|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
1-432 |
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: 821.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 1 MWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLREiCWDKAGHFFDLPDFLSWKATGVTARSLCSLVC 80
Cdd:cd07782 105 LWMDHRAVEEAERINATGHEVLKYVGGKISPEMEPPKLLWLKENLPE-TWAKAGHFFDLPDFLTWKATGSLTRSLCSLVC 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 81 KWTYSA----EKGWDDSFWKMIGLEDFVADNYSKIGNQVLPPGASLGNGLTPEAARDLGLLPGIAVAASLIDAHAGGLGV 156
Cdd:cd07782 184 KWTYLAhegsEGGWDDDFFKEIGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAKELGLPEGTPVGVSLIDAHAGGLGT 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 157 IGADVrgHGLICEGQPVTSRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAF 236
Cdd:cd07782 264 LGADV--GGLPCEADPLTRRLALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGLWLNEGGQSATGALLDHIIETHPAY 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 237 PELQVKATARCQSIYAYLNSHLDLIKKAQ--PVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLA 314
Cdd:cd07782 342 PELKEEAKAAGKSIYEYLNERLEQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALLYLA 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 315 TVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEA 394
Cdd:cd07782 422 TLQALAYGTRHIIEAMNAAGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDA 501
|
410 420 430
....*....|....*....|....*....|....*...
gi 1184725759 395 MAKMSKVGKVVFPRLQDKKYYDKKYQVFLKLVEHQKEY 432
Cdd:cd07782 502 MAAMSGPGKVVEPNEELKKYHDRKYEVFLKMYEDQREY 539
|
|
| 5C_CHO_kinase |
TIGR01315 |
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ... |
1-432 |
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: 551.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 1 MWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVC 80
Cdd:TIGR01315 105 LWMDHRALAEAEKINATNHNLLRYVGGKMSVEMEIPKVLWLKNNMPPE-LFARCKFFDLTDFLTWRATGKEIRSFCSVVC 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 81 KWTY----SAEKGWDDSFWKMIGLEDFVADNYSKIGNQVLPPGASLGNGLTPEAARDLGLLPGIAVAASLIDAHAGGLGV 156
Cdd:TIGR01315 184 KWGFvpvdGSNKGWQEDFYETIGLGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQELGLPAGTAVGSGLIDAHAGWIGT 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 157 IGADVRGHGLICEGQpvtSRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAF 236
Cdd:TIGR01315 264 VGAKVAENGDVSQAF---TRLAAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGYWLAEGGQSAAGELMDHMLETHVAY 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 237 PELQVKATARCQSIYAYLNSHLdLIKKAQP----VGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILY 312
Cdd:TIGR01315 341 DETVKEAEAAGKNIYDYLNEHL-KEMAAKTnapsISYLVRHFHVYPDLWGNRSPIADPNMRGVIIGLSMDRSKDGLALLY 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 313 LATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 392
Cdd:TIGR01315 420 YATMEFIAYGTRQIVEAMNTAGHTIKSIFMSGGQCQNPLLMQLIADACDMPVLIPYVNEAVLHGAAMLGAKAAGTTESLW 499
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1184725759 393 EAMAKMSKVGKVVFPRLQ-DKKYYDKKYQVFLKLVEHQKEY 432
Cdd:TIGR01315 500 DAMDRMSKPGKTVWPRGDpAKKLHDRKYEIFLQLARTQQEY 540
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
1-432 |
4.74e-173 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 495.40 E-value: 4.74e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 1 MWLDHRAVSQVNRINE----TKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLC 76
Cdd:COG1069 117 LWKDHTAQEEAERINElakaRGEDYLRYVGGIISSEWFWPKILHLLREDPEV-YEAADSFVELCDWITWQLTGSLKRSRC 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 77 SLVCKWTYSA-EKGW-DDSFWKMIGLE-DFVADnysKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGG 153
Cdd:COG1069 196 TAGHKALWHAhEGGYpSEEFFAALDPLlDGLAD---RLGTEIYPLGEPAGT-LTAEWAARLGLPPGTAVAVGAIDAHAGA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 154 LGVIGadvrghglICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGH 233
Cdd:COG1069 272 VGAGG--------VEPGT-----LVKVMGTSTCHMLVSPEERFVPGICGQVDGSIVPGMWGYEAGQSAVGDIFAWFVRLL 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 234 AAFPELQVKATARCQSIYAYLNshldliKKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDlaiLYL 313
Cdd:COG1069 339 VPPLEYEKEAEERGISLHPLLT------EEAAKLPPGESGLHALDWFNGNRSPLADQRLKGVILGLTLGTDAED---IYR 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 314 ATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 392
Cdd:COG1069 410 ALVEATAFGTRAIIERFEEEGVPIDEIIACGGIAtKNPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVE 489
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1184725759 393 EAMAKMSKV-GKVVFPRLQDKKYYDKKYQVFLKLVEHQKEY 432
Cdd:COG1069 490 EAMAAMGSGfDKVYTPDPENVAVYDALYAEYLQLHDYFGRG 530
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
1-422 |
6.91e-127 |
|
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: 377.35 E-value: 6.91e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 1 MWLDHRAVSQVNRINETKHSVLQ-YVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLV 79
Cdd:cd07768 107 FWMDHSAVNEAQWINMQCPQQLLdYLGGKISPEMGVPKLKYFLDEYSHL-RDKHFHIFDLHDYIAYELTRLYEWNICGLL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 80 CKWTYSA-EKGWDDSFWKMIGLEDfVADNYSKIGNQVLPPGASLGNGLtPEAARDLGLLPGIAVAASLIDAHAGGLGVIG 158
Cdd:cd07768 186 GKENLDGeESGWSSSFFKNIDPRL-EHLTTTKNLPSNVPIGTTSGVAL-PEMAEKMGLHPGTAVVVSCIDAHASWFAVAS 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 159 ADVRGhglicegqpvtsRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPE 238
Cdd:cd07768 264 PHLET------------SLFMIAGTSSCHMYGTTISDRIPGVWGPFDTIIDPDYSVYEAGQSATGKLIEHLFESHPCARK 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 239 LqVKATARCQSIYAYLNshlDLIKKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATVQA 318
Cdd:cd07768 332 F-DEALKKGADIYQVLE---QTIRQIEKNNGLSIHILTLDMFFGNRSEFADPRLKGSFIGESLDTSMLNLTYKYIAILEA 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 319 IALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFA---SVQEAM 395
Cdd:cd07768 408 LAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAAVLAKVAAGKKQladSITEAD 487
|
410 420
....*....|....*....|....*...
gi 1184725759 396 AKMSKVGKVVFPRLQD-KKYYDKKYQVF 422
Cdd:cd07768 488 ISNDRKSETFEPLAYRlGADYILLYKLL 515
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
1-425 |
2.33e-121 |
|
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: 362.62 E-value: 2.33e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 1 MWLDHRAVSQVNRINETKHSV----LQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLC 76
Cdd:cd07781 100 LWMDHRAQEEAAEINETAHPAleyyLAYYGGVYSSEWMWPKALWLKRNAPEV-YDAAYTIVEACDWINARLTGRWVRSRC 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 77 SLVCKWTYSAEKG-WDDSFWKMIGLEDfvADNYSKIGNQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLG 155
Cdd:cd07781 179 AAGHKWMYNEWGGgPPREFLAALDPGL--LKLREKLPGEVVPVGEPAG-TLTAEAAERLGLPAGIPVAQGGIDAHMGAIG 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 156 VigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIdhmvqghAA 235
Cdd:cd07781 256 A--------GVVEPGT-----LALIMGTSTCHLMVSPKPVDIPGICGPVPDAVVPGLYGLEAGQSAVGDIF-------AW 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 236 FPELQVKATA-RCQSIYAYLNshlDLIKKAQPV--GFLTVDlhvWpdFHGNRSPLADLTLKGMVTGLKLSQDLddlAILY 312
Cdd:cd07781 316 FVRLFVPPAEeRGDSIYALLS---EEAAKLPPGesGLVALD---W--FNGNRTPLVDPRLRGAIVGLTLGTTP---AHIY 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 313 LATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASV 391
Cdd:cd07781 385 RALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVAAGVYADI 464
|
410 420 430
....*....|....*....|....*....|....
gi 1184725759 392 QEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKL 425
Cdd:cd07781 465 EEAADAMVRVDRVYEPDPENHAVYEELYALYKEL 498
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
2-436 |
6.65e-75 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 243.99 E-value: 6.65e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 2 WLDHRAVSQVNRINETKHS-----VLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTA---- 72
Cdd:PRK04123 119 WKDHTAQEEAEEINRLAHErgeadLSRYIGGIYSSEWFWAKILHVLREDPAV-YEAAASWVEACDWVVALLTGTTDpqdi 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 73 -RSLCSLVCKWTYSAEKG--WDDSFWKMI--GLEDFVADnysKIGNQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLI 147
Cdd:PRK04123 198 vRSRCAAGHKALWHESWGglPSADFFDALdpLLARGLRD---KLFTETWTAGEPAG-TLTAEWAQRLGLPEGVAVSVGAF 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 148 DAHAGglgVIGADVRGHGLicegqpvtsrLAVIcGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLID 227
Cdd:PRK04123 274 DAHMG---AVGAGAEPGTL----------VKVM-GTSTCDILLADKQRAVPGICGQVDGSIVPGLIGYEAGQSAVGDIFA 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 228 HMVQgHAAFPELQVKATARCQSIYAYLNshldliKKA--QPVG---FLTVDlhvWpdFHGNRSPLADLTLKGMVTGLKLS 302
Cdd:PRK04123 340 WFAR-LLVPPEYKDEAEARGKQLLELLT------EAAakQPPGehgLVALD---W--FNGRRTPLADQRLKGVITGLTLG 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 303 QDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLG 381
Cdd:PRK04123 408 TDAPDI---YRALIEATAFGTRAIMECFEDQGVPVEEVIAAGGIArKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFA 484
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1184725759 382 ACASGDFASVQEAMAKM-SKVGKVVFPRLQDKKYYDKKYQVFLKLVE-HQKEYLAIM 436
Cdd:PRK04123 485 AVAAGAYPDIPEAQQAMaSPVEKTYQPDPENVARYEQLYQEYKQLHDyFGRGGNAVM 541
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
1-431 |
3.78e-71 |
|
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: 232.42 E-value: 3.78e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 1 MWLDHRAVSQVNRINET--KHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATG--VTARSLC 76
Cdd:COG1070 98 LWNDTRAAAEAAELREElgEEALYEITGNPLHPGFTAPKLLWLKENEPEI-FARIAKVLLPKDYLRYRLTGefVTDYSDA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 77 SlvckWT--YSAEKG-WDDSFWKMIGL-EDFVAdnyskignQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAG 152
Cdd:COG1070 177 S----GTglLDVRTRdWSDELLEALGIdRELLP--------ELVPPGEVAG-TLTAEAAAETGLPAGTPVVAGAGDNAAA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 153 GLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQg 232
Cdd:COG1070 244 ALGA--------GAVEPGD-----AAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAVPGRWLPMGATNNGGSALRWFRD- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 233 haafpelqvKATARCQSIYAYLNshlDLIKKAqPVG-----FLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDD 307
Cdd:COG1070 310 ---------LFADGELDDYEELN---ALAAEV-PPGadgllFL-------PYLSGERTPHWDPNARGAFFGLTLSHTRAH 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 308 LailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGD 387
Cdd:COG1070 370 L---ARAVLEGVAFALRDGLEALEEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGL 446
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1184725759 388 FASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKLVEHQKE 431
Cdd:COG1070 447 YDDLEEAAAAMVRVGETIEPDPENVAAYDELYERYRELYPALKP 490
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
177-384 |
6.63e-61 |
|
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: 196.39 E-value: 6.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 177 LAVICGTSSCHMGISKDP-IFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQvkATARCQSIYAYLN 255
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPvLSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELR--DAGNVESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 256 SHLDLikkaqpvgfLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLddlAILYLATVQAIALGTRFIIEAMEA-AG 334
Cdd:pfam02782 79 LAAVA---------PAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTL---AHLYRAILESLALQLRQILEALTKqEG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1184725759 335 HSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACA 384
Cdd:pfam02782 147 HPIDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| L-ribulokinase |
TIGR01234 |
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely ... |
1-433 |
2.56e-57 |
|
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: 197.45 E-value: 2.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 1 MWLDHRAVSQVNRINETKHS----VLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLC 76
Cdd:TIGR01234 121 LWKHHAAQEEADRINRLAHApgevDLSRYGGIISSEWFWAKILQITEEDPAI-YQAADRWIELADWIVAQLSGDIRRGRC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 77 SLVCKWTYSAEKGW-DDSFWKMI--GLEDFVADNYSK-IGNQVLPPGAslgngLTPEAARDLGLLPGIAVAASLIDAHag 152
Cdd:TIGR01234 200 TAGYKALWHESWGYpSASFFDELnpILNRHLPDKLFTdIWTAGEPAGT-----LTPEWAQRTGLPEGVVVAVGNFDAH-- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 153 gLGVIGADVrghgliceGQPvtSRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQg 232
Cdd:TIGR01234 273 -VGAVAAGI--------AQP--GALVKIMGTSTCHVLIGDKQRAVPGMCGVVDGGIVPGFIGYEAGQSAVGDIFAWFGK- 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 233 HAAFPELQVKATARCQSiyayLNSHLDLIKKAQPV---GFLTVDlhvWpdFHGNRSPLADLTLKGMVTGLKLSQDLDDla 309
Cdd:TIGR01234 341 VCVPPELKTEANASQKQ----LHEALSEAAAKQPSgehGLVALD---W--FNGNRSPLVDQRLKGVITGLTLATDAPL-- 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 310 iLYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDF 388
Cdd:TIGR01234 410 -LYRALIEATAFGTRMIMETFTDSGVPVEELMAAGGIArKNPVIMQIYADVTNRPLQIVASDQAPALGAAIFAAVAAGVY 488
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1184725759 389 ASVQEAMAKMSKVGKVVF-PRLQDKKYYDKKYQVFLKLVEHQKEYL 433
Cdd:TIGR01234 489 ADIPSAQAKMGSAVEKTLtPCSENAQRYEQLYARYQELAMSFGQYN 534
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
1-385 |
6.25e-57 |
|
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: 196.47 E-value: 6.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 1 MWLDHRAVSQVNRINE-TKHSVLQYVGGVMSVEMQAPKLLWLKENLREICWDKAgHFFDLPDFLSWKatgvtarsLCSLV 79
Cdd:cd07778 111 FWMDHRASEETQWLNNiLPDDILDYLGGGFIPEMAIPKLKYLIDLIKEDTFKKL-EVFDLHDWISYM--------LATNL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 80 CKW--TYSAE------------KGWDDSFWKMIGLEDFVAD--NYSKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVA 143
Cdd:cd07778 182 GHSniVPVNAppsigigidgslKGWSKDFYSKLKISTKVCNvgNTFKEAPPLPYAGIPIGK-VNVILASYLGIDKSTVVG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 144 ASLIDAHAGGLGVIgadvrghgliCEGQPVTSRLAVICGTSSCHMGISKDPI--FVPGVWGPyFSAMVPGFWLNEGGQSV 221
Cdd:cd07778 261 HGCIDCYAGWFSTF----------AAAKTLDTTLFMVAGTSTCFLYATSSSQvgPIPGIWGP-FDQLLKNYSVYEGGQSA 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 222 TGKLIDHMVQGHAAFPELQVKATarcqSIYAYLNSHLDLI--KKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGL 299
Cdd:cd07778 330 TGKLIEKLFNSHPAIIELLKSDA----NFFETVEEKIDKYerLLGQSIHYLTRHMFFYGDYLGNRTPYNDPNMSGSFIGE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 300 KLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVV---LSQEVESVLVG 376
Cdd:cd07778 406 STDSSLTDLVLKYILILEFLAFQTKLIIDNFQKEKIIIQKVVISGSQAKNARLLQLLSTVLSKIHIivpLSDSKYAVVKG 485
|
....*....
gi 1184725759 377 AAVLGACAS 385
Cdd:cd07778 486 AALLGKAAF 494
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
1-423 |
5.80e-52 |
|
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: 181.56 E-value: 5.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 1 MWLDHRAVSQVNRINET---KHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCS 77
Cdd:cd07805 97 IWSDTRAAEEAEEIAGGlggIEGYRLGGGNPPSGKDPLAKILWLKENEPEI-YAKTHKFLDAKDYLNFRLTGRAATDPST 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 78 LVCKWTYSAEKG-WDDSFWKMIGLEDfvadnySKIgNQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGV 156
Cdd:cd07805 176 ASTTGLMDLRKRrWSEELLRAAGIDP------DKL-PELVPSTEVVG-ELTPEAAAELGLPAGTPVVGGGGDAAAAALGA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 157 iGADVRGHGLICegqpvtsrlaviCGTSS---CHmgiSKDPIFVPGvwGPYFS--AMVPGFWLNEGGQSVTGKLIDHMVQ 231
Cdd:cd07805 248 -GAVEEGDAHIY------------LGTSGwvaAH---VPKPKTDPD--HGIFTlaSADPGRYLLAAEQETAGGALEWARD 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 232 gHAAFPELQVKatarcqSIYAYLNshlDLIKKAQP----VGFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDD 307
Cdd:cd07805 310 -NLGGDEDLGA------DDYELLD---ELAAEAPPgsngLLFL-------PWLNGERSPVEDPNARGAFIGLSLEHTRAD 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 308 LAilyLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPV-VLSQEVESVLVGAAVLGACASG 386
Cdd:cd07805 373 LA---RAVLEGVAFNLRWLLEALEKLTRKIDELRLVGGGARSDLWCQILADVLGRPVeVPENPQEAGALGAALLAAVGLG 449
|
410 420 430
....*....|....*....|....*....|....*..
gi 1184725759 387 DFASVQEAmAKMSKVGKVVFPRLQDKKYYDKKYQVFL 423
Cdd:cd07805 450 LLKSFDEA-KALVKVEKVFEPDPENRARYDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
48-415 |
1.17e-51 |
|
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: 179.64 E-value: 1.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 48 ICW-DK-AGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEdfvADNYSKIgnqvLPPGASLGN 124
Cdd:cd07779 96 ISWqDKrTAKFLTVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRdWSDDLLDAFGID---RDKLPEL----VPPGTVIGT 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 125 gLTPEAARDLGLLPGIAVAASlidAHAGGLGVIGADVRGHGLICegqpvtsrlaVICGTSSCHMGISKDPIFVPGVWGPY 204
Cdd:cd07779 169 -LTKEAAEETGLPEGTPVVAG---GGDQQCAALGAGVLEPGTAS----------LSLGTAAVVIAVSDKPVEDPERRIPC 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 205 FSAMVPGFWLNEGGQSVTGKLIDHMVQghaAFPELQVKATARCQSIYAYLNSHLDLIkkaqPVGFLtvDLHVWPDFHGNR 284
Cdd:cd07779 235 NPSAVPGKWVLEGSINTGGSAVRWFRD---EFGQDEVAEKELGVSPYELLNEEAAKS----PPGSD--GLLFLPYLAGAG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 285 SPLADLTLKGMVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPV 364
Cdd:cd07779 306 TPYWNPEARGAFIGLTLSHTRAHL---ARAILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPV 382
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1184725759 365 VLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYY 415
Cdd:cd07779 383 ERPETSEATALGAAILAAVGAGIYPDFEEAVKAMVRVTDTFEPDPENVAIY 433
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
1-425 |
1.24e-49 |
|
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: 175.42 E-value: 1.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 1 MWLDHRAVSQVNRINET-KHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFdLP-DFLSWKATGVTAR----- 73
Cdd:cd07808 97 LWNDQRSAAECEELEARlGDEILIITGNPPLPGFTLPKLLWLKENEPEI-FARIRKIL-LPkDYLRYRLTGELATdpsda 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 74 --SLCslvckwtYSAEKG-WDDSFWKMIGLEdfvadnyskigNQVLPP---GASLGNGLTPEAARDLGLLPGIAVAASLI 147
Cdd:cd07808 175 sgTLL-------FDVEKReWSEELLEALGLD-----------PSILPPiveSTEIVGTLTPEAAEELGLPEGTPVVAGAG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 148 DAHAGGLGVigadvrghGLICEGQPV----TSrlAVICGTSSCHMGISKDPIF-----VPGVW---GPYFSAmvpGF--- 212
Cdd:cd07808 237 DNAAAALGA--------GVVEPGDALislgTS--GVVFAPTDKPVPDPKGRLHtfphaVPGKWyamGVTLSA---GLslr 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 213 WLNE--GGQSVTGKLIDHMVQGHAAfpelqvkatarcqsiyaylnshldlikKAQPVGFLtvdlhvwPDFHGNRSPLADL 290
Cdd:cd07808 304 WLRDlfGPDRESFDELDAEAAKVPP---------------------------GSEGLLFL-------PYLSGERTPYWDP 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 291 TLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEV 370
Cdd:cd07808 350 NARGSFFGLSLSHTRAHLA---RAVLEGVAFSLRDSLEVLKELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEE 426
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1184725759 371 ESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKL 425
Cdd:cd07808 427 EGSAYGAALLAAVGAGVFDDLEEAAAACIKIEKTIEPDPERHEAYDELYARYREL 481
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
1-386 |
8.16e-41 |
|
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: 150.82 E-value: 8.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 1 MWLDHRAVSQVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLcSL 78
Cdd:cd07773 95 VWFDPRGKEEAEELAEriGAEELYRITGLPPSPMYSLAKLLWLREHEPEI-FAKAAKWLSVADYIAYRLTGEPVTDY-SL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 79 VCKWTY--SAEKGWDDSFWKMIGLEdfvADNYSkignQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGV 156
Cdd:cd07773 173 ASRTMLfdIRKRTWSEELLEAAGID---ASLLP----ELVPSGTVIGT-VTPEAAEELGLPAGTPVVVGGHDHLCAALGA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 157 igadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFS---AMVPGFWLNEGGQSvTGKLIDHMVQGH 233
Cdd:cd07773 245 --------GVIEPGD-----VLDSTGTAEALLAVVDEPPLDEMLAEGGLSyghHVPGGYYYLAGSLP-GGALLEWFRDLF 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 234 AAFPELQVKATARCQSIYAylnshldlikKAQPVGFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLailYL 313
Cdd:cd07773 311 GGDESDLAAADELAEAAPP----------GPTGLLFL-------PHLSGSGTPDFDPDARGAFLGLTLGTTRADL---LR 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1184725759 314 ATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 386
Cdd:cd07773 371 AILEGLAFELRLNLEALEKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
1-386 |
1.06e-40 |
|
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: 150.75 E-value: 1.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 1 MWLDHRAVSQVNRINETKHS--VLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATG--VTARSLC 76
Cdd:cd07804 97 LYGDRRATEEIEWLNENIGEdrIFEITGNPLDSQSVGPKLLWIKRNEPEV-FKKTRKFLGAYDYIVYKLTGeyVIDYSSA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 77 SLvckwtYS-----AEKGWDDSFWKMIGLEdfvadnySKIGNQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHA 151
Cdd:cd07804 176 GN-----EGglfdiRKRTWDEELLEALGID-------PDLLPELVPSTEIVG-EVTKEAAEETGLAEGTPVVAGTVDAAA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 152 GGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFSamVPGFWLNEGGQSVTGKLIDHMVQ 231
Cdd:cd07804 243 SALSA--------GVVEPGD-----LLLMLGTAGDIGVVTDKLPTDPRLWLDYHD--IPGTYVLNGGMATSGSLLRWFRD 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 232 GHAafPELQVKATARCQSIYAYLNshldliKKAQ--PVGfltVD-LHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDL 308
Cdd:cd07804 308 EFA--GEEVEAEKSGGDSAYDLLD------EEAEkiPPG---SDgLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHL 376
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184725759 309 ailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 386
Cdd:cd07804 377 ---YRALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
51-381 |
6.51e-38 |
|
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: 141.93 E-value: 6.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 51 DKAGHFFDLPDFLSWKATGVTA--RSLCSLVCKWTYsAEKGWDDSFWKMIGL-EDFVADnyskignqVLPPGASLGnGLT 127
Cdd:cd00366 100 DRRAKFLQPNDYIVFRLTGEFAidYSNASGTGLYDI-KTGDWSEELLDALGIpREKLPP--------IVESGEVVG-RVT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 128 PEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVtsrlaVICGTSSCHMGISKDPIFVPGVWGPYFSA 207
Cdd:cd00366 170 PEAAEETGLPAGTPVVAGGGDTAAAALGA--------GVVEPGDAV-----DSTGTSSVLSVCTDEPVPPDPRLLNRCHV 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 208 mVPGFWLNEGGQSVTGKLIDHMVQghaafpelqvkATARCQSIYAYLNSHLDLIKKAQP----VGFLtvdlhvwPDFHGN 283
Cdd:cd00366 237 -VPGLWLLEGAINTGGASLRWFRD-----------EFGEEEDSDAEYEGLDELAAEVPPgsdgLIFL-------PYLSGE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 284 RSPLADLTLKGMVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMP 363
Cdd:cd00366 298 RSPIWDPAARGVFFGLTLSHTRAHL---IRAVLEGVAYALRDNLEILEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVP 374
|
330
....*....|....*...
gi 1184725759 364 VVLSQEVESVLVGAAVLG 381
Cdd:cd00366 375 VVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
1-382 |
7.33e-38 |
|
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: 142.36 E-value: 7.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 1 MWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVC 80
Cdd:cd07783 95 MYNDARAVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEV-LAKTAKFLHQADWLAGRLTGDRGVTDYNNAL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 81 KWTYSAEKG-WDDSFWKMIGLEdfvadnySKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGViga 159
Cdd:cd07783 174 KLGYDPETGrWPSWLLALLGIP-------PDLLPRVVAPGTVIGT-LTAEAAEELGLPAGTPVVAGTTDSIAAFLAS--- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 160 dvrghGLICEGQPVTSrlaviCGTSSCHMGISKDPIFVPGVwGPYFSAMVPGFWLNEGGQSVTGKLIDHmvqghaAFPEL 239
Cdd:cd07783 243 -----GAVRPGDAVTS-----LGTTLVLKLLSDKRVPDPGG-GVYSHRHGDGYWLVGGASNTGGAVLRW------FFSDD 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 240 QVKAtarcqsiyaylnshldLIKKAQPVGflTVDLHVWP-DFHGNRSPLADLTLKGMVTGLKlsqdlDDLAILYLATVQA 318
Cdd:cd07783 306 ELAE----------------LSAQADPPG--PSGLIYYPlPLRGERFPFWDPDARGFLLPRP-----HDRAEFLRALLEG 362
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184725759 319 IALGTRFIIEAMEAAGHS-ISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLvGAAVLGA 382
Cdd:cd07783 363 IAFIERLGYERLEELGAPpVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEAAL-GAALLAA 426
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
1-386 |
2.85e-37 |
|
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: 141.15 E-value: 2.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 1 MWLDHRAVSQVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVtarslcsL 78
Cdd:cd07802 97 LSNDSRAADIVDRWEEdgTLEKVYPLTGQPLWPGQPVALLRWLKENEPER-YDRIRTVLFCKDWIRYRLTGE-------I 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 79 VCKWT-YSA------EKGWDDSFWKMIGLEDFvadnYSKIGnQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHA 151
Cdd:cd07802 169 STDYTdAGSslldldTGEYDDELLDLLGIEEL----KDKLP-PLVPSTEIAG-RVTAEAAALTGLPEGTPVAAGAFDVVA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 152 GGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGpYFSAMVPGFWLNEGGQSVTGKLIDHMVQ 231
Cdd:cd07802 243 SALGA--------GAVDEGQ-----LCVILGTWSINEVVTDEPVVPDSVGS-NSLHADPGLYLIVEASPTSASNLDWFLD 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 232 ghaafpELQVKATARCQSIYAYLNshlDLIKKAQPVG----FLtvdlhvwPDFHGNRsplADLTLKGMVTGLKLSQDLDD 307
Cdd:cd07802 309 ------TLLGEEKEAGGSDYDELD---ELIAAVPPGSsgviFL-------PYLYGSG---ANPNARGGFFGLTAWHTRAH 369
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184725759 308 LAilyLATVQAIALGTRFIIEAMEAAGHsISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 386
Cdd:cd07802 370 LL---RAVYEGIAFSHRDHLERLLVARK-PETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
2-426 |
9.37e-37 |
|
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: 140.38 E-value: 9.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 2 WLDHRAVSQVNRI--NETKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATG--VTARSLCS 77
Cdd:cd07770 96 WADTRAAEEAERLrkEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPEL-FAKAAKFVSIKEYLLYRLTGelVTDYSTAS 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 78 lvckWT---YSAEKGWDDSFWKMIGLEdfvADNYSKIgnqvLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDahaGGL 154
Cdd:cd07770 175 ----GTgllNIHTLDWDEEALELLGID---EEQLPEL----VDPTEVLP-GLKPEFAERLGLLAGTPVVLGASD---GAL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 155 GVIGAdvrghGLICEGqpvtsRLAVICGTSschmG----ISKDPIFVP--GVWgPYFSAmvPGFWL-----NEGGqSVTG 223
Cdd:cd07770 240 ANLGS-----GALDPG-----RAALTVGTS----GairvVSDRPVLDPpgRLW-CYRLD--ENRWLvggaiNNGG-NVLD 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 224 KLIDHMVQGHAAFPELQVKATArcqsiyAYLNSHlDLIkkaqpvgFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQ 303
Cdd:cd07770 302 WLRDTLLLSGDDYEELDKLAEA------VPPGSH-GLI-------FL-------PYLAGERAPGWNPDARGAFFGLTLNH 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 304 DLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGAC 383
Cdd:cd07770 361 TRADI---LRAVLEGVAFNLKSIYEALEELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALE 437
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1184725759 384 ASGDFASVQEamAKMSKVGKVVFPRLQDKKYYDKKYQVFLKLV 426
Cdd:cd07770 438 ALGLISSLEA--DELVKIGKVVEPDPENHAIYAELYERFKKLY 478
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
4-386 |
2.18e-27 |
|
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: 113.47 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 4 DHRAVSQVNRINETKHSVLQYVGGVMSVEMQAP-KLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVtarslcsLVCKW 82
Cdd:cd07798 101 DARGVEEAAEIDDEFGEEIYTTTGHWPTELFPAaRLLWFKENRPEI-FERIATVLSISDWIGYRLTGE-------LVSEP 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 83 TYSAEKG--------WDDSFWKMIGLEDfvadnysKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGL 154
Cdd:cd07798 173 SQASETQlfdikkreWSQELLEALGLPP-------EILPEIVPSGTVLGT-VSEEAARELGLPEGTPVVVGGADTQCALL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 155 GVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVP--GVW-GPYfsaMVPGFWLNEGGQSVTGKLIDHMVQ 231
Cdd:cd07798 245 GS--------GAIEPGD-----IGIVAGTTTPVQMVTDEPIIDPerRLWtGCH---LVPGKWVLESNAGVTGLNYQWLKE 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 232 GHAAFPELQvkatarcqsiYAYLNSHLDLIKKAQP--VGFLTVDLhvwpdFHGNRSPLADLTLKGMVTGLKLSQDLDDLA 309
Cdd:cd07798 309 LLYGDPEDS----------YEVLEEEASEIPPGANgvLAFLGPQI-----FDARLSGLKNGGFLFPTPLSASELTRGDFA 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184725759 310 IlylATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 386
Cdd:cd07798 374 R---AILENIAFAIRANLEQLEEvSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
1-386 |
1.78e-25 |
|
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: 108.02 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 1 MWLDHRAVSQVNRINET-KHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAgHFFDLP-DFLSWKATG--VTARSLC 76
Cdd:cd07809 98 LWCDTRTAPEAEELTEAlGGKKCLLVGLNIPARFTASKLLWLKENEPEH-YARI-AKILLPhDYLNWKLTGekVTGLGDA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 77 SLVckwtysaekGWDDSF-----WKMIGLEDFVADNYSKIGnQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHA 151
Cdd:cd07809 176 SGT---------FPIDPRtrdydAELLAAIDPSRDLRDLLP-EVLPAGEVAG-RLTPEGAEELGLPAGIPVAPGEGDNMT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 152 GGLGVigadvrghGLICEGQPVTSrlaviCGTSSCHMGISKDPIFVPgvwgpyfSAMVPGF--------WLNEG---GQS 220
Cdd:cd07809 245 GALGT--------GVVNPGTVAVS-----LGTSGTAYGVSDKPVSDP-------HGRVATFcdstggmlPLINTtncLTA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 221 VTGKLIDHMVQGHAAFPELQVKATARCQSIYAYlnshldlikkaqpvgfltvdlhvwPDFHGNRSP-LADLTlkGMVTGL 299
Cdd:cd07809 305 WTELFRELLGVSYEELDELAAQAPPGAGGLLLL------------------------PFLNGERTPnLPHGR--ASLVGL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 300 KLSQDldDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAV 379
Cdd:cd07809 359 TLSNF--TRANLARAALEGATFGLRYGLDILRELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAAL 436
|
....*..
gi 1184725759 380 LGACASG 386
Cdd:cd07809 437 QAAWGAG 443
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
1-386 |
5.59e-22 |
|
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: 97.70 E-value: 5.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 1 MWLDHRAVSQVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLREICwDKAGHFFDLPDFLSWKATGVTA--RSLC 76
Cdd:cd24121 97 LWLDGRAADIVERWQAdgIAEAVFEITGTGLFPGSQAAQLAWLKENEPERL-ERARTALHCKDWLFYKLTGEIAtdPSDA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 77 SLVCkwtYSAEKG-WDDSFWKMIGLEDFVAdnyskignqVLPP-GASLGNG--LTPEAARDLGLLPGIAVAASLIDAHAG 152
Cdd:cd24121 176 SLTF---LDFRTRqYDDEVLDLLGLEELRH---------LLPPiRPGTEVIgpLTPEAAAATGLPAGTPVVLGPFDVVAT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 153 GLGViGADVRGHGLicegqpvtsrlaVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGqSVTGKL-IDHMVQ 231
Cdd:cd24121 244 ALGS-GAIEPGDAC------------SILGTTGVHEVVVDEPDLEPEGVGYTICLGVPGRWLRAMA-NMAGTPnLDWFLR 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 232 --GHAAFPELQVKATarcqSIYAYLNSHLdlikKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLA 309
Cdd:cd24121 310 elGEVLKEGAEPAGS----DLFQDLEELA----ASSPPGAEGVLYHPYLSPAGERAPFVNPNARAQFTGLSLEHTRADLL 381
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184725759 310 ilyLATVQAIALGTRFIIEAMeaaGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 386
Cdd:cd24121 382 ---RAVYEGVALAMRDCYEHM---GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
4-420 |
7.44e-22 |
|
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466794 [Multi-domain] Cd Length: 492 Bit Score: 97.79 E-value: 7.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 4 DHRAVSQVNRINETKHSVLQ--YVGGVMSVEMQA-PKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTAR--SLCSL 78
Cdd:cd07775 101 DARAAEEVSELKELYNTLEEevYRISGQTFALGAiPRLLWLKNNRPEI-YRKAAKITMLSDWIAYKLSGELAVepSNGST 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 79 VCKWTySAEKGWDDSFWKMIGLEDFvadnyskIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVig 158
Cdd:cd07775 180 TGLFD-LKTRDWDPEILEMAGLKAD-------ILPPVVESGTVIGK-VTKEAAEETGLKEGTPVVVGGGDVQLGCLGL-- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 159 advrghGLICEGQpvtsrlAVICGTSSCHMGI-SKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQghAAFP 237
Cdd:cd07775 249 ------GVVRPGQ------TAVLGGSFWQQEVnTAAPVTDPAMNIRVNCHVIPDMWQAEGISFFPGLVMRWFRD--AFCA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 238 ELQVKATARCQSIYAYLNshldliKKAQ--PVGF-----LTVDL-------HVWPDFhgnrspladltlkgmvTGLKLSQ 303
Cdd:cd07775 315 EEKEIAERLGIDAYDLLE------EMAKdvPPGSygimpIFSDVmnyknwrHAAPSF----------------LNLDIDP 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 304 DLDDLAILYLATVQAIALGTRFIIEAMEAA-GHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGA 382
Cdd:cd07775 373 EKCNKATFFRAIMENAAIVSAGNLERIAEFsGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAG 452
|
410 420 430
....*....|....*....|....*....|....*...
gi 1184725759 383 CASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQ 420
Cdd:cd07775 453 VGAGIYSSLEEAVESLVKWEREYLPNPENHEVYQDLYE 490
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
278-427 |
4.20e-16 |
|
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466789 [Multi-domain] Cd Length: 486 Bit Score: 80.20 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 278 PDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMH 356
Cdd:cd07769 341 PAFSGLGAPYWDPDARGAIVGLTRGTTKAHIV---RAALESIAYQTRDVLEAMEKdSGIKLKELRVDGGATANNFLMQFQ 417
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184725759 357 ADITGMPVVLSQEVESVLVGAAVLGACASGdFASVQEAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 427
Cdd:cd07769 418 ADILGVPVVRPKVAETTALGAAYLAGLAVG-FWKDLDELASLWQVDKRFEPSMDEEE-RERLYRGWKKAVE 486
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
314-427 |
1.80e-15 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466802 [Multi-domain] Cd Length: 499 Bit Score: 78.33 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 314 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 392
Cdd:cd07792 384 AALEAVCFQTREILDAMNKdSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLD 463
|
90 100 110
....*....|....*....|....*....|....*
gi 1184725759 393 EAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 427
Cdd:cd07792 464 ELKSLNEGGRTVFEPQISEEE-RERRYKRWKKAVE 497
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
293-427 |
1.97e-15 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 78.18 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 293 KGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVE 371
Cdd:COG0554 359 RGAIFGLTRGTTRAHIA---RAALESIAYQTRDVLDAMEAdSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTE 435
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1184725759 372 SVLVGAAVLGACASGDFASVQEaMAKMSKVGKVVFPRLqDKKYYDKKYQVFLKLVE 427
Cdd:COG0554 436 TTALGAAYLAGLAVGFWKSLEE-LAALWKVDRRFEPQM-DEEERERLYAGWKKAVE 489
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
314-427 |
1.40e-14 |
|
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases
Pssm-ID: 198361 [Multi-domain] Cd Length: 486 Bit Score: 75.61 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 314 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 392
Cdd:cd07786 374 AALESIAYQTRDLLEAMEAdSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLD 453
|
90 100 110
....*....|....*....|....*....|....*
gi 1184725759 393 EAmAKMSKVGKVVFPRLqDKKYYDKKYQVFLKLVE 427
Cdd:cd07786 454 EL-AKLWQVDRRFEPSM-SEEEREALYAGWKKAVK 486
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
314-414 |
1.55e-14 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 75.40 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 314 ATVQAIALGTRFIIEAME-AAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 392
Cdd:PTZ00294 383 AALEAIALQTNDVIESMEkDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLE 462
|
90 100
....*....|....*....|..
gi 1184725759 393 EAMAKMSKVGKVVFPRLQDKKY 414
Cdd:PTZ00294 463 EVKKLIRRSNSTFSPQMSAEER 484
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
278-427 |
2.92e-13 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466803 [Multi-domain] Cd Length: 501 Bit Score: 71.44 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 278 PDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAIlylATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMH 356
Cdd:cd07793 356 PAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVR---AILESIAFRVKQLLETMEKeTSIKISSIRVDGGVSNNDFILQLI 432
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184725759 357 ADITGMPVVLSQEVESVLVGAAVLGACASGDFASVqEAMAKMSKVGKVVFPRlQDKKYYDKKYQVFLKLVE 427
Cdd:cd07793 433 ADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSK-EELKKLRKIEKIFEPK-MDNEKREELYKNWKKAVK 501
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
314-428 |
4.24e-12 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 67.93 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 314 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 392
Cdd:PRK00047 380 ATLESIAYQTRDVLDAMQAdSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLD 459
|
90 100 110
....*....|....*....|....*....|....*.
gi 1184725759 393 EaMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVEH 428
Cdd:PRK00047 460 E-LKEQWKIDRRFEPQMDEEE-REKLYAGWKKAVKR 493
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
1-425 |
3.45e-11 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 64.99 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 1 MWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLREICWDKAGHFfdLP-DFLSWKATGVTARSLCSLV 79
Cdd:PRK15027 95 LWNDGRCAQECALLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVL--LPkDYLRLRMTGEFASDMSDAA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 80 -CKWTYSAEKGWDDSfwkMIGLEDFVADNYSkignqVLPPGASLGNGLTPEAARDLGlLPGIAVAASLIDAHAGGLGVig 158
Cdd:PRK15027 173 gTMWLDVAKRDWSDV---MLQACHLSRDQMP-----ALYEGSEITGALLPEVAKAWG-MATVPVVAGGGDNAAGAVGV-- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 159 advrghGLICEGQPVTSrlaviCGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWlneggqsvtgKLIDHMVQGhAAFPE 238
Cdd:PRK15027 242 ------GMVDANQAMLS-----LGTSGVYFAVSEGFLSKPESAVHSFCHALPQRW----------HLMSVMLSA-ASCLD 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 239 LQVKATARcQSIYAYLNSHLDLIKKAQPVGFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATV-Q 317
Cdd:PRK15027 300 WAAKLTGL-SNVPALIAAAQQADESAEPVWFL-------PYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVgY 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 318 AIALGtrfiIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQ--EVESVLvGAAVLGACASGDFASVQEAM 395
Cdd:PRK15027 372 ALADG----MDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTggDVGPAL-GAARLAQIAANPEKSLIELL 446
|
410 420 430
....*....|....*....|....*....|
gi 1184725759 396 AKMSkVGKVVFPRLQDKKYYDKKYQVFLKL 425
Cdd:PRK15027 447 PQLP-LEQSHLPDAQRYAAYQPRRETFRRL 475
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
37-414 |
3.84e-10 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 61.58 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 37 KLLWLKENLREIcWDKAGHFFDLPDFLSWKATGV--TARSLCSlVCKWTYSAEKGWDDSFWKMIGLEdfvadnyskigNQ 114
Cdd:PRK10331 137 KLVWLKENHPQL-LEQAHAWLFISSLINHRLTGEftTDITMAG-TSQMLDIQQRDFSPEILQATGLS-----------RR 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 115 VLPP----GASLGNgLTPEAARDLGLLPGIAVAASlidAHAGGLGVIGAdvrGHGLiceGQPV----------------- 173
Cdd:PRK10331 204 LFPRlveaGEQIGT-LQPSAAALLGLPVGIPVISA---GHDTQFALFGS---GAGQ---NQPVlssgtweilmvrsaqvd 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 174 TSRLAVICGtSSCHMGiSKDPIFVPGVWgpyfsamvpgfWLNEGGQSVTGKLI-------DHMVQGHAAFPelqvkatAR 246
Cdd:PRK10331 274 TSLLSQYAG-STCELD-SQSGLYNPGMQ-----------WLASGVLEWVRKLFwtaetpyQTMIEEARAIP-------PG 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 247 CQSIYayLNSHLDLIKKAQPVGfLTVdlhvwpdfHGNRSPLADLTLKGMvtGLKLSQDLDDLailylatvqaialgtrfi 326
Cdd:PRK10331 334 ADGVK--MQCDLLACQNAGWQG-VTL--------NTTRGHFYRAALEGL--TAQLKRNLQVL------------------ 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 327 ieamEAAGH-SISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVV 405
Cdd:PRK10331 383 ----EKIGHfKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQARAQMKYQYRYF 458
|
....*....
gi 1184725759 406 FPRLQDKKY 414
Cdd:PRK10331 459 YPQTEPEFI 467
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
4-428 |
1.38e-09 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 60.02 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 4 DHRAVSQVNRINETkHSVLQYvgGVMSVEMQA------PKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTA----- 72
Cdd:PRK10939 104 DARASREVSELKEL-HNNFEE--EVYRCSGQTlalgalPRLLWLAHHRPDI-YRQAHTITMISDWIAYMLSGELAvdpsn 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 73 ---RSLCSLVckwtysaEKGWDDSFWKMIGLEDfvadnysKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDA 149
Cdd:PRK10939 180 agtTGLLDLV-------TRDWDPALLEMAGLRA-------DILPPVKETGTVLGH-VTAKAAAETGLRAGTPVVMGGGDV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 150 HAGGLGVigadvrghGLICEGQpvtsrLAVICGT------------SSCHMGISKDPifvpgvwgpyfsAMVPGFWLNEG 217
Cdd:PRK10939 245 QLGCLGL--------GVVRPGQ-----TAVLGGTfwqqvvnlpapvTDPNMNIRINP------------HVIPGMVQAES 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 218 GQSVTGkLIdhMVQGHAAF-PELQVKATARCQSIYAYLNshldliKKAQ--PVGFLTV-----DL-------HVWPDFhg 282
Cdd:PRK10939 300 ISFFTG-LT--MRWFRDAFcAEEKLLAERLGIDAYSLLE------EMASrvPVGSHGIipifsDVmrfkswyHAAPSF-- 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 283 nrspladltlkgmvtgLKLSQDLD--DLAILYLATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADI 359
Cdd:PRK10939 369 ----------------INLSIDPEkcNKATLFRALEENAAIVSACNLQQIAAfSGVFPSSLVFAGGGSKGKLWSQILADV 432
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184725759 360 TGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKK-------YQVFLKLVEH 428
Cdd:PRK10939 433 TGLPVKVPVVKEATALGCAIAAGVGAGIYSSLAETGERLVRWERTFEPNPENHELYQEAkekwqavYADQLGLVDH 508
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
36-394 |
1.42e-08 |
|
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.
Pssm-ID: 466791 [Multi-domain] Cd Length: 460 Bit Score: 56.77 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 36 PKLLWLKENLREIcWDKAGHFFDLPDFLSWKATG--VTARSLCSlvckwT---YSAEKG-WDDSFWKMIGLEdfvadnyS 109
Cdd:cd07771 132 YQLYALKKEGPEL-LERADKLLMLPDLLNYLLTGekVAEYTIAS-----TtqlLDPRTKdWSEELLEKLGLP-------R 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 110 KIGNQVLPPGASLGNgLTPEAARDLGL--LPGIAVA----ASLIDAhagglgvIGADVRGHGLICegqpvtsrlaviCGT 183
Cdd:cd07771 199 DLFPPIVPPGTVLGT-LKPEVAEELGLkgIPVIAVAshdtASAVAA-------VPAEDEDAAFIS------------SGT 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 184 SSChMGI-SKDPIFVPgvwgpyfSAMVPGFwLNEGG--------QSVTGkLidHMVQghaafpEL--QVKATARCQSiYA 252
Cdd:cd07771 259 WSL-IGVeLDEPVITE-------EAFEAGF-TNEGGadgtirllKNITG-L--WLLQ------ECrrEWEEEGKDYS-YD 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 253 YLNShldLIKKAQPVGFLtVDlhvwPD---FhgnRSPladltlKGMV---------TGLKLSQDLDDLA-ILYlatvQAI 319
Cdd:cd07771 320 ELVA---LAEEAPPFGAF-ID----PDdprF---LNP------GDMPeairaycreTGQPVPESPGEIArCIY----ESL 378
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184725759 320 ALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSqEVESVLVGAAVLGACASGDFASVQEA 394
Cdd:cd07771 379 ALKYAKTIEELEElTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAG-PVEATAIGNLLVQLIALGEIKSLEEG 453
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
38-380 |
7.26e-08 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466792 [Multi-domain] Cd Length: 424 Bit Score: 54.19 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 38 LLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVC--------KWTYS---AEKGWDDSFWKMigledfvad 106
Cdd:cd07772 129 LYWLKREKPEL-FARAKTILPLPQYWAWRLTGKAASEITSLGChtdlwdfeKNEYSslvKKEGWDKLFPPL--------- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 107 nyskignqvLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAgglgvigadvrghglicegqpvtSRLAvicgtssc 186
Cdd:cd07772 199 ---------RKAWEVLGP-LRPDLARRTGLPKDIPVGCGIHDSNA-----------------------ALLP-------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 187 HMGISKDPiFV---PGVWgpyFSAMVPGF-----WLNEG-----GQSVTGKLIdhmvqGHAAFP-----ELQVKataRCQ 248
Cdd:cd07772 238 YLAAGKEP-FTllsTGTW---CIAMNPGNdlpltELDLArdclyNLDVFGRPV-----KTARFMggreyERLVE---RIA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 249 SIYAYLNSHLDLIKkaqpvgFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATVQAIALgtrfiie 328
Cdd:cd07772 306 KSFPQLPSLADLAK------LLARGTFALPSFAPGGGPFPGSGGRGVLSAFPSAEEAYALAILYLALMTDYAL------- 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1184725759 329 amEAAGHSISTLFLCGGLSKNPLFVQMHADI-TGMPVVLSQEVESVLVGAAVL 380
Cdd:cd07772 373 --DLLGSGVGRIIVEGGFAKNPVFLRLLAALrPDQPVYLSDDSEGTALGAALL 423
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
314-427 |
1.87e-07 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 53.16 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 314 ATVQAIALGTRFIIEAM------EAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGD 387
Cdd:PLN02295 384 AVLESMCFQVKDVLDAMrkdageEKSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGL 463
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1184725759 388 FASVQEAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 427
Cdd:PLN02295 464 WTEEEIFASEKWKNTTTFRPKLDEEE-RAKRYASWCKAVE 502
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
248-378 |
2.36e-07 |
|
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: 52.61 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 248 QSIYAYLNShLDLIKKAQPvgfLTVDlhvwPDFHGNRSplaDLTLKGMVTGLklsqDLDDLAI--LYLATVQAIALGTRF 325
Cdd:cd07777 315 DEIWEKLDE-LAESEESSD---LSVD----PTFFGERH---DPEGRGSITNI----GESNFTLgnLFRALCRGIAENLHE 379
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1184725759 326 IIEAMEAAGHSISTLFLCGG-LSKNPLFVQMHADITGMPVVLSQEVESVLVGAA 378
Cdd:cd07777 380 MLPRLDLDLSGIERIVGSGGaLRKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAA 433
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
2-155 |
1.27e-06 |
|
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.
Pssm-ID: 395295 [Multi-domain] Cd Length: 245 Bit Score: 49.26 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 2 WLDHRAVSQVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVtarslcsLV 79
Cdd:pfam00370 98 WKDRRTAEIVENLKEegNNQKLYEITGLPIWPGFTLSKLRWIKENEPEV-FEKIHKFLTIHDYLRWRLTGV-------FV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 80 CKWTYSAEKG--------WDDSFWKMIGLEdfvadnyskigNQVLPP----GASLGNgLTPEAARDLGLLPGIAVAASLI 147
Cdd:pfam00370 170 TDHTNASRSMmfnihkldWDPELLAALGIP-----------RDHLPPlvesSEIYGE-LNPELAAMWGLDEGVPVVGGGG 237
|
....*...
gi 1184725759 148 DAHAGGLG 155
Cdd:pfam00370 238 DQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
334-417 |
1.39e-03 |
|
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466795 [Multi-domain] Cd Length: 514 Bit Score: 41.00 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725759 334 GHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKV----GKVVFPRL 409
Cdd:cd07776 423 DIPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVVFSaeepKLVAEPDP 502
|
....*...
gi 1184725759 410 QDKKYYDK 417
Cdd:cd07776 503 EAAEVYDK 510
|
|
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