|
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 ... |
66-647 |
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: 984.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 66 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKKWEPQFNHHEQSSEDIWAACCVVTKGevgkellfpftfenlkarelsd 145
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKE---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 146 fptvtqvVCDKAelrflglklpgcvkvvqGIDLNQIRGLGFDATCSLVVLDKQFRPLPVNHEEDSHRNVIMWLDHRAVSQ 225
Cdd:cd07782 59 -------VLEGA-----------------GVDPEQVKGIGFDATCSLVVLDAEGKPVSVSPSGDDERNVILWMDHRAVEE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 226 VNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLRETcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA---- 301
Cdd:cd07782 115 AERINATGHEVLKYVGGKISPEMEPPKLLWLKENLPET-WAKAGHFFDLPDFLTWKATGSLTRSLCSLVCKWTYLAhegs 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 302 ERGWDDSFWKMIGLEDFVADNYSKIGNQVLPPGASLGNGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIGADVKGHgl 381
Cdd:cd07782 194 EGGWDDDFFKEIGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAKELGLPEGTPVGVSLIDAHAGGLGTLGADVGGL-- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 382 VCEGQPVTSRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVEGHAAFPELQVKARAR 461
Cdd:cd07782 272 PCEADPLTRRLALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGLWLNEGGQSATGALLDHIIETHPAYPELKEEAKAA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 462 CQSVYAYLNSHLDLIKKAQ--PVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATVQAIALGTR 539
Cdd:cd07782 352 GKSIYEYLNERLEQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALLYLATLQALAYGTR 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 540 FIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGACASGDFASVQEAMAKMSKVGKV 619
Cdd:cd07782 432 HIIEAMNAAGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDAMAAMSGPGKV 511
|
570 580
....*....|....*....|....*...
gi 1622832061 620 VFPRLQDKKYYDKKYQVFLKLVEHQKEY 647
Cdd:cd07782 512 VEPNEELKKYHDRKYEVFLKMYEDQREY 539
|
|
| 5C_CHO_kinase |
TIGR01315 |
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ... |
66-647 |
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: 657.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 66 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKKWEPQFNHHEQSSEDIWAACCVVTKGEVGKellfpftfenlkarelsd 145
Cdd:TIGR01315 1 HYIGVDVGTGSARACIIDSTGDILALAAQNIKTWTPSSGLEGQSSVYIWQAICNCVKQVLAE------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 146 fptvtqvvcdkaelrflglklpgcvkvvQGIDLNQIRGLGFDATCSLVVLDKQFRPLPVNHEEDSHRNVIMWLDHRAVSQ 225
Cdd:TIGR01315 63 ----------------------------SKVDPNSVKGIGFDATCSLVVLTHDGEPLPVSKNGGADQNIILWMDHRALAE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 226 VNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLRETcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTY----SA 301
Cdd:TIGR01315 115 AEKINATNHNLLRYVGGKMSVEMEIPKVLWLKNNMPPE-LFARCKFFDLTDFLTWRATGKEIRSFCSVVCKWGFvpvdGS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 302 ERGWDDSFWKMIGLEDFVADNYSKIGNQVLPPGASLGNGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIGADVKGHGL 381
Cdd:TIGR01315 194 NKGWQEDFYETIGLGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQELGLPAGTAVGSGLIDAHAGWIGTVGAKVAENGD 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 382 VCEGQpvtSRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVEGHAAFPELQVKARAR 461
Cdd:TIGR01315 274 VSQAF---TRLAAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGYWLAEGGQSAAGELMDHMLETHVAYDETVKEAEAA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 462 CQSVYAYLNSHLdLIKKAQP----VGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATVQAIALG 537
Cdd:TIGR01315 351 GKNIYDYLNEHL-KEMAAKTnapsISYLVRHFHVYPDLWGNRSPIADPNMRGVIIGLSMDRSKDGLALLYYATMEFIAYG 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 538 TRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGACASGDFASVQEAMAKMSKVG 617
Cdd:TIGR01315 430 TRQIVEAMNTAGHTIKSIFMSGGQCQNPLLMQLIADACDMPVLIPYVNEAVLHGAAMLGAKAAGTTESLWDAMDRMSKPG 509
|
570 580 590
....*....|....*....|....*....|.
gi 1622832061 618 KVVFPRLQ-DKKYYDKKYQVFLKLVEHQKEY 647
Cdd:TIGR01315 510 KTVWPRGDpAKKLHDRKYEIFLQLARTQQEY 540
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
64-647 |
0e+00 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 589.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 64 ERYYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKKWEP---------QFnhhEQSSEDIWAACCVVtkgevgkellfpf 133
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDaADGEELASAVHPYPRWVIglylppppdQA---RQHPLDYLEALEAA------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 134 tfenlkarelsdfptvtqvvcdkaelrflglkLPGCVKVVqGIDLNQIRGLGFDAT-CSLVVLDKQFRPLPVNHE--EDS 210
Cdd:COG1069 65 --------------------------------VREALAQA-GVDPADVVGIGVDATgCTPVPVDADGTPLALLPEfaENP 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 211 HRNVIMWLDHRAVSQVNRINE----TKHSVLQYVGGVMSVEMQAPKLLWLKENLRETcWDKAGHFFDLPDFLSWKATGVT 286
Cdd:COG1069 112 HAMVILWKDHTAQEEAERINElakaRGEDYLRYVGGIISSEWFWPKILHLLREDPEV-YEAADSFVELCDWITWQLTGSL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 287 ARSLCSLVCKWTYSA-ERGW-DDSFWKMIGLE-DFVADnysKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLID 363
Cdd:COG1069 191 KRSRCTAGHKALWHAhEGGYpSEEFFAALDPLlDGLAD---RLGTEIYPLGEPAGT-LTAEWAARLGLPPGTAVAVGAID 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 364 AHAGGLGVIGadvkghglVCEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDH 443
Cdd:COG1069 267 AHAGAVGAGG--------VEPGT-----LVKVMGTSTCHMLVSPEERFVPGICGQVDGSIVPGMWGYEAGQSAVGDIFAW 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 444 MVEGHAAFPELQVKARARCQSVYAYLNshldliKKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDl 523
Cdd:COG1069 334 FVRLLVPPLEYEKEAEERGISLHPLLT------EEAAKLPPGESGLHALDWFNGNRSPLADQRLKGVILGLTLGTDAED- 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 524 aiLYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGACASGD 602
Cdd:COG1069 407 --IYRALVEATAFGTRAIIERFEEEGVPIDEIIACGGIAtKNPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGA 484
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1622832061 603 FASVQEAMAKMSKV-GKVVFPRLQDKKYYDKKYQVFLKLVEHQKEY 647
Cdd:COG1069 485 YPDVEEAMAAMGSGfDKVYTPDPENVAVYDALYAEYLQLHDYFGRG 530
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
66-640 |
2.55e-147 |
|
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: 437.44 E-value: 2.55e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 66 YYVGVDVGTGSVRAALVDQS-GVLLAFADQPIKKWE-PQFNHHEQSSEDIWAACCVVTKGEVGKEllfpftfenlkarel 143
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDLYaGLEMAQEPVPYYQDSsKKSWKFWQKSTEIIKALQKCVQKLNIRE--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 144 sdfptvtqvvcdkaelrflglklpgcvkvvqGIDLNQIRGLGFDATCSLVVLDKQFRPLPVNHEEDSHRNVIMWLDHRAV 223
Cdd:cd07768 66 -------------------------------GVDAYEVKGCGVDATCSLAIFDREGTPLMALIPYPNEDNVIFWMDHSAV 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 224 SQVNRINETKHSVLQ-YVGGVMSVEMQAPKLLWLKENLRETcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA- 301
Cdd:cd07768 115 NEAQWINMQCPQQLLdYLGGKISPEMGVPKLKYFLDEYSHL-RDKHFHIFDLHDYIAYELTRLYEWNICGLLGKENLDGe 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 302 ERGWDDSFWKMIGLEDfVADNYSKIGNQVLPPGASLGNGLtPEAARDLGLLPGIAVAASLIDAHAGGLGVIGADVKGhgl 381
Cdd:cd07768 194 ESGWSSSFFKNIDPRL-EHLTTTKNLPSNVPIGTTSGVAL-PEMAEKMGLHPGTAVVVSCIDAHASWFAVASPHLET--- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 382 vcegqpvtsRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVEGHAAFPELqVKARAR 461
Cdd:cd07768 269 ---------SLFMIAGTSSCHMYGTTISDRIPGVWGPFDTIIDPDYSVYEAGQSATGKLIEHLFESHPCARKF-DEALKK 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 462 CQSVYAYLNshlDLIKKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATVQAIALGTRFI 541
Cdd:cd07768 339 GADIYQVLE---QTIRQIEKNNGLSIHILTLDMFFGNRSEFADPRLKGSFIGESLDTSMLNLTYKYIAILEALAFGTRLI 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 542 IEAMEAAGHSISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGACASGDFA---SVQEAMAKMSKVGK 618
Cdd:cd07768 416 IDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAAVLAKVAAGKKQladSITEADISNDRKSE 495
|
570 580
....*....|....*....|...
gi 1622832061 619 VVFPRLQD-KKYYDKKYQVFLKL 640
Cdd:cd07768 496 TFEPLAYRlGADYILLYKLLCVK 518
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
66-640 |
4.16e-144 |
|
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: 428.49 E-value: 4.16e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 66 YYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKKWE--PQFNHHEQSSEDIWAACCVVTKGevgkellfpftfenlkare 142
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRG------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 143 lsdfptvtqvVCDKAelrflglklpgcvkvvqGIDLNQIRGLGFDATCS-LVVLDKQFRPlpvnheedsHRNVIMWLDHR 221
Cdd:cd07781 62 ----------ALAEA-----------------GVDPEDVVGIGVDTTSStVVPVDEDGNP---------LAPAILWMDHR 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 222 AVSQVNRINETKHSV----LQYVGGVMSVEMQAPKLLWLKENLRETcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKW 297
Cdd:cd07781 106 AQEEAAEINETAHPAleyyLAYYGGVYSSEWMWPKALWLKRNAPEV-YDAAYTIVEACDWINARLTGRWVRSRCAAGHKW 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 298 TYSAERG-WDDSFWKMIGLEDfvADNYSKIGNQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadv 376
Cdd:cd07781 185 MYNEWGGgPPREFLAALDPGL--LKLREKLPGEVVPVGEPAG-TLTAEAAERLGLPAGIPVAQGGIDAHMGAIGA----- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 377 kghGLVCEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIdhmveghAAFPELQV 456
Cdd:cd07781 257 ---GVVEPGT-----LALIMGTSTCHLMVSPKPVDIPGICGPVPDAVVPGLYGLEAGQSAVGDIF-------AWFVRLFV 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 457 K-ARARCQSVYAYLNshlDLIKKAQPV--GFLTVDlhvWpdFHGNRSPLADLTLKGMVTGLKLSQDLddlAILYLATVQA 533
Cdd:cd07781 322 PpAEERGDSIYALLS---EEAAKLPPGesGLVALD---W--FNGNRTPLVDPRLRGAIVGLTLGTTP---AHIYRALLEA 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 534 IALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGACASGDFASVQEAMAK 612
Cdd:cd07781 391 TAFGTRAIIERFEEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVAAGVYADIEEAADA 470
|
570 580
....*....|....*....|....*...
gi 1622832061 613 MSKVGKVVFPRLQDKKYYDKKYQVFLKL 640
Cdd:cd07781 471 MVRVDRVYEPDPENHAVYEELYALYKEL 498
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
65-646 |
2.25e-94 |
|
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: 299.83 E-value: 2.25e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 65 RYYVGVDVGTGSVRAALVDQSGVLLAFADQPIKKWEPQFNHHEQSSEDIWAACCvvtkgevgkellfpftfenlkarels 144
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVV-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 145 dfpTVTQVVCDKAelrflglklpgcvkvvqGIDLNQIRGLGFDAT-CSLVVLDKQFRPLpvnheedshRNVIMWLDHRAV 223
Cdd:COG1070 55 ---EAIRELLAKA-----------------GVDPEEIAAIGVSGQmHGLVLLDADGEPL---------RPAILWNDTRAA 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 224 SQVNRINET--KHSVLQYVGGVMSVEMQAPKLLWLKENLRETcWDKAGHFFDLPDFLSWKATG--VTARSLCSlvckWTY 299
Cdd:COG1070 106 AEAAELREElgEEALYEITGNPLHPGFTAPKLLWLKENEPEI-FARIAKVLLPKDYLRYRLTGefVTDYSDAS----GTG 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 300 ---SAERGWDDSFWKMIGL-EDFVAdnyskignQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigad 375
Cdd:COG1070 181 lldVRTRDWSDELLEALGIdRELLP--------ELVPPGEVAG-TLTAEAAAETGLPAGTPVVAGAGDNAAAALGA---- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 376 vkghGLVCEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVEghaafpelq 455
Cdd:COG1070 248 ----GAVEPGD-----AAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAVPGRWLPMGATNNGGSALRWFRD--------- 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 456 vKARARCQSVYAYLNshlDLIKKAqPVG-----FLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLailYLAT 530
Cdd:COG1070 310 -LFADGELDDYEELN---ALAAEV-PPGadgllFL-------PYLSGERTPHWDPNARGAFFGLTLSHTRAHL---ARAV 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 531 VQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGACASGDFASVQEAM 610
Cdd:COG1070 375 LEGVAFALRDGLEALEEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAA 454
|
570 580 590
....*....|....*....|....*....|....*.
gi 1622832061 611 AKMSKVGKVVFPRLQDKKYYDKKYQVFLKLVEHQKE 646
Cdd:COG1070 455 AAMVRVGETIEPDPENVAAYDELYERYRELYPALKP 490
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
64-651 |
5.48e-85 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 276.73 E-value: 5.48e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 64 ERYYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKKW---------EPQFNHHEQSSEDIWAAccvvtkgevgkellfpf 133
Cdd:PRK04123 2 MAYVIGLDFGTDSVRALLVDcATGEELATAVVEYPHWvkgryldlpPNQALQHPLDYIESLEA----------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 134 tfenlkarelsdfpTVTQVVCDkaelrflglklpgcvkvvQGIDLNQIRGLGFDAT-CSLVVLDKQFRPLPVN--HEEDS 210
Cdd:PRK04123 65 --------------AIPAVLKE------------------AGVDPAAVVGIGVDFTgSTPAPVDADGTPLALLpeFAENP 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 211 HRNVIMWLDHRAVSQVNRINETKHS-----VLQYVGGVMSVEMQAPKLL-WLKEN--LREtcwdKAGHFFDLPDFLSWKA 282
Cdd:PRK04123 113 HAMVKLWKDHTAQEEAEEINRLAHErgeadLSRYIGGIYSSEWFWAKILhVLREDpaVYE----AAASWVEACDWVVALL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 283 TGVTA-----RSLCSLVCKWTYSAERG--WDDSFWKMI--GLEDFVADnysKIGNQVLPPGASLGnGLTPEAARDLGLLP 353
Cdd:PRK04123 189 TGTTDpqdivRSRCAAGHKALWHESWGglPSADFFDALdpLLARGLRD---KLFTETWTAGEPAG-TLTAEWAQRLGLPE 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 354 GIAVAASLIDAHAGglgVIGADVKGHGLVcegqpvtsrlAVIcGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGG 433
Cdd:PRK04123 265 GVAVSVGAFDAHMG---AVGAGAEPGTLV----------KVM-GTSTCDILLADKQRAVPGICGQVDGSIVPGLIGYEAG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 434 QSVTGKLIDHMVEgHAAFPELQVKARARCQSVYAYLNshldliKKA--QPVG---FLTVDlhvWpdFHGNRSPLADLTLK 508
Cdd:PRK04123 331 QSAVGDIFAWFAR-LLVPPEYKDEAEARGKQLLELLT------EAAakQPPGehgLVALD---W--FNGRRTPLADQRLK 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 509 GMVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHADVTGMPVVLSQEVES 587
Cdd:PRK04123 399 GVITGLTLGTDAPDI---YRALIEATAFGTRAIMECFEDQGVPVEEVIAAGGIArKNPVLMQIYADVLNRPIQVVASDQC 475
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622832061 588 VLVGAAILGACASGDFASVQEAMAKM-SKVGKVVFPRLQDKKYYDKKYQVFLKLVE-HQKEYLAIM 651
Cdd:PRK04123 476 PALGAAIFAAVAAGAYPDIPEAQQAMaSPVEKTYQPDPENVARYEQLYQEYKQLHDyFGRGGNAVM 541
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
67-600 |
8.51e-76 |
|
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: 252.71 E-value: 8.51e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 67 YVGVDVGTGSVRAALVDQSGVLLAFADQPI--KKWEPQFNHHEQSSEDIWAAC--CVvtkgevgKELLfpftfenlkaRE 142
Cdd:cd07778 2 GIGIDVGSTSVRIGIFDYHGTLLATSERPIsyKQDPKDLWFVTQSSTEIWKAIktAL-------KELI----------EE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 143 LSDFptvtqvvcdkaelrflglklpgcvkvvqgidlnQIRGLGFDATCSLVVLDKQ-----FRPLPVNHEE-DSHRNVIM 216
Cdd:cd07778 65 LSDY---------------------------------IVSGIGVSATCSMVVMQRDsdtsyLVPYNVIHEKsNPDQDIIF 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 217 WLDHRAVSQVNRINE-TKHSVLQYVGGVMSVEMQAPKLLWLKENLRETCWDKAgHFFDLPDFLSWKatgvtarsLCSLVC 295
Cdd:cd07778 112 WMDHRASEETQWLNNiLPDDILDYLGGGFIPEMAIPKLKYLIDLIKEDTFKKL-EVFDLHDWISYM--------LATNLG 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 296 KW--TYSAER------------GWDDSFWKMIGLEDFVAD--NYSKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAA 359
Cdd:cd07778 183 HSniVPVNAPpsigigidgslkGWSKDFYSKLKISTKVCNvgNTFKEAPPLPYAGIPIGK-VNVILASYLGIDKSTVVGH 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 360 SLIDAHAGGLGVIGADVKghglvcegqpVTSRLAVICGTSSCHMGISKDPI--FVPGVWGPyFSAMVPGFWLNEGGQSVT 437
Cdd:cd07778 262 GCIDCYAGWFSTFAAAKT----------LDTTLFMVAGTSTCFLYATSSSQvgPIPGIWGP-FDQLLKNYSVYEGGQSAT 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 438 GKLIDHMVEGHAAFPELQvKARArcqSVYAYLNSHLDLI--KKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLK 515
Cdd:cd07778 331 GKLIEKLFNSHPAIIELL-KSDA---NFFETVEEKIDKYerLLGQSIHYLTRHMFFYGDYLGNRTPYNDPNMSGSFIGES 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 516 LSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADVTGMPVV---LSQEVESVLVGA 592
Cdd:cd07778 407 TDSSLTDLVLKYILILEFLAFQTKLIIDNFQKEKIIIQKVVISGSQAKNARLLQLLSTVLSKIHIivpLSDSKYAVVKGA 486
|
....*...
gi 1622832061 593 AILGACAS 600
Cdd:cd07778 487 ALLGKAAF 494
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
66-638 |
2.12e-71 |
|
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: 238.96 E-value: 2.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 66 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKKWEPQFNHHEQSSEDIWAACCVVTKgevgkELLfpftfenlkarelsd 145
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATR-----ALL--------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 146 fptvtqvvcDKAelrflglklpgcvkvvqGIDLNQIRGLGFDAT-CSLVVLDKQFRPLpvnheedshRNVIMWLDHRAVS 224
Cdd:cd07805 61 ---------EKS-----------------GIDPSDIAAIAFSGQmQGVVPVDKDGNPL---------RNAIIWSDTRAAE 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 225 QVNRINET---KHSVLQYVGGVMSVEMQAPKLLWLKENLRETcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA 301
Cdd:cd07805 106 EAEEIAGGlggIEGYRLGGGNPPSGKDPLAKILWLKENEPEI-YAKTHKFLDAKDYLNFRLTGRAATDPSTASTTGLMDL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 302 -ERGWDDSFWKMIGLEDfvadnySKIgNQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGViGADVKGHG 380
Cdd:cd07805 185 rKRRWSEELLRAAGIDP------DKL-PELVPSTEVVG-ELTPEAAAELGLPAGTPVVGGGGDAAAAALGA-GAVEEGDA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 381 LVCegqpvtsrlaviCGTSS---CHmgiSKDPIFVPGvwGPYFS--AMVPGFWLNEGGQSVTGKLIDHMVEgHAAFPELQ 455
Cdd:cd07805 256 HIY------------LGTSGwvaAH---VPKPKTDPD--HGIFTlaSADPGRYLLAAEQETAGGALEWARD-NLGGDEDL 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 456 VKararcqSVYAYLNshlDLIKKAQP----VGFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAilyLATV 531
Cdd:cd07805 318 GA------DDYELLD---ELAAEAPPgsngLLFL-------PWLNGERSPVEDPNARGAFIGLSLEHTRADLA---RAVL 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 532 QAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADVTGMPV-VLSQEVESVLVGAAILGACASGDFASVQEAm 610
Cdd:cd07805 379 EGVAFNLRWLLEALEKLTRKIDELRLVGGGARSDLWCQILADVLGRPVeVPENPQEAGALGAALLAAVGLGLLKSFDEA- 457
|
570 580
....*....|....*....|....*...
gi 1622832061 611 AKMSKVGKVVFPRLQDKKYYDKKYQVFL 638
Cdd:cd07805 458 KALVKVEKVFEPDPENRARYDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
66-640 |
1.80e-69 |
|
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: 233.97 E-value: 1.80e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 66 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKKWEPQFNHHEQSSEDIWAACCVVTKgEVGKEllfpftfenlkarelsd 145
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALR-ELLAK----------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 146 fptvtqvvcdkaelrflglklpgcvkvvQGIDLNQIRGLGFDA-TCSLVVLDKQFRPLpvnheedshRNVIMWLDHRAVS 224
Cdd:cd07808 63 ----------------------------AGISPSDIAAIGLTGqMHGLVLLDKNGRPL---------RPAILWNDQRSAA 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 225 QVNRINET-KHSVLQYVGGVMSVEMQAPKLLWLKENLRETcWDKAGHFFdLP-DFLSWKATGVTArslcslvckwT-YS- 300
Cdd:cd07808 106 ECEELEARlGDEILIITGNPPLPGFTLPKLLWLKENEPEI-FARIRKIL-LPkDYLRYRLTGELA----------TdPSd 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 301 ---------AERGWDDSFWKMIGLEdfvadnyskigNQVLPP---GASLGNGLTPEAARDLGLLPGIAVAASLIDAHAGG 368
Cdd:cd07808 174 asgtllfdvEKREWSEELLEALGLD-----------PSILPPiveSTEIVGTLTPEAAEELGLPEGTPVVAGAGDNAAAA 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 369 LGVigadvkghGLVCEGQPV----TSrlAVICGTSSCHMGISKDPIF-----VPGVW---GPYFSAmvpGF---WLNE-- 431
Cdd:cd07808 243 LGA--------GVVEPGDALislgTS--GVVFAPTDKPVPDPKGRLHtfphaVPGKWyamGVTLSA---GLslrWLRDlf 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 432 GGQSVTGKLIDHMVEGHAAfpelqvkararcqsvyaylnshldlikKAQPVGFLtvdlhvwPDFHGNRSPLADLTLKGMV 511
Cdd:cd07808 310 GPDRESFDELDAEAAKVPP---------------------------GSEGLLFL-------PYLSGERTPYWDPNARGSF 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 512 TGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLVG 591
Cdd:cd07808 356 FGLSLSHTRAHLA---RAVLEGVAFSLRDSLEVLKELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYG 432
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1622832061 592 AAILGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKL 640
Cdd:cd07808 433 AALLAAVGAGVFDDLEEAAAACIKIEKTIEPDPERHEAYDELYARYREL 481
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
66-630 |
3.00e-67 |
|
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: 226.63 E-value: 3.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 66 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKKWEPQFNHHEQSSEDIWAACCVVTKGevgkellfpftfenlkarelsd 145
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKE---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 146 fptvtqvVCDKAelrflglklpgcvkvvqGIDLNQIRGLGFDAT-CSLVVLDKQFRPLpvnheedshRNVIMWLDHRAVs 224
Cdd:cd07779 59 -------AVAKA-----------------GVDPEDIAAIGLTSQrSTFVPVDEDGRPL---------RPAISWQDKRTA- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 225 qvnrinetkhsvlqyvggvmsvemqapkllwlkenlretcwdkagHFFDLPDFLSWKATGVtarslcsLVCKWTYSAERG 304
Cdd:cd07779 105 ---------------------------------------------KFLTVQDYLLYRLTGE-------FVTDTTSASRTG 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 305 --------WDDSFWKMIGLEdfvADNYSKIgnqvLPPGASLGNgLTPEAARDLGLLPGIAVAASlidAHAGGLGVIGADV 376
Cdd:cd07779 133 lpdirtrdWSDDLLDAFGID---RDKLPEL----VPPGTVIGT-LTKEAAEETGLPEGTPVVAG---GGDQQCAALGAGV 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 377 KGHGLVCegqpvtsrlaVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVEghaAFPELQV 456
Cdd:cd07779 202 LEPGTAS----------LSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWVLEGSINTGGSAVRWFRD---EFGQDEV 268
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 457 KARARCQSVYAYLNSHLDLIkkaqPVGFLtvDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLailYLATVQAIAL 536
Cdd:cd07779 269 AEKELGVSPYELLNEEAAKS----PPGSD--GLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHL---ARAILEGIAF 339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 537 GTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGACASGDFASVQEAMAKMSKV 616
Cdd:cd07779 340 ELRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAMVRV 419
|
570
....*....|....
gi 1622832061 617 GKVVFPRLQDKKYY 630
Cdd:cd07779 420 TDTFEPDPENVAIY 433
|
|
| L-ribulokinase |
TIGR01234 |
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely ... |
66-648 |
1.92e-62 |
|
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: 216.71 E-value: 1.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 66 YYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKKWEpqfnhheqssediwaaccvvtKGEVgkellFPFTFENLKARELS 144
Cdd:TIGR01234 2 YAIGVDFGTLSGRALAVDvATGEEIATAVEWYRHWV---------------------KGQF-----LPKTGAKLPNDQAL 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 145 DFPTvtqvvcDKAELrfLGLKLPGCVKVVqGIDLNQIRGLGFDAT-CSLVVLDKQFRPLPV--NHEEDSHRNVIMWLDHR 221
Cdd:TIGR01234 56 QHPA------DYIEV--LEAAIPTVLAEL-GVDPADVVGIGVDFTaCTPAPIDSDGNPLCLlpEFAENPHAYFKLWKHHA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 222 AVSQVNRINETKHS----VLQYVGGVMSVEMQAPKLLWLKENLRETcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKW 297
Cdd:TIGR01234 127 AQEEADRINRLAHApgevDLSRYGGIISSEWFWAKILQITEEDPAI-YQAADRWIELADWIVAQLSGDIRRGRCTAGYKA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 298 TYSAERGW-DDSFWKMI--GLEDFVADNYSK-IGNQVLPPGAslgngLTPEAARDLGLLPGIAVAASLIDAHaggLGVIG 373
Cdd:TIGR01234 206 LWHESWGYpSASFFDELnpILNRHLPDKLFTdIWTAGEPAGT-----LTPEWAQRTGLPEGVVVAVGNFDAH---VGAVA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 374 ADVkghglvceGQPvtSRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVEgHAAFPE 453
Cdd:TIGR01234 278 AGI--------AQP--GALVKIMGTSTCHVLIGDKQRAVPGMCGVVDGGIVPGFIGYEAGQSAVGDIFAWFGK-VCVPPE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 454 LQVKARARCQSVYaylnSHLDLIKKAQPV---GFLTVDlhvWpdFHGNRSPLADLTLKGMVTGLKLSQDLDDlaiLYLAT 530
Cdd:TIGR01234 347 LKTEANASQKQLH----EALSEAAAKQPSgehGLVALD---W--FNGNRSPLVDQRLKGVITGLTLATDAPL---LYRAL 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 531 VQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGACASGDFASVQEA 609
Cdd:TIGR01234 415 IEATAFGTRMIMETFTDSGVPVEELMAAGGIArKNPVIMQIYADVTNRPLQIVASDQAPALGAAIFAAVAAGVYADIPSA 494
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1622832061 610 MAKMSKVGKVVF-PRLQDKKYYDKKYQVFLKLVEHQKEYL 648
Cdd:TIGR01234 495 QAKMGSAVEKTLtPCSENAQRYEQLYARYQELAMSFGQYN 534
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
392-599 |
3.11e-59 |
|
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: 197.16 E-value: 3.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 392 LAVICGTSSCHMGISKDP-IFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVEGHAAFPELQvkARARCQSVYAYLN 470
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPvLSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELR--DAGNVESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 471 SHLDLikkaqpvgfLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLddlAILYLATVQAIALGTRFIIEAMEA-AG 549
Cdd:pfam02782 79 LAAVA---------PAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTL---AHLYRAILESLALQLRQILEALTKqEG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622832061 550 HSISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGACA 599
Cdd:pfam02782 147 HPIDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
66-597 |
3.61e-58 |
|
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: 202.07 E-value: 3.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 66 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKKWEPQFNHHEQSSEDIWAACCvvtkgevgkELLfpftfenlkaRELSd 145
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALR---------SLL----------RELP- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 146 fptvtqvvcdkAELRflglklpgcvkvvqgidLNQIRGLGFDATC-SLVVLDKQFRPLpvnheedshRNVIMWLDHRAVS 224
Cdd:cd07783 61 -----------AELR-----------------PRRVVAIAVDGTSgTLVLVDREGEPL---------RPAIMYNDARAVA 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 225 QVNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLRETcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAERG 304
Cdd:cd07783 104 EAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEV-LAKTAKFLHQADWLAGRLTGDRGVTDYNNALKLGYDPETG 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 305 -WDDSFWKMIGLEdfvadnySKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvkghGLVC 383
Cdd:cd07783 183 rWPSWLLALLGIP-------PDLLPRVVAPGTVIGT-LTAEAAEELGLPAGTPVVAGTTDSIAAFLAS--------GAVR 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 384 EGQPVTSrlaviCGTSSCHMGISKDPIFVPGVwGPYFSAMVPGFWLNEGGQSVTGKLIDHmveghaAFPELQVKArarcq 463
Cdd:cd07783 247 PGDAVTS-----LGTTLVLKLLSDKRVPDPGG-GVYSHRHGDGYWLVGGASNTGGAVLRW------FFSDDELAE----- 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 464 svyaylnshldLIKKAQPVGflTVDLHVWP-DFHGNRSPLADLTLKGMVTGLKlsqdlDDLAILYLATVQAIALGTRFII 542
Cdd:cd07783 310 -----------LSAQADPPG--PSGLIYYPlPLRGERFPFWDPDARGFLLPRP-----HDRAEFLRALLEGIAFIERLGY 371
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622832061 543 EAMEAAGHS-ISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLvGAAILGA 597
Cdd:cd07783 372 ERLEELGAPpVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEAAL-GAALLAA 426
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
66-596 |
1.22e-57 |
|
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466787 [Multi-domain] Cd Length: 392 Bit Score: 199.71 E-value: 1.22e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 66 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKKWEPQFNHHEQSSEDIWAACCvvtkgevgkellfpftfENLKArelsd 145
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVV-----------------EAIRE----- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 146 fptvtqvVCDKAelrflglklpgcvkvvqGIDLNQIRGLGFDAT-CSLVVLDKQFRPLpvnheedshRNVIMWLDHRAvs 224
Cdd:cd00366 59 -------VLAKA-----------------GIDPSDIAAIGISGQmPGVVLVDADGNPL---------RPAIIWLDRRA-- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 225 qvnrinetkhsvlqyvggvmsvemqapkllwlkenlretcwdkagHFFDLPDFLSWKATGVTA--RSLCSLVCKWTYsAE 302
Cdd:cd00366 104 ---------------------------------------------KFLQPNDYIVFRLTGEFAidYSNASGTGLYDI-KT 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 303 RGWDDSFWKMIGL-EDFVADnyskignqVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvkghGL 381
Cdd:cd00366 138 GDWSEELLDALGIpREKLPP--------IVESGEVVG-RVTPEAAEETGLPAGTPVVAGGGDTAAAALGA--------GV 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 382 VCEGQPVtsrlaVICGTSSCHMGISKDPIFVPGVWGPYFSAmVPGFWLNEGGQSVTGKLIDHMVEghaafpelqvkARAR 461
Cdd:cd00366 201 VEPGDAV-----DSTGTSSVLSVCTDEPVPPDPRLLNRCHV-VPGLWLLEGAINTGGASLRWFRD-----------EFGE 263
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 462 CQSVYAYLNSHLDLIKKAQP----VGFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLailYLATVQAIALG 537
Cdd:cd00366 264 EEDSDAEYEGLDELAAEVPPgsdgLIFL-------PYLSGERSPIWDPAARGVFFGLTLSHTRAHL---IRAVLEGVAYA 333
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622832061 538 TRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLVGAAILG 596
Cdd:cd00366 334 LRDNLEILEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
66-601 |
5.96e-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: 5.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 66 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKKWEPQFNHHEQSSEDIWAACCvvtkgEVGKELLfpftfenlkarelsd 145
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVC-----EIIRELL--------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 146 fptvtqvvcDKAelrflglklpgcvkvvqGIDLNQIRGLGfdatCS-----LVVLDKQFRPLpvnheedshRNVIMWLDH 220
Cdd:cd07804 61 ---------AKA-----------------GISPKEIAAIG----VSglvpaLVPVDENGKPL---------RPAILYGDR 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 221 RAVSQVNRINETKHS--VLQYVGGVMSVEMQAPKLLWLKENLRETcWDKAGHFFDLPDFLSWKATG--VTARSLCSLvck 296
Cdd:cd07804 102 RATEEIEWLNENIGEdrIFEITGNPLDSQSVGPKLLWIKRNEPEV-FKKTRKFLGAYDYIVYKLTGeyVIDYSSAGN--- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 297 wtYS-----AERGWDDSFWKMIGLEdfvadnySKIGNQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGV 371
Cdd:cd07804 178 --EGglfdiRKRTWDEELLEALGID-------PDLLPELVPSTEIVG-EVTKEAAEETGLAEGTPVVAGTVDAAASALSA 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 372 igadvkghGLVCEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFSamVPGFWLNEGGQSVTGKLIDHMVEGHAaf 451
Cdd:cd07804 248 --------GVVEPGD-----LLLMLGTAGDIGVVTDKLPTDPRLWLDYHD--IPGTYVLNGGMATSGSLLRWFRDEFA-- 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 452 PELQVKARARCQSVYAYLNshldliKKAQ--PVGfltVD-LHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLailYL 528
Cdd:cd07804 311 GEEVEAEKSGGDSAYDLLD------EEAEkiPPG---SDgLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHL---YR 378
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622832061 529 ATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGACASG 601
Cdd:cd07804 379 ALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
66-601 |
1.77e-53 |
|
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: 189.72 E-value: 1.77e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 66 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKKWEPQFNHHEQSSEDIWAACCVVTKgevgkellfpftfenlkarelsd 145
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIR----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 146 fptvtqvvcdkaelrflglklpgcvKVVQGIDLNQIRGLGFdAT--CSLVVLDKQFRPLpvnheedshRNVIMWLDHRAV 223
Cdd:cd07773 58 -------------------------EAAAQAGPDPIAAISV-SSqgESGVPVDRDGEPL---------GPAIVWFDPRGK 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 224 SQVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLRETcWDKAGHFFDLPDFLSWKATGVTARSLcSLVCKWTY-- 299
Cdd:cd07773 103 EEAEELAEriGAEELYRITGLPPSPMYSLAKLLWLREHEPEI-FAKAAKWLSVADYIAYRLTGEPVTDY-SLASRTMLfd 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 300 SAERGWDDSfwkmigLEDFVADNYSKIGnQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvkgh 379
Cdd:cd07773 181 IRKRTWSEE------LLEAAGIDASLLP-ELVPSGTVIGT-VTPEAAEELGLPAGTPVVVGGHDHLCAALGA-------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 380 GLVCEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFS---AMVPGFWLNEGGQSvTGKLIDHMVEGHAAFPELQV 456
Cdd:cd07773 245 GVIEPGD-----VLDSTGTAEALLAVVDEPPLDEMLAEGGLSyghHVPGGYYYLAGSLP-GGALLEWFRDLFGGDESDLA 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 457 KARARCQSVYAylnshldlikKAQPVGFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDDlaiLYLATVQAIAL 536
Cdd:cd07773 319 AADELAEAAPP----------GPTGLLFL-------PHLSGSGTPDFDPDARGAFLGLTLGTTRAD---LLRAILEGLAF 378
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622832061 537 GTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGACASG 601
Cdd:cd07773 379 ELRLNLEALEKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
66-601 |
3.81e-53 |
|
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: 3.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 66 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKKWEPQFNHHEQSSEDIWAACCVVTKGevgkellfpftfenlkarelsd 145
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRE---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 146 fptvtqvVCDKAelrflglklpgcvkvvqGIDLNQIRGLGFDAT-CSLVVLDKQFRPLpvnheedshRNVIMWLDHRAVS 224
Cdd:cd07802 59 -------LLEKS-----------------GVDPSDIAGVGVTGHgNGLYLVDKDGKPV---------RNAILSNDSRAAD 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 225 QVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLRETcWDKAGHFFDLPDFLSWKATGVtarslcsLVCKWT-YSA 301
Cdd:cd07802 106 IVDRWEEdgTLEKVYPLTGQPLWPGQPVALLRWLKENEPER-YDRIRTVLFCKDWIRYRLTGE-------ISTDYTdAGS 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 302 ------ERGWDDSFWKMIGLEDFvadnYSKIGnQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigad 375
Cdd:cd07802 178 slldldTGEYDDELLDLLGIEEL----KDKLP-PLVPSTEIAG-RVTAEAAALTGLPEGTPVAAGAFDVVASALGA---- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 376 vkghGLVCEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGpYFSAMVPGFWLNEGGQSVTGKLIDHMVEghaafpELQ 455
Cdd:cd07802 248 ----GAVDEGQ-----LCVILGTWSINEVVTDEPVVPDSVGS-NSLHADPGLYLIVEASPTSASNLDWFLD------TLL 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 456 VKARARCQSVYAYLNshlDLIKKAQPVG----FLtvdlhvwPDFHGNRsplADLTLKGMVTGLKLSQDLDDLAilyLATV 531
Cdd:cd07802 312 GEEKEAGGSDYDELD---ELIAAVPPGSsgviFL-------PYLYGSG---ANPNARGGFFGLTAWHTRAHLL---RAVY 375
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 532 QAIALGTRFIIEAMEAAGHsISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGACASG 601
Cdd:cd07802 376 EGIAFSHRDHLERLLVARK-PETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
66-641 |
1.97e-51 |
|
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: 185.07 E-value: 1.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 66 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKKWEPQFNHHEQSSEDIWAAccvvtkgevgkellfpfTFENLKarelsd 145
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEA-----------------VLEALK------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 146 fptvtqvvcdkaelrflglklpgcvKVVQGIDLNQIRGLGFDATC-SLVVLDKQFRPLpvnheedshRNVIMWLDHRAVS 224
Cdd:cd07770 58 -------------------------EVLAKLGGGEVDAIGFSSAMhSLLGVDEDGEPL---------TPVITWADTRAAE 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 225 QVNRI--NETKHSVLQYVGGVMSVEMQAPKLLWLKENLRETcWDKAGHFFDLPDFLSWKATG--VTARSLCSlvckWT-- 298
Cdd:cd07770 104 EAERLrkEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPEL-FAKAAKFVSIKEYLLYRLTGelVTDYSTAS----GTgl 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 299 -YSAERGWDDSFWKMIGLEdfvADNYSKIgnqvLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGViGADVK 377
Cdd:cd07770 179 lNIHTLDWDEEALELLGID---EEQLPEL----VDPTEVLP-GLKPEFAERLGLLAGTPVVLGASDGALANLGS-GALDP 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 378 GhglvcegqpvtsRLAVICGTSschmG----ISKDPIFVP--GVWgPYFSAmvPGFWL-----NEGGqSVTGKLIDHMVE 446
Cdd:cd07770 250 G------------RAALTVGTS----GairvVSDRPVLDPpgRLW-CYRLD--ENRWLvggaiNNGG-NVLDWLRDTLLL 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 447 GHAAFPELQVKARArcqsvyAYLNSHlDLIkkaqpvgFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLail 526
Cdd:cd07770 310 SGDDYEELDKLAEA------VPPGSH-GLI-------FL-------PYLAGERAPGWNPDARGAFFGLTLNHTRADI--- 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 527 YLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGACASGDFASV 606
Cdd:cd07770 366 LRAVLEGVAFNLKSIYEALEELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSL 445
|
570 580 590
....*....|....*....|....*....|....*
gi 1622832061 607 QEamAKMSKVGKVVFPRLQDKKYYDKKYQVFLKLV 641
Cdd:cd07770 446 EA--DELVKIGKVVEPDPENHAIYAELYERFKKLY 478
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
66-601 |
2.80e-37 |
|
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: 144.62 E-value: 2.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 66 YYVGVDVGTGSVRAALVD-QSGVLLAFADQPikkWEPQFNHH---EQSSEDIWAACCVVTKgevgkellfpftfenlKAR 141
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAP---HENILIDPgwaEQDPEDWWDALQAAFA----------------QLL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 142 ELSdfptvtqvvcdkaelrflglklpgcvkvvqGIDLNQIRGLGFDATC-SLVVLDKQFRPLpvnheedshRNVIMWLDH 220
Cdd:cd07809 62 KDA------------------------------GAELRDVAAIGISGQMhGLVALDADGKVL---------RPAKLWCDT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 221 RAVSQVNRINET-KHSVLQYVGGVMSVEMQAPKLLWLKENlRETCWDKAgHFFDLP-DFLSWKATG--VTARSLCSLVCk 296
Cdd:cd07809 103 RTAPEAEELTEAlGGKKCLLVGLNIPARFTASKLLWLKEN-EPEHYARI-AKILLPhDYLNWKLTGekVTGLGDASGTF- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 297 WTYSAERGWDdsfWKMIGLEDFVADNYSKIGnQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadv 376
Cdd:cd07809 180 PIDPRTRDYD---AELLAAIDPSRDLRDLLP-EVLPAGEVAG-RLTPEGAEELGLPAGIPVAPGEGDNMTGALGT----- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 377 kghGLVCEGQPVTSrlaviCGTSSCHMGISKDPIFVPgvwgpyfSAMVPGF--------WLNEG---GQSVTGKLIDHMV 445
Cdd:cd07809 250 ---GVVNPGTVAVS-----LGTSGTAYGVSDKPVSDP-------HGRVATFcdstggmlPLINTtncLTAWTELFRELLG 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 446 EGHAAFPELQVKARARCQSVYAYlnshldlikkaqpvgfltvdlhvwPDFHGNRSP-LADLTlkGMVTGLKLSQdlDDLA 524
Cdd:cd07809 315 VSYEELDELAAQAPPGAGGLLLL------------------------PFLNGERTPnLPHGR--ASLVGLTLSN--FTRA 366
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622832061 525 ILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGACASG 601
Cdd:cd07809 367 NLARAALEGATFGLRYGLDILRELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
66-601 |
6.37e-35 |
|
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: 137.74 E-value: 6.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 66 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKKWEPQFNHH--EQSSEDIWAACCVVTKgevgkELLFpftfenlkarel 143
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYPDakEFDPEELWEKICEAIR-----EALK------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 144 sdfptvtqvvcdKAelrflglklpgcvkvvqGIDLNQIRGLgfdATCS----LVVLDKQFRPL---PvNHeedshrnvim 216
Cdd:cd07798 64 ------------KA-----------------GISPEDISAV---SSTSqregIVFLDKDGRELyagP-NI---------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 217 wlDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAP-KLLWLKENlRETCWDKAGHFFDLPDFLSWKATGVtarslcsLVC 295
Cdd:cd07798 101 --DARGVEEAAEIDDEFGEEIYTTTGHWPTELFPAaRLLWFKEN-RPEIFERIATVLSISDWIGYRLTGE-------LVS 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 296 KWTYSAE--------RGWDDSFWKMIGLEDfvadnysKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAG 367
Cdd:cd07798 171 EPSQASEtqlfdikkREWSQELLEALGLPP-------EILPEIVPSGTVLGT-VSEEAARELGLPEGTPVVVGGADTQCA 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 368 GLGViGADVKGHglvcegqpvtsrLAVICGTSSCHMGISKDPIFVP--GVW-GPYfsaMVPGFWLNEGGQSVTGKLIDHM 444
Cdd:cd07798 243 LLGS-GAIEPGD------------IGIVAGTTTPVQMVTDEPIIDPerRLWtGCH---LVPGKWVLESNAGVTGLNYQWL 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 445 VEGHAAFPelqvkararcQSVYAYLNSHLDLIKKAQP--VGFLTVDLhvwpdFHGNRSPLADLTLKGMVTGLKLSQDLDD 522
Cdd:cd07798 307 KELLYGDP----------EDSYEVLEEEASEIPPGANgvLAFLGPQI-----FDARLSGLKNGGFLFPTPLSASELTRGD 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 523 LAIlylATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGACASG 601
Cdd:cd07798 372 FAR---AILENIAFAIRANLEQLEEvSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
66-601 |
7.29e-30 |
|
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: 123.12 E-value: 7.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 66 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKKWEPQFNHHEQSSEDIWAACcvvtkgevgkellfpftfenlkarelsd 145
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAV---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 146 FPTVTQVVcDKAELRFlglklpgcvkvvqgidlNQIRGLGFDAT---CSLVvlDKQFRPLpvnheedshRNVIMWLDHRA 222
Cdd:cd24121 53 VATIREVV-AKLDVLP-----------------DRVAAIGVTGQgdgTWLV--DEDGRPV---------RDAILWLDGRA 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 223 VSQVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLRETCwDKAGHFFDLPDFLSWKATGVTA--RSLCSLvckwT 298
Cdd:cd24121 104 ADIVERWQAdgIAEAVFEITGTGLFPGSQAAQLAWLKENEPERL-ERARTALHCKDWLFYKLTGEIAtdPSDASL----T 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 299 Y--SAERGWDDSFWKMIGLEDFVAdnyskignqVLPP-GASLGNG--LTPEAARDLGLLPGIAVAASLIDAHAGGLGViG 373
Cdd:cd24121 179 FldFRTRQYDDEVLDLLGLEELRH---------LLPPiRPGTEVIgpLTPEAAAATGLPAGTPVVLGPFDVVATALGS-G 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 374 ADVKGHGLvcegqpvtsrlaVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWL----NEGGQSVTGKLIDHMVEGHA 449
Cdd:cd24121 249 AIEPGDAC------------SILGTTGVHEVVVDEPDLEPEGVGYTICLGVPGRWLramaNMAGTPNLDWFLRELGEVLK 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 450 AFPELQVKARARcqsvyaylnsHLDLIKKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAilyLA 529
Cdd:cd24121 317 EGAEPAGSDLFQ----------DLEELAASSPPGAEGVLYHPYLSPAGERAPFVNPNARAQFTGLSLEHTRADLL---RA 383
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622832061 530 TVQAIALGTRFIIEAMeaaGHSISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGACASG 601
Cdd:cd24121 384 VYEGVALAMRDCYEHM---GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
66-635 |
7.95e-25 |
|
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: 108.57 E-value: 7.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 66 YYVGVDVGTGSVRAALVDQSGVLLAFADqpiKKWEPQFNHHEQSSEDiwaaccvvtkgevgkellfpFTFENlkarelsd 145
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQ---REWRHKEVPDVPGSMD--------------------FDTEK-------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 146 fptVTQVVCDkaelrflglklpgCVKVV---QGIDLNQIRGLgfdATCS----LVVLDKQFRPLPVNHeedshrNVimwl 218
Cdd:cd07775 50 ---NWKLICE-------------CIREAlkkAGIAPKSIAAI---STTSmregIVLYDNEGEEIWACA------NV---- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 219 DHRAVSQVNRINETKHSVLQ--YVGGVMSVEMQA-PKLLWLKENLRETcWDKAGHFFDLPDFLSWKATGVTAR--SLCSL 293
Cdd:cd07775 101 DARAAEEVSELKELYNTLEEevYRISGQTFALGAiPRLLWLKNNRPEI-YRKAAKITMLSDWIAYKLSGELAVepSNGST 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 294 VCKWTySAERGWDDSFWKMIGLEDFvadnyskIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVig 373
Cdd:cd07775 180 TGLFD-LKTRDWDPEILEMAGLKAD-------ILPPVVESGTVIGK-VTKEAAEETGLKEGTPVVVGGGDVQLGCLGL-- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 374 advkghGLVCEGQpvtsrlAVICGTSSCHMGI-SKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVEghAAFP 452
Cdd:cd07775 249 ------GVVRPGQ------TAVLGGSFWQQEVnTAAPVTDPAMNIRVNCHVIPDMWQAEGISFFPGLVMRWFRD--AFCA 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 453 ELQVKARARCQSVYAYLNshldliKKAQ--PVGF-----LTVDL-------HVWPDFhgnrspladltlkgmvTGLKLSQ 518
Cdd:cd07775 315 EEKEIAERLGIDAYDLLE------EMAKdvPPGSygimpIFSDVmnyknwrHAAPSF----------------LNLDIDP 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 519 DLDDLAILYLATVQAIALGTRFIIEAMEAA-GHSISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGA 597
Cdd:cd07775 373 EKCNKATFFRAIMENAAIVSAGNLERIAEFsGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAG 452
|
570 580 590
....*....|....*....|....*....|....*...
gi 1622832061 598 CASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQ 635
Cdd:cd07775 453 VGAGIYSSLEEAVESLVKWEREYLPNPENHEVYQDLYE 490
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
66-370 |
5.31e-23 |
|
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: 98.56 E-value: 5.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 66 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKKWEPQFNHHEQSSEDIWAACCvvtkgevgkellfpftfenlkarelsd 145
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVA--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 146 fpTVTQVVCDKAelrflglklpgcvkvvqGIDLNQIRGLGFDATC-SLVVLDKQFRPLpvnheedshRNVIMWLDHRAVS 224
Cdd:pfam00370 54 --QCIAKTLSQL-----------------GISLKQIKGIGISNQGhGTVLLDKNDKPL---------YNAILWKDRRTAE 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 225 QVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLRETcWDKAGHFFDLPDFLSWKATG--VTARSLCSlVCKWTYS 300
Cdd:pfam00370 106 IVENLKEegNNQKLYEITGLPIWPGFTLSKLRWIKENEPEV-FEKIHKFLTIHDYLRWRLTGvfVTDHTNAS-RSMMFNI 183
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622832061 301 AERGWDDSFWKMIGLEdfvadnyskigNQVLPP----GASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLG 370
Cdd:pfam00370 184 HKLDWDPELLAALGIP-----------RDHLPPlvesSEIYGE-LNPELAAMWGLDEGVPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
493-642 |
2.48e-15 |
|
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466789 [Multi-domain] Cd Length: 486 Bit Score: 79.05 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 493 PDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMH 571
Cdd:cd07769 341 PAFSGLGAPYWDPDARGAIVGLTRGTTKAHIV---RAALESIAYQTRDVLEAMEKdSGIKLKELRVDGGATANNFLMQFQ 417
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622832061 572 ADVTGMPVVLSQEVESVLVGAAILGACASGdFASVQEAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 642
Cdd:cd07769 418 ADILGVPVVRPKVAETTALGAAYLAGLAVG-FWKDLDELASLWQVDKRFEPSMDEEE-RERLYRGWKKAVE 486
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
67-640 |
5.56e-15 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 78.09 E-value: 5.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 67 YVGVDVGTGSVRAALVDQSGVLLAFADQPIKKWEPQFNHHEQSSEDIWAACCVVTKGeVGKEllfpFTFENLKArelsdf 146
Cdd:PRK15027 2 YIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKA-LGDQ----HSLQDVKA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 147 ptvtqvvcdkaelrfLGLKlpgcvkvvqgidlNQIRGlgfdATcslvVLDKQFRPLpvnheedshRNVIMWLDHRAVSQV 226
Cdd:PRK15027 71 ---------------LGIA-------------GQMHG----AT----LLDAQQRVL---------RPAILWNDGRCAQEC 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 227 NRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLRETCWDKAGHFfdLP-DFLSWKATGVTARSLCSLV-CKWTYSAERG 304
Cdd:PRK15027 106 ALLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVL--LPkDYLRLRMTGEFASDMSDAAgTMWLDVAKRD 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 305 WDDSfwkMIGLEDFVADNYSkignqVLPPGASLGNGLTPEAARDLGlLPGIAVAASLIDAHAGGLGVigadvkghGLVCE 384
Cdd:PRK15027 184 WSDV---MLQACHLSRDQMP-----ALYEGSEITGALLPEVAKAWG-MATVPVVAGGGDNAAGAVGV--------GMVDA 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 385 GQPVTSrlaviCGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWlneggqsvtgKLIDHMVeghAAFPELQVKARARCQ- 463
Cdd:PRK15027 247 NQAMLS-----LGTSGVYFAVSEGFLSKPESAVHSFCHALPQRW----------HLMSVML---SAASCLDWAAKLTGLs 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 464 SVYAYLNSHLDLIKKAQPVGFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATV-QAIALGtrfiI 542
Cdd:PRK15027 309 NVPALIAAAQQADESAEPVWFL-------PYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVgYALADG----M 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 543 EAMEAAGHSISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQ--EVESVLvGAAILGACASGDFASVQEAMAKMSkVGKVV 620
Cdd:PRK15027 378 DVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTggDVGPAL-GAARLAQIAANPEKSLIELLPQLP-LEQSH 455
|
570 580
....*....|....*....|
gi 1622832061 621 FPRLQDKKYYDKKYQVFLKL 640
Cdd:PRK15027 456 LPDAQRYAAYQPRRETFRRL 475
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
529-642 |
9.78e-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: 77.18 E-value: 9.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 529 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGACASGDFASVQ 607
Cdd:cd07792 384 AALEAVCFQTREILDAMNKdSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLD 463
|
90 100 110
....*....|....*....|....*....|....*
gi 1622832061 608 EAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 642
Cdd:cd07792 464 ELKSLNEGGRTVFEPQISEEE-RERRYKRWKKAVE 497
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
529-642 |
5.42e-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: 74.83 E-value: 5.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 529 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGACASGDFASVQ 607
Cdd:cd07786 374 AALESIAYQTRDLLEAMEAdSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLD 453
|
90 100 110
....*....|....*....|....*....|....*
gi 1622832061 608 EAmAKMSKVGKVVFPRLqDKKYYDKKYQVFLKLVE 642
Cdd:cd07786 454 EL-AKLWQVDRRFEPSM-SEEEREALYAGWKKAVK 486
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
529-629 |
6.00e-14 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 74.63 E-value: 6.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 529 ATVQAIALGTRFIIEAME-AAGHSISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGACASGDFASVQ 607
Cdd:PTZ00294 383 AALEAIALQTNDVIESMEkDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLE 462
|
90 100
....*....|....*....|..
gi 1622832061 608 EAMAKMSKVGKVVFPRLQDKKY 629
Cdd:PTZ00294 463 EVKKLIRRSNSTFSPQMSAEER 484
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
66-643 |
2.13e-13 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 73.12 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 66 YYVGVDVGTGSVRAALVDQSGVLLAFADqpiKKWEpqfnhHeQSSEDIwaaccvvtkgevgkellfPFTFEnlkarelSD 145
Cdd:PRK10939 4 YLMALDAGTGSIRAVIFDLNGNQIAVGQ---AEWR-----H-LAVPDV------------------PGSME-------FD 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 146 FPTVTQVVCDkaelrflglklpgCVKVV---QGIDLNQIRGLgfdATCSL----VVLDKQFRPLpvnheedshrnvimW- 217
Cdd:PRK10939 50 LEKNWQLACQ-------------CIRQAlqkAGIPASDIAAV---SATSMregiVLYDRNGTEI--------------Wa 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 218 ---LDHRAVSQVNRINETkHSVLQYvgGVMSVEMQA------PKLLWLKENLRETcWDKAGHFFDLPDFLSWKATGVTA- 287
Cdd:PRK10939 100 canVDARASREVSELKEL-HNNFEE--EVYRCSGQTlalgalPRLLWLAHHRPDI-YRQAHTITMISDWIAYMLSGELAv 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 288 -------RSLCSLVckwtysaERGWDDSFWKMIGLEDfvadnysKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAAS 360
Cdd:PRK10939 176 dpsnagtTGLLDLV-------TRDWDPALLEMAGLRA-------DILPPVKETGTVLGH-VTAKAAAETGLRAGTPVVMG 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 361 LIDAHAGGLGVigadvkghGLVCEGQpvtsrLAVICGT------------SSCHMGISKDPifvpgvwgpyfsAMVPGFW 428
Cdd:PRK10939 241 GGDVQLGCLGL--------GVVRPGQ-----TAVLGGTfwqqvvnlpapvTDPNMNIRINP------------HVIPGMV 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 429 LNEGGQSVTGkLIdhMVEGHAAF-PELQVKARARCQSVYAYLNshldliKKAQ--PVGFLTV-----DL-------HVWP 493
Cdd:PRK10939 296 QAESISFFTG-LT--MRWFRDAFcAEEKLLAERLGIDAYSLLE------EMASrvPVGSHGIipifsDVmrfkswyHAAP 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 494 DFhgnrspladltlkgmvtgLKLSQDLD--DLAILYLATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQM 570
Cdd:PRK10939 367 SF------------------INLSIDPEkcNKATLFRALEENAAIVSACNLQQIAAfSGVFPSSLVFAGGGSKGKLWSQI 428
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 571 HADVTGMPVVLSQEVESVLVGAAILGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKK-------YQVFLKLVEH 643
Cdd:PRK10939 429 LADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSLAETGERLVRWERTFEPNPENHELYQEAkekwqavYADQLGLVDH 508
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
493-642 |
7.52e-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: 71.05 E-value: 7.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 493 PDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAIlylATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMH 571
Cdd:cd07793 356 PAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVR---AILESIAFRVKQLLETMEKeTSIKISSIRVDGGVSNNDFILQLI 432
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622832061 572 ADVTGMPVVLSQEVESVLVGAAILGACASGDFASVqEAMAKMSKVGKVVFPRlQDKKYYDKKYQVFLKLVE 642
Cdd:cd07793 433 ADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSK-EELKKLRKIEKIFEPK-MDNEKREELYKNWKKAVK 501
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
66-595 |
1.45e-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: 66.86 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 66 YYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKKWEPQ--FNHHEQSSEDIWAACcvvtkgevgKELLfpftfENLKARE 142
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDlESGRILESVSRPTPAPISSddPGRSEQDPEKILEAV---------RNLI-----DELPREY 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 143 LSDfptvtqvvcdkaelrflglklpgcvkvVQGIDL-NQIRGLgfdatcslVVLDKQFRPLpvnheedshRNVIMWLDHR 221
Cdd:cd07777 67 LSD---------------------------VTGIGItGQMHGI--------VLWDEDGNPV---------SPLITWQDQR 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 222 AvsqvnriNETKHSVLQYVGGVMSVEMQAP--------KLLWLKENLRETcwDKAGHFFDLPDFLSWKATGvTARSLCSL 293
Cdd:cd07777 103 C-------SEEFLGGLSTYGEELLPKSGMRlkpgyglaTLFWLLRNGPLP--SKADRAGTIGDYIVARLTG-LPKPVMHP 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 294 VCK--WTY--SAERGWDDSFWKMIGLEdfvadnySKIGNQVLPPGASLGNgLTPEAARDLGLLPGI-----AVAASLIDA 364
Cdd:cd07777 173 TNAasWGLfdLETGTWNKDLLEALGLP-------VILLPEIVPSGEIVGT-LSSALPKGIPVYVALgdnqaSVLGSGLNE 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 365 HagglgvigadvkghglvcegqpvtSRLAVICGTSScHMGISKDPIFVPGVWG--PYFSamvpGFWLNeggqSVT----G 438
Cdd:cd07777 245 E------------------------NDAVLNIGTGA-QLSFLTPKFELSGSVEirPFFD----GRYLL----VAAslpgG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 439 KLIDHMVE-----GHAAFPELQVkararcQSVYAYLNShLDLIKKAQPvgfLTVDlhvwPDFHGNRSplaDLTLKGMVTG 513
Cdd:cd07777 292 RALAVLVDflrewLRELGGSLSD------DEIWEKLDE-LAESEESSD---LSVD----PTFFGERH---DPEGRGSITN 354
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 514 LklsqDLDDLAI--LYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGG-LSKNPLFVQMHADVTGMPVVLSQEVESVLV 590
Cdd:cd07777 355 I----GESNFTLgnLFRALCRGIAENLHEMLPRLDLDLSGIERIVGSGGaLRKNPVLRRIIEKRFGLPVVLSEGSEEAAV 430
|
....*
gi 1622832061 591 GAAIL 595
Cdd:cd07777 431 GAALL 435
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
252-629 |
1.82e-11 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 66.59 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 252 KLLWLKENlRETCWDKAGHFFDLPDFLSWKATGV--TARSLCSlVCKWTYSAERGWDDSFWKMIGLEdfvadnyskigNQ 329
Cdd:PRK10331 137 KLVWLKEN-HPQLLEQAHAWLFISSLINHRLTGEftTDITMAG-TSQMLDIQQRDFSPEILQATGLS-----------RR 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 330 VLPP----GASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGViGAD----VKGHG-----LVCEGQPVTSRLAVIC 396
Cdd:PRK10331 204 LFPRlveaGEQIGT-LQPSAAALLGLPVGIPVISAGHDTQFALFGS-GAGqnqpVLSSGtweilMVRSAQVDTSLLSQYA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 397 GtSSCHMGiSKDPIFVPGVWgpyfsamvpgfWLNEGGQSVTGKLI-------DHMVEGHAAFPelqvkarARCQSVYayL 469
Cdd:PRK10331 282 G-STCELD-SQSGLYNPGMQ-----------WLASGVLEWVRKLFwtaetpyQTMIEEARAIP-------PGADGVK--M 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 470 NSHLDLIKKAQPVGfLTVdlhvwpdfHGNRSPLADLTLKGMvtGLKLSQDLDDLailylatvqaialgtrfiieamEAAG 549
Cdd:PRK10331 340 QCDLLACQNAGWQG-VTL--------NTTRGHFYRAALEGL--TAQLKRNLQVL----------------------EKIG 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 550 H-SISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGACASGDFASVQEAMAKMSKVGKVVFPRLQDKK 628
Cdd:PRK10331 387 HfKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQARAQMKYQYRYFYPQTEPEF 466
|
.
gi 1622832061 629 Y 629
Cdd:PRK10331 467 I 467
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
529-643 |
2.08e-11 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 66.77 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 529 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGACASGDFASVQ 607
Cdd:PRK00047 380 ATLESIAYQTRDVLDAMQAdSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLD 459
|
90 100 110
....*....|....*....|....*....|....*.
gi 1622832061 608 EaMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVEH 643
Cdd:PRK00047 460 E-LKEQWKIDRRFEPQMDEEE-REKLYAGWKKAVKR 493
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
253-595 |
2.98e-08 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466792 [Multi-domain] Cd Length: 424 Bit Score: 56.50 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 253 LLWLKENLRETcWDKAGHFFDLPDFLSWKATGVTARSLCSLVC--------KWTYS---AERGWDDSFWKMigledfvad 321
Cdd:cd07772 129 LYWLKREKPEL-FARAKTILPLPQYWAWRLTGKAASEITSLGChtdlwdfeKNEYSslvKKEGWDKLFPPL--------- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 322 nyskignqvLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAgglgvigadvkghglvcegqpvtSRLAvicgtssc 401
Cdd:cd07772 199 ---------RKAWEVLGP-LRPDLARRTGLPKDIPVGCGIHDSNA-----------------------ALLP-------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 402 HMGISKDPiFV---PGVWgpyFSAMVPGF-----WLNEG-----GQSVTGKLIdhmveGHAAFP-----ELQVKARARCQ 463
Cdd:cd07772 238 YLAAGKEP-FTllsTGTW---CIAMNPGNdlpltELDLArdclyNLDVFGRPV-----KTARFMggreyERLVERIAKSF 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 464 SVYAYLNSHLDLIkkAQPVGFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATVQAIALgtrfiie 543
Cdd:cd07772 309 PQLPSLADLAKLL--ARGTFAL-------PSFAPGGGPFPGSGGRGVLSAFPSAEEAYALAILYLALMTDYAL------- 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1622832061 544 amEAAGHSISTLFLCGGLSKNPLFVQMHADV-TGMPVVLSQEVESVLVGAAIL 595
Cdd:cd07772 373 --DLLGSGVGRIIVEGGFAKNPVFLRLLAALrPDQPVYLSDDSEGTALGAALL 423
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
534-609 |
4.43e-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: 56.00 E-value: 4.43e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622832061 534 IALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADVTGMPVVLSqEVESVLVGAAILGACASGDFASVQEA 609
Cdd:cd07771 378 LALKYAKTIEELEElTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAG-PVEATAIGNLLVQLIALGEIKSLEEG 453
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
529-642 |
8.10e-07 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 52.01 E-value: 8.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 529 ATVQAIALGTRFIIEAM------EAAGHSISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGACASGD 602
Cdd:PLN02295 384 AVLESMCFQVKDVLDAMrkdageEKSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGL 463
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1622832061 603 FASVQEAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 642
Cdd:PLN02295 464 WTEEEIFASEKWKNTTTFRPKLDEEE-RAKRYASWCKAVE 502
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
549-632 |
9.38e-04 |
|
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: 42.16 E-value: 9.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622832061 549 GHSISTLFLCGGLSKNPLFVQMHADVTGMPVVLSQEVESVLVGAAILGACASGDFASVQEAMAKMSKV----GKVVFPRL 624
Cdd:cd07776 423 DIPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVVFSaeepKLVAEPDP 502
|
....*...
gi 1622832061 625 QDKKYYDK 632
Cdd:cd07776 503 EAAEVYDK 510
|
|
| |
