|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
11-473 |
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: 875.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDATCS 88
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEgaGVDPEQVKGIGFDATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 89 LVVLDKQFHPLPVNQEGDSHRNVIMWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLREiCWDKAGHF 168
Cdd:cd07782 81 LVVLDAEGKPVSVSPSGDDERNVILWMDHRAVEEAERINATGHEVLKYVGGKISPEMEPPKLLWLKENLPE-TWAKAGHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 169 FDLPDFLSWKATGVTARSLCSLVCKWTYSA----EKGWDDSFWKMIGLEDFVADNYSKIGNQVLPPGASLGNGLTPEAAR 244
Cdd:cd07782 160 FDLPDFLTWKATGSLTRSLCSLVCKWTYLAhegsEGGWDDDFFKEIGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 245 DLGLLPGIAVAASLIDAHAGGLGVIGADVrgHGLICEGQPVTSRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGF 324
Cdd:cd07782 240 ELGLPEGTPVGVSLIDAHAGGLGTLGADV--GGLPCEADPLTRRLALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 325 WLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNSHLDLIKKAQ--PVGFLTVDLHVWPDFHGNRSPLADL 402
Cdd:cd07782 318 WLNEGGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNERLEQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADP 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184725755 403 TLKGMVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITG 473
Cdd:cd07782 398 TLRGMISGLTLDTSLDDLALLYLATLQALAYGTRHIIEAMNAAGHKIDTIFMCGGLSKNPLFVQLHADVTG 468
|
|
| 5C_CHO_kinase |
TIGR01315 |
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ... |
11-473 |
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: 597.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVV--QGIDLNQIRGLGFDATCS 88
Cdd:TIGR01315 1 HYIGVDVGTGSARACIIDSTGDILALAAQNIKTWTPSSGLEGQSSVYIWQAICNCVKQVLaeSKVDPNSVKGIGFDATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 89 LVVLDKQFHPLPVNQEGDSHRNVIMWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHF 168
Cdd:TIGR01315 81 LVVLTHDGEPLPVSKNGGADQNIILWMDHRALAEAEKINATNHNLLRYVGGKMSVEMEIPKVLWLKNNMPPE-LFARCKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 169 FDLPDFLSWKATGVTARSLCSLVCKWTY----SAEKGWDDSFWKMIGLEDFVADNYSKIGNQVLPPGASLGNGLTPEAAR 244
Cdd:TIGR01315 160 FDLTDFLTWRATGKEIRSFCSVVCKWGFvpvdGSNKGWQEDFYETIGLGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 245 DLGLLPGIAVAASLIDAHAGGLGVIGADVRGHGLICEGQpvtSRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGF 324
Cdd:TIGR01315 240 ELGLPAGTAVGSGLIDAHAGWIGTVGAKVAENGDVSQAF---TRLAAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 325 WLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNSHLdLIKKAQP----VGFLTVDLHVWPDFHGNRSPLA 400
Cdd:TIGR01315 317 WLAEGGQSAAGELMDHMLETHVAYDETVKEAEAAGKNIYDYLNEHL-KEMAAKTnapsISYLVRHFHVYPDLWGNRSPIA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1184725755 401 DLTLKGMVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITG 473
Cdd:TIGR01315 396 DPNMRGVIIGLSMDRSKDGLALLYYATMEFIAYGTRQIVEAMNTAGHTIKSIFMSGGQCQNPLLMQLIADACD 468
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
9-473 |
0e+00 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 526.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 9 ERYYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKNWEP---------QFnhhEQSSEDIWAACCVVTKKVVQ--GIDLN 76
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDaADGEELASAVHPYPRWVIglylppppdQA---RQHPLDYLEALEAAVREALAqaGVDPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 77 QIRGLGFDAT-CSLVVLDKQFHPLPVNQE--GDSHRNVIMWLDHRAVSQVNRINE----TKHSVLQYVGGVMSVEMQAPK 149
Cdd:COG1069 78 DVVGIGVDATgCTPVPVDADGTPLALLPEfaENPHAMVILWKDHTAQEEAERINElakaRGEDYLRYVGGIISSEWFWPK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 150 LLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGW-DDSFWKMIGLE-DFVADnysKIGNQ 226
Cdd:COG1069 158 ILHLLREDPEV-YEAADSFVELCDWITWQLTGSLKRSRCTAGHKALWHAhEGGYpSEEFFAALDPLlDGLAD---RLGTE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 227 VLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIGadvrghglICEGQpvtsrLAVICGTSSCHMGISKDP 306
Cdd:COG1069 234 IYPLGEPAGT-LTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGG--------VEPGT-----LVKVMGTSTCHMLVSPEE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 307 IFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNshldliKKAQPVGFLTVDL 386
Cdd:COG1069 300 RFVPGICGQVDGSIVPGMWGYEAGQSAVGDIFAWFVRLLVPPLEYEKEAEERGISLHPLLT------EEAAKLPPGESGL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 387 HVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDlaiLYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFV 465
Cdd:COG1069 374 HALDWFNGNRSPLADQRLKGVILGLTLGTDAED---IYRALVEATAFGTRAIIERFEEEGVPIDEIIACGGIAtKNPLVM 450
|
....*...
gi 1184725755 466 QMHADITG 473
Cdd:COG1069 451 QIYADVTG 458
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
11-473 |
3.93e-142 |
|
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: 418.18 E-value: 3.93e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVDQS-GVLLAFADQPIKNWE-PQFNHHEQSSEDIWAACCVVTKKVV--QGIDLNQIRGLGFDAT 86
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDLYaGLEMAQEPVPYYQDSsKKSWKFWQKSTEIIKALQKCVQKLNirEGVDAYEVKGCGVDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 87 CSLVVLDKQFHPLPVNQEGDSHRNVIMWLDHRAVSQVNRINETKHSVLQ-YVGGVMSVEMQAPKLLWLKENLREIcWDKA 165
Cdd:cd07768 81 CSLAIFDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWINMQCPQQLLdYLGGKISPEMGVPKLKYFLDEYSHL-RDKH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 166 GHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGWDDSFWKMIGLEDfVADNYSKIGNQVLPPGASLGNGLtPEAAR 244
Cdd:cd07768 160 FHIFDLHDYIAYELTRLYEWNICGLLGKENLDGeESGWSSSFFKNIDPRL-EHLTTTKNLPSNVPIGTTSGVAL-PEMAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 245 DLGLLPGIAVAASLIDAHAGGLGVIGADVRGhglicegqpvtsRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGF 324
Cdd:cd07768 238 KMGLHPGTAVVVSCIDAHASWFAVASPHLET------------SLFMIAGTSSCHMYGTTISDRIPGVWGPFDTIIDPDY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 325 WLNEGGQSVTGKLIDHMVQGHAAFPELqVKATARCQSIYAYLNshlDLIKKAQPVGFLTVDLHVWPDFHGNRSPLADLTL 404
Cdd:cd07768 306 SVYEAGQSATGKLIEHLFESHPCARKF-DEALKKGADIYQVLE---QTIRQIEKNNGLSIHILTLDMFFGNRSEFADPRL 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184725755 405 KGMVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITG 473
Cdd:cd07768 382 KGSFIGESLDTSMLNLTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTN 450
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
11-473 |
1.20e-130 |
|
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: 388.05 E-value: 1.20e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKNWE--PQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDA 85
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAeaGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 86 TCSLVVldkqfhplPVNQEGDSHRNVIMWLDHRAVSQVNRINETKHSV----LQYVGGVMSVEMQAPKLLWLKENLREIc 161
Cdd:cd07781 81 TSSTVV--------PVDEDGNPLAPAILWMDHRAQEEAAEINETAHPAleyyLAYYGGVYSSEWMWPKALWLKRNAPEV- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 162 WDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEDfvADNYSKIGNQVLPPGASLGnGLTP 240
Cdd:cd07781 152 YDAAYTIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGgPPREFLAALDPGL--LKLREKLPGEVVPVGEPAG-TLTA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 241 EAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFSAM 320
Cdd:cd07781 229 EAAERLGLPAGIPVAQGGIDAHMGAIGA--------GVVEPGT-----LALIMGTSTCHLMVSPKPVDIPGICGPVPDAV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 321 VPGFWLNEGGQSVTGKLIdhmvqghAAFPELQVKATA-RCQSIYAYLNshlDLIKKAQPV--GFLTVDlhvWpdFHGNRS 397
Cdd:cd07781 296 VPGLYGLEAGQSAVGDIF-------AWFVRLFVPPAEeRGDSIYALLS---EEAAKLPPGesGLVALD---W--FNGNRT 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184725755 398 PLADLTLKGMVTGLKLSQdldDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHADITG 473
Cdd:cd07781 361 PLVDPRLRGAIVGLTLGT---TPAHIYRALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAeKNPLWMQIYADVLG 434
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
12-467 |
1.86e-80 |
|
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: 260.03 E-value: 1.86e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 12 YVGVDVGTGSVRAALVDQSGVLLAFADQPI--KNWEPQFNHHEQSSEDIWAACCVVTKKVVQGIDLNQIRGLGFDATCSL 89
Cdd:cd07778 2 GIGIDVGSTSVRIGIFDYHGTLLATSERPIsyKQDPKDLWFVTQSSTEIWKAIKTALKELIEELSDYIVSGIGVSATCSM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 90 VVLDKQ-----FHPLPVNQE-GDSHRNVIMWLDHRAVSQVNRINE-TKHSVLQYVGGVMSVEMQAPKLLWLKENLREICW 162
Cdd:cd07778 82 VVMQRDsdtsyLVPYNVIHEkSNPDQDIIFWMDHRASEETQWLNNiLPDDILDYLGGGFIPEMAIPKLKYLIDLIKEDTF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 163 DKAgHFFDLPDFLSWKatgvtarsLCSLVCKW--TYSAE------------KGWDDSFWKMIGLEDFVAD--NYSKIGNQ 226
Cdd:cd07778 162 KKL-EVFDLHDWISYM--------LATNLGHSniVPVNAppsigigidgslKGWSKDFYSKLKISTKVCNvgNTFKEAPP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 227 VLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIgadvrghgliCEGQPVTSRLAVICGTSSCHMGISKDP 306
Cdd:cd07778 233 LPYAGIPIGK-VNVILASYLGIDKSTVVGHGCIDCYAGWFSTF----------AAAKTLDTTLFMVAGTSTCFLYATSSS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 307 I--FVPGVWGPyFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATarcqSIYAYLNSHLDLI--KKAQPVGFL 382
Cdd:cd07778 302 QvgPIPGIWGP-FDQLLKNYSVYEGGQSATGKLIEKLFNSHPAIIELLKSDA----NFFETVEEKIDKYerLLGQSIHYL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 383 TVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNP 462
Cdd:cd07778 377 TRHMFFYGDYLGNRTPYNDPNMSGSFIGESTDSSLTDLVLKYILILEFLAFQTKLIIDNFQKEKIIIQKVVISGSQAKNA 456
|
....*
gi 1184725755 463 LFVQM 467
Cdd:cd07778 457 RLLQL 461
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
10-473 |
3.51e-79 |
|
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: 255.14 E-value: 3.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 10 RYYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDAT- 86
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAkaGVDPEEIAAIGVSGQm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 87 CSLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINET--KHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDK 164
Cdd:COG1070 81 HGLVLLDADGEPL---------RPAILWNDTRAAAEAAELREElgEEALYEITGNPLHPGFTAPKLLWLKENEPEI-FAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 165 AGHFFDLPDFLSWKATG--VTARSLCSlvckWT--YSAEKG-WDDSFWKMIGL-EDFVAdnyskignQVLPPGASLGnGL 238
Cdd:COG1070 151 IAKVLLPKDYLRYRLTGefVTDYSDAS----GTglLDVRTRdWSDELLEALGIdRELLP--------ELVPPGEVAG-TL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 239 TPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFS 318
Cdd:COG1070 218 TAEAAAETGLPAGTPVVAGAGDNAAAALGA--------GAVEPGD-----AAVSLGTSGVVFVVSDKPLPDPEGRVHTFC 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 319 AMVPGFWLNEGGQSVTGKLIDHMVQghaafpelqvKATARCQSIYAYLNshlDLIKKAqPVG-----FLtvdlhvwPDFH 393
Cdd:COG1070 285 HAVPGRWLPMGATNNGGSALRWFRD----------LFADGELDDYEELN---ALAAEV-PPGadgllFL-------PYLS 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 394 GNRSPLADLTLKGMVTGLKLSQDLDDlaiLYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITG 473
Cdd:COG1070 344 GERTPHWDPNARGAFFGLTLSHTRAH---LARAVLEGVAFALRDGLEALEEAGVKIDRIRATGGGARSPLWRQILADVLG 420
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
9-473 |
7.52e-74 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 242.83 E-value: 7.52e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 9 ERYYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKNW---------EPQFNHHEQSSEDIWAAccvVTKKVVQ--GIDLN 76
Cdd:PRK04123 2 MAYVIGLDFGTDSVRALLVDcATGEELATAVVEYPHWvkgryldlpPNQALQHPLDYIESLEA---AIPAVLKeaGVDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 77 QIRGLGFDAT-CSLVVLDKQFHPLPVNQEGDSHRN--VIMWLDHRAVSQVNRINETKHS-----VLQYVGGVMSVEMQAP 148
Cdd:PRK04123 79 AVVGIGVDFTgSTPAPVDADGTPLALLPEFAENPHamVKLWKDHTAQEEAEEINRLAHErgeadLSRYIGGIYSSEWFWA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 149 KLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTA-----RSLCSLVCKWTYSAEKG--WDDSFWKMI--GLEDFVADn 219
Cdd:PRK04123 159 KILHVLREDPAV-YEAAASWVEACDWVVALLTGTTDpqdivRSRCAAGHKALWHESWGglPSADFFDALdpLLARGLRD- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 220 ysKIGNQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAgglGVIGADVRGHGLicegqpvtsrLAVIcGTSSCH 299
Cdd:PRK04123 237 --KLFTETWTAGEPAG-TLTAEWAQRLGLPEGVAVSVGAFDAHM---GAVGAGAEPGTL----------VKVM-GTSTCD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 300 MGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQgHAAFPELQVKATARCQSIYAYLNshldliKKA--Q 377
Cdd:PRK04123 300 ILLADKQRAVPGICGQVDGSIVPGLIGYEAGQSAVGDIFAWFAR-LLVPPEYKDEAEARGKQLLELLT------EAAakQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 378 PV---GFLTVDlhvWpdFHGNRSPLADLTLKGMVTGLKLSQDLDDlaiLYLATVQAIALGTRFIIEAMEAAGHSISTLFL 454
Cdd:PRK04123 373 PPgehGLVALD---W--FNGRRTPLADQRLKGVITGLTLGTDAPD---IYRALIEATAFGTRAIMECFEDQGVPVEEVIA 444
|
490 500
....*....|....*....|
gi 1184725755 455 CGGLS-KNPLFVQMHADITG 473
Cdd:PRK04123 445 AGGIArKNPVLMQIYADVLN 464
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
11-473 |
1.29e-67 |
|
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: 224.71 E-value: 1.29e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDAT-C 87
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEksGIDPSDIAAIAFSGQmQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 88 SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINET---KHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDK 164
Cdd:cd07805 81 GVVPVDKDGNPL---------RNAIIWSDTRAAEEAEEIAGGlggIEGYRLGGGNPPSGKDPLAKILWLKENEPEI-YAK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 165 AGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEDfvadnySKIgNQVLPPGASLGnGLTPEAA 243
Cdd:cd07805 151 THKFLDAKDYLNFRLTGRAATDPSTASTTGLMDLRKRrWSEELLRAAGIDP------DKL-PELVPSTEVVG-ELTPEAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 244 RDLGLLPGIAVAASLIDAHAGGLGViGADVRGHGLICegqpvtsrlaviCGTSS---CHmgiSKDPIFVPGvwGPYFS-- 318
Cdd:cd07805 223 AELGLPAGTPVVGGGGDAAAAALGA-GAVEEGDAHIY------------LGTSGwvaAH---VPKPKTDPD--HGIFTla 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 319 AMVPGFWLNEGGQSVTGKLIDHMVQgHAAFPELQVKatarcqSIYAYLNshlDLIKKAQP----VGFLtvdlhvwPDFHG 394
Cdd:cd07805 285 SADPGRYLLAAEQETAGGALEWARD-NLGGDEDLGA------DDYELLD---ELAAEAPPgsngLLFL-------PWLNG 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184725755 395 NRSPLADLTLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITG 473
Cdd:cd07805 348 ERSPVEDPNARGAFIGLSLEHTRADLA---RAVLEGVAFNLRWLLEALEKLTRKIDELRLVGGGARSDLWCQILADVLG 423
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
11-473 |
2.80e-60 |
|
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: 203.99 E-value: 2.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQGIDLNQIRGLGFDATC-SL 89
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPRRVVAIAVDGTSgTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 90 VVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFF 169
Cdd:cd07783 81 VLVDREGEPL---------RPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEV-LAKTAKFL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 170 DLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEdfvadnySKIGNQVLPPGASLGNgLTPEAARDLGL 248
Cdd:cd07783 151 HQADWLAGRLTGDRGVTDYNNALKLGYDPETGrWPSWLLALLGIP-------PDLLPRVVAPGTVIGT-LTAEAAEELGL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 249 LPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVTSrlaviCGTSSCHMGISKDPIFVPGVwGPYFSAMVPGFWLNE 328
Cdd:cd07783 223 PAGTPVVAGTTDSIAAFLAS--------GAVRPGDAVTS-----LGTTLVLKLLSDKRVPDPGG-GVYSHRHGDGYWLVG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 329 GGQSVTGKLIDHmvqghaAFPELQVKAtarcqsiyaylnshldLIKKAQPVGflTVDLHVWP-DFHGNRSPLADLTLKGM 407
Cdd:cd07783 289 GASNTGGAVLRW------FFSDDELAE----------------LSAQADPPG--PSGLIYYPlPLRGERFPFWDPDARGF 344
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184725755 408 VTGLKlsqdlDDLAILYLATVQAIALGTRFIIEAMEAAGHS-ISTLFLCGGLSKNPLFVQMHADITG 473
Cdd:cd07783 345 LLPRP-----HDRAEFLRALLEGIAFIERLGYERLEELGAPpVEEVRTAGGGARNDLWNQIRADVLG 406
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
11-473 |
1.01e-55 |
|
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: 190.85 E-value: 1.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDAT-C 87
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAkaGIDPSDIAAIGISGQmP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 88 SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAvsqvnrinetkhsvlqyvggvmsvemqapkllwlkenlreicwdkagH 167
Cdd:cd00366 81 GVVLVDADGNPL---------RPAIIWLDRRA-----------------------------------------------K 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 168 FFDLPDFLSWKATGVTA--RSLCSLVCKWTYsAEKGWDDSFWKMIGL-EDFVADnyskignqVLPPGASLGnGLTPEAAR 244
Cdd:cd00366 105 FLQPNDYIVFRLTGEFAidYSNASGTGLYDI-KTGDWSEELLDALGIpREKLPP--------IVESGEVVG-RVTPEAAE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 245 DLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVtsrlaVICGTSSCHMGISKDPIFVPGVWGPYFSAmVPGF 324
Cdd:cd00366 175 ETGLPAGTPVVAGGGDTAAAALGA--------GVVEPGDAV-----DSTGTSSVLSVCTDEPVPPDPRLLNRCHV-VPGL 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 325 WLNEGGQSVTGKLIDHMVQghaafpelqvkATARCQSIYAYLNSHLDLIKKAQP----VGFLtvdlhvwPDFHGNRSPLA 400
Cdd:cd00366 241 WLLEGAINTGGASLRWFRD-----------EFGEEEDSDAEYEGLDELAAEVPPgsdgLIFL-------PYLSGERSPIW 302
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1184725755 401 DLTLKGMVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITG 473
Cdd:cd00366 303 DPAARGVFFGLTLSHTRAHL---IRAVLEGVAYALRDNLEILEELGVKIKEIRVTGGGAKSRLWNQIKADVLG 372
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
11-473 |
3.40e-55 |
|
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: 190.81 E-value: 3.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQP--IKNwePQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDA- 85
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEhdLLT--PKPGWAEHDPEVWWGAVCEIIRELLAkaGISPKEIAAIGVSGl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 86 TCSLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINETKHS--VLQYVGGVMSVEMQAPKLLWLKENLREIcWD 163
Cdd:cd07804 79 VPALVPVDENGKPL---------RPAILYGDRRATEEIEWLNENIGEdrIFEITGNPLDSQSVGPKLLWIKRNEPEV-FK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 164 KAGHFFDLPDFLSWKATG--VTARSLCSLvckwtYS-----AEKGWDDSFWKMIGLEdfvadnySKIGNQVLPPGASLGn 236
Cdd:cd07804 149 KTRKFLGAYDYIVYKLTGeyVIDYSSAGN-----EGglfdiRKRTWDEELLEALGID-------PDLLPELVPSTEIVG- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 237 GLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPY 316
Cdd:cd07804 216 EVTKEAAEETGLAEGTPVVAGTVDAAASALSA--------GVVEPGD-----LLLMLGTAGDIGVVTDKLPTDPRLWLDY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 317 FSamVPGFWLNEGGQSVTGKLIDHMVQGHAafPELQVKATARCQSIYAYLNshldliKKAQ--PVGfltVD-LHVWPDFH 393
Cdd:cd07804 283 HD--IPGTYVLNGGMATSGSLLRWFRDEFA--GEEVEAEKSGGDSAYDLLD------EEAEkiPPG---SDgLIVLPYFM 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 394 GNRSPLADLTLKGMVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITG 473
Cdd:cd07804 350 GERTPIWDPDARGVIFGLTLSHTRAHL---YRALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTG 426
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
11-473 |
1.15e-54 |
|
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: 188.88 E-value: 1.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDAT-C 87
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAkaGVDPEDIAAIGLTSQrS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 88 SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVsqvnrinetkhsvlqyvggvmsvemqapkllwlkenlreicwdkagH 167
Cdd:cd07779 81 TFVPVDEDGRPL---------RPAISWQDKRTA----------------------------------------------K 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 168 FFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEdfvADNYSKIgnqvLPPGASLGNgLTPEAARDL 246
Cdd:cd07779 106 FLTVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRdWSDDLLDAFGID---RDKLPEL----VPPGTVIGT-LTKEAAEET 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 247 GLLPGIAVAASlidAHAGGLGVIGADVRGHGLICegqpvtsrlaVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWL 326
Cdd:cd07779 178 GLPEGTPVVAG---GGDQQCAALGAGVLEPGTAS----------LSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWV 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 327 NEGGQSVTGKLIDHMVQghaAFPELQVKATARCQSIYAYLNSHLDLIkkaqPVGFLtvDLHVWPDFHGNRSPLADLTLKG 406
Cdd:cd07779 245 LEGSINTGGSAVRWFRD---EFGQDEVAEKELGVSPYELLNEEAAKS----PPGSD--GLLFLPYLAGAGTPYWNPEARG 315
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184725755 407 MVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITG 473
Cdd:cd07779 316 AFIGLTLSHTRAHL---ARAILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFG 379
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
11-473 |
2.34e-54 |
|
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: 189.29 E-value: 2.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVV--QGIDLNQIRGLGFDA-TC 87
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLakAGISPSDIAAIGLTGqMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 88 SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINET-KHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAG 166
Cdd:cd07808 81 GLVLLDKNGRPL---------RPAILWNDQRSAAECEELEARlGDEILIITGNPPLPGFTLPKLLWLKENEPEI-FARIR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 167 HFFdLP-DFLSWKATGVTAR-------SLCslvckwtYSAEKG-WDDSFWKMIGLEdfvadnyskigNQVLPP---GASL 234
Cdd:cd07808 151 KIL-LPkDYLRYRLTGELATdpsdasgTLL-------FDVEKReWSEELLEALGLD-----------PSILPPiveSTEI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 235 GNGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPV----TSrlAVICGTSSCHMGISKDPIF-- 308
Cdd:cd07808 212 VGTLTPEAAEELGLPEGTPVVAGAGDNAAAALGA--------GVVEPGDALislgTS--GVVFAPTDKPVPDPKGRLHtf 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 309 ---VPGVW---GPYFSAmvpGF---WLNE--GGQSVTGKLIDHMVQGHAAfpelqvkatarcqsiyaylnshldlikKAQ 377
Cdd:cd07808 282 phaVPGKWyamGVTLSA---GLslrWLRDlfGPDRESFDELDAEAAKVPP---------------------------GSE 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 378 PVGFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEAAGHSISTLFLCGG 457
Cdd:cd07808 332 GLLFL-------PYLSGERTPYWDPNARGSFFGLSLSHTRAHLA---RAVLEGVAFSLRDSLEVLKELGIKVKEIRLIGG 401
|
490
....*....|....*.
gi 1184725755 458 LSKNPLFVQMHADITG 473
Cdd:cd07808 402 GAKSPLWRQILADVLG 417
|
|
| L-ribulokinase |
TIGR01234 |
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely ... |
11-473 |
6.05e-54 |
|
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: 189.75 E-value: 6.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKNWE--------------PQFNHHEQSSEDIWAAccvVTKKVVQ--GI 73
Cdd:TIGR01234 2 YAIGVDFGTLSGRALAVDvATGEEIATAVEWYRHWVkgqflpktgaklpnDQALQHPADYIEVLEA---AIPTVLAelGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 74 DLNQIRGLGFDAT-CSLVVLDKQFHPLPVNQE--GDSHRNVIMWLDHRAVSQVNRINETKHS----VLQYVGGVMSVEMQ 146
Cdd:TIGR01234 79 DPADVVGIGVDFTaCTPAPIDSDGNPLCLLPEfaENPHAYFKLWKHHAAQEEADRINRLAHApgevDLSRYGGIISSEWF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 147 APKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKGW-DDSFWKMI--GLEDFVADNYSK- 222
Cdd:TIGR01234 159 WAKILQITEEDPAI-YQAADRWIELADWIVAQLSGDIRRGRCTAGYKALWHESWGYpSASFFDELnpILNRHLPDKLFTd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 223 IGNQVLPPGAslgngLTPEAARDLGLLPGIAVAASLIDAHaggLGVIGADVrghgliceGQPvtSRLAVICGTSSCHMGI 302
Cdd:TIGR01234 238 IWTAGEPAGT-----LTPEWAQRTGLPEGVVVAVGNFDAH---VGAVAAGI--------AQP--GALVKIMGTSTCHVLI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 303 SKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQgHAAFPELQVKATARCQSiyayLNSHLDLIKKAQPV--- 379
Cdd:TIGR01234 300 GDKQRAVPGMCGVVDGGIVPGFIGYEAGQSAVGDIFAWFGK-VCVPPELKTEANASQKQ----LHEALSEAAAKQPSgeh 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 380 GFLTVDlhvWpdFHGNRSPLADLTLKGMVTGLKLSQDLDDlaiLYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS 459
Cdd:TIGR01234 375 GLVALD---W--FNGNRSPLVDQRLKGVITGLTLATDAPL---LYRALIEATAFGTRMIMETFTDSGVPVEELMAAGGIA 446
|
490
....*....|....*
gi 1184725755 460 -KNPLFVQMHADITG 473
Cdd:TIGR01234 447 rKNPVIMQIYADVTN 461
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
11-473 |
8.10e-53 |
|
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466793 [Multi-domain] Cd Length: 443 Bit Score: 184.33 E-value: 8.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQGIDLNQIRGLGFdAT--CS 88
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGPDPIAAISV-SSqgES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 89 LVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAG 166
Cdd:cd07773 80 GVPVDRDGEPL---------GPAIVWFDPRGKEEAEELAEriGAEELYRITGLPPSPMYSLAKLLWLREHEPEI-FAKAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 167 HFFDLPDFLSWKATGVTARSLcSLVCKWTY--SAEKGWDDSFWKMIGLEdfvADNYSkignQVLPPGASLGNgLTPEAAR 244
Cdd:cd07773 150 KWLSVADYIAYRLTGEPVTDY-SLASRTMLfdIRKRTWSEELLEAAGID---ASLLP----ELVPSGTVIGT-VTPEAAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 245 DLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFS---AMV 321
Cdd:cd07773 221 ELGLPAGTPVVVGGHDHLCAALGA--------GVIEPGD-----VLDSTGTAEALLAVVDEPPLDEMLAEGGLSyghHVP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 322 PGFWLNEGGQSvTGKLIDHMVQGHAAFPELQVKATARCQSIYAylnshldlikKAQPVGFLtvdlhvwPDFHGNRSPLAD 401
Cdd:cd07773 288 GGYYYLAGSLP-GGALLEWFRDLFGGDESDLAAADELAEAAPP----------GPTGLLFL-------PHLSGSGTPDFD 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184725755 402 LTLKGMVTGLKLSQDLDDlaiLYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITG 473
Cdd:cd07773 350 PDARGAFLGLTLGTTRAD---LLRAILEGLAFELRLNLEALEKAGIPIDEIRAVGGGARSPLWLQLKADILG 418
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
11-473 |
6.57e-51 |
|
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: 179.28 E-value: 6.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDAT-C 87
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEksGVDPSDIAGVGVTGHgN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 88 SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKA 165
Cdd:cd07802 81 GLYLVDKDGKPV---------RNAILSNDSRAADIVDRWEEdgTLEKVYPLTGQPLWPGQPVALLRWLKENEPER-YDRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 166 GHFFDLPDFLSWKATGVtarslcsLVCKWT-YSA------EKGWDDSFWKMIGLEDFvadnYSKIGnQVLPPGASLGnGL 238
Cdd:cd07802 151 RTVLFCKDWIRYRLTGE-------ISTDYTdAGSslldldTGEYDDELLDLLGIEEL----KDKLP-PLVPSTEIAG-RV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 239 TPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGpYFS 318
Cdd:cd07802 218 TAEAAALTGLPEGTPVAAGAFDVVASALGA--------GAVDEGQ-----LCVILGTWSINEVVTDEPVVPDSVGS-NSL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 319 AMVPGFWLNEGGQSVTGKLIDHMVQghaafpELQVKATARCQSIYAYLNshlDLIKKAQPVG----FLtvdlhvwPDFHG 394
Cdd:cd07802 284 HADPGLYLIVEASPTSASNLDWFLD------TLLGEEKEAGGSDYDELD---ELIAAVPPGSsgviFL-------PYLYG 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184725755 395 NRsplADLTLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEAAGHsISTLFLCGGLSKNPLFVQMHADITG 473
Cdd:cd07802 348 SG---ANPNARGGFFGLTAWHTRAHLL---RAVYEGIAFSHRDHLERLLVARK-PETIRLTGGGARSPVWAQIFADVLG 419
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
289-473 |
1.17e-50 |
|
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: 171.35 E-value: 1.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 289 LAVICGTSSCHMGISKDP-IFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQvkATARCQSIYAYLN 367
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPvLSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELR--DAGNVESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 368 SHLDLikkaqpvgfLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQdldDLAILYLATVQAIALGTRFIIEAMEA-AG 446
Cdd:pfam02782 79 LAAVA---------PAGGLLFYPDFSGNRAPGADPGARGSITGLSSPT---TLAHLYRAILESLALQLRQILEALTKqEG 146
|
170 180
....*....|....*....|....*..
gi 1184725755 447 HSISTLFLCGGLSKNPLFVQMHADITG 473
Cdd:pfam02782 147 HPIDTIHVSGGGSRNPLLLQLLADALG 173
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
11-473 |
4.09e-43 |
|
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: 158.87 E-value: 4.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQGIDLNQIRGLGFDATC-SL 89
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVDAIGFSSAMhSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 90 VVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRI--NETKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGH 167
Cdd:cd07770 81 LGVDEDGEPL---------TPVITWADTRAAEEAERLrkEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPEL-FAKAAK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 168 FFDLPDFLSWKATG--VTARSLCSlvckWT---YSAEKGWDDSFWKMIGLEdfvADNYSKIgnqvLPPGASLGnGLTPEA 242
Cdd:cd07770 151 FVSIKEYLLYRLTGelVTDYSTAS----GTgllNIHTLDWDEEALELLGID---EEQLPEL----VDPTEVLP-GLKPEF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 243 ARDLGLLPGIAVAASLIDahaGGLGVIGAdvrghGLICEGqpvtsRLAVICGTSschmG----ISKDPIFVP--GVWgPY 316
Cdd:cd07770 219 AERLGLLAGTPVVLGASD---GALANLGS-----GALDPG-----RAALTVGTS----GairvVSDRPVLDPpgRLW-CY 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 317 FSAmvPGFWL-----NEGGqSVTGKLIDHMVQGHAAFPELQVKATArcqsiyAYLNSHlDLIkkaqpvgFLtvdlhvwPD 391
Cdd:cd07770 281 RLD--ENRWLvggaiNNGG-NVLDWLRDTLLLSGDDYEELDKLAEA------VPPGSH-GLI-------FL-------PY 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 392 FHGNRSPLADLTLKGMVTGLKLSQDLDDlaiLYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADI 471
Cdd:cd07770 337 LAGERAPGWNPDARGAFFGLTLNHTRAD---ILRAVLEGVAFNLKSIYEALEELAGPVKEIRASGGFLRSPLWLQILADV 413
|
..
gi 1184725755 472 TG 473
Cdd:cd07770 414 LG 415
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
11-473 |
6.61e-37 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 141.15 E-value: 6.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDATC 87
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKdaGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 88 -SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINET-KHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKA 165
Cdd:cd07809 81 hGLVALDADGKVL---------RPAKLWCDTRTAPEAEELTEAlGGKKCLLVGLNIPARFTASKLLWLKENEPEH-YARI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 166 gHFFDLP-DFLSWKATG--VTARSLCSLVckwtysaekGWDDSF-----WKMIGLEDFVADNYSKIGnQVLPPGASLGnG 237
Cdd:cd07809 151 -AKILLPhDYLNWKLTGekVTGLGDASGT---------FPIDPRtrdydAELLAAIDPSRDLRDLLP-EVLPAGEVAG-R 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 238 LTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVTSrlaviCGTSSCHMGISKDPIFVPgvwgpyf 317
Cdd:cd07809 219 LTPEGAEELGLPAGIPVAPGEGDNMTGALGT--------GVVNPGTVAVS-----LGTSGTAYGVSDKPVSDP------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 318 SAMVPGF--------WLNEG---GQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYlnshldlikkaqpvgfltvdl 386
Cdd:cd07809 279 HGRVATFcdstggmlPLINTtncLTAWTELFRELLGVSYEELDELAAQAPPGAGGLLLL--------------------- 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 387 hvwPDFHGNRSP-LADLTlkGMVTGLKLSQdlDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFV 465
Cdd:cd07809 338 ---PFLNGERTPnLPHGR--ASLVGLTLSN--FTRANLARAALEGATFGLRYGLDILRELGVEIDEIRLIGGGSKSPVWR 410
|
....*...
gi 1184725755 466 QMHADITG 473
Cdd:cd07809 411 QILADVFG 418
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
11-473 |
8.09e-34 |
|
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: 132.73 E-value: 8.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHH--EQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLgfdAT 86
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYPDakEFDPEELWEKICEAIREALKkaGISPEDISAV---SS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 87 CS----LVVLDKQFHPL---PvnqegdshrNVimwlDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAP-KLLWLKENLR 158
Cdd:cd07798 78 TSqregIVFLDKDGRELyagP---------NI----DARGVEEAAEIDDEFGEEIYTTTGHWPTELFPAaRLLWFKENRP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 159 EIcWDKAGHFFDLPDFLSWKATGVtarslcsLVCKWTYSAEKG--------WDDSFWKMIGLEDfvadnysKIGNQVLPP 230
Cdd:cd07798 145 EI-FERIATVLSISDWIGYRLTGE-------LVSEPSQASETQlfdikkreWSQELLEALGLPP-------EILPEIVPS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 231 GASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVP 310
Cdd:cd07798 210 GTVLGT-VSEEAARELGLPEGTPVVVGGADTQCALLGS--------GAIEPGD-----IGIVAGTTTPVQMVTDEPIIDP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 311 --GVW-GPYfsaMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQvkatarcqsiYAYLNSHLDLIKKAQP--VGFLTVD 385
Cdd:cd07798 276 erRLWtGCH---LVPGKWVLESNAGVTGLNYQWLKELLYGDPEDS----------YEVLEEEASEIPPGANgvLAFLGPQ 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 386 LhvwpdFHGNRSPLADLTLKGMVTGLKLSQDLDDLAIlylATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLF 464
Cdd:cd07798 343 I-----FDARLSGLKNGGFLFPTPLSASELTRGDFAR---AILENIAFAIRANLEQLEEvSGREIPYIILCGGGSRSALL 414
|
....*....
gi 1184725755 465 VQMHADITG 473
Cdd:cd07798 415 CQILADVLG 423
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
11-473 |
1.50e-31 |
|
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). It catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466971 [Multi-domain] Cd Length: 452 Bit Score: 126.20 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQGIDL--NQIRGLGFDAT-- 86
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVlpDRVAAIGVTGQgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 87 -CSLVvlDKqfhplpvnqEGDSHRNVIMWLDHRAVSQVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLREICwD 163
Cdd:cd24121 81 gTWLV--DE---------DGRPVRDAILWLDGRAADIVERWQAdgIAEAVFEITGTGLFPGSQAAQLAWLKENEPERL-E 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 164 KAGHFFDLPDFLSWKATGVTA--RSLCSLVCkwtYSAEKG-WDDSFWKMIGLEDFVAdnyskignqVLPP-GASLGNG-- 237
Cdd:cd24121 149 RARTALHCKDWLFYKLTGEIAtdPSDASLTF---LDFRTRqYDDEVLDLLGLEELRH---------LLPPiRPGTEVIgp 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 238 LTPEAARDLGLLPGIAVAASLIDAHAGGLGViGADVRGHGLicegqpvtsrlaVICGTSSCHMGISKDPIFVPGVWGPYF 317
Cdd:cd24121 217 LTPEAAAATGLPAGTPVVLGPFDVVATALGS-GAIEPGDAC------------SILGTTGVHEVVVDEPDLEPEGVGYTI 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 318 SAMVPGFWLNEGGqSVTGKL-IDHMVQ--GHAAFPELQVKATarcqSIYAYLNSHLdlikKAQPVGFLTVDLHVWPDFHG 394
Cdd:cd24121 284 CLGVPGRWLRAMA-NMAGTPnLDWFLRelGEVLKEGAEPAGS----DLFQDLEELA----ASSPPGAEGVLYHPYLSPAG 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184725755 395 NRSPLADLTLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMeaaGHSISTLFLCGGLSKNPLFVQMHADITG 473
Cdd:cd24121 355 ERAPFVNPNARAQFTGLSLEHTRADLL---RAVYEGVALAMRDCYEHM---GEDPGELRLSGGGARSDTWCQILADALG 427
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
11-267 |
6.21e-28 |
|
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.
Pssm-ID: 395295 [Multi-domain] Cd Length: 245 Bit Score: 111.66 E-value: 6.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFDATC- 87
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSqlGISLKQIKGIGISNQGh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 88 SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKA 165
Cdd:pfam00370 81 GTVLLDKNDKPL---------YNAILWKDRRTAEIVENLKEegNNQKLYEITGLPIWPGFTLSKLRWIKENEPEV-FEKI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 166 GHFFDLPDFLSWKATGVtarslcsLVCKWTYSAEKG--------WDDSFWKMIGLEdfvadnyskigNQVLPP----GAS 233
Cdd:pfam00370 151 HKFLTIHDYLRWRLTGV-------FVTDHTNASRSMmfnihkldWDPELLAALGIP-----------RDHLPPlvesSEI 212
|
250 260 270
....*....|....*....|....*....|....
gi 1184725755 234 LGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLG 267
Cdd:pfam00370 213 YGE-LNPELAAMWGLDEGVPVVGGGGDQQAAAFG 245
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
12-473 |
9.41e-20 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 91.95 E-value: 9.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 12 YVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQGIDLNQIRGLGFDATC-SLV 90
Cdd:PRK15027 2 YIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQMhGAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 91 VLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLREICWDKAGHFfd 170
Cdd:PRK15027 82 LLDAQQRVL---------RPAILWNDGRCAQECALLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVL-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 171 LP-DFLSWKATGVTARSLCSLV-CKWTYSAEKGWDDSfwkMIGLEDFVADNYSkignqVLPPGASLGNGLTPEAARDLGl 248
Cdd:PRK15027 151 LPkDYLRLRMTGEFASDMSDAAgTMWLDVAKRDWSDV---MLQACHLSRDQMP-----ALYEGSEITGALLPEVAKAWG- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 249 LPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVTSrlaviCGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWlne 328
Cdd:PRK15027 222 MATVPVVAGGGDNAAGAVGV--------GMVDANQAMLS-----LGTSGVYFAVSEGFLSKPESAVHSFCHALPQRW--- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 329 ggqsvtgKLIDHMVQGhAAFPELQVKATARcQSIYAYLNSHLDLIKKAQPVGFLtvdlhvwPDFHGNRSPLADLTLKGMV 408
Cdd:PRK15027 286 -------HLMSVMLSA-ASCLDWAAKLTGL-SNVPALIAAAQQADESAEPVWFL-------PYLSGERTPHNNPQAKGVF 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184725755 409 TGLKLSQDLDDLAILYLATV-QAIALGtrfiIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITG 473
Cdd:PRK15027 350 FGLTHQHGPNELARAVLEGVgYALADG----MDVVHACGIKPQSVTLIGGGARSEYWRQMLADISG 411
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
11-474 |
1.12e-19 |
|
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: 91.63 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPiknWEPQFNHHEQSSEDI-----WAACCVVTKKVVQ--GIDLNQIRGLgf 83
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQRE---WRHKEVPDVPGSMDFdteknWKLICECIREALKkaGIAPKSIAAI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 84 dATCS----LVVLDKQFHPLpvnqegdshrnvimW----LDHRAVSQVNRINETKHSVLQ--YVGGVMSVEMQA-PKLLW 152
Cdd:cd07775 76 -STTSmregIVLYDNEGEEI--------------WacanVDARAAEEVSELKELYNTLEEevYRISGQTFALGAiPRLLW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 153 LKENLREIcWDKAGHFFDLPDFLSWKATGVTAR--SLCSLVCKWTySAEKGWDDSFWKMIGLEDFvadnyskIGNQVLPP 230
Cdd:cd07775 141 LKNNRPEI-YRKAAKITMLSDWIAYKLSGELAVepSNGSTTGLFD-LKTRDWDPEILEMAGLKAD-------ILPPVVES 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 231 GASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrlAVICGTSSCHMGI-SKDPIFV 309
Cdd:cd07775 212 GTVIGK-VTKEAAEETGLKEGTPVVVGGGDVQLGCLGL--------GVVRPGQ------TAVLGGSFWQQEVnTAAPVTD 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 310 PGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQghAAFPELQVKATARCQSIYAYLNshldliKKAQ--PVGF-----L 382
Cdd:cd07775 277 PAMNIRVNCHVIPDMWQAEGISFFPGLVMRWFRD--AFCAEEKEIAERLGIDAYDLLE------EMAKdvPPGSygimpI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 383 TVDL-------HVWPDFhgnrspladltlkgmvTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAA-GHSISTLFL 454
Cdd:cd07775 349 FSDVmnyknwrHAAPSF----------------LNLDIDPEKCNKATFFRAIMENAAIVSAGNLERIAEFsGIFPDSLVF 412
|
490 500
....*....|....*....|
gi 1184725755 455 CGGLSKNPLFVQMHADITGS 474
Cdd:cd07775 413 AGGASKGKLWCQILADVLGL 432
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
11-313 |
1.94e-11 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 66.18 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVDQSGVLLAFADqpiKNW----EPQF-NHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLgf 83
Cdd:PRK10939 4 YLMALDAGTGSIRAVIFDLNGNQIAVGQ---AEWrhlaVPDVpGSMEFDLEKNWQLACQCIRQALQkaGIPASDIAAV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 84 dATCSL----VVLDKQFHPLpvnqegdshrnvimW----LDHRAVSQVNRINEtKHSVLQYvgGVMSVEMQA------PK 149
Cdd:PRK10939 79 -SATSMregiVLYDRNGTEI--------------WacanVDARASREVSELKE-LHNNFEE--EVYRCSGQTlalgalPR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 150 LLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTA--------RSLCSLVckwtysaEKGWDDSFWKMIGLEDfvadnys 221
Cdd:PRK10939 141 LLWLAHHRPDI-YRQAHTITMISDWIAYMLSGELAvdpsnagtTGLLDLV-------TRDWDPALLEMAGLRA------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 222 KIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGT------ 295
Cdd:PRK10939 206 DILPPVKETGTVLGH-VTAKAAAETGLRAGTPVVMGGGDVQLGCLGL--------GVVRPGQ-----TAVLGGTfwqqvv 271
|
330 340
....*....|....*....|....
gi 1184725755 296 ------SSCHMGISKDPIFVPGVW 313
Cdd:PRK10939 272 nlpapvTDPNMNIRINPHVIPGMV 295
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
11-473 |
1.71e-10 |
|
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: 62.87 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFdaTC- 87
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAkaGISASDIAAIGI--TNq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 88 --SLVVLDKqfhplpvnQEGDSHRNVIMWLDHRAVSQVNRINETKHS--VLQYVGGVMSVEMQAPKLLWLKEN---LREI 160
Cdd:cd07769 79 reTTVVWDK--------KTGKPLYNAIVWQDRRTADICEELKAKGLEerIREKTGLPLDPYFSATKIKWILDNvpgARER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 161 CwdKAGHF-FDLPD-FLSWKATG----VT-----ARSLcsLvckwtYSAEKG-WDDsfwkMIgLEDFvadnysKIGNQVL 228
Cdd:cd07769 151 A--ERGELlFGTIDtWLIWKLTGgkvhVTdvtnaSRTM--L-----FNIHTLeWDD----EL-LELF------GIPRSML 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 229 P---PGASLgNGLTPEAardlGLLPGIAVAASLIDAHAgglgvigADVrGHGLICEG------------------QPVTS 287
Cdd:cd07769 211 PevrPSSEV-FGYTDPE----GLGAGIPIAGILGDQQA-------ALF-GQGCFEPGmakntygtgcfllmntgeKPVPS 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 288 R---LAVICgtsschMGISKDP-------IFVPGvwgpyfSAMVpgfWLNEGgqsvtGKLIDHMvqghaafPELQvkata 357
Cdd:cd07769 278 KnglLTTIA------WQIGGKVtyalegsIFIAG------AAIQ---WLRDN-----LGLIEDA-------AETE----- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 358 rcqsiyaylnshlDLIKKAQPVGfltvDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRF 437
Cdd:cd07769 326 -------------ELARSVEDNG----GVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIV---RAALESIAYQTRD 385
|
490 500 510
....*....|....*....|....*....|....*..
gi 1184725755 438 IIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITG 473
Cdd:cd07769 386 VLEAMEKdSGIKLKELRVDGGATANNFLMQFQADILG 422
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
11-473 |
7.74e-10 |
|
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: 61.04 E-value: 7.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFdAT-- 86
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKnaGLTPEDIAAIGI-STqr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 87 CSLVVLDKQ----FHplpvnqegdshrNVIMWLDHRAVSQVNRINE-----------------TKH------SVLQYVGG 139
Cdd:cd07793 80 NTFLTWDKKtgkpLH------------NFITWQDLRAAELCESWNRslllkalrggskflhflTRNkrflaaSVLKFSTA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 140 vmsveMQAPKLLWLKENLREICWDKAGH---FFDLPDFLSWKATG----VTARSLCSlvckwtysaEKGWDDSF---WKM 209
Cdd:cd07793 148 -----HVSIRLLWILQNNPELKEAAEKGellFGTIDTWLLWKLTGgkvhATDYSNAS---------ATGLFDPFtleWSP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 210 IGLEDFvadnysKIGNQVLPPgaslgngltpeaardlgllpgiavaaslIDAHAGGLGVIGADVRGHGLicegqPVTsrl 289
Cdd:cd07793 214 ILLSLF------GIPSSILPE----------------------------VKDTSGDFGSTDPSIFGAEI-----PIT--- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 290 AVI-----------C---GTSSCHMGISkdpIFVPGVWGPYFSAMVPGF-----W--------LNEGGQSVTGKLIDHmv 342
Cdd:cd07793 252 AVVadqqaalfgecCfdkGDVKITMGTG---TFIDINTGSKPHASVKGLyplvgWkiggeityLAEGNASDTGTVIDW-- 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 343 qghaafpelqvkatarCQSIyAYLNSHLDLIKKAQPVGfLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAI 422
Cdd:cd07793 327 ----------------AKSI-GLFDDPSETEDIAESVE-DTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVR 388
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1184725755 423 lylATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITG 473
Cdd:cd07793 389 ---AILESIAFRVKQLLETMEKeTSIKISSIRVDGGVSNNDFILQLIADLLG 437
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
12-473 |
8.03e-08 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 54.59 E-value: 8.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 12 YVG-VDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCvvtKKVVQGIDLNQIRGLGFDATC--- 87
Cdd:PTZ00294 3 YIGsIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVY---KCMNEAIKKLREKGPSFKIKAigi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 88 -----SLVVLDKQfhplpvnqEGDSHRNVIMWLDHRAVSQVNRINET--KHSVLQYVGG-VMSVEMQAPKLLWLKENLRE 159
Cdd:PTZ00294 80 tnqreTVVAWDKV--------TGKPLYNAIVWLDTRTYDIVNELTKKygGSNFFQKITGlPISTYFSAFKIRWMLENVPA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 160 IcwDKAGH-----FFDLPDFLSWKATG-------VTARSLCSLVCKWTYSaekgWDDSFWKMIGledfvadnyskIGNQV 227
Cdd:PTZ00294 152 V--KDAVKegtllFGTIDTWLIWNLTGgkshvtdVTNASRTFLMNIKTLK----WDEELLNKFG-----------IPKET 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 228 LP---PGASLGNGLTPEAArdlGLLPGIAVAASLIDAHAGGLGvigadvrgHGLICEGQPVTSRlavicGTSsCH--MGI 302
Cdd:PTZ00294 215 LPeikSSSENFGTISGEAV---PLLEGVPITGCIGDQQAALIG--------HGCFEKGDAKNTY-----GTG-CFllMNT 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 303 SKDPIFVP-GVWGpyfsamVPGFWLNEGGQSVtgklidHMVQGhaafpelqvkATARCQSIYAYLNSHLDLIKKAQPVGF 381
Cdd:PTZ00294 278 GTEIVFSKhGLLT------TVCYQLGPNGPTV------YALEG----------SIAVAGAGVEWLRDNMGLISHPSEIEK 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 382 L------TVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAME-AAGHSISTLFL 454
Cdd:PTZ00294 336 LarsvkdTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIV---RAALEAIALQTNDVIESMEkDAGIELNSLRV 412
|
490
....*....|....*....
gi 1184725755 455 CGGLSKNPLFVQMHADITG 473
Cdd:PTZ00294 413 DGGLTKNKLLMQFQADILG 431
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
11-473 |
9.22e-08 |
|
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: 54.15 E-value: 9.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKNWEPQ--FNHHEQSSEDIWAAccvvTKKVVQGID---LNQIRGLGFD 84
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDlESGRILESVSRPTPAPISSddPGRSEQDPEKILEA----VRNLIDELPreyLSDVTGIGIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 85 AtcslvvldkQFHP-LPVNQEGDSHRNVIMWLDHRAvsqvnriNETKHSVLQYVGGVMSVEMQAP--------KLLWLKE 155
Cdd:cd07777 77 G---------QMHGiVLWDEDGNPVSPLITWQDQRC-------SEEFLGGLSTYGEELLPKSGMRlkpgyglaTLFWLLR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 156 NLREIcwDKAGHFFDLPDFLSWKATGvTARSLCSLVCK--WTY--SAEKGWDDSFWKMIGLEdfvadnySKIGNQVLPPG 231
Cdd:cd07777 141 NGPLP--SKADRAGTIGDYIVARLTG-LPKPVMHPTNAasWGLfdLETGTWNKDLLEALGLP-------VILLPEIVPSG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 232 ASLGNgLTPEAARDLGLLPGI-----AVAASLIDAHagglgvigadvrghglicegqpvtSRLAVICGTSScHMGISKDP 306
Cdd:cd07777 211 EIVGT-LSSALPKGIPVYVALgdnqaSVLGSGLNEE------------------------NDAVLNIGTGA-QLSFLTPK 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 307 IFVPGVWG--PYFSamvpGFWLNeggqSVT----GKLIDHMVQ-----GHAAFPELQVkatarcQSIYAYLNShLDLIKK 375
Cdd:cd07777 265 FELSGSVEirPFFD----GRYLL----VAAslpgGRALAVLVDflrewLRELGGSLSD------DEIWEKLDE-LAESEE 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 376 AQPvgfLTVDlhvwPDFHGNRSplaDLTLKGMVTGLklsqDLDDLAI--LYLATVQAIALGTRFIIEAMEAAGHSISTLF 453
Cdd:cd07777 330 SSD---LSVD----PTFFGERH---DPEGRGSITNI----GESNFTLgnLFRALCRGIAENLHEMLPRLDLDLSGIERIV 395
|
490 500
....*....|....*....|.
gi 1184725755 454 LCGG-LSKNPLFVQMHADITG 473
Cdd:cd07777 396 GSGGaLRKNPVLRRIIEKRFG 416
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
11-132 |
3.77e-07 |
|
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: 52.49 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQ--GIDLNQIRGLGFD---A 85
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAkaGIRASDIAAIGITnqrE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1184725755 86 TCslVVLDKqfhplpvnQEGDSHRNVIMWLDHRAVSQVNRINETKHS 132
Cdd:cd07786 81 TT--VVWDR--------ETGKPVYNAIVWQDRRTADICEELKAEGHE 117
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
12-160 |
6.85e-07 |
|
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: 51.76 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 12 YVG-VDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAAC--CV---VTKKVVQGIDLNQIRGLGFda 85
Cdd:cd07792 2 LVGaIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVyeCIeeaVEKLKALGISPSDIKAIGI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 86 TC---SLVVLDKqfhplpvnQEGDSHRNVIMWLDHRAVSQVNR-INETKHSVLQYV---GGVMSVEMQAPKLLWLKENLR 158
Cdd:cd07792 80 TNqreTTVVWDK--------STGKPLYNAIVWLDTRTSDTVEElSAKTPGGKDHFRkktGLPISTYFSAVKLRWLLDNVP 151
|
..
gi 1184725755 159 EI 160
Cdd:cd07792 152 EV 153
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
15-466 |
2.18e-06 |
|
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: 49.95 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 15 VDVGTGSVRAALVDQSGVLLAFADQPIKN-WEPQFNHHEqsSEDIWAAccvVTKKVVQGIDLNQIRGLGFdaTC---SLV 90
Cdd:cd07772 5 FDIGKTNKKLLLFDENGEVLAERSTPNPEiEEDGYPCED--VEAIWEW---LLDSLAELAKRHRIDAINF--TThgaTFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 91 VLDKQFHP-LPV---NQEGDShrnvimWLDHRAVSQVNRINETKHSVLqyvGGVMSVEMQapkLLWLKENLREIcWDKAG 166
Cdd:cd07772 78 LLDENGELaLPVydyEKPIPD------EINEAYYAERGPFEETGSPPL---PGGLNLGKQ---LYWLKREKPEL-FARAK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 167 HFFDLPDFLSWKATGVTARSLCSLVC--------KWTYS---AEKGWDDSFWKMigledfvadnyskignqvLPPGASLG 235
Cdd:cd07772 145 TILPLPQYWAWRLTGKAASEITSLGChtdlwdfeKNEYSslvKKEGWDKLFPPL------------------RKAWEVLG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 236 NgLTPEAARDLGLLPGIAVAASLIDAHAgglgvigadvrghglicegqpvtSRLAvicgtsscHMGISKDPiFV---PGV 312
Cdd:cd07772 207 P-LRPDLARRTGLPKDIPVGCGIHDSNA-----------------------ALLP--------YLAAGKEP-FTllsTGT 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 313 WgpyFSAMVPGF-----WLNEG-----GQSVTGKLIdhmvqGHAAFP-----ELQVKataRCQSIYAYLNSHLDLIKkaq 377
Cdd:cd07772 254 W---CIAMNPGNdlpltELDLArdclyNLDVFGRPV-----KTARFMggreyERLVE---RIAKSFPQLPSLADLAK--- 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 378 pvgFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATVQAIALgtrfiieamEAAGHSISTLFLCGG 457
Cdd:cd07772 320 ---LLARGTFALPSFAPGGGPFPGSGGRGVLSAFPSAEEAYALAILYLALMTDYAL---------DLLGSGVGRIIVEGG 387
|
....*....
gi 1184725755 458 LSKNPLFVQ 466
Cdd:cd07772 388 FAKNPVFLR 396
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
16-287 |
2.62e-06 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 49.64 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 16 DVGTGSVRAALVDQSGVLLAFADQP------IKNwePQFnhHEQSSEDIW---AACCvvtKKVVQGIDLNQIRGL----- 81
Cdd:PRK10331 8 DCGATNVRAIAVDRQGKIVARASTPnasdiaAEN--SDW--HQWSLDAILqrfADCC---RQINSELTECHIRGItvttf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 82 GFDATcslvvldkqfhplPVNQEGDSHRNVIMWLDHRAVSQVNRI-NETKHSVLQYVGGVMSVEMQAP-KLLWLKENLRE 159
Cdd:PRK10331 81 GVDGA-------------LVDKQGNLLYPIISWKCPRTAAVMENIeRYISAQQLQQISGVGAFSFNTLyKLVWLKENHPQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 160 IcWDKAGHFFDLPDFLSWKATGV--TARSLCSlVCKWTYSAEKGWDDSFWKMIGLEdfvadnyskigNQVLPP----GAS 233
Cdd:PRK10331 148 L-LEQAHAWLFISSLINHRLTGEftTDITMAG-TSQMLDIQQRDFSPEILQATGLS-----------RRLFPRlveaGEQ 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1184725755 234 LGNgLTPEAARDLGLLPGIAVAASlidAHAGGLGVIGAdvrGHGLiceGQPVTS 287
Cdd:PRK10331 215 IGT-LQPSAAALLGLPVGIPVISA---GHDTQFALFGS---GAGQ---NQPVLS 258
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
426-473 |
1.10e-05 |
|
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: 47.87 E-value: 1.10e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1184725755 426 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITG 473
Cdd:cd07786 374 AALESIAYQTRDLLEAMEAdSGIPLKELRVDGGASANDFLMQFQADILG 422
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
426-473 |
1.27e-05 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 47.51 E-value: 1.27e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1184725755 426 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITG 473
Cdd:PRK00047 380 ATLESIAYQTRDVLDAMQAdSGIRLKELRVDGGAVANNFLMQFQADILG 428
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
11-473 |
1.37e-04 |
|
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: 44.44 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 11 YYVGVDVGTGSVRAALV--DQSGVLLA----FADQPIKN-----WEpqFNHheqssedIWAACCVVTKKVVQgiDLNQIR 79
Cdd:cd07771 1 NYLAVDLGASSGRVILGslDGGKLELEeihrFPNRPVEInghlyWD--IDR-------LFDEIKEGLKKAAE--QGGDID 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 80 GLGFDAT-CSLVVLDKQFHPL--PVnqegdSHRN---------VIMWLDHRAV-----SQVNRINetkhSVLQyvggvms 142
Cdd:cd07771 70 SIGIDTWgVDFGLLDKNGELLgnPV-----HYRDprtegmmeeLFEKISKEELyertgIQFQPIN----TLYQ------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 143 vemqapkLLWLKENLREIcWDKAGHFFDLPDFLSWKATG--VTARSLCSlvckwT---YSAEKG-WDDSFWKMIGLEdfv 216
Cdd:cd07771 134 -------LYALKKEGPEL-LERADKLLMLPDLLNYLLTGekVAEYTIAS-----TtqlLDPRTKdWSEELLEKLGLP--- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 217 adnySKIGNQVLPPGASLGNgLTPEAARDLGL--LPGIAVA----ASLIDAhagglgvIGADVRGHGLICegqpvtsrla 290
Cdd:cd07771 198 ----RDLFPPIVPPGTVLGT-LKPEVAEELGLkgIPVIAVAshdtASAVAA-------VPAEDEDAAFIS---------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 291 viCGTSSChMGI-SKDPIFVPgvwgpyfSAMVPGFwLNEGG--------QSVTGkLidHMVQghaafpEL--QVKATARC 359
Cdd:cd07771 256 --SGTWSL-IGVeLDEPVITE-------EAFEAGF-TNEGGadgtirllKNITG-L--WLLQ------ECrrEWEEEGKD 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725755 360 QSiYAYLNShldLIKKAQPVGFLtVDlhvwPD---FhgnRSPladltlKGMV---------TGLKLSQDLDDLA-ILYla 426
Cdd:cd07771 316 YS-YDELVA---LAEEAPPFGAF-ID----PDdprF---LNP------GDMPeairaycreTGQPVPESPGEIArCIY-- 375
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1184725755 427 tvQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITG 473
Cdd:cd07771 376 --ESLALKYAKTIEELEElTGKRIDRIHIVGGGSRNALLCQLTADATG 421
|
|
| |
