEGGQSVTGKLIDHMVQgHAAFPELQVKatarcqSIYAYLNshlDLIKKAQP----VGFLtvdlhvwPDFHG 394
Cdd:cd07805 285 SADPGRYLLAAEQETAGGALEWARD-NLGGDEDLGA------DDYELLD---ELAAEAPPgsngLLFL-------PWLNG 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 395 NRSPLADLTLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGM 474
Cdd:cd07805 348 ERSPVEDPNARGAFIGLSLEHTRADLA---RAVLEGVAFNLRWLLEALEKLTRKIDELRLVGGGARSDLWCQILADVLGR 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164663828 475 PV-VLSQEVESVLVGAAVLGACASGDFASVQEAmAKMSKVGKVVFPRLQDKKYYDKKYQVFL 535
Cdd:cd07805 425 PVeVPENPQEAGALGAALLAAVGLGLLKSFDEA-KALVKVEKVFEPDPENRARYDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
11-537 |
3.67e-76 |
|
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: 248.99 E-value: 3.67e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVV--QGIDLNQIRGLGFDA-TC 87
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLakAGISPSDIAAIGLTGqMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 88 SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINET-KHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAG 166
Cdd:cd07808 81 GLVLLDKNGRPL---------RPAILWNDQRSAAECEELEARlGDEILIITGNPPLPGFTLPKLLWLKENEPEI-FARIR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 167 HFFdLP-DFLSWKATGVTAR-------SLCslvckwtYSAEKG-WDDSFWKMIGLEdfvadnyskigNQVLPP---GASL 234
Cdd:cd07808 151 KIL-LPkDYLRYRLTGELATdpsdasgTLL-------FDVEKReWSEELLEALGLD-----------PSILPPiveSTEI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 235 GNGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPV----TSrlAVICGTSSCHMGISKDPIF-- 308
Cdd:cd07808 212 VGTLTPEAAEELGLPEGTPVVAGAGDNAAAALGA--------GVVEPGDALislgTS--GVVFAPTDKPVPDPKGRLHtf 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 309 ---VPGVW---GPYFSAmvpGF---WLNE--GGQSVTGKLIDHMVQGHAAfpelqvkatarcqsiyaylnshldlikKAQ 377
Cdd:cd07808 282 phaVPGKWyamGVTLSA---GLslrWLRDlfGPDRESFDELDAEAAKVPP---------------------------GSE 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 378 PVGFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEAAGHSISTLFLCGG 457
Cdd:cd07808 332 GLLFL-------PYLSGERTPYWDPNARGSFFGLSLSHTRAHLA---RAVLEGVAFSLRDSLEVLKELGIKVKEIRLIGG 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 458 LSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKL 537
Cdd:cd07808 402 GAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACIKIEKTIEPDPERHEAYDELYARYREL 481
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
11-527 |
3.71e-73 |
|
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: 239.34 E-value: 3.71e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDAT-C 87
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAkaGVDPEDIAAIGLTSQrS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 88 SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVsqvnrinetkhsvlqyvggvmsvemqapkllwlkenlreicwdkagH 167
Cdd:cd07779 81 TFVPVDEDGRPL---------RPAISWQDKRTA----------------------------------------------K 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 168 FFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEdfvADNYSKIgnqvLPPGASLGNgLTPEAARDL 246
Cdd:cd07779 106 FLTVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRdWSDDLLDAFGID---RDKLPEL----VPPGTVIGT-LTKEAAEET 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 247 GLLPGIAVAASlidAHAGGLGVIGADVRGHGLICegqpvtsrlaVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWL 326
Cdd:cd07779 178 GLPEGTPVVAG---GGDQQCAALGAGVLEPGTAS----------LSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWV 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 327 NEGGQSVTGKLIDHMVQghaAFPELQVKATARCQSIYAYLNSHLDLIkkaqPVGFLtvDLHVWPDFHGNRSPLADLTLKG 406
Cdd:cd07779 245 LEGSINTGGSAVRWFRD---EFGQDEVAEKELGVSPYELLNEEAAKS----PPGSD--GLLFLPYLAGAGTPYWNPEARG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 407 MVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVL 486
Cdd:cd07779 316 AFIGLTLSHTRAHL---ARAILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATA 392
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 164663828 487 VGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYY 527
Cdd:cd07779 393 LGAAILAAVGAGIYPDFEEAVKAMVRVTDTFEPDPENVAIY 433
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
11-494 |
4.80e-67 |
|
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: 223.25 E-value: 4.80e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQGIDLNQIRGLGFDATC-SL 89
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPRRVVAIAVDGTSgTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 90 VVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFF 169
Cdd:cd07783 81 VLVDREGEPL---------RPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEV-LAKTAKFL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 170 DLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEdfvadnySKIGNQVLPPGASLGNgLTPEAARDLGL 248
Cdd:cd07783 151 HQADWLAGRLTGDRGVTDYNNALKLGYDPETGrWPSWLLALLGIP-------PDLLPRVVAPGTVIGT-LTAEAAEELGL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 249 LPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVTSrlaviCGTSSCHMGISKDPIFVPGVwGPYFSAMVPGFWLNE 328
Cdd:cd07783 223 PAGTPVVAGTTDSIAAFLAS--------GAVRPGDAVTS-----LGTTLVLKLLSDKRVPDPGG-GVYSHRHGDGYWLVG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 329 GGQSVTGKLIDHmvqghaAFPELQVKAtarcqsiyaylnshldLIKKAQPVGflTVDLHVWP-DFHGNRSPLADLTLKGM 407
Cdd:cd07783 289 GASNTGGAVLRW------FFSDDELAE----------------LSAQADPPG--PSGLIYYPlPLRGERFPFWDPDARGF 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 408 VTGLKlsqdlDDLAILYLATVQAIALGTRFIIEAMEAAGHS-ISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVL 486
Cdd:cd07783 345 LLPRP-----HDRAEFLRALLEGIAFIERLGYERLEELGAPpVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEAAL 419
|
....*...
gi 164663828 487 vGAAVLGA 494
Cdd:cd07783 420 -GAALLAA 426
|
|
| L-ribulokinase |
TIGR01234 |
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely ... |
11-545 |
1.03e-65 |
|
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: 222.88 E-value: 1.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKNWE--------------PQFNHHEQSSEDIWAAccvVTKKVVQ--GI 73
Cdd:TIGR01234 2 YAIGVDFGTLSGRALAVDvATGEEIATAVEWYRHWVkgqflpktgaklpnDQALQHPADYIEVLEA---AIPTVLAelGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 74 DLNQIRGLGFDAT-CSLVVLDKQFHPLPVNQE--GDSHRNVIMWLDHRAVSQVNRINETKHS----VLQYVGGVMSVEMQ 146
Cdd:TIGR01234 79 DPADVVGIGVDFTaCTPAPIDSDGNPLCLLPEfaENPHAYFKLWKHHAAQEEADRINRLAHApgevDLSRYGGIISSEWF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 147 APKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKGW-DDSFWKMI--GLEDFVADNYSK- 222
Cdd:TIGR01234 159 WAKILQITEEDPAI-YQAADRWIELADWIVAQLSGDIRRGRCTAGYKALWHESWGYpSASFFDELnpILNRHLPDKLFTd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 223 IGNQVLPPGAslgngLTPEAARDLGLLPGIAVAASLIDAHaggLGVIGADVrghgliceGQPvtSRLAVICGTSSCHMGI 302
Cdd:TIGR01234 238 IWTAGEPAGT-----LTPEWAQRTGLPEGVVVAVGNFDAH---VGAVAAGI--------AQP--GALVKIMGTSTCHVLI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 303 SKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQgHAAFPELQVKATARCQSiyayLNSHLDLIKKAQPV--- 379
Cdd:TIGR01234 300 GDKQRAVPGMCGVVDGGIVPGFIGYEAGQSAVGDIFAWFGK-VCVPPELKTEANASQKQ----LHEALSEAAAKQPSgeh 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 380 GFLTVDlhvWpdFHGNRSPLADLTLKGMVTGLKLSQDLDDlaiLYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS 459
Cdd:TIGR01234 375 GLVALD---W--FNGNRSPLVDQRLKGVITGLTLATDAPL---LYRALIEATAFGTRMIMETFTDSGVPVEELMAAGGIA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 460 -KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVF-PRLQDKKYYDKKYQVFLKL 537
Cdd:TIGR01234 447 rKNPVIMQIYADVTNRPLQIVASDQAPALGAAIFAAVAAGVYADIPSAQAKMGSAVEKTLtPCSENAQRYEQLYARYQEL 526
|
....*...
gi 164663828 538 VEHQKEYL 545
Cdd:TIGR01234 527 AMSFGQYN 534
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
11-493 |
1.80e-63 |
|
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: 212.81 E-value: 1.80e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDAT-C 87
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAkaGIDPSDIAAIGISGQmP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 88 SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAvsqvnrinetkhsvlqyvggvmsvemqapkllwlkenlreicwdkagH 167
Cdd:cd00366 81 GVVLVDADGNPL---------RPAIIWLDRRA-----------------------------------------------K 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 168 FFDLPDFLSWKATGVTA--RSLCSLVCKWTYsAEKGWDDSFWKMIGL-EDFVADnyskignqVLPPGASLGnGLTPEAAR 244
Cdd:cd00366 105 FLQPNDYIVFRLTGEFAidYSNASGTGLYDI-KTGDWSEELLDALGIpREKLPP--------IVESGEVVG-RVTPEAAE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 245 DLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVtsrlaVICGTSSCHMGISKDPIFVPGVWGPYFSAmVPGF 324
Cdd:cd00366 175 ETGLPAGTPVVAGGGDTAAAALGA--------GVVEPGDAV-----DSTGTSSVLSVCTDEPVPPDPRLLNRCHV-VPGL 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 325 WLNEGGQSVTGKLIDHMVQghaafpelqvkATARCQSIYAYLNSHLDLIKKAQP----VGFLtvdlhvwPDFHGNRSPLA 400
Cdd:cd00366 241 WLLEGAINTGGASLRWFRD-----------EFGEEEDSDAEYEGLDELAAEVPPgsdgLIFL-------PYLSGERSPIW 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 401 DLTLKGMVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQ 480
Cdd:cd00366 303 DPAARGVFFGLTLSHTRAHL---IRAVLEGVAYALRDNLEILEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPE 379
|
490
....*....|...
gi 164663828 481 EVESVLVGAAVLG 493
Cdd:cd00366 380 VAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
11-498 |
2.30e-62 |
|
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: 211.29 E-value: 2.30e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQGIDLNQIRGLGFdAT--CS 88
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGPDPIAAISV-SSqgES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 89 LVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAG 166
Cdd:cd07773 80 GVPVDRDGEPL---------GPAIVWFDPRGKEEAEELAEriGAEELYRITGLPPSPMYSLAKLLWLREHEPEI-FAKAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 167 HFFDLPDFLSWKATGVTARSLcSLVCKWTY--SAEKGWDDSfwkmigLEDFVADNYSKIGnQVLPPGASLGNgLTPEAAR 244
Cdd:cd07773 150 KWLSVADYIAYRLTGEPVTDY-SLASRTMLfdIRKRTWSEE------LLEAAGIDASLLP-ELVPSGTVIGT-VTPEAAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 245 DLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFS---AMV 321
Cdd:cd07773 221 ELGLPAGTPVVVGGHDHLCAALGA--------GVIEPGD-----VLDSTGTAEALLAVVDEPPLDEMLAEGGLSyghHVP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 322 PGFWLNEGGQSvTGKLIDHMVQGHAAFPELQVKATARCQSIYAylnshldlikKAQPVGFLtvdlhvwPDFHGNRSPLAD 401
Cdd:cd07773 288 GGYYYLAGSLP-GGALLEWFRDLFGGDESDLAAADELAEAAPP----------GPTGLLFL-------PHLSGSGTPDFD 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 402 LTLKGMVTGLKLSQDLDDlaiLYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQE 481
Cdd:cd07773 350 PDARGAFLGLTLGTTRAD---LLRAILEGLAFELRLNLEALEKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEV 426
|
490
....*....|....*..
gi 164663828 482 VESVLVGAAVLGACASG 498
Cdd:cd07773 427 PEATALGAALLAGVGAG 443
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
289-496 |
1.01e-60 |
|
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: 199.09 E-value: 1.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 289 LAVICGTSSCHMGISKDP-IFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQvkATARCQSIYAYLN 367
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPvLSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELR--DAGNVESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 368 SHLDLikkaqpvgfLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLddlAILYLATVQAIALGTRFIIEAMEA-AG 446
Cdd:pfam02782 79 LAAVA---------PAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTL---AHLYRAILESLALQLRQILEALTKqEG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 164663828 447 HSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACA 496
Cdd:pfam02782 147 HPIDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
11-538 |
3.63e-60 |
|
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466790 [Multi-domain] Cd Length: 478 Bit Score: 206.25 E-value: 3.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQGIDLNQIRGLGFDATC-SL 89
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVDAIGFSSAMhSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 90 VVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRI--NETKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGH 167
Cdd:cd07770 81 LGVDEDGEPL---------TPVITWADTRAAEEAERLrkEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPEL-FAKAAK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 168 FFDLPDFLSWKATG--VTARSLCSlvckWT---YSAEKGWDDSFWKMIGLEdfvADNYSKIgnqvLPPGASLGnGLTPEA 242
Cdd:cd07770 151 FVSIKEYLLYRLTGelVTDYSTAS----GTgllNIHTLDWDEEALELLGID---EEQLPEL----VDPTEVLP-GLKPEF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 243 ARDLGLLPGIAVAASLIDahaGGLGVIGAdvrghGLICEGqpvtsRLAVICGTSschmG----ISKDPIFVP--GVWgPY 316
Cdd:cd07770 219 AERLGLLAGTPVVLGASD---GALANLGS-----GALDPG-----RAALTVGTS----GairvVSDRPVLDPpgRLW-CY 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 317 FSAmvPGFWL-----NEGGqSVTGKLIDHMVQGHAAFPELQVKATArcqsiyAYLNSHlDLIkkaqpvgFLtvdlhvwPD 391
Cdd:cd07770 281 RLD--ENRWLvggaiNNGG-NVLDWLRDTLLLSGDDYEELDKLAEA------VPPGSH-GLI-------FL-------PY 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 392 FHGNRSPLADLTLKGMVTGLKLSQDLDDlaiLYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADI 471
Cdd:cd07770 337 LAGERAPGWNPDARGAFFGLTLNHTRAD---ILRAVLEGVAFNLKSIYEALEELAGPVKEIRASGGFLRSPLWLQILADV 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164663828 472 TGMPVVLSQEVESVLVGAAVLGACASGDFASVQEamAKMSKVGKVVFPRLQDKKYYDKKYQVFLKLV 538
Cdd:cd07770 414 LGRPVLVPEEEEASALGAALLALEALGLISSLEA--DELVKIGKVVEPDPENHAIYAELYERFKKLY 478
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
11-498 |
1.03e-59 |
|
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: 204.68 E-value: 1.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQP--IKNwePQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGfdat 86
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEhdLLT--PKPGWAEHDPEVWWGAVCEIIRELLAkaGISPKEIAAIG---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 87 CS-----LVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINETKHS--VLQYVGGVMSVEMQAPKLLWLKENLRE 159
Cdd:cd07804 75 VSglvpaLVPVDENGKPL---------RPAILYGDRRATEEIEWLNENIGEdrIFEITGNPLDSQSVGPKLLWIKRNEPE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 160 IcWDKAGHFFDLPDFLSWKATG--VTARSLCSLvckwtYS-----AEKGWDDSFWKMIGLEdfvadnySKIGNQVLPPGA 232
Cdd:cd07804 146 V-FKKTRKFLGAYDYIVYKLTGeyVIDYSSAGN-----EGglfdiRKRTWDEELLEALGID-------PDLLPELVPSTE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 233 SLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGV 312
Cdd:cd07804 213 IVG-EVTKEAAEETGLAEGTPVVAGTVDAAASALSA--------GVVEPGD-----LLLMLGTAGDIGVVTDKLPTDPRL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 313 WGPYFSamVPGFWLNEGGQSVTGKLIDHMVQGHAafPELQVKATARCQSIYAYLNshldliKKAQ--PVGfltVD-LHVW 389
Cdd:cd07804 279 WLDYHD--IPGTYVLNGGMATSGSLLRWFRDEFA--GEEVEAEKSGGDSAYDLLD------EEAEkiPPG---SDgLIVL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 390 PDFHGNRSPLADLTLKGMVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHA 469
Cdd:cd07804 346 PYFMGERTPIWDPDARGVIFGLTLSHTRAHL---YRALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVA 422
|
490 500
....*....|....*....|....*....
gi 164663828 470 DITGMPVVLSQEVESVLVGAAVLGACASG 498
Cdd:cd07804 423 DVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
11-498 |
9.64e-58 |
|
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: 198.93 E-value: 9.64e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDAT-C 87
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEksGVDPSDIAGVGVTGHgN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 88 SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKA 165
Cdd:cd07802 81 GLYLVDKDGKPV---------RNAILSNDSRAADIVDRWEEdgTLEKVYPLTGQPLWPGQPVALLRWLKENEPER-YDRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 166 GHFFDLPDFLSWKATGVtarslcsLVCKWT-YSA------EKGWDDSFWKMIGLEDFvadnYSKIGnQVLPPGASLGnGL 238
Cdd:cd07802 151 RTVLFCKDWIRYRLTGE-------ISTDYTdAGSslldldTGEYDDELLDLLGIEEL----KDKLP-PLVPSTEIAG-RV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 239 TPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGpYFS 318
Cdd:cd07802 218 TAEAAALTGLPEGTPVAAGAFDVVASALGA--------GAVDEGQ-----LCVILGTWSINEVVTDEPVVPDSVGS-NSL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 319 AMVPGFWLNEGGQSVTGKLIDHMVQghaafpELQVKATARCQSIYAYLNshlDLIKKAQPVG----FLtvdlhvwPDFHG 394
Cdd:cd07802 284 HADPGLYLIVEASPTSASNLDWFLD------TLLGEEKEAGGSDYDELD---ELIAAVPPGSsgviFL-------PYLYG 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 395 NRsplADLTLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEAAGHsISTLFLCGGLSKNPLFVQMHADITGM 474
Cdd:cd07802 348 SG---ANPNARGGFFGLTAWHTRAHLL---RAVYEGIAFSHRDHLERLLVARK-PETIRLTGGGARSPVWAQIFADVLGL 420
|
490 500
....*....|....*....|....
gi 164663828 475 PVVLSQEVESVLVGAAVLGACASG 498
Cdd:cd07802 421 PVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
11-498 |
1.70e-44 |
|
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: 163.10 E-value: 1.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDATC 87
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKdaGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 88 -SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINET-KHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKA 165
Cdd:cd07809 81 hGLVALDADGKVL---------RPAKLWCDTRTAPEAEELTEAlGGKKCLLVGLNIPARFTASKLLWLKENEPEH-YARI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 166 gHFFDLP-DFLSWKATG--VTARSLCSLVckwtysaekGWDDSF-----WKMIGLEDFVADNYSKIGnQVLPPGASLGnG 237
Cdd:cd07809 151 -AKILLPhDYLNWKLTGekVTGLGDASGT---------FPIDPRtrdydAELLAAIDPSRDLRDLLP-EVLPAGEVAG-R 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 238 LTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVTSrlaviCGTSSCHMGISKDPIFVPgvwgpyf 317
Cdd:cd07809 219 LTPEGAEELGLPAGIPVAPGEGDNMTGALGT--------GVVNPGTVAVS-----LGTSGTAYGVSDKPVSDP------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 318 SAMVPGF--------WLNEG---GQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYlnshldlikkaqpvgfltvdl 386
Cdd:cd07809 279 HGRVATFcdstggmlPLINTtncLTAWTELFRELLGVSYEELDELAAQAPPGAGGLLLL--------------------- 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 387 hvwPDFHGNRSP-LADLTlkGMVTGLKLSQdlDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFV 465
Cdd:cd07809 338 ---PFLNGERTPnLPHGR--ASLVGLTLSN--FTRANLARAALEGATFGLRYGLDILRELGVEIDEIRLIGGGSKSPVWR 410
|
490 500 510
....*....|....*....|....*....|...
gi 164663828 466 QMHADITGMPVVLSQEVESVLVGAAVLGACASG 498
Cdd:cd07809 411 QILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
11-498 |
3.62e-40 |
|
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to Bacillus subtilis sugar kinase YoaC. It is part of the yoaDCB operon and induced by sulfate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466804 [Multi-domain] Cd Length: 448 Bit Score: 151.22 E-value: 3.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHH--EQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLgfdAT 86
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYPDakEFDPEELWEKICEAIREALKkaGISPEDISAV---SS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 87 CS----LVVLDKQFHPL---PvnqegdshrNVimwlDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAP-KLLWLKENLR 158
Cdd:cd07798 78 TSqregIVFLDKDGRELyagP---------NI----DARGVEEAAEIDDEFGEEIYTTTGHWPTELFPAaRLLWFKENRP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 159 EIcWDKAGHFFDLPDFLSWKATGVtarslcsLVCKWTYSAEKG--------WDDSFWKMIGLEDfvadnysKIGNQVLPP 230
Cdd:cd07798 145 EI-FERIATVLSISDWIGYRLTGE-------LVSEPSQASETQlfdikkreWSQELLEALGLPP-------EILPEIVPS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 231 GASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVP 310
Cdd:cd07798 210 GTVLGT-VSEEAARELGLPEGTPVVVGGADTQCALLGS--------GAIEPGD-----IGIVAGTTTPVQMVTDEPIIDP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 311 --GVW-GPYfsaMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQvkatarcqsiYAYLNSHLDLIKKAQP--VGFLTVD 385
Cdd:cd07798 276 erRLWtGCH---LVPGKWVLESNAGVTGLNYQWLKELLYGDPEDS----------YEVLEEEASEIPPGANgvLAFLGPQ 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 386 LhvwpdFHGNRSPLADLTLKGMVTGLKLSQDLDDLAIlylATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLF 464
Cdd:cd07798 343 I-----FDARLSGLKNGGFLFPTPLSASELTRGDFAR---AILENIAFAIRANLEQLEEvSGREIPYIILCGGGSRSALL 414
|
490 500 510
....*....|....*....|....*....|....
gi 164663828 465 VQMHADITGMPVVLSQEVESVLVGAAVLGACASG 498
Cdd:cd07798 415 CQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
11-498 |
1.00e-35 |
|
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: 138.91 E-value: 1.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQGIDL--NQIRGLGFDAT-- 86
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVlpDRVAAIGVTGQgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 87 -CSLVvlDKqfhplpvnqEGDSHRNVIMWLDHRAVSQVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLREICwD 163
Cdd:cd24121 81 gTWLV--DE---------DGRPVRDAILWLDGRAADIVERWQAdgIAEAVFEITGTGLFPGSQAAQLAWLKENEPERL-E 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 164 KAGHFFDLPDFLSWKATGVTA--RSLCSLVCkwtYSAEKG-WDDSFWKMIGLEDFVAdnyskignqVLPP-GASLGNG-- 237
Cdd:cd24121 149 RARTALHCKDWLFYKLTGEIAtdPSDASLTF---LDFRTRqYDDEVLDLLGLEELRH---------LLPPiRPGTEVIgp 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 238 LTPEAARDLGLLPGIAVAASLIDAHAGGLGViGADVRGHGLicegqpvtsrlaVICGTSSCHMGISKDPIFVPGVWGPYF 317
Cdd:cd24121 217 LTPEAAAATGLPAGTPVVLGPFDVVATALGS-GAIEPGDAC------------SILGTTGVHEVVVDEPDLEPEGVGYTI 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 318 SAMVPGFWLNEGGqSVTGKL-IDHMVQ--GHAAFPELQVKATarcqSIYAYLNSHLdlikKAQPVGFLTVDLHVWPDFHG 394
Cdd:cd24121 284 CLGVPGRWLRAMA-NMAGTPnLDWFLRelGEVLKEGAEPAGS----DLFQDLEELA----ASSPPGAEGVLYHPYLSPAG 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 395 NRSPLADLTLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMeaaGHSISTLFLCGGLSKNPLFVQMHADITGM 474
Cdd:cd24121 355 ERAPFVNPNARAQFTGLSLEHTRADLL---RAVYEGVALAMRDCYEHM---GEDPGELRLSGGGARSDTWCQILADALGV 428
|
490 500
....*....|....*....|....
gi 164663828 475 PVVLSQEVESVLVGAAVLGACASG 498
Cdd:cd24121 429 PVRVPAGEEFGARGAAMNAAVALG 452
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
11-267 |
4.11e-28 |
|
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: 112.82 E-value: 4.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDATC- 87
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSqlGISLKQIKGIGISNQGh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 88 SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKA 165
Cdd:pfam00370 81 GTVLLDKNDKPL---------YNAILWKDRRTAEIVENLKEegNNQKLYEITGLPIWPGFTLSKLRWIKENEPEV-FEKI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 166 GHFFDLPDFLSWKATGVtarslcsLVCKWTYSAEKG--------WDDSFWKMIGLEdfvadnyskigNQVLPP----GAS 233
Cdd:pfam00370 151 HKFLTIHDYLRWRLTGV-------FVTDHTNASRSMmfnihkldWDPELLAALGIP-----------RDHLPPlvesSEI 212
|
250 260 270
....*....|....*....|....*....|....
gi 164663828 234 LGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLG 267
Cdd:pfam00370 213 YGE-LNPELAAMWGLDEGVPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
11-532 |
7.98e-28 |
|
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466794 [Multi-domain] Cd Length: 492 Bit Score: 116.66 E-value: 7.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPiknWEPQFNHHEQSSEDI-----WAACCVVTKKVVQ--GIDLNQIRGLgf 83
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQRE---WRHKEVPDVPGSMDFdteknWKLICECIREALKkaGIAPKSIAAI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 84 dATCS----LVVLDKQFHPLpvnqegdshrnvimW----LDHRAVSQVNRINETKHSVLQ--YVGGVMSVEMQA-PKLLW 152
Cdd:cd07775 76 -STTSmregIVLYDNEGEEI--------------WacanVDARAAEEVSELKELYNTLEEevYRISGQTFALGAiPRLLW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 153 LKENLREIcWDKAGHFFDLPDFLSWKATGVTAR--SLCSLVCKWTySAEKGWDDSFWKMIGLEDFvadnyskIGNQVLPP 230
Cdd:cd07775 141 LKNNRPEI-YRKAAKITMLSDWIAYKLSGELAVepSNGSTTGLFD-LKTRDWDPEILEMAGLKAD-------ILPPVVES 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 231 GASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrlAVICGTSSCHMGI-SKDPIFV 309
Cdd:cd07775 212 GTVIGK-VTKEAAEETGLKEGTPVVVGGGDVQLGCLGL--------GVVRPGQ------TAVLGGSFWQQEVnTAAPVTD 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 310 PGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQghAAFPELQVKATARCQSIYAYLNshldliKKAQ--PVGF-----L 382
Cdd:cd07775 277 PAMNIRVNCHVIPDMWQAEGISFFPGLVMRWFRD--AFCAEEKEIAERLGIDAYDLLE------EMAKdvPPGSygimpI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 383 TVDL-------HVWPDFhgnrspladltlkgmvTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAA-GHSISTLFL 454
Cdd:cd07775 349 FSDVmnyknwrHAAPSF----------------LNLDIDPEKCNKATFFRAIMENAAIVSAGNLERIAEFsGIFPDSLVF 412
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164663828 455 CGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQ 532
Cdd:cd07775 413 AGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAGIYSSLEEAVESLVKWEREYLPNPENHEVYQDLYE 490
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
12-537 |
8.77e-21 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 95.42 E-value: 8.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 12 YVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQGIDLNQIRGLGFDATC-SLV 90
Cdd:PRK15027 2 YIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQMhGAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 91 VLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLREICWDKAGHFfd 170
Cdd:PRK15027 82 LLDAQQRVL---------RPAILWNDGRCAQECALLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVL-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 171 LP-DFLSWKATGVTARSLCSLV-CKWTYSAEKGWDDSfwkMIGLEDFVADNYSkignqVLPPGASLGNGLTPEAARDLGl 248
Cdd:PRK15027 151 LPkDYLRLRMTGEFASDMSDAAgTMWLDVAKRDWSDV---MLQACHLSRDQMP-----ALYEGSEITGALLPEVAKAWG- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 249 LPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVTSrlaviCGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWlne 328
Cdd:PRK15027 222 MATVPVVAGGGDNAAGAVGV--------GMVDANQAMLS-----LGTSGVYFAVSEGFLSKPESAVHSFCHALPQRW--- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 329 ggqsvtgKLIDHMVQGhAAFPELQVKATARcQSIYAYLNSHLDLIKKAQPVGFLtvdlhvwPDFHGNRSPLADLTLKGMV 408
Cdd:PRK15027 286 -------HLMSVMLSA-ASCLDWAAKLTGL-SNVPALIAAAQQADESAEPVWFL-------PYLSGERTPHNNPQAKGVF 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 409 TGLKLSQDLDDLAILYLATV-QAIALGtrfiIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQ--EVESV 485
Cdd:PRK15027 350 FGLTHQHGPNELARAVLEGVgYALADG----MDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTggDVGPA 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 164663828 486 LvGAAVLGACASGDFASVQEAMAKMSkVGKVVFPRLQDKKYYDKKYQVFLKL 537
Cdd:PRK15027 426 L-GAARLAQIAANPEKSLIELLPQLP-LEQSHLPDAQRYAAYQPRRETFRRL 475
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
11-539 |
6.36e-20 |
|
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: 92.91 E-value: 6.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFdaTC- 87
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAkaGISASDIAAIGI--TNq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 88 --SLVVLDKQfhplpvnqEGDSHRNVIMWLDHRAVSQVNRINETKHS--VLQYVGGVMSVEMQAPKLLWLKEN---LREI 160
Cdd:cd07769 79 reTTVVWDKK--------TGKPLYNAIVWQDRRTADICEELKAKGLEerIREKTGLPLDPYFSATKIKWILDNvpgARER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 161 CwdKAGHF-FDLPD-FLSWKATG----VT-----ARSLcsLvckwtYSAEKG-WDDsfwkMIgLEDFvadnysKIGNQVL 228
Cdd:cd07769 151 A--ERGELlFGTIDtWLIWKLTGgkvhVTdvtnaSRTM--L-----FNIHTLeWDD----EL-LELF------GIPRSML 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 229 P---PGASLgNGLTPEAardlGLLPGIAVAASLIDAHAgglgvigADVrGHGLICEGQ------------------PVTS 287
Cdd:cd07769 211 PevrPSSEV-FGYTDPE----GLGAGIPIAGILGDQQA-------ALF-GQGCFEPGMakntygtgcfllmntgekPVPS 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 288 R---LAVICgtsschMGISKDP-------IFVPGvwgpyfSAMVpgfWLNEGGqsvtgKLIDHMvqghaafPELQvkata 357
Cdd:cd07769 278 KnglLTTIA------WQIGGKVtyalegsIFIAG------AAIQ---WLRDNL-----GLIEDA-------AETE----- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 358 rcqsiyaylnshlDLIKKAQPVGfltvDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRF 437
Cdd:cd07769 326 -------------ELARSVEDNG----GVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIV---RAALESIAYQTRD 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 438 IIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGdFASVQEAMAKMSKVGKV 516
Cdd:cd07769 386 VLEAMEKdSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVG-FWKDLDELASLWQVDKR 464
|
570 580
....*....|....*....|...
gi 164663828 517 VFPRLQDKKyYDKKYQVFLKLVE 539
Cdd:cd07769 465 FEPSMDEEE-RERLYRGWKKAVE 486
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
11-539 |
8.88e-18 |
|
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: 86.08 E-value: 8.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFdAT-- 86
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKnaGLTPEDIAAIGI-STqr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 87 CSLVVLDKQ----FHplpvnqegdshrNVIMWLDHRAVSQVNRINE-----------------TKH------SVLQYVGG 139
Cdd:cd07793 80 NTFLTWDKKtgkpLH------------NFITWQDLRAAELCESWNRslllkalrggskflhflTRNkrflaaSVLKFSTA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 140 vmsveMQAPKLLWLKENLREICWDKAGH---FFDLPDFLSWKATG----VTARSLCSLVckwtysaekGWDDSF---WKM 209
Cdd:cd07793 148 -----HVSIRLLWILQNNPELKEAAEKGellFGTIDTWLLWKLTGgkvhATDYSNASAT---------GLFDPFtleWSP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 210 IGLEDFvadnysKIGNQVLPPgaslgngltpeaardlgllpgiavaaslIDAHAGGLGVIGADVRGHGLicegqPVTsrl 289
Cdd:cd07793 214 ILLSLF------GIPSSILPE----------------------------VKDTSGDFGSTDPSIFGAEI-----PIT--- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 290 AVI-----------C---GTSSCHMGISkdpIFVPGVWGPYFSAMVPGF-----W--------LNEGGQSVTGKLIDHmv 342
Cdd:cd07793 252 AVVadqqaalfgecCfdkGDVKITMGTG---TFIDINTGSKPHASVKGLyplvgWkiggeityLAEGNASDTGTVIDW-- 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 343 qghaafpelqvkatarCQSIyAYLNSHLDLIKKAQPVGfLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAI 422
Cdd:cd07793 327 ----------------AKSI-GLFDDPSETEDIAESVE-DTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVR 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 423 lylATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFA 501
Cdd:cd07793 389 ---AILESIAFRVKQLLETMEKeTSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWK 465
|
570 580 590
....*....|....*....|....*....|....*...
gi 164663828 502 SVqEAMAKMSKVGKVVFPRlQDKKYYDKKYQVFLKLVE 539
Cdd:cd07793 466 SK-EELKKLRKIEKIFEPK-MDNEKREELYKNWKKAVK 501
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
9-539 |
6.81e-17 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 83.57 E-value: 6.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 9 ERYYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFD-- 84
Cdd:COG0554 2 KKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAkaGISAEDIAAIGITnq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 85 -ATCslVVLDKQF-HPLpvnqegdsHrNVIMWLDHRAVSQVNRINETKHS--VLQYVGGVMSVEMQAPKLLWLKEN---L 157
Cdd:COG0554 82 rETT--VVWDRKTgKPL--------Y-NAIVWQDRRTADICEELKADGLEdlIREKTGLVLDPYFSATKIKWILDNvpgA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 158 REicwdKA--GH-FFDLPD-FLSWKATG----VT-----ARSLCslvckwtYSAEKG-WDDSFwkmigLEDFvadnysKI 223
Cdd:COG0554 151 RE----RAeaGElLFGTIDsWLIWKLTGgkvhVTdvtnaSRTML-------FNIHTLdWDDEL-----LELF------GI 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 224 GNQVLP---PgaSLGN-GLTpeaarDLGLLP-GIAVAASLIDAHAgglgvigADVrGHGLICEG---------------- 282
Cdd:COG0554 209 PRSMLPevrP--SSEVfGET-----DPDLFGaEIPIAGIAGDQQA-------ALF-GQACFEPGmakntygtgcfllmnt 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 283 --QPVTSR---LAVICgtsschmgiskdpifvpgvWG----PYFsAMvpgfwlnEGGQSVTGKLIDhmvqghaafpelqv 353
Cdd:COG0554 274 gdEPVRSKnglLTTIA-------------------WGlggkVTY-AL-------EGSIFVAGAAVQ-------------- 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 354 katarcqsiyaYLNSHLDLIKKAQPVGFL--TVD----LHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAilyLAT 427
Cdd:COG0554 313 -----------WLRDGLGLIDSAAESEALarSVEdnggVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIA---RAA 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 428 VQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEa 506
Cdd:COG0554 379 LESIAYQTRDVLDAMEAdSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEE- 457
|
570 580 590
....*....|....*....|....*....|...
gi 164663828 507 MAKMSKVGKVVFPRLqDKKYYDKKYQVFLKLVE 539
Cdd:COG0554 458 LAALWKVDRRFEPQM-DEEERERLYAGWKKAVE 489
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
12-539 |
6.07e-16 |
|
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: 80.65 E-value: 6.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 12 YVG-VDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAAC--CV---VTKKVVQGIDLNQIRGLGFda 85
Cdd:cd07792 2 LVGaIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVyeCIeeaVEKLKALGISPSDIKAIGI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 86 TC---SLVVLDKQfhplpvnqEGDSHRNVIMWLDHRAVSQVNR-INETKHSVLQYV---GGVMSVEMQAPKLLWLKENLR 158
Cdd:cd07792 80 TNqreTTVVWDKS--------TGKPLYNAIVWLDTRTSDTVEElSAKTPGGKDHFRkktGLPISTYFSAVKLRWLLDNVP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 159 EI---------------CWdkaghffdlpdfLSWKATG----------VTARSLCSLV----CKWtysaekgwDDSFWKM 209
Cdd:cd07792 152 EVkkavddgrllfgtvdSW------------LIWNLTGgknggvhvtdVTNASRTMLMnlrtLQW--------DPELCEF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 210 IGLEDFV-------ADNYSKIGNqvlppgaslgngltpeaardlGLLPGIAVAASLIDAHAgglgvigADVrGHGLICEG 282
Cdd:cd07792 212 FGIPMSIlpeirssSEVYGKIAS---------------------GPLAGVPISGCLGDQQA-------ALV-GQGCFKPG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 283 Q------------------PVTSRlaviCG--TSSCH-MGISKDPIFvpgvwgpyfsAMvpgfwlnEGGQSVTGKLIDhm 341
Cdd:cd07792 263 EakntygtgcfllyntgeePVFSK----HGllTTVAYkLGPDAPPVY----------AL-------EGSIAIAGAAVQ-- 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 342 vqghaafpelqvkatarcqsiyaYLNSHLDLIKKAQPVGFL--TVD----LHVWPDFHGNRSPLADLTLKGMVTGLKLSQ 415
Cdd:cd07792 320 -----------------------WLRDNLGIISSASEVETLaaSVPdtggVYFVPAFSGLFAPYWRPDARGTIVGLTQFT 376
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 416 DLDDLAilyLATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGA 494
Cdd:cd07792 377 TKAHIA---RAALEAVCFQTREILDAMNKdSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAG 453
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 164663828 495 CASGDFASVQEAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 539
Cdd:cd07792 454 LAVGVWKSLDELKSLNEGGRTVFEPQISEEE-RERRYKRWKKAVE 497
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
11-540 |
6.16e-16 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 80.44 E-value: 6.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALVDQSGVLLAFADqpiKNW----EPQF-NHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLgf 83
Cdd:PRK10939 4 YLMALDAGTGSIRAVIFDLNGNQIAVGQ---AEWrhlaVPDVpGSMEFDLEKNWQLACQCIRQALQkaGIPASDIAAV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 84 dATCSL----VVLDKQFHPLpvnqegdshrnvimW----LDHRAVSQVNRINEtKHSVLQYvgGVMSVEMQA------PK 149
Cdd:PRK10939 79 -SATSMregiVLYDRNGTEI--------------WacanVDARASREVSELKE-LHNNFEE--EVYRCSGQTlalgalPR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 150 LLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTA--------RSLCSLVckwtysaEKGWDDSFWKMIGLEDfvadnys 221
Cdd:PRK10939 141 LLWLAHHRPDI-YRQAHTITMISDWIAYMLSGELAvdpsnagtTGLLDLV-------TRDWDPALLEMAGLRA------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 222 KIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGT------ 295
Cdd:PRK10939 206 DILPPVKETGTVLGH-VTAKAAAETGLRAGTPVVMGGGDVQLGCLGL--------GVVRPGQ-----TAVLGGTfwqqvv 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 296 ------SSCHMGISKDPIFVPGVWG----PYFSAMVpgfwlneggqsvtgklidhMVQGHAAF-PELQVKATARCQSIYA 364
Cdd:PRK10939 272 nlpapvTDPNMNIRINPHVIPGMVQaesiSFFTGLT-------------------MRWFRDAFcAEEKLLAERLGIDAYS 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 365 YLNshldliKKAQ--PVGFLTV-----DL-------HVWPDFhgnrspladltlkgmvtgLKLSQDLD--DLAILYLATV 428
Cdd:PRK10939 333 LLE------EMASrvPVGSHGIipifsDVmrfkswyHAAPSF------------------INLSIDPEkcNKATLFRALE 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 429 QAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAM 507
Cdd:PRK10939 389 ENAAIVSACNLQQIAAfSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSLAETG 468
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 164663828 508 AKMSKVGKVVFPRLQDKKYYDKK-------YQVFLKLVEH 540
Cdd:PRK10939 469 ERLVRWERTFEPNPENHELYQEAkekwqavYADQLGLVDH 508
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
11-490 |
3.05e-15 |
|
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: 78.03 E-value: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKNWEPQ--FNHHEQSSEDIWAAccvvTKKVVQGID---LNQIRGLGFD 84
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDlESGRILESVSRPTPAPISSddPGRSEQDPEKILEA----VRNLIDELPreyLSDVTGIGIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 85 AtcslvvldkQFHP-LPVNQEGDSHRNVIMWLDHRAvsqvnriNETKHSVLQYVGGVMSVEMQAP--------KLLWLKE 155
Cdd:cd07777 77 G---------QMHGiVLWDEDGNPVSPLITWQDQRC-------SEEFLGGLSTYGEELLPKSGMRlkpgyglaTLFWLLR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 156 NLREIcwDKAGHFFDLPDFLSWKATGvTARSLCSLVCK--WTY--SAEKGWDDSFWKMIGLEdfvadnySKIGNQVLPPG 231
Cdd:cd07777 141 NGPLP--SKADRAGTIGDYIVARLTG-LPKPVMHPTNAasWGLfdLETGTWNKDLLEALGLP-------VILLPEIVPSG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 232 ASLGNgLTPEAARDLGLLPGI-----AVAASLIDAHagglgvigadvrghglicegqpvtSRLAVICGTSScHMGISKDP 306
Cdd:cd07777 211 EIVGT-LSSALPKGIPVYVALgdnqaSVLGSGLNEE------------------------NDAVLNIGTGA-QLSFLTPK 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 307 IFVPGVWG--PYFSamvpGFWLNeggqSVT----GKLIDHMVQ-----GHAAFPELQVkatarcQSIYAYLNShLDLIKK 375
Cdd:cd07777 265 FELSGSVEirPFFD----GRYLL----VAAslpgGRALAVLVDflrewLRELGGSLSD------DEIWEKLDE-LAESEE 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 376 AQPvgfLTVDlhvwPDFHGNRSplaDLTLKGMVTGLklsqDLDDLAI--LYLATVQAIALGTRFIIEAMEAAGHSISTLF 453
Cdd:cd07777 330 SSD---LSVD----PTFFGERH---DPEGRGSITNI----GESNFTLgnLFRALCRGIAENLHEMLPRLDLDLSGIERIV 395
|
490 500 510
....*....|....*....|....*....|....*...
gi 164663828 454 LCGG-LSKNPLFVQMHADITGMPVVLSQEVESVLVGAA 490
Cdd:cd07777 396 GSGGaLRKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAA 433
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
12-526 |
3.28e-15 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 78.09 E-value: 3.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 12 YVG-VDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCvvtKKVVQGIDLNQIRGLGFDATC--- 87
Cdd:PTZ00294 3 YIGsIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVY---KCMNEAIKKLREKGPSFKIKAigi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 88 -----SLVVLDKQfhplpvnqEGDSHRNVIMWLDHRAVSQVNRINET--KHSVLQYVGG-VMSVEMQAPKLLWLKENLRE 159
Cdd:PTZ00294 80 tnqreTVVAWDKV--------TGKPLYNAIVWLDTRTYDIVNELTKKygGSNFFQKITGlPISTYFSAFKIRWMLENVPA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 160 IcwDKAGH-----FFDLPDFLSWKATG-------VTARSLCSLVCKWTYSaekgWDDSFWKMIGledfvadnyskIGNQV 227
Cdd:PTZ00294 152 V--KDAVKegtllFGTIDTWLIWNLTGgkshvtdVTNASRTFLMNIKTLK----WDEELLNKFG-----------IPKET 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 228 LP---PGASLGNGLTPEAArdlGLLPGIAVAASLIDAHAGGLGvigadvrgHGLICEGQPVTSRlavicGTSsCH--MGI 302
Cdd:PTZ00294 215 LPeikSSSENFGTISGEAV---PLLEGVPITGCIGDQQAALIG--------HGCFEKGDAKNTY-----GTG-CFllMNT 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 303 SKDPIFVP-GVWGpyfsamVPGFWLNEGGQSVtgklidHMVQGhaafpelqvkATARCQSIYAYLNSHLDLIKKAQPVGF 381
Cdd:PTZ00294 278 GTEIVFSKhGLLT------TVCYQLGPNGPTV------YALEG----------SIAVAGAGVEWLRDNMGLISHPSEIEK 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 382 L------TVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAME-AAGHSISTLFL 454
Cdd:PTZ00294 336 LarsvkdTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIV---RAALEAIALQTNDVIESMEkDAGIELNSLRV 412
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164663828 455 CGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKY 526
Cdd:PTZ00294 413 DGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVKKLIRRSNSTFSPQMSAEER 484
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
16-526 |
1.49e-14 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 76.22 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 16 DVGTGSVRAALVDQSGVLLAFADQP------IKNwePQFnhHEQSSEDIW---AACCvvtKKVVQGIDLNQIRGL----- 81
Cdd:PRK10331 8 DCGATNVRAIAVDRQGKIVARASTPnasdiaAEN--SDW--HQWSLDAILqrfADCC---RQINSELTECHIRGItvttf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 82 GFDATcslvvldkqfhplPVNQEGDSHRNVIMWLDHRAVSQVNRI-NETKHSVLQYVGGVMSVEMQAP-KLLWLKENLRE 159
Cdd:PRK10331 81 GVDGA-------------LVDKQGNLLYPIISWKCPRTAAVMENIeRYISAQQLQQISGVGAFSFNTLyKLVWLKENHPQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 160 IcWDKAGHFFDLPDFLSWKATGV--TARSLCSlVCKWTYSAEKGWDDSFWKMIGLEdfvadnyskigNQVLPP----GAS 233
Cdd:PRK10331 148 L-LEQAHAWLFISSLINHRLTGEftTDITMAG-TSQMLDIQQRDFSPEILQATGLS-----------RRLFPRlveaGEQ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 234 LGNgLTPEAARDLGLLPGIAVAASlidAHAGGLGVIGAdvrGHGLiceGQPV-----------------TSRLAVICGtS 296
Cdd:PRK10331 215 IGT-LQPSAAALLGLPVGIPVISA---GHDTQFALFGS---GAGQ---NQPVlssgtweilmvrsaqvdTSLLSQYAG-S 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 297 SCHMGiSKDPIFVPGVWgpyfsamvpgfWLNEGGQSVTGKLI-------DHMVQGHAAFPelqvkatARCQSIYayLNSH 369
Cdd:PRK10331 284 TCELD-SQSGLYNPGMQ-----------WLASGVLEWVRKLFwtaetpyQTMIEEARAIP-------PGADGVK--MQCD 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 370 LDLIKKAQPVGfLTVdlhvwpdfHGNRSPLADLTLKGMvtGLKLSQDLDDLailylatvqaialgtrfiieamEAAGH-S 448
Cdd:PRK10331 343 LLACQNAGWQG-VTL--------NTTRGHFYRAALEGL--TAQLKRNLQVL----------------------EKIGHfK 389
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164663828 449 ISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKY 526
Cdd:PRK10331 390 ASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQARAQMKYQYRYFYPQTEPEFI 467
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
426-539 |
1.87e-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: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 426 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 504
Cdd:cd07786 374 AALESIAYQTRDLLEAMEAdSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLD 453
|
90 100 110
....*....|....*....|....*....|....*
gi 164663828 505 EAmAKMSKVGKVVFPRLqDKKYYDKKYQVFLKLVE 539
Cdd:cd07786 454 EL-AKLWQVDRRFEPSM-SEEEREALYAGWKKAVK 486
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
426-540 |
6.42e-12 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 67.93 E-value: 6.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 426 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 504
Cdd:PRK00047 380 ATLESIAYQTRDVLDAMQAdSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLD 459
|
90 100 110
....*....|....*....|....*....|....*.
gi 164663828 505 EaMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVEH 540
Cdd:PRK00047 460 E-LKEQWKIDRRFEPQMDEEE-REKLYAGWKKAVKR 493
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
11-506 |
8.25e-09 |
|
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.
Pssm-ID: 466791 [Multi-domain] Cd Length: 460 Bit Score: 57.92 E-value: 8.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 11 YYVGVDVGTGSVRAALV--DQSGVLLA----FADQPIKN-----WEpqFNHheqssedIWAACCVVTKKVVQgiDLNQIR 79
Cdd:cd07771 1 NYLAVDLGASSGRVILGslDGGKLELEeihrFPNRPVEInghlyWD--IDR-------LFDEIKEGLKKAAE--QGGDID 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 80 GLGFDAT-CSLVVLDKQFHPL--PVnqegdSHRN---------VIMWLDHRAV-----SQVNRINetkhSVLQyvggvms 142
Cdd:cd07771 70 SIGIDTWgVDFGLLDKNGELLgnPV-----HYRDprtegmmeeLFEKISKEELyertgIQFQPIN----TLYQ------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 143 vemqapkLLWLKENLREIcWDKAGHFFDLPDFLSWKATG--VTARSLCSlvckwT---YSAEKG-WDDSFWKMIGLEdfv 216
Cdd:cd07771 134 -------LYALKKEGPEL-LERADKLLMLPDLLNYLLTGekVAEYTIAS-----TtqlLDPRTKdWSEELLEKLGLP--- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 217 adnySKIGNQVLPPGASLGNgLTPEAARDLGL--LPGIAVA----ASLIDAhagglgvIGADVRGHGLICegqpvtsrla 290
Cdd:cd07771 198 ----RDLFPPIVPPGTVLGT-LKPEVAEELGLkgIPVIAVAshdtASAVAA-------VPAEDEDAAFIS---------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 291 viCGTSSChMGI-SKDPIFVPgvwgpyfSAMVPGFwLNEGG--------QSVTGkLidHMVQghaafpEL--QVKATARC 359
Cdd:cd07771 256 --SGTWSL-IGVeLDEPVITE-------EAFEAGF-TNEGGadgtirllKNITG-L--WLLQ------ECrrEWEEEGKD 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 360 QSiYAYLNShldLIKKAQPVGFLtVDlhvwPD---FhgnRSPladltlKGMV---------TGLKLSQDLDDLA-ILYla 426
Cdd:cd07771 316 YS-YDELVA---LAEEAPPFGAF-ID----PDdprF---LNP------GDMPeairaycreTGQPVPESPGEIArCIY-- 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 427 tvQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSqEVESVLVGAAVLGACASGDFASVQE 505
Cdd:cd07771 376 --ESLALKYAKTIEELEElTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAG-PVEATAIGNLLVQLIALGEIKSLEE 452
|
.
gi 164663828 506 A 506
Cdd:cd07771 453 G 453
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
15-492 |
1.18e-08 |
|
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: 57.27 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 15 VDVGTGSVRAALVDQSGVLLAFADQPIKN-WEPQFNHHEqsSEDIWAAccvVTKKVVQGIDLNQIRGLGFdaTC---SLV 90
Cdd:cd07772 5 FDIGKTNKKLLLFDENGEVLAERSTPNPEiEEDGYPCED--VEAIWEW---LLDSLAELAKRHRIDAINF--TThgaTFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 91 VLDKQFHP-LPV---NQEGDShrnvimWLDHRAVSQVNRINETKHSVLqyvGGVMSVEMQapkLLWLKENLREIcWDKAG 166
Cdd:cd07772 78 LLDENGELaLPVydyEKPIPD------EINEAYYAERGPFEETGSPPL---PGGLNLGKQ---LYWLKREKPEL-FARAK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 167 HFFDLPDFLSWKATGVTARSLCSLVC--------KWTYS---AEKGWDDSFWKMigledfvadnyskignqvLPPGASLG 235
Cdd:cd07772 145 TILPLPQYWAWRLTGKAASEITSLGChtdlwdfeKNEYSslvKKEGWDKLFPPL------------------RKAWEVLG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 236 NgLTPEAARDLGLLPGIAVAASLIDAHAgglgvigadvrghglicegqpvtSRLAvicgtsscHMGISKDPiFV---PGV 312
Cdd:cd07772 207 P-LRPDLARRTGLPKDIPVGCGIHDSNA-----------------------ALLP--------YLAAGKEP-FTllsTGT 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 313 WgpyFSAMVPGF-----WLNEG-----GQSVTGKLIdhmvqGHAAFP-----ELQVKataRCQSIYAYLNSHLDLIKkaq 377
Cdd:cd07772 254 W---CIAMNPGNdlpltELDLArdclyNLDVFGRPV-----KTARFMggreyERLVE---RIAKSFPQLPSLADLAK--- 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 378 pvgFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATVQAIALgtrfiieamEAAGHSISTLFLCGG 457
Cdd:cd07772 320 ---LLARGTFALPSFAPGGGPFPGSGGRGVLSAFPSAEEAYALAILYLALMTDYAL---------DLLGSGVGRIIVEGG 387
|
490 500 510
....*....|....*....|....*....|....*.
gi 164663828 458 LSKNPLFVQMHADI-TGMPVVLSQEVESVLVGAAVL 492
Cdd:cd07772 388 FAKNPVFLRLLAALrPDQPVYLSDDSEGTALGAALL 423
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
12-539 |
5.41e-08 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 55.48 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 12 YVG-VDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAAccvVTKKVVQGIDLNQIRGLGFDATCSLV 90
Cdd:PLN02295 1 FVGaIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILES---VLTCIAKALEKAAAKGHNVDSGLKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 91 VLDKQFHPLPV--NQEGDSHRNVIMWLDHRAVSQVNRINETKHSV----LQYVGGVMSVEMQAPKLLWLKENLREICWD- 163
Cdd:PLN02295 78 GITNQRETTVAwsKSTGRPLYNAIVWMDSRTSSICRRLEKELSGGrkhfVETCGLPISTYFSATKLLWLLENVDAVKEAv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 164 KAGH--FFDLPDFLSWKATGVTARSL----CSLVCKWTYSAEKG--WDDSFwkmigLEDFvadnysKIGNQVLP---PGA 232
Cdd:PLN02295 158 KSGDalFGTIDSWLIWNLTGGASGGVhvtdVTNASRTMLMNLKTldWDKPT-----LEAL------GIPAEILPkivSNS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 233 SLGNGLTPEaardlGLLPGIAVAASLIDAHAGGLGvigadvrghglicegqpvtsrlavicgtSSCHMGISKDpIFVPGV 312
Cdd:PLN02295 227 EVIGTIAKG-----WPLAGVPIAGCLGDQHAAMLG----------------------------QRCRPGEAKS-TYGTGC 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 313 WgpyfsaMVpgfwLNEGGQSVTGKlidhmvqgHAAFPELQVKATARCQSIYA-------------YLNSHLDLIKKAQPV 379
Cdd:PLN02295 273 F------IL----LNTGEEVVPSK--------HGLLTTVAYKLGPDAPTNYAlegsvaiagaavqWLRDNLGIIKSASEI 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 380 GFL--TVD----LHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAM------EAAGH 447
Cdd:PLN02295 335 EALaaTVDdtggVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIA---RAVLESMCFQVKDVLDAMrkdageEKSHK 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 448 SISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKyY 527
Cdd:PLN02295 412 GLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEEEIFASEKWKNTTTFRPKLDEEE-R 490
|
570
....*....|..
gi 164663828 528 DKKYQVFLKLVE 539
Cdd:PLN02295 491 AKRYASWCKAVE 502
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
446-529 |
1.74e-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: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663828 446 GHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKV----GKVVFPRL 521
Cdd:cd07776 423 DIPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVVFSaeepKLVAEPDP 502
|
....*...
gi 164663828 522 QDKKYYDK 529
Cdd:cd07776 503 EAAEVYDK 510
|
|
| |
