|
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 ... |
20-513 |
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: 920.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDATCS 97
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEgaGVDPEQVKGIGFDATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 98 LVVLDKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREiCWDKAGHF 177
Cdd:cd07782 81 LVVLDAEGKPVSVSPSGDDERNVILWMDHRAVEEAERINATGHEVLKYVGGKISPEMEPPKLLWLKENLPE-TWAKAGHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 178 FDLPDFLSWKATGVTARSLCSLVCKWTYSA----EKGWDDSFWKMIGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAAR 253
Cdd:cd07782 160 FDLPDFLTWKATGSLTRSLCSLVCKWTYLAhegsEGGWDDDFFKEIGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 254 ELGLPSGIAVAASLIDAHAGGLGVIGADVrgHGLTCEGQPVTSRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 333
Cdd:cd07782 240 ELGLPEGTPVGVSLIDAHAGGLGTLGADV--GGLPCEADPLTRRLALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 334 WLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNSHLDLIKKAQ--PVGFLTVDLHVWPDFHGNRSPLADL 411
Cdd:cd07782 318 WLNEGGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNERLEQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 412 TLKGMVTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEV 491
Cdd:cd07782 398 TLRGMISGLTLDTSLDDLALLYLATLQALAYGTRHIIEAMNAAGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEP 477
|
490 500
....*....|....*....|..
gi 755508662 492 ESVLVGAAILGACASGDFTSVQ 513
Cdd:cd07782 478 EAVLLGAAILGAVASGDFPSLW 499
|
|
| 5C_CHO_kinase |
TIGR01315 |
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ... |
20-522 |
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: 631.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVV--QGIDAHRIRGLGFDATCS 97
Cdd:TIGR01315 1 HYIGVDVGTGSARACIIDSTGDILALAAQNIKTWTPSSGLEGQSSVYIWQAICNCVKQVLaeSKVDPNSVKGIGFDATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 98 LVVLDKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHF 177
Cdd:TIGR01315 81 LVVLTHDGEPLPVSKNGGADQNIILWMDHRALAEAEKINATNHNLLRYVGGKMSVEMEIPKVLWLKNNMPPE-LFARCKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 178 FDLPDFLSWKATGVTARSLCSLVCKWTY----SAEKGWDDSFWKMIGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAAR 253
Cdd:TIGR01315 160 FDLTDFLTWRATGKEIRSFCSVVCKWGFvpvdGSNKGWQEDFYETIGLGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 254 ELGLPSGIAVAASLIDAHAGGLGVIGADVRGHGltcEGQPVTSRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 333
Cdd:TIGR01315 240 ELGLPAGTAVGSGLIDAHAGWIGTVGAKVAENG---DVSQAFTRLAAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 334 WLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNSHLdLIKKAQP----VGFLTVDLHVWPDFHGNRSPLA 409
Cdd:TIGR01315 317 WLAEGGQSAAGELMDHMLETHVAYDETVKEAEAAGKNIYDYLNEHL-KEMAAKTnapsISYLVRHFHVYPDLWGNRSPIA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 410 DLTLKGMVTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQ 489
Cdd:TIGR01315 396 DPNMRGVIIGLSMDRSKDGLALLYYATMEFIAYGTRQIVEAMNTAGHTIKSIFMSGGQCQNPLLMQLIADACDMPVLIPY 475
|
490 500 510
....*....|....*....|....*....|...
gi 755508662 490 EVESVLVGAAILGACASGDFTSVQIAVPREHGP 522
Cdd:TIGR01315 476 VNEAVLHGAAMLGAKAAGTTESLWDAMDRMSKP 508
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
18-515 |
0e+00 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 547.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 18 SRYYVGIDVGTGSVRAALVDQR-GLLLAFAEQPIKKWEP---------QFnhhEQSSEDIWAACCLVTKEVVQ--GIDAH 85
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDAAdGEELASAVHPYPRWVIglylppppdQA---RQHPLDYLEALEAAVREALAqaGVDPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 86 RIRGLGFDAT-CSLVVLDKEFHPLPVNHE--GDSSRNVIMWLDHRAVSQVHRINE----TKHRVLQYVGGVMSVEMQAPK 158
Cdd:COG1069 78 DVVGIGVDATgCTPVPVDADGTPLALLPEfaENPHAMVILWKDHTAQEEAERINElakaRGEDYLRYVGGIISSEWFWPK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 159 LLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGW-DDSFWKMIG--LEDLIDdnysKIGN 234
Cdd:COG1069 158 ILHLLREDPEV-YEAADSFVELCDWITWQLTGSLKRSRCTAGHKALWHAhEGGYpSEEFFAALDplLDGLAD----RLGT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 235 LVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAGGLGVIGAdvrghgltCEGQpvtsrLAVICGTSSCHMGISKD 314
Cdd:COG1069 233 EIYPLGEPAG-TLTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGV--------EPGT-----LVKVMGTSTCHMLVSPE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 315 PVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNshldliKKAQPVGFLTVD 394
Cdd:COG1069 299 ERFVPGICGQVDGSIVPGMWGYEAGQSAVGDIFAWFVRLLVPPLEYEKEAEERGISLHPLLT------EEAAKLPPGESG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 395 LHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDlaiLYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLS-KNPLF 473
Cdd:COG1069 373 LHALDWFNGNRSPLADQRLKGVILGLTLGTDAED---IYRALVEATAFGTRAIIERFEEEGVPIDEIIACGGIAtKNPLV 449
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 755508662 474 VQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQIA 515
Cdd:COG1069 450 MQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEA 491
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
20-509 |
2.39e-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: 433.20 E-value: 2.39e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKWE-PQFNHHEQSSEDIWAACCLVTKEVV--QGIDAHRIRGLGFDAT 95
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDlYAGLEMAQEPVPYYQDSsKKSWKFWQKSTEIIKALQKCVQKLNirEGVDAYEVKGCGVDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 96 CSLVVLDKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKHRVLQ-YVGGVMSVEMQAPKLLWLKENLREIcWDKA 174
Cdd:cd07768 81 CSLAIFDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWINMQCPQQLLdYLGGKISPEMGVPKLKYFLDEYSHL-RDKH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 175 GHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGWDDSFWKMIGLEDLiDDNYSKIGNLVLLPGAALGIGLtPEAAR 253
Cdd:cd07768 160 FHIFDLHDYIAYELTRLYEWNICGLLGKENLDGeESGWSSSFFKNIDPRLE-HLTTTKNLPSNVPIGTTSGVAL-PEMAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 254 ELGLPSGIAVAASLIDAHAGGLGVIGADVRGhgltcegqpvtsRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 333
Cdd:cd07768 238 KMGLHPGTAVVVSCIDAHASWFAVASPHLET------------SLFMIAGTSSCHMYGTTISDRIPGVWGPFDTIIDPDY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 334 WLNEGGQSVTGKLIDHMVQGHPAFPELQaKATARCQSIYAYLNshlDLIKKAQPVGFLTVDLHVWPDFHGNRSPLADLTL 413
Cdd:cd07768 306 SVYEAGQSATGKLIEHLFESHPCARKFD-EALKKGADIYQVLE---QTIRQIEKNNGLSIHILTLDMFFGNRSEFADPRL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 414 KGMVTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVES 493
Cdd:cd07768 382 KGSFIGESLDTSMLNLTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMM 461
|
490
....*....|....*.
gi 755508662 494 VLVGAAILGACASGDF 509
Cdd:cd07768 462 GILGAAVLAKVAAGKK 477
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
20-516 |
1.22e-140 |
|
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: 415.40 E-value: 1.22e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKWE--PQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDA 94
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAeaGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 95 TCS-LVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRV----LQYVGGVMSVEMQAPKLLWLKENLREI 169
Cdd:cd07781 81 TSStVVPVDEDGNPL---------APAILWMDHRAQEEAAEINETAHPAleyyLAYYGGVYSSEWMWPKALWLKRNAPEV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 170 cWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEDLidDNYSKIGNLVLLPGAALGiGLT 248
Cdd:cd07781 152 -YDAAYTIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGgPPREFLAALDPGLL--KLREKLPGEVVPVGEPAG-TLT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 249 PEAARELGLPSGIAVAASLIDAHAGglgVIGADVRGHGltcegqpvtsRLAVICGTSSCHMGISKDPVFVPGVWGPYYSA 328
Cdd:cd07781 228 AEAAERLGLPAGIPVAQGGIDAHMG---AIGAGVVEPG----------TLALIMGTSTCHLMVSPKPVDIPGICGPVPDA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 329 MVPGFWLNEGGQSVTGKLIDhmvqghpAFPELQAKATA-RCQSIYAYLNshlDLIKKAQPV--GFLTVDlhvWpdFHGNR 405
Cdd:cd07781 295 VVPGLYGLEAGQSAVGDIFA-------WFVRLFVPPAEeRGDSIYALLS---EEAAKLPPGesGLVALD---W--FNGNR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 406 SPLADLTLKGMVTGLTLSQdldDLAILYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLS-KNPLFVQMHADITGMP 484
Cdd:cd07781 360 TPLVDPRLRGAIVGLTLGT---TPAHIYRALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRP 436
|
490 500 510
....*....|....*....|....*....|..
gi 755508662 485 VVLSQEVESVLVGAAILGACASGDFTSVQIAV 516
Cdd:cd07781 437 IKVPKSDQAPALGAAILAAVAAGVYADIEEAA 468
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
19-518 |
5.31e-90 |
|
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: 284.80 E-value: 5.31e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 19 RYYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT- 95
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAkaGVDPEEIAAIGVSGQm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 96 CSLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINET--KHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDK 173
Cdd:COG1070 81 HGLVLLDADGEPL---------RPAILWNDTRAAAEAAELREElgEEALYEITGNPLHPGFTAPKLLWLKENEPEI-FAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 174 AGHFFDLPDFLSWKATG--VTARSLCSlvckWT--YSAEKG-WDDSFWKMIGLEDLIddnyskignL--VLLPGAALGiG 246
Cdd:COG1070 151 IAKVLLPKDYLRYRLTGefVTDYSDAS----GTglLDVRTRdWSDELLEALGIDREL---------LpeLVPPGEVAG-T 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 247 LTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGPYY 326
Cdd:COG1070 217 LTAEAAAETGLPAGTPVVAGAGDNAAAALGA--------GAVEPGD-----AAVSLGTSGVVFVVSDKPLPDPEGRVHTF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 327 SAMVPGFWLNEGGQSVTGKLIDHMVQghpafpELQAKAtarcQSIYAYLNshlDLIKKAqPVG-----FLtvdlhvwPDF 401
Cdd:COG1070 284 CHAVPGRWLPMGATNNGGSALRWFRD------LFADGE----LDDYEELN---ALAAEV-PPGadgllFL-------PYL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 402 HGNRSPLADLTLKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADIT 481
Cdd:COG1070 343 SGERTPHWDPNARGAFFGLTLSHTRAHL---ARAVLEGVAFALRDGLEALEEAGVKIDRIRATGGGARSPLWRQILADVL 419
|
490 500 510
....*....|....*....|....*....|....*..
gi 755508662 482 GMPVVLSQEVESVLVGAAILGACASGDFTSVQIAVPR 518
Cdd:COG1070 420 GRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAA 456
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
21-518 |
1.16e-88 |
|
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: 282.76 E-value: 1.16e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 21 YVGIDVGTGSVRAALVDQRGLLLAFAEQPI--KKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIDAHRIRGLGFDATCSL 98
Cdd:cd07778 2 GIGIDVGSTSVRIGIFDYHGTLLATSERPIsyKQDPKDLWFVTQSSTEIWKAIKTALKELIEELSDYIVSGIGVSATCSM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 99 VVLDKE-----FHPLPVNHE-GDSSRNVIMWLDHRAVSQVHRINE-TKHRVLQYVGGVMSVEMQAPKLLWLKENLREICW 171
Cdd:cd07778 82 VVMQRDsdtsyLVPYNVIHEkSNPDQDIIFWMDHRASEETQWLNNiLPDDILDYLGGGFIPEMAIPKLKYLIDLIKEDTF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 172 DKAgHFFDLPDFLSWKatgvtarsLCSLVCKW--TYSAE------------KGWDDSFWKMIGLEDLIDDNYSKIGNLVL 237
Cdd:cd07778 162 KKL-EVFDLHDWISYM--------LATNLGHSniVPVNAppsigigidgslKGWSKDFYSKLKISTKVCNVGNTFKEAPP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 238 LPGAALGIG-LTPEAARELGLPSGIAVAASLIDAHAGGLGVIgadvrghgltCEGQPVTSRLAVICGTSSCHMGISKDPV 316
Cdd:cd07778 233 LPYAGIPIGkVNVILASYLGIDKSTVVGHGCIDCYAGWFSTF----------AAAKTLDTTLFMVAGTSTCFLYATSSSQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 317 --FVPGVWGPYySAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAKATarcqSIYAYLNSHLDLI--KKAQPVGFLT 392
Cdd:cd07778 303 vgPIPGIWGPF-DQLLKNYSVYEGGQSATGKLIEKLFNSHPAIIELLKSDA----NFFETVEEKIDKYerLLGQSIHYLT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 393 VDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPL 472
Cdd:cd07778 378 RHMFFYGDYLGNRTPYNDPNMSGSFIGESTDSSLTDLVLKYILILEFLAFQTKLIIDNFQKEKIIIQKVVISGSQAKNAR 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 755508662 473 FVQMHADITGMPVV---LSQEVESVLVGAAILGACASGDFTSVQIAVPR 518
Cdd:cd07778 458 LLQLLSTVLSKIHIivpLSDSKYAVVKGAALLGKAAFLHNQSIEERLIS 506
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
20-515 |
3.53e-80 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 260.93 E-value: 3.53e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKW---------EPQFNHHEQSSEDIWAAcclVTKEVVQ--GIDAHRI 87
Cdd:PRK04123 4 YVIGLDFGTDSVRALLVDcATGEELATAVVEYPHWvkgryldlpPNQALQHPLDYIESLEA---AIPAVLKeaGVDPAAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 88 RGLGFDAT-CSLVVLDKEFHPLPVNHEGDSSRN--VIMWLDHRAVSQVHRINETKHR-----VLQYVGGVMSVEMQAPKL 159
Cdd:PRK04123 81 VGIGVDFTgSTPAPVDADGTPLALLPEFAENPHamVKLWKDHTAQEEAEEINRLAHErgeadLSRYIGGIYSSEWFWAKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 160 LWLKENLREIcWDKAGHFFDLPDFLSWKATGVTA-----RSLCSLVCKWTYSAEKG--WDDSFWKMI--GLEDLIDDnys 230
Cdd:PRK04123 161 LHVLREDPAV-YEAAASWVEACDWVVALLTGTTDpqdivRSRCAAGHKALWHESWGglPSADFFDALdpLLARGLRD--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 231 KIGNLVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAgglGVIGADVRGHGLTcegqpvtsrlAVIcGTSSCHMG 310
Cdd:PRK04123 237 KLFTETWTAGEPAG-TLTAEWAQRLGLPEGVAVSVGAFDAHM---GAVGAGAEPGTLV----------KVM-GTSTCDIL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 311 ISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKL----IDHMVQghpafPELQAKATARCQSIYAYLNshldliKKA- 385
Cdd:PRK04123 302 LADKQRAVPGICGQVDGSIVPGLIGYEAGQSAVGDIfawfARLLVP-----PEYKDEAEARGKQLLELLT------EAAa 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 386 -QPV---GFLTVDlhvWpdFHGNRSPLADLTLKGMVTGLTLSQDLDDlaiLYLATVQAIAFGTRFIIETMEAAGHSLSTL 461
Cdd:PRK04123 371 kQPPgehGLVALD---W--FNGRRTPLADQRLKGVITGLTLGTDAPD---IYRALIEATAFGTRAIMECFEDQGVPVEEV 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 755508662 462 FLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQIA 515
Cdd:PRK04123 443 IAAGGIArKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEA 497
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
20-511 |
1.22e-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: 236.65 E-value: 1.22e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT-C 96
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEksGIDPSDIAAIAFSGQmQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 97 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRVLQY---VGGVMSVEMQAPKLLWLKENLREIcWDK 173
Cdd:cd07805 81 GVVPVDKDGNPL---------RNAIIWSDTRAAEEAEEIAGGLGGIEGYrlgGGNPPSGKDPLAKILWLKENEPEI-YAK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 174 AGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLE-DLIDDnyskignlvLLPGAALgIG-LTPE 250
Cdd:cd07805 151 THKFLDAKDYLNFRLTGRAATDPSTASTTGLMDLRKRrWSEELLRAAGIDpDKLPE---------LVPSTEV-VGeLTPE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 251 AARELGLPSGIAVAASLIDAHAGGLGViGADVRGHgltcegqpvtsrlAVIC-GTSS---CHmgiSKDPVFVPGvwGPYY 326
Cdd:cd07805 221 AAAELGLPAGTPVVGGGGDAAAAALGA-GAVEEGD-------------AHIYlGTSGwvaAH---VPKPKTDPD--HGIF 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 327 S--AMVPGFWLNEGGQSVTGKLIDHMVqghpafpELQAKATARCQSIYAYLNshlDLIKKAQP----VGFLtvdlhvwPD 400
Cdd:cd07805 282 TlaSADPGRYLLAAEQETAGGALEWAR-------DNLGGDEDLGADDYELLD---ELAAEAPPgsngLLFL-------PW 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 401 FHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADI 480
Cdd:cd07805 345 LNGERSPVEDPNARGAFIGLSLEHTRADLA---RAVLEGVAFNLRWLLEALEKLTRKIDELRLVGGGARSDLWCQILADV 421
|
490 500 510
....*....|....*....|....*....|..
gi 755508662 481 TGMPV-VLSQEVESVLVGAAILGACASGDFTS 511
Cdd:cd07805 422 LGRPVeVPENPQEAGALGAALLAAVGLGLLKS 453
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
20-516 |
7.33e-69 |
|
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: 227.79 E-value: 7.33e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT-C 96
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAkaGVDPEDIAAIGLTSQrS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 97 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVsqvhrinetkhrvlqyvggvmsvemqapkllwlkenlreicwdkagH 176
Cdd:cd07779 81 TFVPVDEDGRPL---------RPAISWQDKRTA----------------------------------------------K 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 177 FFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEDliddnySKIGNLVLlPGAALGiGLTPEAAREL 255
Cdd:cd07779 106 FLTVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRdWSDDLLDAFGIDR------DKLPELVP-PGTVIG-TLTKEAAEET 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 256 GLPSGIAVAASlidAHAGGLGVIGAdvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWL 335
Cdd:cd07779 178 GLPEGTPVVAG---GGDQQCAALGA-----GVLEPGT-----ASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWV 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 336 NEGGQSVTGKLIDHMVQghpAFPELQAKATARCQSIYAYLNSHLDLIkkaqPVGFLtvDLHVWPDFHGNRSPLADLTLKG 415
Cdd:cd07779 245 LEGSINTGGSAVRWFRD---EFGQDEVAEKELGVSPYELLNEEAAKS----PPGSD--GLLFLPYLAGAGTPYWNPEARG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 416 MVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVL 495
Cdd:cd07779 316 AFIGLTLSHTRAHL---ARAILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATA 392
|
490 500
....*....|....*....|.
gi 755508662 496 VGAAILGACASGDFTSVQIAV 516
Cdd:cd07779 393 LGAAILAAVGAGIYPDFEEAV 413
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
20-518 |
5.12e-68 |
|
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: 227.04 E-value: 5.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVV--QGIDAHRIRGLGFDA-TC 96
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLakAGISPSDIAAIGLTGqMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 97 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINET-KHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAG 175
Cdd:cd07808 81 GLVLLDKNGRPL---------RPAILWNDQRSAAECEELEARlGDEILIITGNPPLPGFTLPKLLWLKENEPEI-FARIR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 176 HFFdLP-DFLSWKATGVTAR-------SLCslvckwtYSAEKG-WDDSFWKMIGLEdliddnyskIGNL--VLLPGAALG 244
Cdd:cd07808 151 KIL-LPkDYLRYRLTGELATdpsdasgTLL-------FDVEKReWSEELLEALGLD---------PSILppIVESTEIVG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 245 iGLTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQPV----TSrlAVICGTSSCHMGISKDPVF--- 317
Cdd:cd07808 214 -TLTPEAAEELGLPEGTPVVAGAGDNAAAALGA--------GVVEPGDALislgTS--GVVFAPTDKPVPDPKGRLHtfp 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 318 --VPGVWgpYYSAMVPGF-----WLNE--GGQSVTGKLIDHMVQGHPAfpelqakatarcqsiyaylnshldlikKAQPV 388
Cdd:cd07808 283 haVPGKW--YAMGVTLSAglslrWLRDlfGPDRESFDELDAEAAKVPP---------------------------GSEGL 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 389 GFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLS 468
Cdd:cd07808 334 LFL-------PYLSGERTPYWDPNARGSFFGLSLSHTRAHLA---RAVLEGVAFSLRDSLEVLKELGIKVKEIRLIGGGA 403
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 755508662 469 KNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQIAVPR 518
Cdd:cd07808 404 KSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAA 453
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
20-502 |
9.54e-68 |
|
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: 223.60 E-value: 9.54e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT-C 96
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAkaGIDPSDIAAIGISGQmP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 97 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAvsqvhrinetkhrvlqyvggvmsvemqapkllwlkenlreicwdkagH 176
Cdd:cd00366 81 GVVLVDADGNPL---------RPAIIWLDRRA-----------------------------------------------K 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 177 FFDLPDFLSWKATGVTA--RSLCSLVCKWTYsAEKGWDDSFWKMIGLEDliddnySKIGNLVLlPGAALGiGLTPEAARE 254
Cdd:cd00366 105 FLQPNDYIVFRLTGEFAidYSNASGTGLYDI-KTGDWSEELLDALGIPR------EKLPPIVE-SGEVVG-RVTPEAAEE 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 255 LGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQPVtsrlaVICGTSSCHMGISKDPVFVPGVWGPYYSAmVPGFW 334
Cdd:cd00366 176 TGLPAGTPVVAGGGDTAAAALGA--------GVVEPGDAV-----DSTGTSSVLSVCTDEPVPPDPRLLNRCHV-VPGLW 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 335 LNEGGQSVTGKLIDHMvqghpafpelqAKATARCQSIYAYLNSHLDLIKKAQP----VGFLtvdlhvwPDFHGNRSPLAD 410
Cdd:cd00366 242 LLEGAINTGGASLRWF-----------RDEFGEEEDSDAEYEGLDELAAEVPPgsdgLIFL-------PYLSGERSPIWD 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 411 LTLKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQE 490
Cdd:cd00366 304 PAARGVFFGLTLSHTRAHL---IRAVLEGVAYALRDNLEILEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEV 380
|
490
....*....|..
gi 755508662 491 VESVLVGAAILG 502
Cdd:cd00366 381 AEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
20-503 |
3.07e-67 |
|
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466801 [Multi-domain] Cd Length: 429 Bit Score: 223.25 E-value: 3.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIDAHRIRGLGFDATC-SL 98
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPRRVVAIAVDGTSgTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 99 VVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFF 178
Cdd:cd07783 81 VLVDREGEPL---------RPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEV-LAKTAKFL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 179 DLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGL-EDLIddnyskigNLVLLPGAALGIgLTPEAARELG 256
Cdd:cd07783 151 HQADWLAGRLTGDRGVTDYNNALKLGYDPETGrWPSWLLALLGIpPDLL--------PRVVAPGTVIGT-LTAEAAEELG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 257 LPSGIAVAASLIDAHAGGLGViGADVRGHGLTcegqpvtsrlavICGTSSCHMGISKDPVFVPGvwGPYYSAMVP-GFWL 335
Cdd:cd07783 222 LPAGTPVVAGTTDSIAAFLAS-GAVRPGDAVT------------SLGTTLVLKLLSDKRVPDPG--GGVYSHRHGdGYWL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 336 NEGGQSVTGKLIDHMVQGHPaFPELQAKATARCQSiyaylnshldlikkaqpvgfltvDLHVWP-DFHGNRSPLADLTLK 414
Cdd:cd07783 287 VGGASNTGGAVLRWFFSDDE-LAELSAQADPPGPS-----------------------GLIYYPlPLRGERFPFWDPDAR 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 415 GMVTGLTlsqdlDDLAILYLATVQAIAFGTRFIIETMEAAGHS-LSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVES 493
Cdd:cd07783 343 GFLLPRP-----HDRAEFLRALLEGIAFIERLGYERLEELGAPpVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEA 417
|
490
....*....|
gi 755508662 494 VLvGAAILGA 503
Cdd:cd07783 418 AL-GAALLAA 426
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
20-507 |
2.42e-64 |
|
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: 216.30 E-value: 2.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIDAHRIRGLGFdAT--CS 97
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGPDPIAAISV-SSqgES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 98 LVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAG 175
Cdd:cd07773 80 GVPVDRDGEPL---------GPAIVWFDPRGKEEAEELAEriGAEELYRITGLPPSPMYSLAKLLWLREHEPEI-FAKAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 176 HFFDLPDFLSWKATGVTARSLcSLVCKWTY--SAEKGWDDSfwkmigLEDLIDDNYSKIGNLVlLPGAALGIgLTPEAAR 253
Cdd:cd07773 150 KWLSVADYIAYRLTGEPVTDY-SLASRTMLfdIRKRTWSEE------LLEAAGIDASLLPELV-PSGTVIGT-VTPEAAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 254 ELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGPYYS---AMV 330
Cdd:cd07773 221 ELGLPAGTPVVVGGHDHLCAALGA--------GVIEPGD-----VLDSTGTAEALLAVVDEPPLDEMLAEGGLSyghHVP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 331 PGFWLNEGGQSvTGKLIDHMVQghpafpELQAKATARCQSIYAYLNShldlIKKAQPVGFLtvdlhvwPDFHGNRSPLAD 410
Cdd:cd07773 288 GGYYYLAGSLP-GGALLEWFRD------LFGGDESDLAAADELAEAA----PPGPTGLLFL-------PHLSGSGTPDFD 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 411 LTLKGMVTGLTLSQDLDDlaiLYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQE 490
Cdd:cd07773 350 PDARGAFLGLTLGTTRAD---LLRAILEGLAFELRLNLEALEKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEV 426
|
490
....*....|....*..
gi 755508662 491 VESVLVGAAILGACASG 507
Cdd:cd07773 427 PEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
20-507 |
6.36e-62 |
|
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: 209.71 E-value: 6.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT-C 96
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEksGVDPSDIAGVGVTGHgN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 97 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKA 174
Cdd:cd07802 81 GLYLVDKDGKPV---------RNAILSNDSRAADIVDRWEEdgTLEKVYPLTGQPLWPGQPVALLRWLKENEPER-YDRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 175 GHFFDLPDFLSWKATGVtarslcsLVCKWT-YSA------EKGWDDSFWKMIGLEDLIDdnysKIGNLVllPGAALGIGL 247
Cdd:cd07802 151 RTVLFCKDWIRYRLTGE-------ISTDYTdAGSslldldTGEYDDELLDLLGIEELKD----KLPPLV--PSTEIAGRV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 248 TPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGpYYS 327
Cdd:cd07802 218 TAEAAALTGLPEGTPVAAGAFDVVASALGA--------GAVDEGQ-----LCVILGTWSINEVVTDEPVVPDSVGS-NSL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 328 AMVPGFWLNEGGQSVTGKLIDHMVQghpafpELQAKATARCQSIYAYLNshlDLIKKAQPVG----FLtvdlhvwPDFHG 403
Cdd:cd07802 284 HADPGLYLIVEASPTSASNLDWFLD------TLLGEEKEAGGSDYDELD---ELIAAVPPGSsgviFL-------PYLYG 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 404 NRsplADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEAAGHsLSTLFLCGGLSKNPLFVQMHADITGM 483
Cdd:cd07802 348 SG---ANPNARGGFFGLTAWHTRAHLL---RAVYEGIAFSHRDHLERLLVARK-PETIRLTGGGARSPVWAQIFADVLGL 420
|
490 500
....*....|....*....|....
gi 755508662 484 PVVLSQEVESVLVGAAILGACASG 507
Cdd:cd07802 421 PVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
20-507 |
1.14e-61 |
|
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: 209.30 E-value: 1.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVDQRGLLLAFA--EQPIKKwePQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDA- 94
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASAsiEHDLLT--PKPGWAEHDPEVWWGAVCEIIRELLAkaGISPKEIAAIGVSGl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 95 TCSLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINET--KHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWD 172
Cdd:cd07804 79 VPALVPVDENGKPL---------RPAILYGDRRATEEIEWLNENigEDRIFEITGNPLDSQSVGPKLLWIKRNEPEV-FK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 173 KAGHFFDLPDFLSWKATG--VTARSLCSLvckwtYS-----AEKGWDDSFWKMIGL-EDLIDDNYSkignlvllPGAALG 244
Cdd:cd07804 149 KTRKFLGAYDYIVYKLTGeyVIDYSSAGN-----EGglfdiRKRTWDEELLEALGIdPDLLPELVP--------STEIVG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 245 iGLTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGP 324
Cdd:cd07804 216 -EVTKEAAEETGLAEGTPVVAGTVDAAASALSA--------GVVEPGD-----LLLMLGTAGDIGVVTDKLPTDPRLWLD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 325 YYSamVPGFWLNEGGQSVTGKLIDHMVQGhpAFPELQAKATARCQSIYAYLNshldliKKAQPVGFLTVDLHVWPDFHGN 404
Cdd:cd07804 282 YHD--IPGTYVLNGGMATSGSLLRWFRDE--FAGEEVEAEKSGGDSAYDLLD------EEAEKIPPGSDGLIVLPYFMGE 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 405 RSPLADLTLKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMP 484
Cdd:cd07804 352 RTPIWDPDARGVIFGLTLSHTRAHL---YRALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVP 428
|
490 500
....*....|....*....|...
gi 755508662 485 VVLSQEVESVLVGAAILGACASG 507
Cdd:cd07804 429 QEYVKDTVGASLGDAFLAGVGVG 451
|
|
| L-ribulokinase |
TIGR01234 |
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely ... |
20-518 |
2.41e-60 |
|
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely related protein subfamily outside the scope of this model includes ribitol kinase from E. coli. [Energy metabolism, Sugars]
Pssm-ID: 130301 [Multi-domain] Cd Length: 536 Bit Score: 207.85 E-value: 2.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKWE--------------PQFNHHEQSSEDIWAAcclVTKEVVQ--GI 82
Cdd:TIGR01234 2 YAIGVDFGTLSGRALAVDvATGEEIATAVEWYRHWVkgqflpktgaklpnDQALQHPADYIEVLEA---AIPTVLAelGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 83 DAHRIRGLGFDAT-CSLVVLDKEFHPLPVNHEGDSSRN--VIMWLDHRAVSQVHRINETKHR----VLQYVGGVMSVEMQ 155
Cdd:TIGR01234 79 DPADVVGIGVDFTaCTPAPIDSDGNPLCLLPEFAENPHayFKLWKHHAAQEEADRINRLAHApgevDLSRYGGIISSEWF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 156 APKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKGW-DDSFWKMI--GLEDLIDDNYSK- 231
Cdd:TIGR01234 159 WAKILQITEEDPAI-YQAADRWIELADWIVAQLSGDIRRGRCTAGYKALWHESWGYpSASFFDELnpILNRHLPDKLFTd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 232 IGNLvllpGAALGiGLTPEAARELGLPSGIAVAASLIDAHaggLGVIGADVrghgltceGQPvtSRLAVICGTSSCHMGI 311
Cdd:TIGR01234 238 IWTA----GEPAG-TLTPEWAQRTGLPEGVVVAVGNFDAH---VGAVAAGI--------AQP--GALVKIMGTSTCHVLI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 312 SKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQgHPAFPELQAKATARCQSiyayLNSHLDLIKKAQPV--- 388
Cdd:TIGR01234 300 GDKQRAVPGMCGVVDGGIVPGFIGYEAGQSAVGDIFAWFGK-VCVPPELKTEANASQKQ----LHEALSEAAAKQPSgeh 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 389 GFLTVDlhvWpdFHGNRSPLADLTLKGMVTGLTLSQDLDDlaiLYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLS 468
Cdd:TIGR01234 375 GLVALD---W--FNGNRSPLVDQRLKGVITGLTLATDAPL---LYRALIEATAFGTRMIMETFTDSGVPVEELMAAGGIA 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 755508662 469 -KNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQIAVPR 518
Cdd:TIGR01234 447 rKNPVIMQIYADVTNRPLQIVASDQAPALGAAIFAAVAAGVYADIPSAQAK 497
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
298-505 |
1.70e-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: 195.24 E-value: 1.70e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 298 LAVICGTSSCHMGISKDPV-FVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAkaTARCQSIYAYLN 376
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVlSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRD--AGNVESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 377 SHLDLikkaqpvgfLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLddlAILYLATVQAIAFGTRFIIETMEA-AG 455
Cdd:pfam02782 79 LAAVA---------PAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTL---AHLYRAILESLALQLRQILEALTKqEG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 755508662 456 HSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACA 505
Cdd:pfam02782 147 HPIDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
20-526 |
5.27e-55 |
|
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466790 [Multi-domain] Cd Length: 478 Bit Score: 192.39 E-value: 5.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIDAHRIRGLGFDATC-SL 98
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVDAIGFSSAMhSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 99 VVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRI--NETKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGH 176
Cdd:cd07770 81 LGVDEDGEPL---------TPVITWADTRAAEEAERLrkEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPEL-FAKAAK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 177 FFDLPDFLSWKATG--VTARSLCSlvckWT---YSAEKGWDDSFWKMIGLEDlidDNYSKignlvLLPGAALGIGLTPEA 251
Cdd:cd07770 151 FVSIKEYLLYRLTGelVTDYSTAS----GTgllNIHTLDWDEEALELLGIDE---EQLPE-----LVDPTEVLPGLKPEF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 252 ARELGLPSGIAVAASLIDAHAGGLGViGADVRGhgltcegqpvtsRLAVICGTSschmG----ISKDPVFVP--GVWgPY 325
Cdd:cd07770 219 AERLGLLAGTPVVLGASDGALANLGS-GALDPG------------RAALTVGTS----GairvVSDRPVLDPpgRLW-CY 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 326 YSAmvPGFWL-----NEGGqSVTGKLIDHMVQGHPAFPELQAKATArcqsiyAYLNSHlDLIkkaqpvgFLtvdlhvwPD 400
Cdd:cd07770 281 RLD--ENRWLvggaiNNGG-NVLDWLRDTLLLSGDDYEELDKLAEA------VPPGSH-GLI-------FL-------PY 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 401 FHGNRSPLADLTLKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADI 480
Cdd:cd07770 337 LAGERAPGWNPDARGAFFGLTLNHTRADI---LRAVLEGVAFNLKSIYEALEELAGPVKEIRASGGFLRSPLWLQILADV 413
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 755508662 481 TGMPVVLSQEVESVLVGAAILGACASGDFTSVQIAVPREHGPLLHP 526
Cdd:cd07770 414 LGRPVLVPEEEEASALGAALLALEALGLISSLEADELVKIGKVVEP 459
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
20-507 |
1.60e-43 |
|
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: 160.47 E-value: 1.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHH--EQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLgfdAT 95
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYPDakEFDPEELWEKICEAIREALKkaGISPEDISAV---SS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 96 CS----LVVLDKEFHPL---PvNHegdssrnvimwlDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAP-KLLWLKENLR 167
Cdd:cd07798 78 TSqregIVFLDKDGRELyagP-NI------------DARGVEEAAEIDDEFGEEIYTTTGHWPTELFPAaRLLWFKENRP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 168 EIcWDKAGHFFDLPDFLSWKATGVtarslcsLVCKWTYSAEKG--------WDDSFWKMIGLEDLIddnyskignL--VL 237
Cdd:cd07798 145 EI-FERIATVLSISDWIGYRLTGE-------LVSEPSQASETQlfdikkreWSQELLEALGLPPEI---------LpeIV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 238 LPGAALGIgLTPEAARELGLPSGIAVAASLIDAHAGGLGViGADVRGHgltcegqpvtsrLAVICGTSSCHMGISKDPVF 317
Cdd:cd07798 208 PSGTVLGT-VSEEAARELGLPEGTPVVVGGADTQCALLGS-GAIEPGD------------IGIVAGTTTPVQMVTDEPII 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 318 VP--GVW-GPYysaMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQakatarcqsiYAYLNSHLDLIKKAQP--VGFLT 392
Cdd:cd07798 274 DPerRLWtGCH---LVPGKWVLESNAGVTGLNYQWLKELLYGDPEDS----------YEVLEEEASEIPPGANgvLAFLG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 393 VDLhvwpdFHGNRSPLADLTLKGMVTGLTLSQDLDDLAIlylATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNP 471
Cdd:cd07798 341 PQI-----FDARLSGLKNGGFLFPTPLSASELTRGDFAR---AILENIAFAIRANLEQLEEvSGREIPYIILCGGGSRSA 412
|
490 500 510
....*....|....*....|....*....|....*.
gi 755508662 472 LFVQMHADITGMPVVLSQEVESVLVGAAILGACASG 507
Cdd:cd07798 413 LLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
20-507 |
5.17e-42 |
|
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: 156.17 E-value: 5.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPikkWEPQFNHH---EQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFD 93
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAP---HENILIDPgwaEQDPEDWWDALQAAFAQLLKdaGAELRDVAAIGIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 94 ATC-SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINET-KHRVLQYVGGVMSVEMQAPKLLWLKENLREIcW 171
Cdd:cd07809 78 GQMhGLVALDADGKVL---------RPAKLWCDTRTAPEAEELTEAlGGKKCLLVGLNIPARFTASKLLWLKENEPEH-Y 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 172 DKAgHFFDLP-DFLSWKATG--VTARSLCSLVckwtysaekGWDDSF-----WKMIGLEDLIDDNYSKIGNlVLLPGAAL 243
Cdd:cd07809 148 ARI-AKILLPhDYLNWKLTGekVTGLGDASGT---------FPIDPRtrdydAELLAAIDPSRDLRDLLPE-VLPAGEVA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 244 GiGLTPEAARELGLPSGIAVAASLIDAHAG--GLGVIGadvrghgltcEGQPVTSrlaviCGTSSCHMGISKDPVFVPgv 321
Cdd:cd07809 217 G-RLTPEGAEELGLPAGIPVAPGEGDNMTGalGTGVVN----------PGTVAVS-----LGTSGTAYGVSDKPVSDP-- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 322 wgpyySAMVPGF--------WLNEG---GQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYlnshldlikkaqpvgf 390
Cdd:cd07809 279 -----HGRVATFcdstggmlPLINTtncLTAWTELFRELLGVSYEELDELAAQAPPGAGGLLLL---------------- 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 391 ltvdlhvwPDFHGNRSP-LADLTlkGMVTGLTLSQdlDDLAILYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSK 469
Cdd:cd07809 338 --------PFLNGERTPnLPHGR--ASLVGLTLSN--FTRANLARAALEGATFGLRYGLDILRELGVEIDEIRLIGGGSK 405
|
490 500 510
....*....|....*....|....*....|....*...
gi 755508662 470 NPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASG 507
Cdd:cd07809 406 SPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
20-507 |
3.41e-40 |
|
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: 151.24 E-value: 3.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGID--AHRIRGLGFDAT-- 95
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDvlPDRVAAIGVTGQgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 96 -CSLVvlDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREICwD 172
Cdd:cd24121 81 gTWLV--DEDGRPV---------RDAILWLDGRAADIVERWQAdgIAEAVFEITGTGLFPGSQAAQLAWLKENEPERL-E 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 173 KAGHFFDLPDFLSWKATGVTA--RSLCSLVCkwtYSAEKG-WDDSFWKMIGLEDLIDdnyskignlvLLPGAALGIG--- 246
Cdd:cd24121 149 RARTALHCKDWLFYKLTGEIAtdPSDASLTF---LDFRTRqYDDEVLDLLGLEELRH----------LLPPIRPGTEvig 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 247 -LTPEAARELGLPSGIAVAASLIDAHAGGLGViGADVRGHGLTcegqpvtsrlavICGTSSCHMGISKDPVFvpgvwGPY 325
Cdd:cd24121 216 pLTPEAAAATGLPAGTPVVLGPFDVVATALGS-GAIEPGDACS------------ILGTTGVHEVVVDEPDL-----EPE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 326 YSAM-----VPGFWLNEGGqSVTGKL-IDHMVQghPAFPELQAKATARCQSIYAYLNSHLdlikKAQPVGFLTVDLHVWP 399
Cdd:cd24121 278 GVGYticlgVPGRWLRAMA-NMAGTPnLDWFLR--ELGEVLKEGAEPAGSDLFQDLEELA----ASSPPGAEGVLYHPYL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 400 DFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRfiiETMEAAGHSLSTLFLCGGLSKNPLFVQMHAD 479
Cdd:cd24121 351 SPAGERAPFVNPNARAQFTGLSLEHTRADLL---RAVYEGVALAMR---DCYEHMGEDPGELRLSGGGARSDTWCQILAD 424
|
490 500
....*....|....*....|....*...
gi 755508662 480 ITGMPVVLSQEVESVLVGAAILGACASG 507
Cdd:cd24121 425 ALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
20-276 |
6.15e-26 |
|
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: 106.27 E-value: 6.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDATC- 96
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSqlGISLKQIKGIGISNQGh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 97 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKA 174
Cdd:pfam00370 81 GTVLLDKNDKPL---------YNAILWKDRRTAEIVENLKEegNNQKLYEITGLPIWPGFTLSKLRWIKENEPEV-FEKI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 175 GHFFDLPDFLSWKATGVtarslcsLVCKWTYSAEKG--------WDDSFWKMIGLEdliDDNYSKignlvLLPGAALGIG 246
Cdd:pfam00370 151 HKFLTIHDYLRWRLTGV-------FVTDHTNASRSMmfnihkldWDPELLAALGIP---RDHLPP-----LVESSEIYGE 215
|
250 260 270
....*....|....*....|....*....|
gi 755508662 247 LTPEAARELGLPSGIAVAASLIDAHAGGLG 276
Cdd:pfam00370 216 LNPELAAMWGLDEGVPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
20-516 |
7.01e-24 |
|
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466794 [Multi-domain] Cd Length: 492 Bit Score: 104.72 E-value: 7.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVDQRGLLLAFAEqpiKKWEPQFNHHEQSSEDI-----WAACCLVTKEVVQ--GIDAHRIRGLgf 92
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQ---REWRHKEVPDVPGSMDFdteknWKLICECIREALKkaGIAPKSIAAI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 93 dATCS----LVVLDKEFHPLPVNHegdssrNVimwlDHRAVSQVHRINETKH---RVLQYVGGVMSVEMQAPKLLWLKEN 165
Cdd:cd07775 76 -STTSmregIVLYDNEGEEIWACA------NV----DARAAEEVSELKELYNtleEEVYRISGQTFALGAIPRLLWLKNN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 166 LREIcWDKAGHFFDLPDFLSWKATGVTAR--SLCSLVCKWTySAEKGWDDSFWKMIGLEDLIDDNyskignlVLLPGAAL 243
Cdd:cd07775 145 RPEI-YRKAAKITMLSDWIAYKLSGELAVepSNGSTTGLFD-LKTRDWDPEILEMAGLKADILPP-------VVESGTVI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 244 GIgLTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrlAVICGTSSCHMGI-SKDPVFVPGVW 322
Cdd:cd07775 216 GK-VTKEAAEETGLKEGTPVVVGGGDVQLGCLGL--------GVVRPGQ------TAVLGGSFWQQEVnTAAPVTDPAMN 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 323 GPYYSAMVPGFWLNEGGQSVTGKLIDHMVQghpAF-PELQAKATARCQSIYAYLNshldliKKAQ--PVGF-----LTVD 394
Cdd:cd07775 281 IRVNCHVIPDMWQAEGISFFPGLVMRWFRD---AFcAEEKEIAERLGIDAYDLLE------EMAKdvPPGSygimpIFSD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 395 L-------HVWPDFhgnrspladltlkgmvTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAA-GHSLSTLFLCGG 466
Cdd:cd07775 352 VmnyknwrHAAPSF----------------LNLDIDPEKCNKATFFRAIMENAAIVSAGNLERIAEFsGIFPDSLVFAGG 415
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 755508662 467 LSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQIAV 516
Cdd:cd07775 416 ASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAGIYSSLEEAV 465
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
21-483 |
3.13e-19 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 90.41 E-value: 3.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 21 YVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAAC-----CLVTKEVVQGIDAHRIRGLGFDAT 95
Cdd:PRK15027 2 YIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATdramkALGDQHSLQDVKALGIAGQMHGAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 96 cslvVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREICWDKAG 175
Cdd:PRK15027 82 ----LLDAQQRVL---------RPAILWNDGRCAQECALLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 176 HFfdLP-DFLSWKATGVTARSLCSLV-CKWTYSAEKGWDDSfwkMIGLEDLIDDNYSkignlVLLPGAALGIGLTPEAAR 253
Cdd:PRK15027 149 VL--LPkDYLRLRMTGEFASDMSDAAgTMWLDVAKRDWSDV---MLQACHLSRDQMP-----ALYEGSEITGALLPEVAK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 254 ELGLPSgIAVAASLIDAHAGGLGVigadvrghGLTCEGQPVTSrlaviCGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 333
Cdd:PRK15027 219 AWGMAT-VPVVAGGGDNAAGAVGV--------GMVDANQAMLS-----LGTSGVYFAVSEGFLSKPESAVHSFCHALPQR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 334 WlneggqsvtgKLIDHMVQGHPAFpELQAKATARcQSIYAYLNSHLDLIKKAQPVGFLtvdlhvwPDFHGNRSPLADLTL 413
Cdd:PRK15027 285 W----------HLMSVMLSAASCL-DWAAKLTGL-SNVPALIAAAQQADESAEPVWFL-------PYLSGERTPHNNPQA 345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 414 KGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGM 483
Cdd:PRK15027 346 KGVFFGLTHQHGPNELA---RAVLEGVGYALADGMDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQ 412
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
20-511 |
1.06e-18 |
|
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: 89.06 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFdaTC- 96
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAkaGISASDIAAIGI--TNq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 97 --SLVVLDKefhplpvnHEGDSSRNVIMWLDHRAVSQVHRINETKH--RVLQYVGGVMSVEMQAPKLLWLKEN---LREI 169
Cdd:cd07769 79 reTTVVWDK--------KTGKPLYNAIVWQDRRTADICEELKAKGLeeRIREKTGLPLDPYFSATKIKWILDNvpgARER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 170 CwdKAGHF-FDLPD-FLSWKATG----VT-----ARSLcsLvckwtYSAEKG-WDDSfwkmigLEDLIDdnyskignlvl 237
Cdd:cd07769 151 A--ERGELlFGTIDtWLIWKLTGgkvhVTdvtnaSRTM--L-----FNIHTLeWDDE------LLELFG----------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 238 LPGAALgigltPE---------AARELGLPSGIAVAASLIDAHAgglgvigADVrGHGLTCEGQpvtsrlaVIC--GT-S 305
Cdd:cd07769 205 IPRSML-----PEvrpssevfgYTDPEGLGAGIPIAGILGDQQA-------ALF-GQGCFEPGM-------AKNtyGTgC 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 306 SCHMGISKDPVFV-PGV-----WG----PYYSAmvpgfwlnEGGQSVTGKLIDHMVQGhpafpelqakatarcqsiyayl 375
Cdd:cd07769 265 FLLMNTGEKPVPSkNGLlttiaWQiggkVTYAL--------EGSIFIAGAAIQWLRDN---------------------- 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 376 nshLDLIKKAQPVGFL--TVD----LHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIE 449
Cdd:cd07769 315 ---LGLIEDAAETEELarSVEdnggVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIV---RAALESIAYQTRDVLE 388
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755508662 450 TMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTS 511
Cdd:cd07769 389 AMEKdSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKD 451
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
18-513 |
5.53e-18 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 86.66 E-value: 5.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 18 SRYYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFD-- 93
Cdd:COG0554 2 KKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAkaGISAEDIAAIGITnq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 94 -ATCslVVLDKEF-HPLpvnHegdssrNVIMWLDHRAVSQVHRINETKH--RVLQYVGGVMSVEMQAPKLLWLKEN---L 166
Cdd:COG0554 82 rETT--VVWDRKTgKPL---Y------NAIVWQDRRTADICEELKADGLedLIREKTGLVLDPYFSATKIKWILDNvpgA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 167 REicwdKA--GH-FFDLPD-FLSWKATG----VT-----ARSLCslvckwtYSAEKG-WDDSFWKMIGLedliddnyski 232
Cdd:COG0554 151 RE----RAeaGElLFGTIDsWLIWKLTGgkvhVTdvtnaSRTML-------FNIHTLdWDDELLELFGI----------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 233 gnlvllPGAALgigltPE---------AARELGLPSGIAVAASLIDAHAgglgvigADVrGHGLTCEG------------ 291
Cdd:COG0554 209 ------PRSML-----PEvrpssevfgETDPDLFGAEIPIAGIAGDQQA-------ALF-GQACFEPGmakntygtgcfl 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 292 ------QPVTSR---LAVICgtsschmgiskdpvfvpgvWG----PYYsAMvpgfwlnEGGQSVTGKLIDhmvqghpafp 358
Cdd:COG0554 270 lmntgdEPVRSKnglLTTIA-------------------WGlggkVTY-AL-------EGSIFVAGAAVQ---------- 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 359 elqakatarcqsiyaYLNSHLDLIKKAQPVGFL--TVD----LHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAil 432
Cdd:COG0554 313 ---------------WLRDGLGLIDSAAESEALarSVEdnggVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIA-- 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 433 yLATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTS 511
Cdd:COG0554 376 -RAALESIAYQTRDVLDAMEAdSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKS 454
|
..
gi 755508662 512 VQ 513
Cdd:COG0554 455 LE 456
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
20-512 |
3.65e-16 |
|
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: 81.07 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFdAT-- 95
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKnaGLTPEDIAAIGI-STqr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 96 CSLVVLDKE----FHplpvnhegdssrNVIMWLDHRAVSQVHRINE-TKHRVLQYVGGVM-----------------SVE 153
Cdd:cd07793 80 NTFLTWDKKtgkpLH------------NFITWQDLRAAELCESWNRsLLLKALRGGSKFLhfltrnkrflaasvlkfSTA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 154 MQAPKLLWLKENLREICWDKAGH---FFDLPDFLSWKATG----VTARSLCSLVckwtysaekgwddsfwkmiGLEDLID 226
Cdd:cd07793 148 HVSIRLLWILQNNPELKEAAEKGellFGTIDTWLLWKLTGgkvhATDYSNASAT-------------------GLFDPFT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 227 DNYSK-IGNLVLLPGAALgigltPEaarelglpsgiavaaslIDAHAGGLGVIGADVRGHGLtcegqPVTSrlavICGTS 305
Cdd:cd07793 209 LEWSPiLLSLFGIPSSIL-----PE-----------------VKDTSGDFGSTDPSIFGAEI-----PITA----VVADQ 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 306 SCHMgiskdpvFVPGVWGPYYSAMVPG---FW-LNEGGQ---SVTG--KLIDHMVQGHPAF-PELQAKATARC----QSI 371
Cdd:cd07793 258 QAAL-------FGECCFDKGDVKITMGtgtFIdINTGSKphaSVKGlyPLVGWKIGGEITYlAEGNASDTGTVidwaKSI 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 372 yAYLNSHLDLIKKAQPVGfLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAIlylATVQAIAFGTRFIIETM 451
Cdd:cd07793 331 -GLFDDPSETEDIAESVE-DTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVR---AILESIAFRVKQLLETM 405
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755508662 452 EA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSV 512
Cdd:cd07793 406 EKeTSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSK 467
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
25-515 |
9.46e-15 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 76.61 E-value: 9.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 25 DVGTGSVRAALVDQRGLLLAFAEQP----IKKWEPQFnhHEQSSEDIW---AACClvtKEVVQGIDAHRIRGL-----GF 92
Cdd:PRK10331 8 DCGATNVRAIAVDRQGKIVARASTPnasdIAAENSDW--HQWSLDAILqrfADCC---RQINSELTECHIRGItvttfGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 93 DATcslvvldkefhplPVNHEGDSSRNVIMWLDHRAVSQVHRI-NETKHRVLQYVGGVMSVEMQAP-KLLWLKENLREIc 170
Cdd:PRK10331 83 DGA-------------LVDKQGNLLYPIISWKCPRTAAVMENIeRYISAQQLQQISGVGAFSFNTLyKLVWLKENHPQL- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 171 WDKAGHFFDLPDFLSWKATGV--TARSLCSlVCKWTYSAEKGWDDSFWKMIGL-EDL---IDDNYSKIGNlvllpgaalg 244
Cdd:PRK10331 149 LEQAHAWLFISSLINHRLTGEftTDITMAG-TSQMLDIQQRDFSPEILQATGLsRRLfprLVEAGEQIGT---------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 245 igLTPEAARELGLPSGIAVAASlidAHAGGLGVIGAdvrGHGLtceGQPV-----------------TSRLAVICGtSSC 307
Cdd:PRK10331 218 --LQPSAAALLGLPVGIPVISA---GHDTQFALFGS---GAGQ---NQPVlssgtweilmvrsaqvdTSLLSQYAG-STC 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 308 HMGiSKDPVFVPGVWgpyysamvpgfWLNEGGQSVTGKLIdhmvqghpaFPELQAKATarcqsiyaylnshldLIKKAQP 387
Cdd:PRK10331 286 ELD-SQSGLYNPGMQ-----------WLASGVLEWVRKLF---------WTAETPYQT---------------MIEEARA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 388 VGFLTVDLHVWPDFHGNRspladltlKGMVTGLTLSQDLDDlaiLYLATVQAIAFGTRFIIETMEAAGH-SLSTLFLCGG 466
Cdd:PRK10331 330 IPPGADGVKMQCDLLACQ--------NAGWQGVTLNTTRGH---FYRAALEGLTAQLKRNLQVLEKIGHfKASELLLVGG 398
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 755508662 467 LSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQIA 515
Cdd:PRK10331 399 GSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQA 447
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
21-514 |
1.35e-14 |
|
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: 76.02 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 21 YVG-IDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAAC--CL---VTKEVVQGIDAHRIRGLGFda 94
Cdd:cd07792 2 LVGaIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVyeCIeeaVEKLKALGISPSDIKAIGI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 95 TC---SLVVLDKEfhplpvnhEGDSSRNVIMWLDHRAVSQVHR----INETKHRVLQYVGGVMSVEMQAPKLLWLKENLR 167
Cdd:cd07792 80 TNqreTTVVWDKS--------TGKPLYNAIVWLDTRTSDTVEElsakTPGGKDHFRKKTGLPISTYFSAVKLRWLLDNVP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 168 EI---------------CWdkaghffdlpdfLSWKATG----------VTARSLCSLV----CKWtysaekgwDDSFWKM 218
Cdd:cd07792 152 EVkkavddgrllfgtvdSW------------LIWNLTGgknggvhvtdVTNASRTMLMnlrtLQW--------DPELCEF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 219 IGLedliddnyskignlvllPGAALgigltPE---AARELGLPS-----GIAVAASLIDAHAgglgvigADVrGHGLTCE 290
Cdd:cd07792 212 FGI-----------------PMSIL-----PEirsSSEVYGKIAsgplaGVPISGCLGDQQA-------ALV-GQGCFKP 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 291 GQ------------------PVTSRlaviCG--TSSCH-MGISKDPVFvpgvwgpyysAMvpgfwlnEGGQSVTGKLIDh 349
Cdd:cd07792 262 GEakntygtgcfllyntgeePVFSK----HGllTTVAYkLGPDAPPVY----------AL-------EGSIAIAGAAVQ- 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 350 mvqghpafpelqakatarcqsiyaYLNSHLDLIKKAQPVGFL--TVD----LHVWPDFHGNRSPLADLTLKGMVTGLTLS 423
Cdd:cd07792 320 ------------------------WLRDNLGIISSASEVETLaaSVPdtggVYFVPAFSGLFAPYWRPDARGTIVGLTQF 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 424 QDLDDLAilyLATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILG 502
Cdd:cd07792 376 TTKAHIA---RAALEAVCFQTREILDAMNKdSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAA 452
|
570
....*....|..
gi 755508662 503 ACASGDFTSVQI 514
Cdd:cd07792 453 GLAVGVWKSLDE 464
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
20-501 |
1.94e-14 |
|
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: 75.34 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKWEPQ--FNHHEQSSEDIWAAcclvTKEVVQGIDAH---RIRGLGFd 93
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDlESGRILESVSRPTPAPISSddPGRSEQDPEKILEA----VRNLIDELPREylsDVTGIGI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 94 aTC---SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRVLQYVGGV-MSVEMQAPKLLWLKENLREI 169
Cdd:cd07777 76 -TGqmhGIVLWDEDGNPV---------SPLITWQDQRCSEEFLGGLSTYGEELLPKSGMrLKPGYGLATLFWLLRNGPLP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 170 cwDKAGHFFDLPDFLSWKATGvTARSLCSLVCK--WTY--SAEKGWDDSFWKMIGLEDLIddnYSKIGNlvllPGAALGi 245
Cdd:cd07777 146 --SKADRAGTIGDYIVARLTG-LPKPVMHPTNAasWGLfdLETGTWNKDLLEALGLPVIL---LPEIVP----SGEIVG- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 246 GLTPEaarelgLPSGIAVAASLIDAHAGglgVIGADVRGHGltcegqpvtsRLAVICGTSScHMGISKDPVFVPGVWG-- 323
Cdd:cd07777 215 TLSSA------LPKGIPVYVALGDNQAS---VLGSGLNEEN----------DAVLNIGTGA-QLSFLTPKFELSGSVEir 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 324 PYYSamvpGFWLNeggqSVT----GKLIDHMVQghpAFPELQAKATARC--QSIYAYLNShLDLIKKAQPvgfLTVDlhv 397
Cdd:cd07777 275 PFFD----GRYLL----VAAslpgGRALAVLVD---FLREWLRELGGSLsdDEIWEKLDE-LAESEESSD---LSVD--- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 398 wPDFHGNRSplaDLTLKGMVTGLTLsqdlDDLAI--LYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGG-LSKNPLFV 474
Cdd:cd07777 337 -PTFFGERH---DPEGRGSITNIGE----SNFTLgnLFRALCRGIAENLHEMLPRLDLDLSGIERIVGSGGaLRKNPVLR 408
|
490 500
....*....|....*....|....*..
gi 755508662 475 QMHADITGMPVVLSQEVESVLVGAAIL 501
Cdd:cd07777 409 RIIEKRFGLPVVLSEGSEEAAVGAALL 435
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
21-530 |
5.01e-14 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 74.63 E-value: 5.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 21 YVG-IDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIdahRIRGLGFDATC--- 96
Cdd:PTZ00294 3 YIGsIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKL---REKGPSFKIKAigi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 97 -----SLVVLDKefhplpvnHEGDSSRNVIMWLDHRAVSQVHRINET--KHRVLQYVGG-VMSVEMQAPKLLWLKENLRE 168
Cdd:PTZ00294 80 tnqreTVVAWDK--------VTGKPLYNAIVWLDTRTYDIVNELTKKygGSNFFQKITGlPISTYFSAFKIRWMLENVPA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 169 IcwDKAGH-----FFDLPDFLSWKATG-------VTARSLCSLVCKWTYSaekgWDDSFWKMIGL--EDL--IDDNYSKI 232
Cdd:PTZ00294 152 V--KDAVKegtllFGTIDTWLIWNLTGgkshvtdVTNASRTFLMNIKTLK----WDEELLNKFGIpkETLpeIKSSSENF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 233 GNLVLLPGAALgigltpeaarelglpSGIAVAASLIDAHAGGLGvigadvrgHGLTCEGQPVTSRlavicGTSsCH--MG 310
Cdd:PTZ00294 226 GTISGEAVPLL---------------EGVPITGCIGDQQAALIG--------HGCFEKGDAKNTY-----GTG-CFllMN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 311 ISKDPVFVP-GVWGpyysamVPGFWLNEGGQSVtgklidHMVQGhpafpelqakATARCQSIYAYLNSHLDLIKKAQPVG 389
Cdd:PTZ00294 277 TGTEIVFSKhGLLT------TVCYQLGPNGPTV------YALEG----------SIAVAGAGVEWLRDNMGLISHPSEIE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 390 FL------TVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETME-AAGHSLSTLF 462
Cdd:PTZ00294 335 KLarsvkdTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIV---RAALEAIALQTNDVIESMEkDAGIELNSLR 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 463 LCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQI--AVPREHGPLLHPCLSA 530
Cdd:PTZ00294 412 VDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEvkKLIRRSNSTFSPQMSA 481
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
20-512 |
5.77e-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: 74.06 E-value: 5.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFD---A 94
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAkaGIRASDIAAIGITnqrE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 95 TCslVVLDKEfhplpvnhEGDSSRNVIMWLDHRAVSQVHRINETKH--RVLQYVGGVMSVEMQAPKLLWLKEN---LREI 169
Cdd:cd07786 81 TT--VVWDRE--------TGKPVYNAIVWQDRRTADICEELKAEGHeeMIREKTGLVLDPYFSATKIRWILDNvpgARER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 170 cwDKAGH-FFDLPD-FLSWKATG----VT-----ARSLcslvckwTYSAEKG-WDDsfwkmiGLEDLIDdnyskignlvl 237
Cdd:cd07786 151 --AERGElAFGTIDsWLIWKLTGgkvhATdvtnaSRTM-------LFNIHTLeWDD------ELLELFG----------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 238 LPGAALgigltPE---------AARELGLPSGIAVAASLIDAHAgglgvigADVrGHGLTCEGQpvtsrlaVIC--GTSS 306
Cdd:cd07786 205 IPASML-----PEvkpssevfgYTDPDLLGAEIPIAGIAGDQQA-------ALF-GQACFEPGM-------AKNtyGTGC 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 307 -CHMGISKDPVFVPG------VWG----PYYsAMvpgfwlnEGGQSVTGKLIDhmvqghpafpelqakatarcqsiyaYL 375
Cdd:cd07786 265 fMLMNTGEKPVRSKNgllttiAWQlggkVTY-AL-------EGSIFIAGAAVQ-------------------------WL 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 376 NSHLDLIKKAQPVGFL--TVD----LHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIE 449
Cdd:cd07786 312 RDGLGLIESAAETEALarSVPdnggVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIA---RAALESIAYQTRDLLE 388
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755508662 450 TMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSV 512
Cdd:cd07786 389 AMEAdSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSL 452
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
20-511 |
6.70e-14 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 74.27 E-value: 6.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 20 YYVGIDVGTGSVRAALVDQRGLLLAFAEqpiKKW----EPQF-NHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLgf 92
Cdd:PRK10939 4 YLMALDAGTGSIRAVIFDLNGNQIAVGQ---AEWrhlaVPDVpGSMEFDLEKNWQLACQCIRQALQkaGIPASDIAAV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 93 dATCSL----VVLDKEFHPLpvnhegdssrnvimW----LDHRAVSQV----HRINETKHRVLQYVGGVMSVEmQAPKLL 160
Cdd:PRK10939 79 -SATSMregiVLYDRNGTEI--------------WacanVDARASREVselkELHNNFEEEVYRCSGQTLALG-ALPRLL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 161 WLKENLREIcWDKAGHFFDLPDFLSWKATGVTA--------RSLCSLVckwtysaEKGWDDSFWKMIGledLIDDNYSKi 232
Cdd:PRK10939 143 WLAHHRPDI-YRQAHTITMISDWIAYMLSGELAvdpsnagtTGLLDLV-------TRDWDPALLEMAG---LRADILPP- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 233 gnlVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGT-------- 304
Cdd:PRK10939 211 ---VKETGTVLG-HVTAKAAAETGLRAGTPVVMGGGDVQLGCLGL--------GVVRPGQ-----TAVLGGTfwqqvvnl 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 305 ----SSCHMGISKDPvfvpgvwgpyysAMVPGFWLNEGGQSVTGkLIdhMVQGHPAF-PELQAKATARCQSIYAYLNshl 379
Cdd:PRK10939 274 papvTDPNMNIRINP------------HVIPGMVQAESISFFTG-LT--MRWFRDAFcAEEKLLAERLGIDAYSLLE--- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 380 dliKKAQ--PVGFLTVdLHVWPD-------FHGNRSPLadltlkgmvtGLTLSQDLDDLAILYLATVQAIAFGTRFIIET 450
Cdd:PRK10939 336 ---EMASrvPVGSHGI-IPIFSDvmrfkswYHAAPSFI----------NLSIDPEKCNKATLFRALEENAAIVSACNLQQ 401
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755508662 451 MEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTS 511
Cdd:PRK10939 402 IAAfSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSS 463
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
396-507 |
2.04e-10 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 62.92 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 396 HVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFV 474
Cdd:PRK00047 344 YVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHII---RATLESIAYQTRDVLDAMQAdSGIRLKELRVDGGAVANNFLM 420
|
90 100 110
....*....|....*....|....*....|...
gi 755508662 475 QMHADITGMPVVLSQEVESVLVGAAILGACASG 507
Cdd:PRK00047 421 QFQADILGVPVERPVVAETTALGAAYLAGLAVG 453
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
21-514 |
3.96e-08 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 55.86 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 21 YVG-IDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAAcclVTKEVVQGIDAHRIRGLGFDATCSLV 99
Cdd:PLN02295 1 FVGaIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILES---VLTCIAKALEKAAAKGHNVDSGLKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 100 VL--DKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKH----RVLQYVGGVMSVEMQAPKLLWLKENLREICWD- 172
Cdd:PLN02295 78 GItnQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKELSggrkHFVETCGLPISTYFSATKLLWLLENVDAVKEAv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 173 KAGH--FFDLPDFLSWKATGVTARSL----CSLVCKWTYSAEKG--WDDSFWKMIGL--EDL--IDDNYSKIGnlvllpG 240
Cdd:PLN02295 158 KSGDalFGTIDSWLIWNLTGGASGGVhvtdVTNASRTMLMNLKTldWDKPTLEALGIpaEILpkIVSNSEVIG------T 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 241 AALGIGLtpeaarelglpSGIAVAASLIDAHAGGLGvigadvrghgltcegqpvtsrlavicgtSSCHMGISKDpVFVPG 320
Cdd:PLN02295 232 IAKGWPL-----------AGVPIAGCLGDQHAAMLG----------------------------QRCRPGEAKS-TYGTG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 321 VWgpyysaMVpgfwLNEGGQSVTGKlidHMVQGHPAFpELQAKATARcqsiYA-------------YLNSHLDLIKKAQP 387
Cdd:PLN02295 272 CF------IL----LNTGEEVVPSK---HGLLTTVAY-KLGPDAPTN----YAlegsvaiagaavqWLRDNLGIIKSASE 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 388 VGFL--TVD----LHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETM------EAAG 455
Cdd:PLN02295 334 IEALaaTVDdtggVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIA---RAVLESMCFQVKDVLDAMrkdageEKSH 410
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 755508662 456 HSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQI 514
Cdd:PLN02295 411 KGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEEEI 469
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
24-501 |
7.16e-07 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466792 [Multi-domain] Cd Length: 424 Bit Score: 51.49 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 24 IDVGTGSVRAALVDQRGLLLAFAEQPIK-KWEPQFNHHEqsSEDIWAACCLVTKEVVQGidaHRIRGLGFdaTC---SLV 99
Cdd:cd07772 5 FDIGKTNKKLLLFDENGEVLAERSTPNPeIEEDGYPCED--VEAIWEWLLDSLAELAKR---HRIDAINF--TThgaTFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 100 VLDKEFHP-LPV---NHEGDSSrnvimwldhravsqvhrINEtkhrvlQY--------------VGGVMSVEMQapkLLW 161
Cdd:cd07772 78 LLDENGELaLPVydyEKPIPDE-----------------INE------AYyaergpfeetgsppLPGGLNLGKQ---LYW 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 162 LKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVC--------KWTYS---AEKGWDDSFWKMigledliddnys 230
Cdd:cd07772 132 LKREKPEL-FARAKTILPLPQYWAWRLTGKAASEITSLGChtdlwdfeKNEYSslvKKEGWDKLFPPL------------ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 231 kignlvLLPGAALGIgLTPEAARELGLPSGIAVAASLIDAHAgglgvigadvrghgltcegqpvtSRLAvicgtsscHMG 310
Cdd:cd07772 199 ------RKAWEVLGP-LRPDLARRTGLPKDIPVGCGIHDSNA-----------------------ALLP--------YLA 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 311 ISKDPvFV---PGVWgpyYSAMVPGFWLNEGGQSVTGKLIDHM-VQGHPA----FP-----ELQAKataRCQSIYAYLNS 377
Cdd:cd07772 241 AGKEP-FTllsTGTW---CIAMNPGNDLPLTELDLARDCLYNLdVFGRPVktarFMggreyERLVE---RIAKSFPQLPS 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 378 HLDLIKkaqpvgFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAILYLATVQAIAfgtrfiietMEAAGHS 457
Cdd:cd07772 314 LADLAK------LLARGTFALPSFAPGGGPFPGSGGRGVLSAFPSAEEAYALAILYLALMTDYA---------LDLLGSG 378
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 755508662 458 LSTLFLCGGLSKNPLFVQMHADI-TGMPVVLSQEVESVLVGAAIL 501
Cdd:cd07772 379 VGRIIVEGGFAKNPVFLRLLAALrPDQPVYLSDDSEGTALGAALL 423
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
440-513 |
3.26e-06 |
|
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: 49.45 E-value: 3.26e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755508662 440 IAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSqEVESVLVGAAILGACASGDFTSVQ 513
Cdd:cd07771 378 LALKYAKTIEELEElTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAG-PVEATAIGNLLVQLIALGEIKSLE 451
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
19-92 |
5.57e-03 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 39.11 E-value: 5.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755508662 19 RYYVGIDVGTGSVRAALVDQRGLLLAFAEQPIkkwepqfnHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGF 92
Cdd:COG1940 5 GYVIGIDIGGTKIKAALVDLDGEVLARERIPT--------PAGAGPEAVLEAIAELIEELLAeaGISRGRILGIGI 72
|
|
| |
