|
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 ... |
12-488 |
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: 897.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 12 KVVQ--GIDLNQIRGLGFDATCSLVVLDKQFHPLPVNQEGDSHRNVIMWLDHRAVSQVNRINETKHSVLQYVGGVMSVEM 89
Cdd:cd07782 58 EVLEgaGVDPEQVKGIGFDATCSLVVLDAEGKPVSVSPSGDDERNVILWMDHRAVEEAERINATGHEVLKYVGGKISPEM 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 90 QAPKLLWLKENLREiCWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA----EKGWDDSFWKMIGLEDFVADNYS 165
Cdd:cd07782 138 EPPKLLWLKENLPE-TWAKAGHFFDLPDFLTWKATGSLTRSLCSLVCKWTYLAhegsEGGWDDDFFKEIGLEDLVEDNFA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 166 KIGNQVLPPGASLGNGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIGADVrgHGLICEGQPVTSRLAVICGTSSCHMG 245
Cdd:cd07782 217 KIGSVVLPPGEPVGGGLTAEAAKELGLPEGTPVGVSLIDAHAGGLGTLGADV--GGLPCEADPLTRRLALICGTSSCHMA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 246 ISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNSHLDLIKKAQ--PV 323
Cdd:cd07782 295 VSPEPVFVPGVWGPYYSAMLPGLWLNEGGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNERLEQLAEEKglPL 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 324 GFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS 403
Cdd:cd07782 375 AYLTRDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALLYLATLQALAYGTRHIIEAMNAAGHKIDTIFMCGGLS 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 404 KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKLVE 483
Cdd:cd07782 455 KNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDAMAAMSGPGKVVEPNEELKKYHDRKYEVFLKMYE 534
|
....*
gi 1184725753 484 HQKEY 488
Cdd:cd07782 535 DQREY 539
|
|
| 5C_CHO_kinase |
TIGR01315 |
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ... |
16-488 |
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: 613.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 16 GIDLNQIRGLGFDATCSLVVLDKQFHPLPVNQEGDSHRNVIMWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLL 95
Cdd:TIGR01315 64 KVDPNSVKGIGFDATCSLVVLTHDGEPLPVSKNGGADQNIILWMDHRALAEAEKINATNHNLLRYVGGKMSVEMEIPKVL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 96 WLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTY----SAEKGWDDSFWKMIGLEDFVADNYSKIGNQV 171
Cdd:TIGR01315 144 WLKNNMPPE-LFARCKFFDLTDFLTWRATGKEIRSFCSVVCKWGFvpvdGSNKGWQEDFYETIGLGELVTDNFIRMGGSW 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 172 LPPGASLGNGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIGADVRGHGLICEGQpvtSRLAVICGTSSCHMGISKDPI 251
Cdd:TIGR01315 223 MSPGELVGGGLTAEAAQELGLPAGTAVGSGLIDAHAGWIGTVGAKVAENGDVSQAF---TRLAAVAGTSTCHMAMTKGPV 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 252 FVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNSHLdLIKKAQP----VGFLT 327
Cdd:TIGR01315 300 FVPGVWGPYRDALIPGYWLAEGGQSAAGELMDHMLETHVAYDETVKEAEAAGKNIYDYLNEHL-KEMAAKTnapsISYLV 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 328 VDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPL 407
Cdd:TIGR01315 379 RHFHVYPDLWGNRSPIADPNMRGVIIGLSMDRSKDGLALLYYATMEFIAYGTRQIVEAMNTAGHTIKSIFMSGGQCQNPL 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 408 FVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQ-DKKYYDKKYQVFLKLVEHQK 486
Cdd:TIGR01315 459 LMQLIADACDMPVLIPYVNEAVLHGAAMLGAKAAGTTESLWDAMDRMSKPGKTVWPRGDpAKKLHDRKYEIFLQLARTQQ 538
|
..
gi 1184725753 487 EY 488
Cdd:TIGR01315 539 EY 540
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
16-488 |
0e+00 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 543.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 16 GIDLNQIRGLGFDAT-CSLVVLDKQFHPLPVNQE--GDSHRNVIMWLDHRAVSQVNRINE----TKHSVLQYVGGVMSVE 88
Cdd:COG1069 73 GVDPADVVGIGVDATgCTPVPVDADGTPLALLPEfaENPHAMVILWKDHTAQEEAERINElakaRGEDYLRYVGGIISSE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 89 MQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGW-DDSFWKMIGLE-DFVADnys 165
Cdd:COG1069 153 WFWPKILHLLREDPEV-YEAADSFVELCDWITWQLTGSLKRSRCTAGHKALWHAhEGGYpSEEFFAALDPLlDGLAD--- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 166 KIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIGadvrghglICEGQpvtsrLAVICGTSSCHMG 245
Cdd:COG1069 229 RLGTEIYPLGEPAGT-LTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGG--------VEPGT-----LVKVMGTSTCHML 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 246 ISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNshldliKKAQPVGF 325
Cdd:COG1069 295 VSPEERFVPGICGQVDGSIVPGMWGYEAGQSAVGDIFAWFVRLLVPPLEYEKEAEERGISLHPLLT------EEAAKLPP 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 326 LTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDlaiLYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-K 404
Cdd:COG1069 369 GESGLHALDWFNGNRSPLADQRLKGVILGLTLGTDAED---IYRALVEATAFGTRAIIERFEEEGVPIDEIIACGGIAtK 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 405 NPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKV-GKVVFPRLQDKKYYDKKYQVFLKLVE 483
Cdd:COG1069 446 NPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMAAMGSGfDKVYTPDPENVAVYDALYAEYLQLHD 525
|
....*
gi 1184725753 484 HQKEY 488
Cdd:COG1069 526 YFGRG 530
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
3-481 |
3.69e-144 |
|
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: 423.57 E-value: 3.69e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 3 NSVPEHHNEkvvQGIDLNQIRGLGFDATCSLVVLDKQFHPLPVNQEGDSHRNVIMWLDHRAVSQVNRINETKHSVLQ-YV 81
Cdd:cd07768 56 KCVQKLNIR---EGVDAYEVKGCGVDATCSLAIFDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWINMQCPQQLLdYL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 82 GGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGWDDSFWKMIGLEDfV 160
Cdd:cd07768 133 GGKISPEMGVPKLKYFLDEYSHL-RDKHFHIFDLHDYIAYELTRLYEWNICGLLGKENLDGeESGWSSSFFKNIDPRL-E 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 161 ADNYSKIGNQVLPPGASLGNGLtPEAARDLGLLPGIAVAASLIDAHAGGLGVIGADVRGhglicegqpvtsRLAVICGTS 240
Cdd:cd07768 211 HLTTTKNLPSNVPIGTTSGVAL-PEMAEKMGLHPGTAVVVSCIDAHASWFAVASPHLET------------SLFMIAGTS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 241 SCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELqVKATARCQSIYAYLNshlDLIKKA 320
Cdd:cd07768 278 SCHMYGTTISDRIPGVWGPFDTIIDPDYSVYEAGQSATGKLIEHLFESHPCARKF-DEALKKGADIYQVLE---QTIRQI 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 321 QPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCG 400
Cdd:cd07768 354 EKNNGLSIHILTLDMFFGNRSEFADPRLKGSFIGESLDTSMLNLTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRASG 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 401 GLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFA---SVQEAMAKMSKVGKVVFPRLQD-KKYYDKKYQ 476
Cdd:cd07768 434 GQAKNERLLQLIALVTNVAIIKPKENMMGILGAAVLAKVAAGKKQladSITEADISNDRKSETFEPLAYRlGADYILLYK 513
|
....*
gi 1184725753 477 VFLKL 481
Cdd:cd07768 514 LLCVK 518
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
16-481 |
8.23e-134 |
|
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: 396.52 E-value: 8.23e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 16 GIDLNQIRGLGFDATCSLVVldkqfhplPVNQEGDSHRNVIMWLDHRAVSQVNRINETKHSV----LQYVGGVMSVEMQA 91
Cdd:cd07781 67 GVDPEDVVGIGVDTTSSTVV--------PVDEDGNPLAPAILWMDHRAQEEAAEINETAHPAleyyLAYYGGVYSSEWMW 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 92 PKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEDfvADNYSKIGNQ 170
Cdd:cd07781 139 PKALWLKRNAPEV-YDAAYTIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGgPPREFLAALDPGL--LKLREKLPGE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 171 VLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDP 250
Cdd:cd07781 216 VVPVGEPAG-TLTAEAAERLGLPAGIPVAQGGIDAHMGAIGA--------GVVEPGT-----LALIMGTSTCHLMVSPKP 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 251 IFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIdhmvqghAAFPELQVKATA-RCQSIYAYLNshlDLIKKAQPV--GFLT 327
Cdd:cd07781 282 VDIPGICGPVPDAVVPGLYGLEAGQSAVGDIF-------AWFVRLFVPPAEeRGDSIYALLS---EEAAKLPPGesGLVA 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 328 VDlhvWpdFHGNRSPLADLTLKGMVTGLKLSQDLddlAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNP 406
Cdd:cd07781 352 LD---W--FNGNRTPLVDPRLRGAIVGLTLGTTP---AHIYRALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAeKNP 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184725753 407 LFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKL 481
Cdd:cd07781 424 LWMQIYADVLGRPIKVPKSDQAPALGAAILAAVAAGVYADIEEAADAMVRVDRVYEPDPENHAVYEELYALYKEL 498
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
15-492 |
2.52e-82 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 265.17 E-value: 2.52e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 15 QGIDLNQIRGLGFDAT-CSLVVLDKQFHPLPVNQEGDSHRN--VIMWLDHRAVSQVNRINETKHS-----VLQYVGGVMS 86
Cdd:PRK04123 73 AGVDPAAVVGIGVDFTgSTPAPVDADGTPLALLPEFAENPHamVKLWKDHTAQEEAEEINRLAHErgeadLSRYIGGIYS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 87 VEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTA-----RSLCSLVCKWTYSAEKG--WDDSFWKMI--GLE 157
Cdd:PRK04123 153 SEWFWAKILHVLREDPAV-YEAAASWVEACDWVVALLTGTTDpqdivRSRCAAGHKALWHESWGglPSADFFDALdpLLA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 158 DFVADnysKIGNQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGglgVIGADVRGHGLicegqpvtsrLAVIc 237
Cdd:PRK04123 232 RGLRD---KLFTETWTAGEPAG-TLTAEWAQRLGLPEGVAVSVGAFDAHMG---AVGAGAEPGTL----------VKVM- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 238 GTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQgHAAFPELQVKATARCQSIYAYLNshldli 317
Cdd:PRK04123 294 GTSTCDILLADKQRAVPGICGQVDGSIVPGLIGYEAGQSAVGDIFAWFAR-LLVPPEYKDEAEARGKQLLELLT------ 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 318 KKA--QPVG---FLTVDlhvWpdFHGNRSPLADLTLKGMVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHS 392
Cdd:PRK04123 367 EAAakQPPGehgLVALD---W--FNGRRTPLADQRLKGVITGLTLGTDAPDI---YRALIEATAFGTRAIMECFEDQGVP 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 393 ISTLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKM-SKVGKVVFPRLQDKKY 470
Cdd:PRK04123 439 VEEVIAAGGIArKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEAQQAMaSPVEKTYQPDPENVAR 518
|
490 500
....*....|....*....|...
gi 1184725753 471 YDKKYQVFLKLVE-HQKEYLAIM 492
Cdd:PRK04123 519 YEQLYQEYKQLHDyFGRGGNAVM 541
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
16-487 |
1.28e-81 |
|
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: 261.69 E-value: 1.28e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 16 GIDLNQIRGLGFDAT-CSLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINET--KHSVLQYVGGVMSVEMQAP 92
Cdd:COG1070 65 GVDPEEIAAIGVSGQmHGLVLLDADGEPL---------RPAILWNDTRAAAEAAELREElgEEALYEITGNPLHPGFTAP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 93 KLLWLKENLREIcWDKAGHFFDLPDFLSWKATG--VTARSLCSlvckWT--YSAEKG-WDDSFWKMIGL-EDFVAdnysk 166
Cdd:COG1070 136 KLLWLKENEPEI-FARIAKVLLPKDYLRYRLTGefVTDYSDAS----GTglLDVRTRdWSDELLEALGIdRELLP----- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 167 ignQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGI 246
Cdd:COG1070 206 ---ELVPPGEVAG-TLTAEAAAETGLPAGTPVVAGAGDNAAAALGA--------GAVEPGD-----AAVSLGTSGVVFVV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 247 SKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQghaafpelqvKATARCQSIYAYLNshlDLIKKAqPVG-- 324
Cdd:COG1070 269 SDKPLPDPEGRVHTFCHAVPGRWLPMGATNNGGSALRWFRD----------LFADGELDDYEELN---ALAAEV-PPGad 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 325 ---FLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGG 401
Cdd:COG1070 335 gllFL-------PYLSGERTPHWDPNARGAFFGLTLSHTRAHL---ARAVLEGVAFALRDGLEALEEAGVKIDRIRATGG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 402 LSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKL 481
Cdd:COG1070 405 GARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMVRVGETIEPDPENVAAYDELYERYREL 484
|
....*.
gi 1184725753 482 VEHQKE 487
Cdd:COG1070 485 YPALKP 490
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
21-441 |
7.12e-68 |
|
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: 227.29 E-value: 7.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 21 QIRGLGFDATCSLVVLDKQ-----FHPLPVNQE-GDSHRNVIMWLDHRAVSQVNRINE-TKHSVLQYVGGVMSVEMQAPK 93
Cdd:cd07778 69 IVSGIGVSATCSMVVMQRDsdtsyLVPYNVIHEkSNPDQDIIFWMDHRASEETQWLNNiLPDDILDYLGGGFIPEMAIPK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 94 LLWLKENLREICWDKAgHFFDLPDFLSWKatgvtarsLCSLVCKW--TYSAE------------KGWDDSFWKMIGLEDF 159
Cdd:cd07778 149 LKYLIDLIKEDTFKKL-EVFDLHDWISYM--------LATNLGHSniVPVNAppsigigidgslKGWSKDFYSKLKISTK 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 160 VAD--NYSKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIgadvrghgliCEGQPVTSRLAVIC 237
Cdd:cd07778 220 VCNvgNTFKEAPPLPYAGIPIGK-VNVILASYLGIDKSTVVGHGCIDCYAGWFSTF----------AAAKTLDTTLFMVA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 238 GTSSCHMGISKDPI--FVPGVWGPyFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATarcqSIYAYLNSHLD 315
Cdd:cd07778 289 GTSTCFLYATSSSQvgPIPGIWGP-FDQLLKNYSVYEGGQSATGKLIEKLFNSHPAIIELLKSDA----NFFETVEEKID 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 316 LI--KKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSI 393
Cdd:cd07778 364 KYerLLGQSIHYLTRHMFFYGDYLGNRTPYNDPNMSGSFIGESTDSSLTDLVLKYILILEFLAFQTKLIIDNFQKEKIII 443
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1184725753 394 STLFLCGGLSKNPLFVQMHADITGMPVV---LSQEVESVLVGAAVLGACAS 441
Cdd:cd07778 444 QKVVISGSQAKNARLLQLLSTVLSKIHIivpLSDSKYAVVKGAALLGKAAF 494
|
|
| L-ribulokinase |
TIGR01234 |
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely ... |
16-489 |
4.31e-62 |
|
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely related protein subfamily outside the scope of this model includes ribitol kinase from E. coli. [Energy metabolism, Sugars]
Pssm-ID: 130301 [Multi-domain] Cd Length: 536 Bit Score: 211.71 E-value: 4.31e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 16 GIDLNQIRGLGFDAT-CSLVVLDKQFHPLPVNQE--GDSHRNVIMWLDHRAVSQVNRINETKHS----VLQYVGGVMSVE 88
Cdd:TIGR01234 77 GVDPADVVGIGVDFTaCTPAPIDSDGNPLCLLPEfaENPHAYFKLWKHHAAQEEADRINRLAHApgevDLSRYGGIISSE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 89 MQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKGW-DDSFWKMI--GLEDFVADNYS 165
Cdd:TIGR01234 157 WFWAKILQITEEDPAI-YQAADRWIELADWIVAQLSGDIRRGRCTAGYKALWHESWGYpSASFFDELnpILNRHLPDKLF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 166 K-IGNQVLPPGAslgngLTPEAARDLGLLPGIAVAASLIDAHaggLGVIGADVrghgliceGQPvtSRLAVICGTSSCHM 244
Cdd:TIGR01234 236 TdIWTAGEPAGT-----LTPEWAQRTGLPEGVVVAVGNFDAH---VGAVAAGI--------AQP--GALVKIMGTSTCHV 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 245 GISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQgHAAFPELQVKATARCQSiyayLNSHLDLIKKAQPV- 323
Cdd:TIGR01234 298 LIGDKQRAVPGMCGVVDGGIVPGFIGYEAGQSAVGDIFAWFGK-VCVPPELKTEANASQKQ----LHEALSEAAAKQPSg 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 324 --GFLTVDlhvWpdFHGNRSPLADLTLKGMVTGLKLSQDLDDlaiLYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGG 401
Cdd:TIGR01234 373 ehGLVALD---W--FNGNRSPLVDQRLKGVITGLTLATDAPL---LYRALIEATAFGTRMIMETFTDSGVPVEELMAAGG 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 402 LS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVF-PRLQDKKYYDKKYQVFL 479
Cdd:TIGR01234 445 IArKNPVIMQIYADVTNRPLQIVASDQAPALGAAIFAAVAAGVYADIPSAQAKMGSAVEKTLtPCSENAQRYEQLYARYQ 524
|
490
....*....|
gi 1184725753 480 KLVEHQKEYL 489
Cdd:TIGR01234 525 ELAMSFGQYN 534
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
233-440 |
3.50e-61 |
|
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.
Pssm-ID: 426979 [Multi-domain] Cd Length: 197 Bit Score: 198.70 E-value: 3.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 233 LAVICGTSSCHMGISKDP-IFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQvkATARCQSIYAYLN 311
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPvLSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELR--DAGNVESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 312 SHLDLikkaqpvgfLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLddlAILYLATVQAIALGTRFIIEAMEA-AG 390
Cdd:pfam02782 79 LAAVA---------PAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTL---AHLYRAILESLALQLRQILEALTKqEG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1184725753 391 HSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACA 440
Cdd:pfam02782 147 HPIDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
16-479 |
1.20e-59 |
|
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: 203.91 E-value: 1.20e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 16 GIDLNQIRGLGFDAT-CSLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINET---KHSVLQYVGGVMSVEMQA 91
Cdd:cd07805 64 GIDPSDIAAIAFSGQmQGVVPVDKDGNPL---------RNAIIWSDTRAAEEAEEIAGGlggIEGYRLGGGNPPSGKDPL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 92 PKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEDfvadnySKIgNQ 170
Cdd:cd07805 135 AKILWLKENEPEI-YAKTHKFLDAKDYLNFRLTGRAATDPSTASTTGLMDLRKRrWSEELLRAAGIDP------DKL-PE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 171 VLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGViGADVRGHGLICegqpvtsrlaviCGTSS---CHmgiS 247
Cdd:cd07805 207 LVPSTEVVG-ELTPEAAAELGLPAGTPVVGGGGDAAAAALGA-GAVEEGDAHIY------------LGTSGwvaAH---V 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 248 KDPIFVPGvwGPYFS--AMVPGFWLNEGGQSVTGKLIDHMVQgHAAFPELQVKatarcqSIYAYLNshlDLIKKAQP--- 322
Cdd:cd07805 270 PKPKTDPD--HGIFTlaSADPGRYLLAAEQETAGGALEWARD-NLGGDEDLGA------DDYELLD---ELAAEAPPgsn 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 323 -VGFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEAAGHSISTLFLCGG 401
Cdd:cd07805 338 gLLFL-------PWLNGERSPVEDPNARGAFIGLSLEHTRADLA---RAVLEGVAFNLRWLLEALEKLTRKIDELRLVGG 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184725753 402 LSKNPLFVQMHADITGMPV-VLSQEVESVLVGAAVLGACASGDFASVQEAmAKMSKVGKVVFPRLQDKKYYDKKYQVFL 479
Cdd:cd07805 408 GARSDLWCQILADVLGRPVeVPENPQEAGALGAALLAAVGLGLLKSFDEA-KALVKVEKVFEPDPENRARYDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
15-481 |
2.92e-59 |
|
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: 202.77 E-value: 2.92e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 15 QGIDLNQIRGLGFDA-TCSLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINET-KHSVLQYVGGVMSVEMQAP 92
Cdd:cd07808 63 AGISPSDIAAIGLTGqMHGLVLLDKNGRPL---------RPAILWNDQRSAAECEELEARlGDEILIITGNPPLPGFTLP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 93 KLLWLKENLREIcWDKAGHFFdLP-DFLSWKATGVTAR-------SLCslvckwtYSAEKG-WDDSFWKMIGLEdfvadn 163
Cdd:cd07808 134 KLLWLKENEPEI-FARIRKIL-LPkDYLRYRLTGELATdpsdasgTLL-------FDVEKReWSEELLEALGLD------ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 164 yskigNQVLPP---GASLGNGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPV----TSrlAVI 236
Cdd:cd07808 199 -----PSILPPiveSTEIVGTLTPEAAEELGLPEGTPVVAGAGDNAAAALGA--------GVVEPGDALislgTS--GVV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 237 CGTSSCHMGISKDPIF-----VPGVW---GPYFSAmvpGF---WLNE--GGQSVTGKLIDHMVQGHAAfpelqvkatarc 303
Cdd:cd07808 264 FAPTDKPVPDPKGRLHtfphaVPGKWyamGVTLSA---GLslrWLRDlfGPDRESFDELDAEAAKVPP------------ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 304 qsiyaylnshldlikKAQPVGFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRFII 383
Cdd:cd07808 329 ---------------GSEGLLFL-------PYLSGERTPYWDPNARGSFFGLSLSHTRAHLA---RAVLEGVAFSLRDSL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 384 EAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFP 463
Cdd:cd07808 384 EVLKELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACIKIEKTIEP 463
|
490
....*....|....*...
gi 1184725753 464 RLQDKKYYDKKYQVFLKL 481
Cdd:cd07808 464 DPERHEAYDELYARYREL 481
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
16-471 |
4.14e-55 |
|
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: 190.42 E-value: 4.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 16 GIDLNQIRGLGFDAT-CSLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVsqvnrinetkhsvlqyvggvmsvemqapkl 94
Cdd:cd07779 64 GVDPEDIAAIGLTSQrSTFVPVDEDGRPL---------RPAISWQDKRTA------------------------------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 95 lwlkenlreicwdkagHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEdfvADNYSKIgnqvLP 173
Cdd:cd07779 105 ----------------KFLTVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRdWSDDLLDAFGID---RDKLPEL----VP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 174 PGASLGNgLTPEAARDLGLLPGIAVAASlidAHAGGLGVIGADVRGHGLICegqpvtsrlaVICGTSSCHMGISKDPIFV 253
Cdd:cd07779 162 PGTVIGT-LTKEAAEETGLPEGTPVVAG---GGDQQCAALGAGVLEPGTAS----------LSLGTAAVVIAVSDKPVED 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 254 PGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQghaAFPELQVKATARCQSIYAYLNSHLDLIkkaqPVGFLtvDLHVW 333
Cdd:cd07779 228 PERRIPCNPSAVPGKWVLEGSINTGGSAVRWFRD---EFGQDEVAEKELGVSPYELLNEEAAKS----PPGSD--GLLFL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 334 PDFHGNRSPLADLTLKGMVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHA 413
Cdd:cd07779 299 PYLAGAGTPYWNPEARGAFIGLTLSHTRAHL---ARAILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIA 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1184725753 414 DITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYY 471
Cdd:cd07779 376 DVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAMVRVTDTFEPDPENVAIY 433
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
11-438 |
7.41e-48 |
|
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: 170.87 E-value: 7.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 11 EKVVQGIDLNQIRGLGFDATC-SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINETKHSVLQYVGGVMSVEM 89
Cdd:cd07783 57 RELPAELRPRRVVAIAVDGTSgTLVLVDREGEPL---------RPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSPSS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 90 QAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEdfvadnySKIG 168
Cdd:cd07783 128 SLAKLLWLKRHEPEV-LAKTAKFLHQADWLAGRLTGDRGVTDYNNALKLGYDPETGrWPSWLLALLGIP-------PDLL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 169 NQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVTSrlaviCGTSSCHMGISK 248
Cdd:cd07783 200 PRVVAPGTVIGT-LTAEAAEELGLPAGTPVVAGTTDSIAAFLAS--------GAVRPGDAVTS-----LGTTLVLKLLSD 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 249 DPIFVPGVwGPYFSAMVPGFWLNEGGQSVTGKLIDHmvqghaAFPELQVKAtarcqsiyaylnshldLIKKAQPVGflTV 328
Cdd:cd07783 266 KRVPDPGG-GVYSHRHGDGYWLVGGASNTGGAVLRW------FFSDDELAE----------------LSAQADPPG--PS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 329 DLHVWP-DFHGNRSPLADLTLKGMVTGLKlsqdlDDLAILYLATVQAIALGTRFIIEAMEAAGHS-ISTLFLCGGLSKNP 406
Cdd:cd07783 321 GLIYYPlPLRGERFPFWDPDARGFLLPRP-----HDRAEFLRALLEGIAFIERLGYERLEELGAPpVEEVRTAGGGARND 395
|
410 420 430
....*....|....*....|....*....|..
gi 1184725753 407 LFVQMHADITGMPVVLSQEVESVLvGAAVLGA 438
Cdd:cd07783 396 LWNQIRADVLGVPVVIAEEEEAAL-GAALLAA 426
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
11-442 |
5.09e-47 |
|
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: 168.92 E-value: 5.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 11 EKVVQGIDLNQIRGLGFdAT--CSLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINE--TKHSVLQYVGGVMS 86
Cdd:cd07773 57 REAAAQAGPDPIAAISV-SSqgESGVPVDRDGEPL---------GPAIVWFDPRGKEEAEELAEriGAEELYRITGLPPS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 87 VEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLcSLVCKWTY--SAEKGWDDSfwkmigLEDFVADNY 164
Cdd:cd07773 127 PMYSLAKLLWLREHEPEI-FAKAAKWLSVADYIAYRLTGEPVTDY-SLASRTMLfdIRKRTWSEE------LLEAAGIDA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 165 SKIGnQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHM 244
Cdd:cd07773 199 SLLP-ELVPSGTVIGT-VTPEAAEELGLPAGTPVVVGGHDHLCAALGA--------GVIEPGD-----VLDSTGTAEALL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 245 GISKDPIFVPGVWGPYFS---AMVPGFWLNEGGQSvTGKLIDHMVQGHAAFPELQVKATARCQSIYAylnshldlikKAQ 321
Cdd:cd07773 264 AVVDEPPLDEMLAEGGLSyghHVPGGYYYLAGSLP-GGALLEWFRDLFGGDESDLAAADELAEAAPP----------GPT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 322 PVGFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDDlaiLYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGG 401
Cdd:cd07773 333 GLLFL-------PHLSGSGTPDFDPDARGAFLGLTLGTTRAD---LLRAILEGLAFELRLNLEALEKAGIPIDEIRAVGG 402
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1184725753 402 LSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 442
Cdd:cd07773 403 GARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
16-442 |
1.86e-45 |
|
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: 165.01 E-value: 1.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 16 GIDLNQIRGLGfdatCS-----LVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINETKHS--VLQYVGGVMSVE 88
Cdd:cd07804 64 GISPKEIAAIG----VSglvpaLVPVDENGKPL---------RPAILYGDRRATEEIEWLNENIGEdrIFEITGNPLDSQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 89 MQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATG--VTARSLCSLvckwtYS-----AEKGWDDSFWKMIGLEdfva 161
Cdd:cd07804 131 SVGPKLLWIKRNEPEV-FKKTRKFLGAYDYIVYKLTGeyVIDYSSAGN-----EGglfdiRKRTWDEELLEALGID---- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 162 dnySKIGNQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSS 241
Cdd:cd07804 201 ---PDLLPELVPSTEIVG-EVTKEAAEETGLAEGTPVVAGTVDAAASALSA--------GVVEPGD-----LLLMLGTAG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 242 CHMGISKDPIFVPGVWGPYFSamVPGFWLNEGGQSVTGKLIDHMVQGHAafPELQVKATARCQSIYAYLNshldliKKAQ 321
Cdd:cd07804 264 DIGVVTDKLPTDPRLWLDYHD--IPGTYVLNGGMATSGSLLRWFRDEFA--GEEVEAEKSGGDSAYDLLD------EEAE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 322 --PVGfltVD-LHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFL 398
Cdd:cd07804 334 kiPPG---SDgLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHL---YRALLEGVAYGLRHHLEVIREAGLPIKRLVA 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1184725753 399 CGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 442
Cdd:cd07804 408 VGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
12-482 |
3.23e-45 |
|
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: 164.65 E-value: 3.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 12 KVVQGIDLNQIRGLGFDATC-SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRI--NETKHSVLQYVGGVMSVE 88
Cdd:cd07770 58 EVLAKLGGGEVDAIGFSSAMhSLLGVDEDGEPL---------TPVITWADTRAAEEAERLrkEGDGSELYRRTGCPIHPM 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 89 MQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATG--VTARSLCSlvckWT---YSAEKGWDDSFWKMIGLEdfvADN 163
Cdd:cd07770 129 YPLAKLLWLKEERPEL-FAKAAKFVSIKEYLLYRLTGelVTDYSTAS----GTgllNIHTLDWDEEALELLGID---EEQ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 164 YSKIgnqvLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDahaGGLGVIGAdvrghGLICEGqpvtsRLAVICGTSsch 243
Cdd:cd07770 201 LPEL----VDPTEVLP-GLKPEFAERLGLLAGTPVVLGASD---GALANLGS-----GALDPG-----RAALTVGTS--- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 244 mG----ISKDPIFVP--GVWgPYFSAmvPGFWL-----NEGGqSVTGKLIDHMVQGHAAFPELQVKATArcqsiyAYLNS 312
Cdd:cd07770 260 -GairvVSDRPVLDPpgRLW-CYRLD--ENRWLvggaiNNGG-NVLDWLRDTLLLSGDDYEELDKLAEA------VPPGS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 313 HlDLIkkaqpvgFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHS 392
Cdd:cd07770 329 H-GLI-------FL-------PYLAGERAPGWNPDARGAFFGLTLNHTRADI---LRAVLEGVAFNLKSIYEALEELAGP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 393 ISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEamAKMSKVGKVVFPRLQDKKYYD 472
Cdd:cd07770 391 VKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSLEA--DELVKIGKVVEPDPENHAIYA 468
|
490
....*....|
gi 1184725753 473 KKYQVFLKLV 482
Cdd:cd07770 469 ELYERFKKLY 478
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
16-437 |
2.57e-43 |
|
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: 157.73 E-value: 2.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 16 GIDLNQIRGLGFDAT-CSLVVLDKQFHPLpvnqegdshRNVIMWLDHRAvsqvnrinetkhsvlqyvggvmsvemqapkl 94
Cdd:cd00366 64 GIDPSDIAAIGISGQmPGVVLVDADGNPL---------RPAIIWLDRRA------------------------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 95 lwlkenlreicwdkagHFFDLPDFLSWKATGVTA--RSLCSLVCKWTYsAEKGWDDSFWKMIGL-EDFVADnyskignqV 171
Cdd:cd00366 104 ----------------KFLQPNDYIVFRLTGEFAidYSNASGTGLYDI-KTGDWSEELLDALGIpREKLPP--------I 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 172 LPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVtsrlaVICGTSSCHMGISKDPI 251
Cdd:cd00366 159 VESGEVVG-RVTPEAAEETGLPAGTPVVAGGGDTAAAALGA--------GVVEPGDAV-----DSTGTSSVLSVCTDEPV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 252 FVPGVWGPYFSAmVPGFWLNEGGQSVTGKLIDHMVQghaafpelqvkATARCQSIYAYLNSHLDLIKKAQP----VGFLt 327
Cdd:cd00366 225 PPDPRLLNRCHV-VPGLWLLEGAINTGGASLRWFRD-----------EFGEEEDSDAEYEGLDELAAEVPPgsdgLIFL- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 328 vdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPL 407
Cdd:cd00366 292 ------PYLSGERSPIWDPAARGVFFGLTLSHTRAHL---IRAVLEGVAYALRDNLEILEELGVKIKEIRVTGGGAKSRL 362
|
410 420 430
....*....|....*....|....*....|
gi 1184725753 408 FVQMHADITGMPVVLSQEVESVLVGAAVLG 437
Cdd:cd00366 363 WNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
16-442 |
1.42e-41 |
|
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: 154.25 E-value: 1.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 16 GIDLNQIRGLGFDAT-CSLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINE--TKHSVLQYVGGVMSVEMQAP 92
Cdd:cd07802 64 GVDPSDIAGVGVTGHgNGLYLVDKDGKPV---------RNAILSNDSRAADIVDRWEEdgTLEKVYPLTGQPLWPGQPVA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 93 KLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVtarslcsLVCKWT-YSA------EKGWDDSFWKMIGLEDFvadnYS 165
Cdd:cd07802 135 LLRWLKENEPER-YDRIRTVLFCKDWIRYRLTGE-------ISTDYTdAGSslldldTGEYDDELLDLLGIEEL----KD 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 166 KIGnQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMG 245
Cdd:cd07802 203 KLP-PLVPSTEIAG-RVTAEAAALTGLPEGTPVAAGAFDVVASALGA--------GAVDEGQ-----LCVILGTWSINEV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 246 ISKDPIFVPGVWGpYFSAMVPGFWLNEGGQSVTGKLIDHMVQghaafpELQVKATARCQSIYAYLNshlDLIKKAQPVG- 324
Cdd:cd07802 268 VTDEPVVPDSVGS-NSLHADPGLYLIVEASPTSASNLDWFLD------TLLGEEKEAGGSDYDELD---ELIAAVPPGSs 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 325 ---FLtvdlhvwPDFHGNRsplADLTLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEAAGHsISTLFLCGG 401
Cdd:cd07802 338 gviFL-------PYLYGSG---ANPNARGGFFGLTAWHTRAHLL---RAVYEGIAFSHRDHLERLLVARK-PETIRLTGG 403
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1184725753 402 LSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 442
Cdd:cd07802 404 GARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
16-442 |
4.75e-32 |
|
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: 127.67 E-value: 4.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 16 GIDLNQIRGLGFDATC-SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINET-KHSVLQYVGGVMSVEMQAPK 93
Cdd:cd07809 65 GAELRDVAAIGISGQMhGLVALDADGKVL---------RPAKLWCDTRTAPEAEELTEAlGGKKCLLVGLNIPARFTASK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 94 LLWLKENLREIcWDKAgHFFDLP-DFLSWKATG--VTARSLCSLVckwtysaekGWDDSF-----WKMIGLEDFVADNYS 165
Cdd:cd07809 136 LLWLKENEPEH-YARI-AKILLPhDYLNWKLTGekVTGLGDASGT---------FPIDPRtrdydAELLAAIDPSRDLRD 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 166 KIGnQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVTSrlaviCGTSSCHMG 245
Cdd:cd07809 205 LLP-EVLPAGEVAG-RLTPEGAEELGLPAGIPVAPGEGDNMTGALGT--------GVVNPGTVAVS-----LGTSGTAYG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 246 ISKDPIFVPgvwgpyfSAMVPGF--------WLNEG---GQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYlnshl 314
Cdd:cd07809 270 VSDKPVSDP-------HGRVATFcdstggmlPLINTtncLTAWTELFRELLGVSYEELDELAAQAPPGAGGLLLL----- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 315 dlikkaqpvgfltvdlhvwPDFHGNRSP-LADLTlkGMVTGLKLSQdlDDLAILYLATVQAIALGTRFIIEAMEAAGHSI 393
Cdd:cd07809 338 -------------------PFLNGERTPnLPHGR--ASLVGLTLSN--FTRANLARAALEGATFGLRYGLDILRELGVEI 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1184725753 394 STLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 442
Cdd:cd07809 395 DEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
16-442 |
3.49e-28 |
|
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: 116.55 E-value: 3.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 16 GIDLNQIRGLgfdATCS----LVVLDKQFHPL---PvnqegdshrNVimwlDHRAVSQVNRINETKHSVLQYVGGVMSVE 88
Cdd:cd07798 66 GISPEDISAV---SSTSqregIVFLDKDGRELyagP---------NI----DARGVEEAAEIDDEFGEEIYTTTGHWPTE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 89 MQAP-KLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVtarslcsLVCKWTYSAEKG--------WDDSFWKMIGLEDf 159
Cdd:cd07798 130 LFPAaRLLWFKENRPEI-FERIATVLSISDWIGYRLTGE-------LVSEPSQASETQlfdikkreWSQELLEALGLPP- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 160 vadnysKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGT 239
Cdd:cd07798 201 ------EILPEIVPSGTVLGT-VSEEAARELGLPEGTPVVVGGADTQCALLGS--------GAIEPGD-----IGIVAGT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 240 SSCHMGISKDPIFVP--GVW-GPYfsaMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQvkatarcqsiYAYLNSHLDL 316
Cdd:cd07798 261 TTPVQMVTDEPIIDPerRLWtGCH---LVPGKWVLESNAGVTGLNYQWLKELLYGDPEDS----------YEVLEEEASE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 317 IKKAQP--VGFLTVDLhvwpdFHGNRSPLADLTLKGMVTGLKLSQDLDDLAIlylATVQAIALGTRFIIEAMEA-AGHSI 393
Cdd:cd07798 328 IPPGANgvLAFLGPQI-----FDARLSGLKNGGFLFPTPLSASELTRGDFAR---AILENIAFAIRANLEQLEEvSGREI 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1184725753 394 STLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 442
Cdd:cd07798 400 PYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
44-442 |
2.94e-24 |
|
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: 105.01 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 44 PVNQEGDSHRNVIMWLDHRAVSQVNRINE--TKHSVLQYVGGVMSVEMQAPKLLWLKENLREICwDKAGHFFDLPDFLSW 121
Cdd:cd24121 84 LVDEDGRPVRDAILWLDGRAADIVERWQAdgIAEAVFEITGTGLFPGSQAAQLAWLKENEPERL-ERARTALHCKDWLFY 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 122 KATGVTA--RSLCSLVCkwtYSAEKG-WDDSFWKMIGLEDFVAdnyskignqVLPP-GASLGNG--LTPEAARDLGLLPG 195
Cdd:cd24121 163 KLTGEIAtdPSDASLTF---LDFRTRqYDDEVLDLLGLEELRH---------LLPPiRPGTEVIgpLTPEAAAATGLPAG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 196 IAVAASLIDAHAGGLGViGADVRGHGLicegqpvtsrlaVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGq 275
Cdd:cd24121 231 TPVVLGPFDVVATALGS-GAIEPGDAC------------SILGTTGVHEVVVDEPDLEPEGVGYTICLGVPGRWLRAMA- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 276 SVTGKL-IDHMVQ--GHAAFPELQVKATarcqSIYAYLNSHLdlikKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMV 352
Cdd:cd24121 297 NMAGTPnLDWFLRelGEVLKEGAEPAGS----DLFQDLEELA----ASSPPGAEGVLYHPYLSPAGERAPFVNPNARAQF 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 353 TGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMeaaGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVG 432
Cdd:cd24121 369 TGLSLEHTRADLL---RAVYEGVALAMRDCYEHM---GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARG 442
|
410
....*....|
gi 1184725753 433 AAVLGACASG 442
Cdd:cd24121 443 AAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
60-476 |
5.45e-22 |
|
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466794 [Multi-domain] Cd Length: 492 Bit Score: 98.56 E-value: 5.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 60 DHRAVSQVNRINETKHSVLQ--YVGGVMSVEMQA-PKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTAR--SLCSL 134
Cdd:cd07775 101 DARAAEEVSELKELYNTLEEevYRISGQTFALGAiPRLLWLKNNRPEI-YRKAAKITMLSDWIAYKLSGELAVepSNGST 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 135 VCKWTySAEKGWDDSFWKMIGLEDFvadnyskIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVig 214
Cdd:cd07775 180 TGLFD-LKTRDWDPEILEMAGLKAD-------ILPPVVESGTVIGK-VTKEAAEETGLKEGTPVVVGGGDVQLGCLGL-- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 215 advrghGLICEGQpvtsrlAVICGTSSCHMGI-SKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQghAAFP 293
Cdd:cd07775 249 ------GVVRPGQ------TAVLGGSFWQQEVnTAAPVTDPAMNIRVNCHVIPDMWQAEGISFFPGLVMRWFRD--AFCA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 294 ELQVKATARCQSIYAYLNshldliKKAQ--PVGF-----LTVDL-------HVWPDFhgnrspladltlkgmvTGLKLSQ 359
Cdd:cd07775 315 EEKEIAERLGIDAYDLLE------EMAKdvPPGSygimpIFSDVmnyknwrHAAPSF----------------LNLDIDP 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 360 DLDDLAILYLATVQAIALGTRFIIEAMEAA-GHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGA 438
Cdd:cd07775 373 EKCNKATFFRAIMENAAIVSAGNLERIAEFsGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAG 452
|
410 420 430
....*....|....*....|....*....|....*...
gi 1184725753 439 CASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQ 476
Cdd:cd07775 453 VGAGIYSSLEEAVESLVKWEREYLPNPENHEVYQDLYE 490
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
334-483 |
4.20e-16 |
|
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466789 [Multi-domain] Cd Length: 486 Bit Score: 80.59 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 334 PDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMH 412
Cdd:cd07769 341 PAFSGLGAPYWDPDARGAIVGLTRGTTKAHIV---RAALESIAYQTRDVLEAMEKdSGIKLKELRVDGGATANNFLMQFQ 417
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184725753 413 ADITGMPVVLSQEVESVLVGAAVLGACASGdFASVQEAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 483
Cdd:cd07769 418 ADILGVPVVRPKVAETTALGAAYLAGLAVG-FWKDLDELASLWQVDKRFEPSMDEEE-RERLYRGWKKAVE 486
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
349-483 |
1.66e-15 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 78.95 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 349 KGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVE 427
Cdd:COG0554 359 RGAIFGLTRGTTRAHIA---RAALESIAYQTRDVLDAMEAdSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTE 435
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1184725753 428 SVLVGAAVLGACASGDFASVQEaMAKMSKVGKVVFPRLqDKKYYDKKYQVFLKLVE 483
Cdd:COG0554 436 TTALGAAYLAGLAVGFWKSLEE-LAALWKVDRRFEPQM-DEEERERLYAGWKKAVE 489
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
370-483 |
2.04e-15 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466802 [Multi-domain] Cd Length: 499 Bit Score: 78.33 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 370 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 448
Cdd:cd07792 384 AALEAVCFQTREILDAMNKdSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLD 463
|
90 100 110
....*....|....*....|....*....|....*
gi 1184725753 449 EAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 483
Cdd:cd07792 464 ELKSLNEGGRTVFEPQISEEE-RERRYKRWKKAVE 497
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
370-483 |
1.26e-14 |
|
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases
Pssm-ID: 198361 [Multi-domain] Cd Length: 486 Bit Score: 75.99 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 370 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 448
Cdd:cd07786 374 AALESIAYQTRDLLEAMEAdSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLD 453
|
90 100 110
....*....|....*....|....*....|....*
gi 1184725753 449 EAmAKMSKVGKVVFPRLqDKKYYDKKYQVFLKLVE 483
Cdd:cd07786 454 EL-AKLWQVDRRFEPSM-SEEEREALYAGWKKAVK 486
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
370-470 |
1.76e-14 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 75.78 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 370 ATVQAIALGTRFIIEAME-AAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 448
Cdd:PTZ00294 383 AALEAIALQTNDVIESMEkDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLE 462
|
90 100
....*....|....*....|..
gi 1184725753 449 EAMAKMSKVGKVVFPRLQDKKY 470
Cdd:PTZ00294 463 EVKKLIRRSNSTFSPQMSAEER 484
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
16-211 |
1.10e-13 |
|
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: 70.83 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 16 GIDLNQIRGLGFDATC-SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINE--TKHSVLQYVGGVMSVEMQAP 92
Cdd:pfam00370 64 GISLKQIKGIGISNQGhGTVLLDKNDKPL---------YNAILWKDRRTAEIVENLKEegNNQKLYEITGLPIWPGFTLS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 93 KLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVtarslcsLVCKWTYSAEKG--------WDDSFWKMIGLEdfvadny 164
Cdd:pfam00370 135 KLRWIKENEPEV-FEKIHKFLTIHDYLRWRLTGV-------FVTDHTNASRSMmfnihkldWDPELLAALGIP------- 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1184725753 165 skigNQVLPP----GASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLG 211
Cdd:pfam00370 200 ----RDHLPPlvesSEIYGE-LNPELAAMWGLDEGVPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
334-483 |
3.10e-13 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466803 [Multi-domain] Cd Length: 501 Bit Score: 71.82 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 334 PDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAIlylATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMH 412
Cdd:cd07793 356 PAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVR---AILESIAFRVKQLLETMEKeTSIKISSIRVDGGVSNNDFILQLI 432
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184725753 413 ADITGMPVVLSQEVESVLVGAAVLGACASGDFASVqEAMAKMSKVGKVVFPRlQDKKYYDKKYQVFLKLVE 483
Cdd:cd07793 433 ADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSK-EELKKLRKIEKIFEPK-MDNEKREELYKNWKKAVK 501
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
19-481 |
1.02e-12 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 70.00 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 19 LNQIRGLGFDATC-SLVVLDKQFHPLpvnqegdshRNVIMWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLLWL 97
Cdd:PRK15027 65 LQDVKALGIAGQMhGATLLDAQQRVL---------RPAILWNDGRCAQECALLEARVPQSRVITGNLMMPGFTAPKLLWV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 98 KENLREICWDKAGHFfdLP-DFLSWKATGVTARSLCSLV-CKWTYSAEKGWDDSfwkMIGLEDFVADNYSkignqVLPPG 175
Cdd:PRK15027 136 QRHEPEIFRQIDKVL--LPkDYLRLRMTGEFASDMSDAAgTMWLDVAKRDWSDV---MLQACHLSRDQMP-----ALYEG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 176 ASLGNGLTPEAARDLGlLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVTSrlaviCGTSSCHMGISKDPIFVPG 255
Cdd:PRK15027 206 SEITGALLPEVAKAWG-MATVPVVAGGGDNAAGAVGV--------GMVDANQAMLS-----LGTSGVYFAVSEGFLSKPE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 256 VWGPYFSAMVPGFWlneggqsvtgKLIDHMVQGhAAFPELQVKATARcQSIYAYLNSHLDLIKKAQPVGFLtvdlhvwPD 335
Cdd:PRK15027 272 SAVHSFCHALPQRW----------HLMSVMLSA-ASCLDWAAKLTGL-SNVPALIAAAQQADESAEPVWFL-------PY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 336 FHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATV-QAIALGtrfiIEAMEAAGHSISTLFLCGGLSKNPLFVQMHAD 414
Cdd:PRK15027 333 LSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVgYALADG----MDVVHACGIKPQSVTLIGGGARSEYWRQMLAD 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184725753 415 ITGMPVVLSQ--EVESVLvGAAVLGACASGDFASVQEAMAKMSkVGKVVFPRLQDKKYYDKKYQVFLKL 481
Cdd:PRK15027 409 ISGQQLDYRTggDVGPAL-GAARLAQIAANPEKSLIELLPQLP-LEQSHLPDAQRYAAYQPRRETFRRL 475
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
370-484 |
4.42e-12 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 67.93 E-value: 4.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 370 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 448
Cdd:PRK00047 380 ATLESIAYQTRDVLDAMQAdSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLD 459
|
90 100 110
....*....|....*....|....*....|....*.
gi 1184725753 449 EaMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVEH 484
Cdd:PRK00047 460 E-LKEQWKIDRRFEPQMDEEE-REKLYAGWKKAVKR 493
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
16-484 |
2.22e-10 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 62.72 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 16 GIDLNQIRGLgfdATCSL----VVLDKQFHPLpvnqegdshrnvimW----LDHRAVSQVNRINETkHSVLQYvgGVMSV 87
Cdd:PRK10939 69 GIPASDIAAV---SATSMregiVLYDRNGTEI--------------WacanVDARASREVSELKEL-HNNFEE--EVYRC 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 88 EMQA------PKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTA--------RSLCSLVckwtysaEKGWDDSFWKM 153
Cdd:PRK10939 129 SGQTlalgalPRLLWLAHHRPDI-YRQAHTITMISDWIAYMLSGELAvdpsnagtTGLLDLV-------TRDWDPALLEM 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 154 IGLEDfvadnysKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrL 233
Cdd:PRK10939 201 AGLRA-------DILPPVKETGTVLGH-VTAKAAAETGLRAGTPVVMGGGDVQLGCLGL--------GVVRPGQ-----T 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 234 AVICGT------------SSCHMGISKDPifvpgvwgpyfsAMVPGFWLNEGGQSVTGkLIdhMVQGHAAF-PELQVKAT 300
Cdd:PRK10939 260 AVLGGTfwqqvvnlpapvTDPNMNIRINP------------HVIPGMVQAESISFFTG-LT--MRWFRDAFcAEEKLLAE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 301 ARCQSIYAYLNshldliKKAQ--PVGFLTV-----DL-------HVWPDFhgnrspladltlkgmvtgLKLSQDLD--DL 364
Cdd:PRK10939 325 RLGIDAYSLLE------EMASrvPVGSHGIipifsDVmrfkswyHAAPSF------------------INLSIDPEkcNK 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 365 AILYLATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGD 443
Cdd:PRK10939 381 ATLFRALEENAAIVSACNLQQIAAfSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGAGI 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1184725753 444 FASVQEAMAKMSKVGKVVFPRLQDKKYYDKK-------YQVFLKLVEH 484
Cdd:PRK10939 461 YSSLAETGERLVRWERTFEPNPENHELYQEAkekwqavYADQLGLVDH 508
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
93-470 |
3.26e-10 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 61.97 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 93 KLLWLKENLREIcWDKAGHFFDLPDFLSWKATGV--TARSLCSlVCKWTYSAEKGWDDSFWKMIGLEdfvadnyskigNQ 170
Cdd:PRK10331 137 KLVWLKENHPQL-LEQAHAWLFISSLINHRLTGEftTDITMAG-TSQMLDIQQRDFSPEILQATGLS-----------RR 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 171 VLPP----GASLGNgLTPEAARDLGLLPGIAVAASlidAHAGGLGVIGAdvrGHGLiceGQPV----------------- 229
Cdd:PRK10331 204 LFPRlveaGEQIGT-LQPSAAALLGLPVGIPVISA---GHDTQFALFGS---GAGQ---NQPVlssgtweilmvrsaqvd 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 230 TSRLAVICGtSSCHMGiSKDPIFVPGVWgpyfsamvpgfWLNEGGQSVTGKLI-------DHMVQGHAAFPelqvkatAR 302
Cdd:PRK10331 274 TSLLSQYAG-STCELD-SQSGLYNPGMQ-----------WLASGVLEWVRKLFwtaetpyQTMIEEARAIP-------PG 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 303 CQSIYayLNSHLDLIKKAQPVGfLTVdlhvwpdfHGNRSPLADLTLKGMvtGLKLSQDLDDLailylatvqaialgtrfi 382
Cdd:PRK10331 334 ADGVK--MQCDLLACQNAGWQG-VTL--------NTTRGHFYRAALEGL--TAQLKRNLQVL------------------ 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 383 ieamEAAGH-SISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVV 461
Cdd:PRK10331 383 ----EKIGHfKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQARAQMKYQYRYF 458
|
....*....
gi 1184725753 462 FPRLQDKKY 470
Cdd:PRK10331 459 YPQTEPEFI 467
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
92-450 |
1.77e-08 |
|
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.
Pssm-ID: 466791 [Multi-domain] Cd Length: 460 Bit Score: 56.77 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 92 PKLLWLKENLREIcWDKAGHFFDLPDFLSWKATG--VTARSLCSlvckwT---YSAEKG-WDDSFWKMIGLEdfvadnyS 165
Cdd:cd07771 132 YQLYALKKEGPEL-LERADKLLMLPDLLNYLLTGekVAEYTIAS-----TtqlLDPRTKdWSEELLEKLGLP-------R 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 166 KIGNQVLPPGASLGNgLTPEAARDLGL--LPGIAVA----ASLIDAhagglgvIGADVRGHGLICegqpvtsrlaviCGT 239
Cdd:cd07771 199 DLFPPIVPPGTVLGT-LKPEVAEELGLkgIPVIAVAshdtASAVAA-------VPAEDEDAAFIS------------SGT 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 240 SSChMGI-SKDPIFVPgvwgpyfSAMVPGFwLNEGG--------QSVTGkLidHMVQghaafpEL--QVKATARCQSiYA 308
Cdd:cd07771 259 WSL-IGVeLDEPVITE-------EAFEAGF-TNEGGadgtirllKNITG-L--WLLQ------ECrrEWEEEGKDYS-YD 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 309 YLNShldLIKKAQPVGFLtVDlhvwPD---FhgnRSPladltlKGMV---------TGLKLSQDLDDLA-ILYlatvQAI 375
Cdd:cd07771 320 ELVA---LAEEAPPFGAF-ID----PDdprF---LNP------GDMPeairaycreTGQPVPESPGEIArCIY----ESL 378
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184725753 376 ALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSqEVESVLVGAAVLGACASGDFASVQEA 450
Cdd:cd07771 379 ALKYAKTIEELEElTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAG-PVEATAIGNLLVQLIALGEIKSLEEG 453
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
94-436 |
4.51e-08 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466792 [Multi-domain] Cd Length: 424 Bit Score: 55.34 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 94 LLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVC--------KWTYS---AEKGWDDSFWKMigledfvad 162
Cdd:cd07772 129 LYWLKREKPEL-FARAKTILPLPQYWAWRLTGKAASEITSLGChtdlwdfeKNEYSslvKKEGWDKLFPPL--------- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 163 nyskignqvLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAgglgvigadvrghglicegqpvtSRLAvicgtssc 242
Cdd:cd07772 199 ---------RKAWEVLGP-LRPDLARRTGLPKDIPVGCGIHDSNA-----------------------ALLP-------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 243 HMGISKDPiFV---PGVWgpyFSAMVPGF-----WLNEG-----GQSVTGKLIdhmvqGHAAFP-----ELQVKataRCQ 304
Cdd:cd07772 238 YLAAGKEP-FTllsTGTW---CIAMNPGNdlpltELDLArdclyNLDVFGRPV-----KTARFMggreyERLVE---RIA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 305 SIYAYLNSHLDLIKkaqpvgFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATVQAIALgtrfiie 384
Cdd:cd07772 306 KSFPQLPSLADLAK------LLARGTFALPSFAPGGGPFPGSGGRGVLSAFPSAEEAYALAILYLALMTDYAL------- 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1184725753 385 amEAAGHSISTLFLCGGLSKNPLFVQMHADI-TGMPVVLSQEVESVLVGAAVL 436
Cdd:cd07772 373 --DLLGSGVGRIIVEGGFAKNPVFLRLLAALrPDQPVYLSDDSEGTALGAALL 423
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
1-434 |
1.34e-07 |
|
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466796 [Multi-domain] Cd Length: 436 Bit Score: 53.76 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 1 MINSVPEHHNEKVvQGIDL-NQIRGlgfdatcslVVLdkqfhplpVNQEGDSHRNVIMWLDHRAvsqvnriNETKHSVLQ 79
Cdd:cd07777 58 LIDELPREYLSDV-TGIGItGQMHG---------IVL--------WDEDGNPVSPLITWQDQRC-------SEEFLGGLS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 80 YVGGVMSVEMQAP--------KLLWLKENLREIcwDKAGHFFDLPDFLSWKATGvTARSLCSLVCK--WTY--SAEKGWD 147
Cdd:cd07777 113 TYGEELLPKSGMRlkpgyglaTLFWLLRNGPLP--SKADRAGTIGDYIVARLTG-LPKPVMHPTNAasWGLfdLETGTWN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 148 DSFWKMIGLEdfvadnySKIGNQVLPPGASLGNgLTPEAARDLGLLPGI-----AVAASLIDAHagglgvigadvrghgl 222
Cdd:cd07777 190 KDLLEALGLP-------VILLPEIVPSGEIVGT-LSSALPKGIPVYVALgdnqaSVLGSGLNEE---------------- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 223 icegqpvtSRLAVICGTSScHMGISKDPIFVPGVWG--PYFSamvpGFWLNeggqSVT----GKLIDHMVQ-----GHAA 291
Cdd:cd07777 246 --------NDAVLNIGTGA-QLSFLTPKFELSGSVEirPFFD----GRYLL----VAAslpgGRALAVLVDflrewLREL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 292 FPELQVkatarcQSIYAYLNShLDLIKKAQPvgfLTVDlhvwPDFHGNRSplaDLTLKGMVTGLklsqDLDDLAI--LYL 369
Cdd:cd07777 309 GGSLSD------DEIWEKLDE-LAESEESSD---LSVD----PTFFGERH---DPEGRGSITNI----GESNFTLgnLFR 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184725753 370 ATVQAIALGTRFIIEAMEAAGHSISTLFLCGG-LSKNPLFVQMHADITGMPVVLSQEVESVLVGAA 434
Cdd:cd07777 368 ALCRGIAENLHEMLPRLDLDLSGIERIVGSGGaLRKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAA 433
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
370-483 |
1.73e-07 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 53.55 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 370 ATVQAIALGTRFIIEAM------EAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGD 443
Cdd:PLN02295 384 AVLESMCFQVKDVLDAMrkdageEKSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGL 463
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1184725753 444 FASVQEAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 483
Cdd:PLN02295 464 WTEEEIFASEKWKNTTTFRPKLDEEE-RAKRYASWCKAVE 502
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
390-473 |
1.48e-03 |
|
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466795 [Multi-domain] Cd Length: 514 Bit Score: 41.00 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725753 390 GHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKV----GKVVFPRL 465
Cdd:cd07776 423 DIPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVVFSaeepKLVAEPDP 502
|
....*...
gi 1184725753 466 QDKKYYDK 473
Cdd:cd07776 503 EAAEVYDK 510
|
|
| |
