|
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 ... |
11-568 |
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: 989.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDATCS 88
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEgaGVDPEQVKGIGFDATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 89 LVVLDKQFHPLPVNQEGDSHRNVIMWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLREiCWDKAGHF 168
Cdd:cd07782 81 LVVLDAEGKPVSVSPSGDDERNVILWMDHRAVEEAERINATGHEVLKYVGGKISPEMEPPKLLWLKENLPE-TWAKAGHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 169 FDLPDFLSWKATGVTARSLCSLVCKWTYSA----EKGWDDSFWKMIGLEDFVADNYSKIGNQVLPPGASLGNGLTPEAAR 244
Cdd:cd07782 160 FDLPDFLTWKATGSLTRSLCSLVCKWTYLAhegsEGGWDDDFFKEIGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 245 DLGLLPGIAVAASLIDAHAGGLGVIGADVrgHGLICEGQPVTSRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGF 324
Cdd:cd07782 240 ELGLPEGTPVGVSLIDAHAGGLGTLGADV--GGLPCEADPLTRRLALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 325 WLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNSHLDLIKKAQ--PVGFLTVDLHVWPDFHGNRSPLADL 402
Cdd:cd07782 318 WLNEGGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNERLEQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 403 TLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGL 482
Cdd:cd07782 398 TLRGM------------------------ISGLTLDTSLDDLALLYLATLQALAYGTRHIIEAMNAAGHKIDTIFMCGGL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 483 SKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKLV 562
Cdd:cd07782 454 SKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDAMAAMSGPGKVVEPNEELKKYHDRKYEVFLKMY 533
|
....*.
gi 1370453747 563 EHQKEY 568
Cdd:cd07782 534 EDQREY 539
|
|
| 5C_CHO_kinase |
TIGR01315 |
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ... |
11-568 |
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: 663.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVV--QGIDLNQIRGLGFDATCS 88
Cdd:TIGR01315 1 HYIGVDVGTGSARACIIDSTGDILALAAQNIKTWTPSSGLEGQSSVYIWQAICNCVKQVLaeSKVDPNSVKGIGFDATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 89 LVVLDKQFHPLPVNQEGDSHRNVIMWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHF 168
Cdd:TIGR01315 81 LVVLTHDGEPLPVSKNGGADQNIILWMDHRALAEAEKINATNHNLLRYVGGKMSVEMEIPKVLWLKNNMPPE-LFARCKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 169 FDLPDFLSWKATGVTARSLCSLVCKWTY----SAEKGWDDSFWKMIGLEDFVADNYSKIGNQVLPPGASLGNGLTPEAAR 244
Cdd:TIGR01315 160 FDLTDFLTWRATGKEIRSFCSVVCKWGFvpvdGSNKGWQEDFYETIGLGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 245 DLGLLPGIAVAASLIDAHAGGLGVIGADVRGHGLICEGQpvtSRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGF 324
Cdd:TIGR01315 240 ELGLPAGTAVGSGLIDAHAGWIGTVGAKVAENGDVSQAF---TRLAAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 325 WLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNSHLdLIKKAQP----VGFLTVDLHVWPDFHGNRSPLA 400
Cdd:TIGR01315 317 WLAEGGQSAAGELMDHMLETHVAYDETVKEAEAAGKNIYDYLNEHL-KEMAAKTnapsISYLVRHFHVYPDLWGNRSPIA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 401 DLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCG 480
Cdd:TIGR01315 396 DPNMRGV------------------------IIGLSMDRSKDGLALLYYATMEFIAYGTRQIVEAMNTAGHTIKSIFMSG 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 481 GLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQ-DKKYYDKKYQVFL 559
Cdd:TIGR01315 452 GQCQNPLLMQLIADACDMPVLIPYVNEAVLHGAAMLGAKAAGTTESLWDAMDRMSKPGKTVWPRGDpAKKLHDRKYEIFL 531
|
....*....
gi 1370453747 560 KLVEHQKEY 568
Cdd:TIGR01315 532 QLARTQQEY 540
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
9-568 |
0e+00 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 588.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 9 ERYYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKNWEP---------QFnhhEQSSEDIWAACCVVTKKVVQ--GIDLN 76
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDaADGEELASAVHPYPRWVIglylppppdQA---RQHPLDYLEALEAAVREALAqaGVDPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 77 QIRGLGFDAT-CSLVVLDKQFHPLPVNQE--GDSHRNVIMWLDHRAVSQVNRINE----TKHSVLQYVGGVMSVEMQAPK 149
Cdd:COG1069 78 DVVGIGVDATgCTPVPVDADGTPLALLPEfaENPHAMVILWKDHTAQEEAERINElakaRGEDYLRYVGGIISSEWFWPK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 150 LLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGW-DDSFWKMIGLE-DFVADnysKIGNQ 226
Cdd:COG1069 158 ILHLLREDPEV-YEAADSFVELCDWITWQLTGSLKRSRCTAGHKALWHAhEGGYpSEEFFAALDPLlDGLAD---RLGTE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 227 VLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIGadvrghglICEGQpvtsrLAVICGTSSCHMGISKDP 306
Cdd:COG1069 234 IYPLGEPAGT-LTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGG--------VEPGT-----LVKVMGTSTCHMLVSPEE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 307 IFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNshldliKKAQPVGFLTVDL 386
Cdd:COG1069 300 RFVPGICGQVDGSIVPGMWGYEAGQSAVGDIFAWFVRLLVPPLEYEKEAEERGISLHPLLT------EEAAKLPPGESGL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 387 HVWPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDlaiLYLATVQAIALGTRFIIEAM 466
Cdd:COG1069 374 HALDWFNGNRSPLADQRLKGV------------------------ILGLTLGTDAED---IYRALVEATAFGTRAIIERF 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 467 EAAGHSISTLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKV-GKVVFPR 544
Cdd:COG1069 427 EEEGVPIDEIIACGGIAtKNPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMAAMGSGfDKVYTPD 506
|
570 580
....*....|....*....|....
gi 1370453747 545 LQDKKYYDKKYQVFLKLVEHQKEY 568
Cdd:COG1069 507 PENVAVYDALYAEYLQLHDYFGRG 530
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
11-558 |
3.52e-150 |
|
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: 442.06 E-value: 3.52e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 11 YYVGVDVGTGSVRAALVDQS-GVLLAFADQPIKNWE-PQFNHHEQSSEDIWAACCVVTKKVV--QGIDLNQIRGLGFDAT 86
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDLYaGLEMAQEPVPYYQDSsKKSWKFWQKSTEIIKALQKCVQKLNirEGVDAYEVKGCGVDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 87 CSLVVLDKQFHPLPVNQEGDSHRNVIMWLDHRAVSQVNRINETKHSVLQ-YVGGVMSVEMQAPKLLWLKENLREIcWDKA 165
Cdd:cd07768 81 CSLAIFDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWINMQCPQQLLdYLGGKISPEMGVPKLKYFLDEYSHL-RDKH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 166 GHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGWDDSFWKMIGLEDfVADNYSKIGNQVLPPGASLGNGLtPEAAR 244
Cdd:cd07768 160 FHIFDLHDYIAYELTRLYEWNICGLLGKENLDGeESGWSSSFFKNIDPRL-EHLTTTKNLPSNVPIGTTSGVAL-PEMAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 245 DLGLLPGIAVAASLIDAHAGGLGVIGADVRGhglicegqpvtsRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGF 324
Cdd:cd07768 238 KMGLHPGTAVVVSCIDAHASWFAVASPHLET------------SLFMIAGTSSCHMYGTTISDRIPGVWGPFDTIIDPDY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 325 WLNEGGQSVTGKLIDHMVQGHAAFPELqVKATARCQSIYAYLNshlDLIKKAQPVGFLTVDLHVWPDFHGNRSPLADLTL 404
Cdd:cd07768 306 SVYEAGQSATGKLIEHLFESHPCARKF-DEALKKGADIYQVLE---QTIRQIEKNNGLSIHILTLDMFFGNRSEFADPRL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 405 KGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSK 484
Cdd:cd07768 382 KGS------------------------FIGESLDTSMLNLTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAK 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370453747 485 NPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFA---SVQEAMAKMSKVGKVVFPRLQD-KKYYDKKYQVF 558
Cdd:cd07768 438 NERLLQLIALVTNVAIIKPKENMMGILGAAVLAKVAAGKKQladSITEADISNDRKSETFEPLAYRlGADYILLYKLL 515
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
11-561 |
3.75e-147 |
|
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: 433.50 E-value: 3.75e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 11 YYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKNWE--PQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDA 85
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAeaGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 86 TCSLVVldkqfhplPVNQEGDSHRNVIMWLDHRAVSQVNRINETKHSV----LQYVGGVMSVEMQAPKLLWLKENLREIc 161
Cdd:cd07781 81 TSSTVV--------PVDEDGNPLAPAILWMDHRAQEEAAEINETAHPAleyyLAYYGGVYSSEWMWPKALWLKRNAPEV- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 162 WDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEDfvADNYSKIGNQVLPPGASLGnGLTP 240
Cdd:cd07781 152 YDAAYTIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGgPPREFLAALDPGL--LKLREKLPGEVVPVGEPAG-TLTA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 241 EAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFSAM 320
Cdd:cd07781 229 EAAERLGLPAGIPVAQGGIDAHMGAIGA--------GVVEPGT-----LALIMGTSTCHLMVSPKPVDIPGICGPVPDAV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 321 VPGFWLNEGGQSVTGKLIdhmvqghAAFPELQVKATA-RCQSIYAYLNshlDLIKKAQPV--GFLTVDlhvWpdFHGNRS 397
Cdd:cd07781 296 VPGLYGLEAGQSAVGDIF-------AWFVRLFVPPAEeRGDSIYALLS---EEAAKLPPGesGLVALD---W--FNGNRT 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 398 PLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLddlAILYLATVQAIALGTRFIIEAMEAAGHSISTLF 477
Cdd:cd07781 361 PLVDPRLRGA------------------------IVGLTLGTTP---AHIYRALLEATAFGTRAIIERFEEAGVPVNRVV 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 478 LCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQ 556
Cdd:cd07781 414 ACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVAAGVYADIEEAADAMVRVDRVYEPDPENHAVYEELYA 493
|
....*
gi 1370453747 557 VFLKL 561
Cdd:cd07781 494 LYKEL 498
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
10-567 |
1.54e-97 |
|
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: 305.60 E-value: 1.54e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 10 RYYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDAT- 86
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAkaGVDPEEIAAIGVSGQm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 87 CSLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINET--KHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDK 164
Cdd:COG1070 81 HGLVLLDADGEPL---------RPAILWNDTRAAAEAAELREElgEEALYEITGNPLHPGFTAPKLLWLKENEPEI-FAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 165 AGHFFDLPDFLSWKATG--VTARSLCSlvckWT--YSAEKG-WDDSFWKMIGL-EDFVAdnyskignQVLPPGASLGnGL 238
Cdd:COG1070 151 IAKVLLPKDYLRYRLTGefVTDYSDAS----GTglLDVRTRdWSDELLEALGIdRELLP--------ELVPPGEVAG-TL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 239 TPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFS 318
Cdd:COG1070 218 TAEAAAETGLPAGTPVVAGAGDNAAAALGA--------GAVEPGD-----AAVSLGTSGVVFVVSDKPLPDPEGRVHTFC 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 319 AMVPGFWLNEGGQSVTGKLIDHMVQghaafpelqvKATARCQSIYAYLNshlDLIKKAqPVG-----FLtvdlhvwPDFH 393
Cdd:COG1070 285 HAVPGRWLPMGATNNGGSALRWFRD----------LFADGELDDYEELN---ALAAEV-PPGadgllFL-------PYLS 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 394 GNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSI 473
Cdd:COG1070 344 GERTPHWDPNARGA------------------------FFGLTLSHTRAHL---ARAVLEGVAFALRDGLEALEEAGVKI 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 474 STLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDK 553
Cdd:COG1070 397 DRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMVRVGETIEPDPENVAAYDE 476
|
570
....*....|....
gi 1370453747 554 KYQVFLKLVEHQKE 567
Cdd:COG1070 477 LYERYRELYPALKP 490
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
9-572 |
9.23e-84 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 271.33 E-value: 9.23e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 9 ERYYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKNW---------EPQFNHHEQSSEDIWAAccvVTKKVVQ--GIDLN 76
Cdd:PRK04123 2 MAYVIGLDFGTDSVRALLVDcATGEELATAVVEYPHWvkgryldlpPNQALQHPLDYIESLEA---AIPAVLKeaGVDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 77 QIRGLGFDAT-CSLVVLDKQFHPLPVNQEGDSHRN--VIMWLDHRAVSQVNRINETKHS-----VLQYVGGVMSVEMQAP 148
Cdd:PRK04123 79 AVVGIGVDFTgSTPAPVDADGTPLALLPEFAENPHamVKLWKDHTAQEEAEEINRLAHErgeadLSRYIGGIYSSEWFWA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 149 KLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTA-----RSLCSLVCKWTYSAEKG--WDDSFWKMI--GLEDFVADn 219
Cdd:PRK04123 159 KILHVLREDPAV-YEAAASWVEACDWVVALLTGTTDpqdivRSRCAAGHKALWHESWGglPSADFFDALdpLLARGLRD- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 220 ysKIGNQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGglgVIGADVRGHGLicegqpvtsrLAVIcGTSSCH 299
Cdd:PRK04123 237 --KLFTETWTAGEPAG-TLTAEWAQRLGLPEGVAVSVGAFDAHMG---AVGAGAEPGTL----------VKVM-GTSTCD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 300 MGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQgHAAFPELQVKATARCQSIYAYLNshldliKKA--Q 377
Cdd:PRK04123 300 ILLADKQRAVPGICGQVDGSIVPGLIGYEAGQSAVGDIFAWFAR-LLVPPEYKDEAEARGKQLLELLT------EAAakQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 378 PVG---FLTVDlhvWpdFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLailYLATVQA 454
Cdd:PRK04123 373 PPGehgLVALD---W--FNGRRTPLADQRLKGV------------------------ITGLTLGTDAPDI---YRALIEA 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 455 IALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAK 533
Cdd:PRK04123 421 TAFGTRAIMECFEDQGVPVEEVIAAGGIArKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEAQQA 500
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1370453747 534 M-SKVGKVVFPRLQDKKYYDKKYQVFLKLVE-HQKEYLAIM 572
Cdd:PRK04123 501 MaSPVEKTYQPDPENVARYEQLYQEYKQLHDyFGRGGNAVM 541
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
12-521 |
1.70e-78 |
|
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: 257.33 E-value: 1.70e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 12 YVGVDVGTGSVRAALVDQSGVLLAFADQPI--KNWEPQFNHHEQSSEDIWAACCVVTKKVVQGIDLNQIRGLGFDATCSL 89
Cdd:cd07778 2 GIGIDVGSTSVRIGIFDYHGTLLATSERPIsyKQDPKDLWFVTQSSTEIWKAIKTALKELIEELSDYIVSGIGVSATCSM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 90 VVLDKQ-----FHPLPVNQE-GDSHRNVIMWLDHRAVSQVNRINE-TKHSVLQYVGGVMSVEMQAPKLLWLKENLREICW 162
Cdd:cd07778 82 VVMQRDsdtsyLVPYNVIHEkSNPDQDIIFWMDHRASEETQWLNNiLPDDILDYLGGGFIPEMAIPKLKYLIDLIKEDTF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 163 DKAgHFFDLPDFLSWKatgvtarsLCSLVCKW--TYSAE------------KGWDDSFWKMIGLEDFVAD--NYSKIGNQ 226
Cdd:cd07778 162 KKL-EVFDLHDWISYM--------LATNLGHSniVPVNAppsigigidgslKGWSKDFYSKLKISTKVCNvgNTFKEAPP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 227 VLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghglICEGQPVTSRLAVICGTSSCHMGISKDP 306
Cdd:cd07778 233 LPYAGIPIGK-VNVILASYLGIDKSTVVGHGCIDCYAGWFST----------FAAAKTLDTTLFMVAGTSTCFLYATSSS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 307 I--FVPGVWGPyFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATarcqSIYAYLNSHLDLI--KKAQPVGFL 382
Cdd:cd07778 302 QvgPIPGIWGP-FDQLLKNYSVYEGGQSATGKLIEKLFNSHPAIIELLKSDA----NFFETVEEKIDKYerLLGQSIHYL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 383 TVDLHVWPDFHGNRSPLADltlkgmrttgylyipalaalhspssllsPQVTG--LKLSQD--LDDLAILYLATVQAIALG 458
Cdd:cd07778 377 TRHMFFYGDYLGNRTPYND----------------------------PNMSGsfIGESTDssLTDLVLKYILILEFLAFQ 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370453747 459 TRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVV---LSQEVESVLVGAAVLGACAS 521
Cdd:cd07778 429 TKLIIDNFQKEKIIIQKVVISGSQAKNARLLQLLSTVLSKIHIivpLSDSKYAVVKGAALLGKAAF 494
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
11-559 |
1.33e-75 |
|
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: 248.20 E-value: 1.33e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDAT-C 87
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEksGIDPSDIAAIAFSGQmQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 88 SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINET---KHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDK 164
Cdd:cd07805 81 GVVPVDKDGNPL---------RNAIIWSDTRAAEEAEEIAGGlggIEGYRLGGGNPPSGKDPLAKILWLKENEPEI-YAK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 165 AGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEDfvadnySKIgNQVLPPGASLGnGLTPEAA 243
Cdd:cd07805 151 THKFLDAKDYLNFRLTGRAATDPSTASTTGLMDLRKRrWSEELLRAAGIDP------DKL-PELVPSTEVVG-ELTPEAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 244 RDLGLLPGIAVAASLIDAHAGGLGViGADVRGHGLICegqpvtsrlaviCGTSS---CHmgiSKDPIFVPGvwGPYFS-- 318
Cdd:cd07805 223 AELGLPAGTPVVGGGGDAAAAALGA-GAVEEGDAHIY------------LGTSGwvaAH---VPKPKTDPD--HGIFTla 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 319 AMVPGFWLNEGGQSVTGKLIDHMVQgHAAFPELQVKatarcqSIYAYLNshlDLIKKAQP----VGFLtvdlhvwPDFHG 394
Cdd:cd07805 285 SADPGRYLLAAEQETAGGALEWARD-NLGGDEDLGA------DDYELLD---ELAAEAPPgsngLLFL-------PWLNG 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 395 NRSPLADLTLKGMrttgylYIpalaalhspssllspqvtGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEAAGHSIS 474
Cdd:cd07805 348 ERSPVEDPNARGA------FI------------------GLSLEHTRADLA---RAVLEGVAFNLRWLLEALEKLTRKID 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 475 TLFLCGGLSKNPLFVQMHADITGMPV-VLSQEVESVLVGAAVLGACASGDFASVQEAmAKMSKVGKVVFPRLQDKKYYDK 553
Cdd:cd07805 401 ELRLVGGGARSDLWCQILADVLGRPVeVPENPQEAGALGAALLAAVGLGLLKSFDEA-KALVKVEKVFEPDPENRARYDR 479
|
....*.
gi 1370453747 554 KYQVFL 559
Cdd:cd07805 480 LYEVFK 485
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
11-561 |
1.12e-70 |
|
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: 235.13 E-value: 1.12e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVV--QGIDLNQIRGLGFDA-TC 87
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLakAGISPSDIAAIGLTGqMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 88 SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINET-KHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAG 166
Cdd:cd07808 81 GLVLLDKNGRPL---------RPAILWNDQRSAAECEELEARlGDEILIITGNPPLPGFTLPKLLWLKENEPEI-FARIR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 167 HFFdLP-DFLSWKATGVTAR-------SLCslvckwtYSAEKG-WDDSFWKMIGLEdfvadnyskigNQVLPP---GASL 234
Cdd:cd07808 151 KIL-LPkDYLRYRLTGELATdpsdasgTLL-------FDVEKReWSEELLEALGLD-----------PSILPPiveSTEI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 235 GNGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPV----TSrlAVICGTSSCHMGISKDPIF-- 308
Cdd:cd07808 212 VGTLTPEAAEELGLPEGTPVVAGAGDNAAAALGA--------GVVEPGDALislgTS--GVVFAPTDKPVPDPKGRLHtf 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 309 ---VPGVW---GPYFSAmvpGF---WLNE--GGQSVTGKLIDHMVQGHAAfpelqvkatarcqsiyaylnshldlikKAQ 377
Cdd:cd07808 282 phaVPGKWyamGVTLSA---GLslrWLRDlfGPDRESFDELDAEAAKVPP---------------------------GSE 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 378 PVGFLtvdlhvwPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLAilyLATVQAIAL 457
Cdd:cd07808 332 GLLFL-------PYLSGERTPYWDPNARGS------------------------FFGLSLSHTRAHLA---RAVLEGVAF 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 458 GTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKV 537
Cdd:cd07808 378 SLRDSLEVLKELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACIKI 457
|
570 580
....*....|....*....|....
gi 1370453747 538 GKVVFPRLQDKKYYDKKYQVFLKL 561
Cdd:cd07808 458 EKTIEPDPERHEAYDELYARYREL 481
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
11-551 |
8.52e-68 |
|
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: 225.86 E-value: 8.52e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDAT-C 87
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAkaGVDPEDIAAIGLTSQrS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 88 SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVsqvnrinetkhsvlqyvggvmsvemqapkllwlkenlreicwdkagH 167
Cdd:cd07779 81 TFVPVDEDGRPL---------RPAISWQDKRTA----------------------------------------------K 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 168 FFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEdfvADNYSKIgnqvLPPGASLGNgLTPEAARDL 246
Cdd:cd07779 106 FLTVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRdWSDDLLDAFGID---RDKLPEL----VPPGTVIGT-LTKEAAEET 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 247 GLLPGIAVAASlidAHAGGLGVIGADVRGHGLICegqpvtsrlaVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWL 326
Cdd:cd07779 178 GLPEGTPVVAG---GGDQQCAALGAGVLEPGTAS----------LSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWV 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 327 NEGGQSVTGKLIDHMVQghaAFPELQVKATARCQSIYAYLNSHLDLIkkaqPVGFLtvDLHVWPDFHGNRSPLADLTLKG 406
Cdd:cd07779 245 LEGSINTGGSAVRWFRD---EFGQDEVAEKELGVSPYELLNEEAAKS----PPGSD--GLLFLPYLAGAGTPYWNPEARG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 407 MrttgylyipalaalhspssllspqVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNP 486
Cdd:cd07779 316 A------------------------FIGLTLSHTRAHL---ARAILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGSKSD 368
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370453747 487 LFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYY 551
Cdd:cd07779 369 LWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAMVRVTDTFEPDPENVAIY 433
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
11-518 |
1.38e-63 |
|
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: 214.78 E-value: 1.38e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQGIDLNQIRGLGFDATC-SL 89
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPRRVVAIAVDGTSgTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 90 VVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFF 169
Cdd:cd07783 81 VLVDREGEPL---------RPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEV-LAKTAKFL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 170 DLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEdfvadnySKIGNQVLPPGASLGNgLTPEAARDLGL 248
Cdd:cd07783 151 HQADWLAGRLTGDRGVTDYNNALKLGYDPETGrWPSWLLALLGIP-------PDLLPRVVAPGTVIGT-LTAEAAEELGL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 249 LPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVTSrlaviCGTSSCHMGISKDPIFVPGVwGPYFSAMVPGFWLNE 328
Cdd:cd07783 223 PAGTPVVAGTTDSIAAFLAS--------GAVRPGDAVTS-----LGTTLVLKLLSDKRVPDPGG-GVYSHRHGDGYWLVG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 329 GGQSVTGKLIDHmvqghaAFPELQVKAtarcqsiyaylnshldLIKKAQPVGflTVDLHVWP-DFHGNRSPLADltlkgm 407
Cdd:cd07783 289 GASNTGGAVLRW------FFSDDELAE----------------LSAQADPPG--PSGLIYYPlPLRGERFPFWD------ 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 408 rttgylyipalaalhspssllsPQVTGLKLSQDLDDlAILYLATVQAIALGTRFIIEAMEAAGHS-ISTLFLCGGLSKNP 486
Cdd:cd07783 339 ----------------------PDARGFLLPRPHDR-AEFLRALLEGIAFIERLGYERLEELGAPpVEEVRTAGGGARND 395
|
490 500 510
....*....|....*....|....*....|..
gi 1370453747 487 LFVQMHADITGMPVVLSQEVESVLvGAAVLGA 518
Cdd:cd07783 396 LWNQIRADVLGVPVVIAEEEEAAL-GAALLAA 426
|
|
| L-ribulokinase |
TIGR01234 |
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely ... |
11-569 |
1.91e-60 |
|
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: 209.40 E-value: 1.91e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 11 YYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKNWE--------------PQFNHHEQSSEDIWAAccvVTKKVVQ--GI 73
Cdd:TIGR01234 2 YAIGVDFGTLSGRALAVDvATGEEIATAVEWYRHWVkgqflpktgaklpnDQALQHPADYIEVLEA---AIPTVLAelGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 74 DLNQIRGLGFDAT-CSLVVLDKQFHPLPVNQE--GDSHRNVIMWLDHRAVSQVNRINETKHS----VLQYVGGVMSVEMQ 146
Cdd:TIGR01234 79 DPADVVGIGVDFTaCTPAPIDSDGNPLCLLPEfaENPHAYFKLWKHHAAQEEADRINRLAHApgevDLSRYGGIISSEWF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 147 APKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKGW-DDSFWKMI--GLEDFVADNYSK- 222
Cdd:TIGR01234 159 WAKILQITEEDPAI-YQAADRWIELADWIVAQLSGDIRRGRCTAGYKALWHESWGYpSASFFDELnpILNRHLPDKLFTd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 223 IGNQVLPPGAslgngLTPEAARDLGLLPGIAVAASLIDAHaggLGVIGADVrghgliceGQPvtSRLAVICGTSSCHMGI 302
Cdd:TIGR01234 238 IWTAGEPAGT-----LTPEWAQRTGLPEGVVVAVGNFDAH---VGAVAAGI--------AQP--GALVKIMGTSTCHVLI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 303 SKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQgHAAFPELQVKATARCQSiyayLNSHLDLIKKAQPV--- 379
Cdd:TIGR01234 300 GDKQRAVPGMCGVVDGGIVPGFIGYEAGQSAVGDIFAWFGK-VCVPPELKTEANASQKQ----LHEALSEAAAKQPSgeh 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 380 GFLTVDlhvWpdFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDlaiLYLATVQAIALGT 459
Cdd:TIGR01234 375 GLVALD---W--FNGNRSPLVDQRLKGV------------------------ITGLTLATDAPL---LYRALIEATAFGT 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 460 RFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVG 538
Cdd:TIGR01234 423 RMIMETFTDSGVPVEELMAAGGIArKNPVIMQIYADVTNRPLQIVASDQAPALGAAIFAAVAAGVYADIPSAQAKMGSAV 502
|
570 580 590
....*....|....*....|....*....|..
gi 1370453747 539 KVVF-PRLQDKKYYDKKYQVFLKLVEHQKEYL 569
Cdd:TIGR01234 503 EKTLtPCSENAQRYEQLYARYQELAMSFGQYN 534
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
11-517 |
3.33e-58 |
|
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: 199.33 E-value: 3.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDAT-C 87
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAkaGIDPSDIAAIGISGQmP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 88 SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAvsqvnrinetkhsvlqyvggvmsvemqapkllwlkenlreicwdkagH 167
Cdd:cd00366 81 GVVLVDADGNPL---------RPAIIWLDRRA-----------------------------------------------K 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 168 FFDLPDFLSWKATGVTA--RSLCSLVCKWTYsAEKGWDDSFWKMIGL-EDFVADnyskignqVLPPGASLGnGLTPEAAR 244
Cdd:cd00366 105 FLQPNDYIVFRLTGEFAidYSNASGTGLYDI-KTGDWSEELLDALGIpREKLPP--------IVESGEVVG-RVTPEAAE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 245 DLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVtsrlaVICGTSSCHMGISKDPIFVPGVWGPYFSAmVPGF 324
Cdd:cd00366 175 ETGLPAGTPVVAGGGDTAAAALGA--------GVVEPGDAV-----DSTGTSSVLSVCTDEPVPPDPRLLNRCHV-VPGL 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 325 WLNEGGQSVTGKLIDHMVQghaafpelqvkATARCQSIYAYLNSHLDLIKKAQP----VGFLtvdlhvwPDFHGNRSPLA 400
Cdd:cd00366 241 WLLEGAINTGGASLRWFRD-----------EFGEEEDSDAEYEGLDELAAEVPPgsdgLIFL-------PYLSGERSPIW 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 401 DLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDlaiLYLATVQAIALGTRFIIEAMEAAGHSISTLFLCG 480
Cdd:cd00366 303 DPAARGV------------------------FFGLTLSHTRAH---LIRAVLEGVAYALRDNLEILEELGVKIKEIRVTG 355
|
490 500 510
....*....|....*....|....*....|....*..
gi 1370453747 481 GLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLG 517
Cdd:cd00366 356 GGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
11-522 |
4.72e-57 |
|
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: 197.81 E-value: 4.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQGIDLNQIRGLGFdAT--CS 88
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGPDPIAAISV-SSqgES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 89 LVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAG 166
Cdd:cd07773 80 GVPVDRDGEPL---------GPAIVWFDPRGKEEAEELAEriGAEELYRITGLPPSPMYSLAKLLWLREHEPEI-FAKAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 167 HFFDLPDFLSWKATGVTARSLcSLVCKWTY--SAEKGWDDSfwkmigLEDFVADNYSKIGnQVLPPGASLGNgLTPEAAR 244
Cdd:cd07773 150 KWLSVADYIAYRLTGEPVTDY-SLASRTMLfdIRKRTWSEE------LLEAAGIDASLLP-ELVPSGTVIGT-VTPEAAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 245 DLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFS---AMV 321
Cdd:cd07773 221 ELGLPAGTPVVVGGHDHLCAALGA--------GVIEPGD-----VLDSTGTAEALLAVVDEPPLDEMLAEGGLSyghHVP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 322 PGFWLNEGGQSvTGKLIDHMVQGHAAFPELQVKATARCQSIYAylnshldlikKAQPVGFLtvdlhvwPDFHGNRSPLAD 401
Cdd:cd07773 288 GGYYYLAGSLP-GGALLEWFRDLFGGDESDLAAADELAEAAPP----------GPTGLLFL-------PHLSGSGTPDFD 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 402 LTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDlaiLYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGG 481
Cdd:cd07773 350 PDARGA------------------------FLGLTLGTTRAD---LLRAILEGLAFELRLNLEALEKAGIPIDEIRAVGG 402
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1370453747 482 LSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 522
Cdd:cd07773 403 GARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
289-520 |
3.42e-55 |
|
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.
Pssm-ID: 426979 [Multi-domain] Cd Length: 197 Bit Score: 184.84 E-value: 3.42e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 289 LAVICGTSSCHMGISKDP-IFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQvkATARCQSIYAYLN 367
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPvLSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELR--DAGNVESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 368 SHLDLikkaqpvgfLTVDLHVWPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLddlAIL 447
Cdd:pfam02782 79 LAAVA---------PAGGLLFYPDFSGNRAPGADPGARGS------------------------ITGLSSPTTL---AHL 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370453747 448 YLATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACA 520
Cdd:pfam02782 123 YRAILESLALQLRQILEALTKqEGHPIDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
11-562 |
1.16e-54 |
|
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: 192.39 E-value: 1.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQGIDLNQIRGLGFDATC-SL 89
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVDAIGFSSAMhSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 90 VVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRI--NETKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGH 167
Cdd:cd07770 81 LGVDEDGEPL---------TPVITWADTRAAEEAERLrkEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPEL-FAKAAK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 168 FFDLPDFLSWKATG--VTARSLCSlvckWT---YSAEKGWDDSFWKMIGLEdfvADNYSKIgnqvLPPGASLGnGLTPEA 242
Cdd:cd07770 151 FVSIKEYLLYRLTGelVTDYSTAS----GTgllNIHTLDWDEEALELLGID---EEQLPEL----VDPTEVLP-GLKPEF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 243 ARDLGLLPGIAVAASLIDahaGGLGVIGAdvrghGLICEGqpvtsRLAVICGTSschmG----ISKDPIFVP--GVWgPY 316
Cdd:cd07770 219 AERLGLLAGTPVVLGASD---GALANLGS-----GALDPG-----RAALTVGTS----GairvVSDRPVLDPpgRLW-CY 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 317 FSAmvPGFWL-----NEGGqSVTGKLIDHMVQGHAAFPELQVKATArcqsiyAYLNSHlDLIkkaqpvgFLtvdlhvwPD 391
Cdd:cd07770 281 RLD--ENRWLvggaiNNGG-NVLDWLRDTLLLSGDDYEELDKLAEA------VPPGSH-GLI-------FL-------PY 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 392 FHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDlaiLYLATVQAIALGTRFIIEAMEAAGH 471
Cdd:cd07770 337 LAGERAPGWNPDARGA------------------------FFGLTLNHTRAD---ILRAVLEGVAFNLKSIYEALEELAG 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 472 SISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEamAKMSKVGKVVFPRLQDKKYY 551
Cdd:cd07770 390 PVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSLEA--DELVKIGKVVEPDPENHAIY 467
|
570
....*....|.
gi 1370453747 552 DKKYQVFLKLV 562
Cdd:cd07770 468 AELYERFKKLY 478
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
11-522 |
1.67e-54 |
|
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: 191.20 E-value: 1.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQP--IKNwePQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGfdat 86
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEhdLLT--PKPGWAEHDPEVWWGAVCEIIRELLAkaGISPKEIAAIG---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 87 CS-----LVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINETKHS--VLQYVGGVMSVEMQAPKLLWLKENLRE 159
Cdd:cd07804 75 VSglvpaLVPVDENGKPL---------RPAILYGDRRATEEIEWLNENIGEdrIFEITGNPLDSQSVGPKLLWIKRNEPE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 160 IcWDKAGHFFDLPDFLSWKATG--VTARSLCSLvckwtYS-----AEKGWDDSFWKMIGLEdfvadnySKIGNQVLPPGA 232
Cdd:cd07804 146 V-FKKTRKFLGAYDYIVYKLTGeyVIDYSSAGN-----EGglfdiRKRTWDEELLEALGID-------PDLLPELVPSTE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 233 SLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGV 312
Cdd:cd07804 213 IVG-EVTKEAAEETGLAEGTPVVAGTVDAAASALSA--------GVVEPGD-----LLLMLGTAGDIGVVTDKLPTDPRL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 313 WGPYFSamVPGFWLNEGGQSVTGKLIDHMVQGHAafPELQVKATARCQSIYAYLNshldliKKAQ--PVGfltVD-LHVW 389
Cdd:cd07804 279 WLDYHD--IPGTYVLNGGMATSGSLLRWFRDEFA--GEEVEAEKSGGDSAYDLLD------EEAEkiPPG---SDgLIVL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 390 PDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAA 469
Cdd:cd07804 346 PYFMGERTPIWDPDARGV------------------------IFGLTLSHTRAHL---YRALLEGVAYGLRHHLEVIREA 398
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1370453747 470 GHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 522
Cdd:cd07804 399 GLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
11-522 |
7.96e-54 |
|
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: 188.91 E-value: 7.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDAT-C 87
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEksGVDPSDIAGVGVTGHgN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 88 SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKA 165
Cdd:cd07802 81 GLYLVDKDGKPV---------RNAILSNDSRAADIVDRWEEdgTLEKVYPLTGQPLWPGQPVALLRWLKENEPER-YDRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 166 GHFFDLPDFLSWKATGVtarslcsLVCKWT-YSA------EKGWDDSFWKMIGLEDFvadnYSKIGnQVLPPGASLGnGL 238
Cdd:cd07802 151 RTVLFCKDWIRYRLTGE-------ISTDYTdAGSslldldTGEYDDELLDLLGIEEL----KDKLP-PLVPSTEIAG-RV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 239 TPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGpYFS 318
Cdd:cd07802 218 TAEAAALTGLPEGTPVAAGAFDVVASALGA--------GAVDEGQ-----LCVILGTWSINEVVTDEPVVPDSVGS-NSL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 319 AMVPGFWLNEGGQSVTGKLIDHMVQghaafpELQVKATARCQSIYAYLNshlDLIKKAQPVgfltvdlhvwpdfhgnrsp 398
Cdd:cd07802 284 HADPGLYLIVEASPTSASNLDWFLD------TLLGEEKEAGGSDYDELD---ELIAAVPPG------------------- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 399 ladltlkgmrTTGYLYIPALAAlhspsSLLSPQVT----GLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEAAGHsIS 474
Cdd:cd07802 336 ----------SSGVIFLPYLYG-----SGANPNARggffGLTAWHTRAHLL---RAVYEGIAFSHRDHLERLLVARK-PE 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1370453747 475 TLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 522
Cdd:cd07802 397 TIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
11-522 |
4.31e-41 |
|
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: 154.25 E-value: 4.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 11 YYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDATC 87
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKdaGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 88 -SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINET-KHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKA 165
Cdd:cd07809 81 hGLVALDADGKVL---------RPAKLWCDTRTAPEAEELTEAlGGKKCLLVGLNIPARFTASKLLWLKENEPEH-YARI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 166 gHFFDLP-DFLSWKATG--VTARSLCSLVckwtysaekGWDDSF-----WKMIGLEDFVADNYSKIGnQVLPPGASLGnG 237
Cdd:cd07809 151 -AKILLPhDYLNWKLTGekVTGLGDASGT---------FPIDPRtrdydAELLAAIDPSRDLRDLLP-EVLPAGEVAG-R 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 238 LTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVTSrlaviCGTSSCHMGISKDPIFVPgvwgpyf 317
Cdd:cd07809 219 LTPEGAEELGLPAGIPVAPGEGDNMTGALGT--------GVVNPGTVAVS-----LGTSGTAYGVSDKPVSDP------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 318 SAMVPGF--------WLNEG---GQSVTGKLIDHMVQGHAAFPELQVKATARCQSI--YAYLNshldlikkaqpvgfltv 384
Cdd:cd07809 279 HGRVATFcdstggmlPLINTtncLTAWTELFRELLGVSYEELDELAAQAPPGAGGLllLPFLN----------------- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 385 dlhvwpdfhgnrspladltlkGMRTTGYlyipalaalhspssllsPQVTGLKLSQDLDD--LAILYLATVQAIALGTRFI 462
Cdd:cd07809 342 ---------------------GERTPNL-----------------PHGRASLVGLTLSNftRANLARAALEGATFGLRYG 383
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 463 IEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 522
Cdd:cd07809 384 LDILRELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
11-522 |
6.39e-38 |
|
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: 145.44 E-value: 6.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHH--EQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLgfdAT 86
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYPDakEFDPEELWEKICEAIREALKkaGISPEDISAV---SS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 87 CS----LVVLDKQFHPL---PvnqegdshrNVimwlDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAP-KLLWLKENLR 158
Cdd:cd07798 78 TSqregIVFLDKDGRELyagP---------NI----DARGVEEAAEIDDEFGEEIYTTTGHWPTELFPAaRLLWFKENRP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 159 EIcWDKAGHFFDLPDFLSWKATGVtarslcsLVCKWTYSAEKG--------WDDSFWKMIGLEDfvadnysKIGNQVLPP 230
Cdd:cd07798 145 EI-FERIATVLSISDWIGYRLTGE-------LVSEPSQASETQlfdikkreWSQELLEALGLPP-------EILPEIVPS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 231 GASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVP 310
Cdd:cd07798 210 GTVLGT-VSEEAARELGLPEGTPVVVGGADTQCALLGS--------GAIEPGD-----IGIVAGTTTPVQMVTDEPIIDP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 311 --GVW-GPYfsaMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQvkatarcqsiYAYLNSHLDLIKKAQP--VGFLTvd 385
Cdd:cd07798 276 erRLWtGCH---LVPGKWVLESNAGVTGLNYQWLKELLYGDPEDS----------YEVLEEEASEIPPGANgvLAFLG-- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 386 lhvwpdfhgnrSPLADLTLKGMRTTGYLYipalaalhspSSLLSPQVTGLKlsqdldDLAIlylATVQAIALGTRFIIEA 465
Cdd:cd07798 341 -----------PQIFDARLSGLKNGGFLF----------PTPLSASELTRG------DFAR---AILENIAFAIRANLEQ 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370453747 466 MEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 522
Cdd:cd07798 391 LEEvSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
11-522 |
1.20e-31 |
|
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: 127.74 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQGIDL--NQIRGLGFDAT-- 86
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVlpDRVAAIGVTGQgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 87 -CSLVvlDKqfhplpvnqEGDSHRNVIMWLDHRAVSQVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLREICwD 163
Cdd:cd24121 81 gTWLV--DE---------DGRPVRDAILWLDGRAADIVERWQAdgIAEAVFEITGTGLFPGSQAAQLAWLKENEPERL-E 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 164 KAGHFFDLPDFLSWKATGVTA--RSLCSLVCkwtYSAEKG-WDDSFWKMIGLEDFVAdnyskignqVLPP-GASLGNG-- 237
Cdd:cd24121 149 RARTALHCKDWLFYKLTGEIAtdPSDASLTF---LDFRTRqYDDEVLDLLGLEELRH---------LLPPiRPGTEVIgp 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 238 LTPEAARDLGLLPGIAVAASLIDAHAGGLGViGADVRGHGLicegqpvtsrlaVICGTSSCHMGISKDPIFVPGVWGPYF 317
Cdd:cd24121 217 LTPEAAAATGLPAGTPVVLGPFDVVATALGS-GAIEPGDAC------------SILGTTGVHEVVVDEPDLEPEGVGYTI 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 318 SAMVPGFWLneggqsvtgklidHMVQGHAAFPELQvkatarcqsiYAylnshLDLIKKAQPVGFLTVDLHVWPDFHG--N 395
Cdd:cd24121 284 CLGVPGRWL-------------RAMANMAGTPNLD----------WF-----LRELGEVLKEGAEPAGSDLFQDLEElaA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 396 RSPLAdltlkgmrTTGYLYIPALaalhSPSSLLSP--------QVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMe 467
Cdd:cd24121 336 SSPPG--------AEGVLYHPYL----SPAGERAPfvnpnaraQFTGLSLEHTRADLL---RAVYEGVALAMRDCYEHM- 399
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1370453747 468 aaGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 522
Cdd:cd24121 400 --GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
11-267 |
3.71e-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: 3.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDATC- 87
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSqlGISLKQIKGIGISNQGh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 88 SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKA 165
Cdd:pfam00370 81 GTVLLDKNDKPL---------YNAILWKDRRTAEIVENLKEegNNQKLYEITGLPIWPGFTLSKLRWIKENEPEV-FEKI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 166 GHFFDLPDFLSWKATGVtarslcsLVCKWTYSAEKG--------WDDSFWKMIGLEdfvadnyskigNQVLPP----GAS 233
Cdd:pfam00370 151 HKFLTIHDYLRWRLTGV-------FVTDHTNASRSMmfnihkldWDPELLAALGIP-----------RDHLPPlvesSEI 212
|
250 260 270
....*....|....*....|....*....|....
gi 1370453747 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; ... |
11-556 |
1.34e-27 |
|
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: 116.28 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPiknWEPQFNHHEQSSEDI-----WAACCVVTKKVVQ--GIDLNQIRGLgf 83
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQRE---WRHKEVPDVPGSMDFdteknWKLICECIREALKkaGIAPKSIAAI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 84 dATCS----LVVLDKQFHPLpvnqegdshrnvimW----LDHRAVSQVNRINETKHSVLQ--YVGGVMSVEMQA-PKLLW 152
Cdd:cd07775 76 -STTSmregIVLYDNEGEEI--------------WacanVDARAAEEVSELKELYNTLEEevYRISGQTFALGAiPRLLW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 153 LKENLREIcWDKAGHFFDLPDFLSWKATGVTAR--SLCSLVCKWTySAEKGWDDSFWKMIGLEDFvadnyskIGNQVLPP 230
Cdd:cd07775 141 LKNNRPEI-YRKAAKITMLSDWIAYKLSGELAVepSNGSTTGLFD-LKTRDWDPEILEMAGLKAD-------ILPPVVES 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 231 GASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrlAVICGTSSCHMGI-SKDPIFV 309
Cdd:cd07775 212 GTVIGK-VTKEAAEETGLKEGTPVVVGGGDVQLGCLGL--------GVVRPGQ------TAVLGGSFWQQEVnTAAPVTD 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 310 PGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQghAAFPELQVKATARCQSIYAYLNshldliKKAQ--PVGfltvdlh 387
Cdd:cd07775 277 PAMNIRVNCHVIPDMWQAEGISFFPGLVMRWFRD--AFCAEEKEIAERLGIDAYDLLE------EMAKdvPPG------- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 388 vwpdFHGNRSPLADLtlkgMRTTGYlYIPAlaalhspssllsPQVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAME 467
Cdd:cd07775 342 ----SYGIMPIFSDV----MNYKNW-RHAA------------PSFLNLDIDPEKCNKATFFRAIMENAAIVSAGNLERIA 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 468 AA-GHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQ 546
Cdd:cd07775 401 EFsGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAGIYSSLEEAVESLVKWEREYLPNPE 480
|
570
....*....|
gi 1370453747 547 DKKYYDKKYQ 556
Cdd:cd07775 481 NHEVYQDLYE 490
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
12-561 |
1.21e-17 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 85.79 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 12 YVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQGIDLNQIRGLGFDATC-SLV 90
Cdd:PRK15027 2 YIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQMhGAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 91 VLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLREICWDKAGHFfd 170
Cdd:PRK15027 82 LLDAQQRVL---------RPAILWNDGRCAQECALLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVL-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 171 LP-DFLSWKATGVTARSLCSLV-CKWTYSAEKGWDDSfwkMIGLEDFVADNYSkignqVLPPGASLGNGLTPEAARDLGl 248
Cdd:PRK15027 151 LPkDYLRLRMTGEFASDMSDAAgTMWLDVAKRDWSDV---MLQACHLSRDQMP-----ALYEGSEITGALLPEVAKAWG- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 249 LPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVTSrlaviCGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWlne 328
Cdd:PRK15027 222 MATVPVVAGGGDNAAGAVGV--------GMVDANQAMLS-----LGTSGVYFAVSEGFLSKPESAVHSFCHALPQRW--- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 329 ggqsvtgKLIDHMVQGhAAFPELQVKATARcQSIYAYLNSHLDLIKKAQPVGFLtvdlhvwPDFHGNRSPLADLTLKGMr 408
Cdd:PRK15027 286 -------HLMSVMLSA-ASCLDWAAKLTGL-SNVPALIAAAQQADESAEPVWFL-------PYLSGERTPHNNPQAKGV- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 409 ttgylyIPALAALHSPSSLLSPQVTGLKLsqdlddlailylatvqAIALGtrfiIEAMEAAGHSISTLFLCGGLSKNPLF 488
Cdd:PRK15027 349 ------FFGLTHQHGPNELARAVLEGVGY----------------ALADG----MDVVHACGIKPQSVTLIGGGARSEYW 402
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370453747 489 VQMHADITGMPVVLSQ--EVESVLvGAAVLGACASGDFASVQEAMAKMSkVGKVVFPRLQDKKYYDKKYQVFLKL 561
Cdd:PRK15027 403 RQMLADISGQQLDYRTggDVGPAL-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), ... |
11-563 |
6.32e-16 |
|
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: 80.59 E-value: 6.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFdaTC- 87
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAkaGISASDIAAIGI--TNq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 88 --SLVVLDKQfhplpvnqEGDSHRNVIMWLDHRAVSQVNRINETKHS--VLQYVGGVMSVEMQAPKLLWLKEN---LREI 160
Cdd:cd07769 79 reTTVVWDKK--------TGKPLYNAIVWQDRRTADICEELKAKGLEerIREKTGLPLDPYFSATKIKWILDNvpgARER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 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 1370453747 229 P---PGASLgNGLTPEAardlGLLPGIAVAASLIDAHAgglgvigADVrGHGLICEGQ------------------PVTS 287
Cdd:cd07769 211 PevrPSSEV-FGYTDPE----GLGAGIPIAGILGDQQA-------ALF-GQGCFEPGMakntygtgcfllmntgekPVPS 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 288 R---LAVICgtsschMGISKDP-------IFVPGvwgpyfSAMVpgfWLNEGGqsvtgKLIDHMvqghaafPELQvkata 357
Cdd:cd07769 278 KnglLTTIA------WQIGGKVtyalegsIFIAG------AAIQ---WLRDNL-----GLIEDA-------AETE----- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 358 rcqsiyaylnshlDLIKKAqpvgfltvdlhvwPDfhgnrspladltlkgmrTTGYLYIPALAALHSP-------SSLLsp 430
Cdd:cd07769 326 -------------ELARSV-------------ED-----------------NGGVYFVPAFSGLGAPywdpdarGAIV-- 360
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 431 qvtGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESV 509
Cdd:cd07769 361 ---GLTRGTTKAHIV---RAALESIAYQTRDVLEAMEKdSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETT 434
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1370453747 510 LVGAAVLGACASGdFASVQEAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 563
Cdd:cd07769 435 ALGAAYLAGLAVG-FWKDLDELASLWQVDKRFEPSMDEEE-RERLYRGWKKAVE 486
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
450-563 |
2.97e-15 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466802 [Multi-domain] Cd Length: 499 Bit Score: 78.33 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 450 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 528
Cdd:cd07792 384 AALEAVCFQTREILDAMNKdSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLD 463
|
90 100 110
....*....|....*....|....*....|....*
gi 1370453747 529 EAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 563
Cdd:cd07792 464 ELKSLNEGGRTVFEPQISEEE-RERRYKRWKKAVE 497
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
450-563 |
3.18e-15 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 78.18 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 450 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 528
Cdd:COG0554 377 AALESIAYQTRDVLDAMEAdSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLE 456
|
90 100 110
....*....|....*....|....*....|....*
gi 1370453747 529 EaMAKMSKVGKVVFPRLqDKKYYDKKYQVFLKLVE 563
Cdd:COG0554 457 E-LAALWKVDRRFEPQM-DEEERERLYAGWKKAVE 489
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
11-564 |
5.48e-15 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 77.74 E-value: 5.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 11 YYVGVDVGTGSVRAALVDQSGVLLAFADqpiKNW----EPQF-NHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLgf 83
Cdd:PRK10939 4 YLMALDAGTGSIRAVIFDLNGNQIAVGQ---AEWrhlaVPDVpGSMEFDLEKNWQLACQCIRQALQkaGIPASDIAAV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 84 dATCSL----VVLDKQFHPLpvnqegdshrnvimW----LDHRAVSQVNRINEtKHSVLQYvgGVMSVEMQA------PK 149
Cdd:PRK10939 79 -SATSMregiVLYDRNGTEI--------------WacanVDARASREVSELKE-LHNNFEE--EVYRCSGQTlalgalPR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 150 LLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTA--------RSLCSLVckwtysaEKGWDDSFWKMIGLEDfvadnys 221
Cdd:PRK10939 141 LLWLAHHRPDI-YRQAHTITMISDWIAYMLSGELAvdpsnagtTGLLDLV-------TRDWDPALLEMAGLRA------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 222 KIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGT------ 295
Cdd:PRK10939 206 DILPPVKETGTVLGH-VTAKAAAETGLRAGTPVVMGGGDVQLGCLGL--------GVVRPGQ-----TAVLGGTfwqqvv 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 296 ------SSCHMGISKDPifvpgvwgpyfsAMVPGFWLNEGGQSVTGkLIdhMVQGHAAF-PELQVKATARCQSIYAYLNs 368
Cdd:PRK10939 272 nlpapvTDPNMNIRINP------------HVIPGMVQAESISFFTG-LT--MRWFRDAFcAEEKLLAERLGIDAYSLLE- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 369 hldliKKAQ--PVGfltvDLHVWPDFHGnrspladltlkGMRtTGYLYipalaalHSPSSLLSpqvtgLKLSQDLDDLAI 446
Cdd:PRK10939 336 -----EMASrvPVG----SHGIIPIFSD-----------VMR-FKSWY-------HAAPSFIN-----LSIDPEKCNKAT 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 447 LYLATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFA 525
Cdd:PRK10939 383 LFRALEENAAIVSACNLQQIAAfSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYS 462
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1370453747 526 SVQEAMAKMSKVGKVVFPRLQDKKYYDKK-------YQVFLKLVEH 564
Cdd:PRK10939 463 SLAETGERLVRWERTFEPNPENHELYQEAkekwqavYADQLGLVDH 508
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
450-563 |
1.95e-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: 75.99 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 450 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 528
Cdd:cd07786 374 AALESIAYQTRDLLEAMEAdSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLD 453
|
90 100 110
....*....|....*....|....*....|....*
gi 1370453747 529 EAmAKMSKVGKVVFPRLqDKKYYDKKYQVFLKLVE 563
Cdd:cd07786 454 EL-AKLWQVDRRFEPSM-SEEEREALYAGWKKAVK 486
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
450-550 |
2.31e-14 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 75.78 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 450 ATVQAIALGTRFIIEAME-AAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 528
Cdd:PTZ00294 383 AALEAIALQTNDVIESMEkDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLE 462
|
90 100
....*....|....*....|..
gi 1370453747 529 EAMAKMSKVGKVVFPRLQDKKY 550
Cdd:PTZ00294 463 EVKKLIRRSNSTFSPQMSAEER 484
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
11-563 |
1.38e-13 |
|
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: 73.36 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFdAT-- 86
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKnaGLTPEDIAAIGI-STqr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 87 CSLVVLDKQ----FHplpvnqegdshrNVIMWLDHRAVSQVNRINE-----------------TKH------SVLQYVGG 139
Cdd:cd07793 80 NTFLTWDKKtgkpLH------------NFITWQDLRAAELCESWNRslllkalrggskflhflTRNkrflaaSVLKFSTA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 140 vmsveMQAPKLLWLKENLREICWDKAGH---FFDLPDFLSWKATG----VTARSLCSlvckwtysaEKGWDDSF---WKM 209
Cdd:cd07793 148 -----HVSIRLLWILQNNPELKEAAEKGellFGTIDTWLLWKLTGgkvhATDYSNAS---------ATGLFDPFtleWSP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 210 IGLEDFvadnysKIGNQVLPPgaslgngltpeaardlgllpgiavaaslIDAHAGGLGVIGADVRGHGLicegqPVTsrl 289
Cdd:cd07793 214 ILLSLF------GIPSSILPE----------------------------VKDTSGDFGSTDPSIFGAEI-----PIT--- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 290 AVI-----------C---GTSSCHMGISkdpIFVPGVWGPYFSAMVPGF-----W--------LNEGGQSVTGKLIDHmv 342
Cdd:cd07793 252 AVVadqqaalfgecCfdkGDVKITMGTG---TFIDINTGSKPHASVKGLyplvgWkiggeityLAEGNASDTGTVIDW-- 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 343 qghaafpelqvkatarCQSIyAYLNSHLDLIKKAQPVGfLTVDLHVWPDFHGNRSPLADLTLKGMrttgylyipalaalh 422
Cdd:cd07793 327 ----------------AKSI-GLFDDPSETEDIAESVE-DTNGVYFVPAFSGLQAPYNDPTACAG--------------- 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 423 spssllspqVTGLKLSQDLDDLAIlylATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVV 501
Cdd:cd07793 374 ---------FIGLTPSTTKAHLVR---AILESIAFRVKQLLETMEKeTSIKISSIRVDGGVSNNDFILQLIADLLGKPVE 441
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370453747 502 LSQEVESVLVGAAVLGACASGDFASVqEAMAKMSKVGKVVFPRlQDKKYYDKKYQVFLKLVE 563
Cdd:cd07793 442 RPKNTEMSALGAAFLAGLASGIWKSK-EELKKLRKIEKIFEPK-MDNEKREELYKNWKKAVK 501
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
16-550 |
3.01e-13 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 71.98 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 16 DVGTGSVRAALVDQSGVLLAFADQP------IKNwePQFnhHEQSSEDIW---AACCvvtKKVVQGIDLNQIRGL----- 81
Cdd:PRK10331 8 DCGATNVRAIAVDRQGKIVARASTPnasdiaAEN--SDW--HQWSLDAILqrfADCC---RQINSELTECHIRGItvttf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 82 GFDATcslvvldkqfhplPVNQEGDSHRNVIMWLDHRAVSQVNRI-NETKHSVLQYVGGVMSVEMQAP-KLLWLKENLRE 159
Cdd:PRK10331 81 GVDGA-------------LVDKQGNLLYPIISWKCPRTAAVMENIeRYISAQQLQQISGVGAFSFNTLyKLVWLKENHPQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 160 IcWDKAGHFFDLPDFLSWKATGV--TARSLCSlVCKWTYSAEKGWDDSFWKMIGLEdfvadnyskigNQVLPP----GAS 233
Cdd:PRK10331 148 L-LEQAHAWLFISSLINHRLTGEftTDITMAG-TSQMLDIQQRDFSPEILQATGLS-----------RRLFPRlveaGEQ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 234 LGNgLTPEAARDLGLLPGIAVAASlidAHAGGLGVIGAdvrGHGLiceGQPV-----------------TSRLAVICGtS 296
Cdd:PRK10331 215 IGT-LQPSAAALLGLPVGIPVISA---GHDTQFALFGS---GAGQ---NQPVlssgtweilmvrsaqvdTSLLSQYAG-S 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 297 SCHMGiSKDPIFVPGVWgpyfsamvpgfWLNEGGQSVTGKLI-------DHMVQGHAAFPelqvkatARCQSIYayLNSH 369
Cdd:PRK10331 284 TCELD-SQSGLYNPGMQ-----------WLASGVLEWVRKLFwtaetpyQTMIEEARAIP-------PGADGVK--MQCD 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 370 LDLIKKAQPVGfltVDLHvwpdfhgnrspladltlkgmRTTGYLYIPALAALhspssllspqvtGLKLSQDLDDLailyl 449
Cdd:PRK10331 343 LLACQNAGWQG---VTLN--------------------TTRGHFYRAALEGL------------TAQLKRNLQVL----- 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 450 atvqaialgtrfiieamEAAGH-SISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 528
Cdd:PRK10331 383 -----------------EKIGHfKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPE 445
|
570 580
....*....|....*....|..
gi 1370453747 529 EAMAKMSKVGKVVFPRLQDKKY 550
Cdd:PRK10331 446 QARAQMKYQYRYFYPQTEPEFI 467
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
450-564 |
6.31e-12 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 67.93 E-value: 6.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 450 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 528
Cdd:PRK00047 380 ATLESIAYQTRDVLDAMQAdSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLD 459
|
90 100 110
....*....|....*....|....*....|....*.
gi 1370453747 529 EaMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVEH 564
Cdd:PRK00047 460 E-LKEQWKIDRRFEPQMDEEE-REKLYAGWKKAVKR 493
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
11-514 |
1.66e-11 |
|
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: 66.48 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 11 YYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKNWEPQ--FNHHEQSSEDIWAAccvvTKKVVQGID---LNQIRGLGFD 84
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDlESGRILESVSRPTPAPISSddPGRSEQDPEKILEA----VRNLIDELPreyLSDVTGIGIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 85 AtcslvvldkQFHP-LPVNQEGDSHRNVIMWLDHRAvsqvnriNETKHSVLQYVGGVMSVEMQAP--------KLLWLKE 155
Cdd:cd07777 77 G---------QMHGiVLWDEDGNPVSPLITWQDQRC-------SEEFLGGLSTYGEELLPKSGMRlkpgyglaTLFWLLR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 156 NLREIcwDKAGHFFDLPDFLSWKATGvTARSLCSLVCK--WTY--SAEKGWDDSFWKMIGLEdfvadnySKIGNQVLPPG 231
Cdd:cd07777 141 NGPLP--SKADRAGTIGDYIVARLTG-LPKPVMHPTNAasWGLfdLETGTWNKDLLEALGLP-------VILLPEIVPSG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 232 ASLGNgLTPEAARDLGLLPGI-----AVAASLIDAHagglgvigadvrghglicegqpvtSRLAVICGTSScHMGISKDP 306
Cdd:cd07777 211 EIVGT-LSSALPKGIPVYVALgdnqaSVLGSGLNEE------------------------NDAVLNIGTGA-QLSFLTPK 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 307 IFVPGVWG--PYFSamvpGFWLNeggqSVT----GKLIDHMVQ-----GHAAFPELQVkatarcQSIYAYLNShLDLIKK 375
Cdd:cd07777 265 FELSGSVEirPFFD----GRYLL----VAAslpgGRALAVLVDflrewLRELGGSLSD------DEIWEKLDE-LAESEE 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 376 AQPvgfLTVDlhvwPDFHGNRspladltlkgmrttgylyipalaalHSPSSLLSpqVTGLklsqDLDDLAI--LYLATVQ 453
Cdd:cd07777 330 SSD---LSVD----PTFFGER-------------------------HDPEGRGS--ITNI----GESNFTLgnLFRALCR 371
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370453747 454 AIALGTRFIIEAMEAAGHSISTLFLCGG-LSKNPLFVQMHADITGMPVVLSQEVESVLVGAA 514
Cdd:cd07777 372 GIAENLHEMLPRLDLDLSGIERIVGSGGaLRKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAA 433
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
455-530 |
4.34e-08 |
|
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.
Pssm-ID: 466791 [Multi-domain] Cd Length: 460 Bit Score: 55.61 E-value: 4.34e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370453747 455 IALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSqEVESVLVGAAVLGACASGDFASVQEA 530
Cdd:cd07771 378 LALKYAKTIEELEElTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAG-PVEATAIGNLLVQLIALGEIKSLEEG 453
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
450-563 |
2.58e-07 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 53.55 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 450 ATVQAIALGTRFIIEAM------EAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGD 523
Cdd:PLN02295 384 AVLESMCFQVKDVLDAMrkdageEKSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGL 463
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1370453747 524 FASVQEAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 563
Cdd:PLN02295 464 WTEEEIFASEKWKNTTTFRPKLDEEE-RAKRYASWCKAVE 502
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
15-516 |
6.32e-07 |
|
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: 51.88 E-value: 6.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 15 VDVGTGSVRAALVDQSGVLLAFADQPIKN-WEPQFNHHEqsSEDIWAAccvVTKKVVQGIDLNQIRGLGFdaTC---SLV 90
Cdd:cd07772 5 FDIGKTNKKLLLFDENGEVLAERSTPNPEiEEDGYPCED--VEAIWEW---LLDSLAELAKRHRIDAINF--TThgaTFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 91 VLDKQFHP-LPV---NQEGDShrnvimWLDHRAVSQVNRINETKHSVLqyvGGVMSVEMQapkLLWLKENLREIcWDKAG 166
Cdd:cd07772 78 LLDENGELaLPVydyEKPIPD------EINEAYYAERGPFEETGSPPL---PGGLNLGKQ---LYWLKREKPEL-FARAK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 167 HFFDLPDFLSWKATGVTARSLCSLVC--------KWTYS---AEKGWDDSFWKMigledfvadnyskignqvLPPGASLG 235
Cdd:cd07772 145 TILPLPQYWAWRLTGKAASEITSLGChtdlwdfeKNEYSslvKKEGWDKLFPPL------------------RKAWEVLG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 236 NgLTPEAARDLGLLPGIAVAASLIDAHAgglgvigadvrghglicegqpvtSRLAvicgtsscHMGISKDPiFV---PGV 312
Cdd:cd07772 207 P-LRPDLARRTGLPKDIPVGCGIHDSNA-----------------------ALLP--------YLAAGKEP-FTllsTGT 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 313 WgpyFSAMVPGF-----WLNEG-----GQSVTGKLIdhmvqGHAAFP-----ELQVKataRCQSIYAYLNSHLDLIKkaq 377
Cdd:cd07772 254 W---CIAMNPGNdlpltELDLArdclyNLDVFGRPV-----KTARFMggreyERLVE---RIAKSFPQLPSLADLAK--- 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 378 pvgFLTVDLHVWPDFHGNRSPladltlkgmrttgylyIPALAALHSPSSLLSPqvtglklsQDLDDLAILYLATVQAIAL 457
Cdd:cd07772 320 ---LLARGTFALPSFAPGGGP----------------FPGSGGRGVLSAFPSA--------EEAYALAILYLALMTDYAL 372
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 458 gtrfiieamEAAGHSISTLFLCGGLSKNPLFVQMHADI-TGMPVVLSQEVESVLVGAAVL 516
Cdd:cd07772 373 ---------DLLGSGVGRIIVEGGFAKNPVFLRLLAALrPDQPVYLSDDSEGTALGAALL 423
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
470-553 |
1.99e-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: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453747 470 GHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKV----GKVVFPRL 545
Cdd:cd07776 423 DIPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVVFSaeepKLVAEPDP 502
|
....*...
gi 1370453747 546 QDKKYYDK 553
Cdd:cd07776 503 EAAEVYDK 510
|
|
| |
