|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
1-410 |
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: 731.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 1 MPRVLWLfwissfthyqstRKNLREiCWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA----EKGWDDSFWKMI 76
Cdd:cd07782 139 PPKLLWL------------KENLPE-TWAKAGHFFDLPDFLTWKATGSLTRSLCSLVCKWTYLAhegsEGGWDDDFFKEI 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 77 GLEDFVADNYSKIGNQVLPPGASLGNGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIGADVrgHGLICEGQPVTSRLA 156
Cdd:cd07782 206 GLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAKELGLPEGTPVGVSLIDAHAGGLGTLGADV--GGLPCEADPLTRRLA 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 157 VICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNSHL 236
Cdd:cd07782 284 LICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGLWLNEGGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNERL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 237 DLIKKAQ--PVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHS 314
Cdd:cd07782 364 EQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALLYLATLQALAYGTRHIIEAMNAAGHK 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 315 ISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYD 394
Cdd:cd07782 444 IDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDAMAAMSGPGKVVEPNEELKKYHD 523
|
410
....*....|....*.
gi 1184725761 395 KKYQVFLKLVEHQKEY 410
Cdd:cd07782 524 RKYEVFLKMYEDQREY 539
|
|
| 5C_CHO_kinase |
TIGR01315 |
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ... |
2-410 |
8.57e-169 |
|
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: 484.01 E-value: 8.57e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 2 PRVLWLfwissfthyqstRKNLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTY----SAEKGWDDSFWKMIG 77
Cdd:TIGR01315 140 PKVLWL------------KNNMPPE-LFARCKFFDLTDFLTWRATGKEIRSFCSVVCKWGFvpvdGSNKGWQEDFYETIG 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 78 LEDFVADNYSKIGNQVLPPGASLGNGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIGADVRGHGLICEGQpvtSRLAV 157
Cdd:TIGR01315 207 LGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQELGLPAGTAVGSGLIDAHAGWIGTVGAKVAENGDVSQAF---TRLAA 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 158 ICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNSHLd 237
Cdd:TIGR01315 284 VAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGYWLAEGGQSAAGELMDHMLETHVAYDETVKEAEAAGKNIYDYLNEHL- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 238 LIKKAQP----VGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGH 313
Cdd:TIGR01315 363 KEMAAKTnapsISYLVRHFHVYPDLWGNRSPIADPNMRGVIIGLSMDRSKDGLALLYYATMEFIAYGTRQIVEAMNTAGH 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 314 SISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQ-DKKY 392
Cdd:TIGR01315 443 TIKSIFMSGGQCQNPLLMQLIADACDMPVLIPYVNEAVLHGAAMLGAKAAGTTESLWDAMDRMSKPGKTVWPRGDpAKKL 522
|
410
....*....|....*...
gi 1184725761 393 YDKKYQVFLKLVEHQKEY 410
Cdd:TIGR01315 523 HDRKYEIFLQLARTQQEY 540
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
2-410 |
1.71e-149 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 434.54 E-value: 1.71e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 2 PRVLWLFwissfthyqstrKNLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGW-DDSFWKMIGLE 79
Cdd:COG1069 156 PKILHLL------------REDPEV-YEAADSFVELCDWITWQLTGSLKRSRCTAGHKALWHAhEGGYpSEEFFAALDPL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 80 -DFVADnysKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIGadvrghglICEGQpvtsrLAVI 158
Cdd:COG1069 223 lDGLAD---RLGTEIYPLGEPAGT-LTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGG--------VEPGT-----LVKV 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 159 CGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNshldl 238
Cdd:COG1069 286 MGTSTCHMLVSPEERFVPGICGQVDGSIVPGMWGYEAGQSAVGDIFAWFVRLLVPPLEYEKEAEERGISLHPLLT----- 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 239 iKKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDlaiLYLATVQAIALGTRFIIEAMEAAGHSISTL 318
Cdd:COG1069 361 -EEAAKLPPGESGLHALDWFNGNRSPLADQRLKGVILGLTLGTDAED---IYRALVEATAFGTRAIIERFEEEGVPIDEI 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 319 FLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKV-GKVVFPRLQDKKYYDKK 396
Cdd:COG1069 437 IACGGIAtKNPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMAAMGSGfDKVYTPDPENVAVYDAL 516
|
410
....*....|....
gi 1184725761 397 YQVFLKLVEHQKEY 410
Cdd:COG1069 517 YAEYLQLHDYFGRG 530
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
2-400 |
3.68e-108 |
|
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: 328.43 E-value: 3.68e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 2 PRVLWLFwissfTHYQSTrknlreicWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGWDDSFWKMIGLED 80
Cdd:cd07768 143 PKLKYFL-----DEYSHL--------RDKHFHIFDLHDYIAYELTRLYEWNICGLLGKENLDGeESGWSSSFFKNIDPRL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 81 fVADNYSKIGNQVLPPGASLGNGLtPEAARDLGLLPGIAVAASLIDAHAGGLGVIGADVRGhglicegqpvtsRLAVICG 160
Cdd:cd07768 210 -EHLTTTKNLPSNVPIGTTSGVAL-PEMAEKMGLHPGTAVVVSCIDAHASWFAVASPHLET------------SLFMIAG 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 161 TSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELqVKATARCQSIYAYLNshlDLIK 240
Cdd:cd07768 276 TSSCHMYGTTISDRIPGVWGPFDTIIDPDYSVYEAGQSATGKLIEHLFESHPCARKF-DEALKKGADIYQVLE---QTIR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 241 KAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFL 320
Cdd:cd07768 352 QIEKNNGLSIHILTLDMFFGNRSEFADPRLKGSFIGESLDTSMLNLTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRA 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 321 CGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFA---SVQEAMAKMSKVGKVVFPRLQD-KKYYDKK 396
Cdd:cd07768 432 SGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAAVLAKVAAGKKQladSITEADISNDRKSETFEPLAYRlGADYILL 511
|
....
gi 1184725761 397 YQVF 400
Cdd:cd07768 512 YKLL 515
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
28-403 |
8.38e-102 |
|
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: 311.39 E-value: 8.38e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 28 WDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEDfvADNYSKIGNQVLPPGASLGnGLTP 106
Cdd:cd07781 152 YDAAYTIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGgPPREFLAALDPGL--LKLREKLPGEVVPVGEPAG-TLTA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 107 EAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFSAM 186
Cdd:cd07781 229 EAAERLGLPAGIPVAQGGIDAHMGAIGA--------GVVEPGT-----LALIMGTSTCHLMVSPKPVDIPGICGPVPDAV 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 187 VPGFWLNEGGQSVTGKLIdhmvqghAAFPELQVKATA-RCQSIYAYLNshlDLIKKAQPV--GFLTVDlhvWpdFHGNRS 263
Cdd:cd07781 296 VPGLYGLEAGQSAVGDIF-------AWFVRLFVPPAEeRGDSIYALLS---EEAAKLPPGesGLVALD---W--FNGNRT 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 264 PLADLTLKGMVTGLKLSQDLddlAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHADITGMPV 342
Cdd:cd07781 361 PLVDPRLRGAIVGLTLGTTP---AHIYRALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPI 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184725761 343 VLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKL 403
Cdd:cd07781 438 KVPKSDQAPALGAAILAAVAAGVYADIEEAADAMVRVDRVYEPDPENHAVYEELYALYKEL 498
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
29-414 |
2.76e-63 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 212.78 E-value: 2.76e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 29 DKAGHFFDLPDFLSWKATGVTA-----RSLCSLVCKWTYSAEKG--WDDSFWKMI--GLEDFVADnysKIGNQVLPPGAS 99
Cdd:PRK04123 172 EAAASWVEACDWVVALLTGTTDpqdivRSRCAAGHKALWHESWGglPSADFFDALdpLLARGLRD---KLFTETWTAGEP 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 100 LGnGLTPEAARDLGLLPGIAVAASLIDAHAGglgVIGADVRGHGLicegqpvtsrLAVIcGTSSCHMGISKDPIFVPGVW 179
Cdd:PRK04123 249 AG-TLTAEWAQRLGLPEGVAVSVGAFDAHMG---AVGAGAEPGTL----------VKVM-GTSTCDILLADKQRAVPGIC 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 180 GPYFSAMVPGFWLNEGGQSVTGKLIDHMVQgHAAFPELQVKATARCQSIYAYLNshldliKKA--QPVG---FLTVDlhv 254
Cdd:PRK04123 314 GQVDGSIVPGLIGYEAGQSAVGDIFAWFAR-LLVPPEYKDEAEARGKQLLELLT------EAAakQPPGehgLVALD--- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 255 WpdFHGNRSPLADLTLKGMVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQM 333
Cdd:PRK04123 384 W--FNGRRTPLADQRLKGVITGLTLGTDAPDI---YRALIEATAFGTRAIMECFEDQGVPVEEVIAAGGIArKNPVLMQI 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 334 HADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKM-SKVGKVVFPRLQDKKYYDKKYQVFLKLVE-HQKEYL 411
Cdd:PRK04123 459 YADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEAQQAMaSPVEKTYQPDPENVARYEQLYQEYKQLHDyFGRGGN 538
|
...
gi 1184725761 412 AIM 414
Cdd:PRK04123 539 AVM 541
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
155-362 |
3.98e-61 |
|
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.
Pssm-ID: 426979 [Multi-domain] Cd Length: 197 Bit Score: 196.39 E-value: 3.98e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 155 LAVICGTSSCHMGISKDP-IFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQvkATARCQSIYAYLN 233
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPvLSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELR--DAGNVESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 234 SHLDLikkaqpvgfLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLddlAILYLATVQAIALGTRFIIEAMEA-AG 312
Cdd:pfam02782 79 LAAVA---------PAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTL---AHLYRAILESLALQLRQILEALTKqEG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1184725761 313 HSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACA 362
Cdd:pfam02782 147 HPIDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
2-409 |
9.37e-60 |
|
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: 201.98 E-value: 9.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 2 PRVLWLfwissfthyqstRKNLREIcWDKAGHFFDLPDFLSWKATG--VTARSLCSlvckWT--YSAEKG-WDDSFWKMI 76
Cdd:COG1070 135 PKLLWL------------KENEPEI-FARIAKVLLPKDYLRYRLTGefVTDYSDAS----GTglLDVRTRdWSDELLEAL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 77 GL-EDFVAdnyskignQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrL 155
Cdd:COG1070 198 GIdRELLP--------ELVPPGEVAG-TLTAEAAAETGLPAGTPVVAGAGDNAAAALGA--------GAVEPGD-----A 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 156 AVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQghaafpelqvKATARCQSIYAYLNsh 235
Cdd:COG1070 256 AVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAVPGRWLPMGATNNGGSALRWFRD----------LFADGELDDYEELN-- 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 236 lDLIKKAqPVG-----FLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEA 310
Cdd:COG1070 324 -ALAAEV-PPGadgllFL-------PYLSGERTPHWDPNARGAFFGLTLSHTRAHL---ARAVLEGVAFALRDGLEALEE 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 311 AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDK 390
Cdd:COG1070 392 AGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMVRVGETIEPDPENV 471
|
410
....*....|....*....
gi 1184725761 391 KYYDKKYQVFLKLVEHQKE 409
Cdd:COG1070 472 AAYDELYERYRELYPALKP 490
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
26-393 |
9.36e-52 |
|
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466798 [Multi-domain] Cd Length: 433 Bit Score: 179.25 E-value: 9.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 26 ICW-DK-AGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEdfvADNYSKIgnqvLPPGASLGN 102
Cdd:cd07779 96 ISWqDKrTAKFLTVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRdWSDDLLDAFGID---RDKLPEL----VPPGTVIGT 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 103 gLTPEAARDLGLLPGIAVAASlidAHAGGLGVIGADVRGHGLICegqpvtsrlaVICGTSSCHMGISKDPIFVPGVWGPY 182
Cdd:cd07779 169 -LTKEAAEETGLPEGTPVVAG---GGDQQCAALGAGVLEPGTAS----------LSLGTAAVVIAVSDKPVEDPERRIPC 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 183 FSAMVPGFWLNEGGQSVTGKLIDHMVQghaAFPELQVKATARCQSIYAYLNSHLDLIkkaqPVGFLtvDLHVWPDFHGNR 262
Cdd:cd07779 235 NPSAVPGKWVLEGSINTGGSAVRWFRD---EFGQDEVAEKELGVSPYELLNEEAAKS----PPGSD--GLLFLPYLAGAG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 263 SPLADLTLKGMVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPV 342
Cdd:cd07779 306 TPYWNPEARGAFIGLTLSHTRAHL---ARAILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPV 382
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1184725761 343 VLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYY 393
Cdd:cd07779 383 ERPETSEATALGAAILAAVGAGIYPDFEEAVKAMVRVTDTFEPDPENVAIY 433
|
|
| L-ribulokinase |
TIGR01234 |
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely ... |
31-411 |
2.61e-49 |
|
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: 175.11 E-value: 2.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 31 AGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKGW-DDSFWKMI--GLEDFVADNYSK-IGNQVLPPGAslgngLTP 106
Cdd:TIGR01234 176 ADRWIELADWIVAQLSGDIRRGRCTAGYKALWHESWGYpSASFFDELnpILNRHLPDKLFTdIWTAGEPAGT-----LTP 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 107 EAARDLGLLPGIAVAASLIDAHaggLGVIGADVrghgliceGQPvtSRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAM 186
Cdd:TIGR01234 251 EWAQRTGLPEGVVVAVGNFDAH---VGAVAAGI--------AQP--GALVKIMGTSTCHVLIGDKQRAVPGMCGVVDGGI 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 187 VPGFWLNEGGQSVTGKLIDHMVQgHAAFPELQVKATARCQSiyayLNSHLDLIKKAQPV---GFLTVDlhvWpdFHGNRS 263
Cdd:TIGR01234 318 VPGFIGYEAGQSAVGDIFAWFGK-VCVPPELKTEANASQKQ----LHEALSEAAAKQPSgehGLVALD---W--FNGNRS 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 264 PLADLTLKGMVTGLKLSQDLDDlaiLYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHADITGMPV 342
Cdd:TIGR01234 388 PLVDQRLKGVITGLTLATDAPL---LYRALIEATAFGTRMIMETFTDSGVPVEELMAAGGIArKNPVIMQIYADVTNRPL 464
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 343 VLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVF-PRLQDKKYYDKKYQVFLKLVEHQKEYL 411
Cdd:TIGR01234 465 QIVASDQAPALGAAIFAAVAAGVYADIPSAQAKMGSAVEKTLtPCSENAQRYEQLYARYQELAMSFGQYN 534
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
1-363 |
8.61e-43 |
|
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: 157.57 E-value: 8.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 1 MPRVLWLFwissfthyqstrKNLREICWDKAgHFFDLPDFLSWKatgvtarsLCSLVCKW--TYSAE------------K 66
Cdd:cd07778 146 IPKLKYLI------------DLIKEDTFKKL-EVFDLHDWISYM--------LATNLGHSniVPVNAppsigigidgslK 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 67 GWDDSFWKMIGLEDFVAD--NYSKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIgadvrghgl 144
Cdd:cd07778 205 GWSKDFYSKLKISTKVCNvgNTFKEAPPLPYAGIPIGK-VNVILASYLGIDKSTVVGHGCIDCYAGWFSTF--------- 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 145 iCEGQPVTSRLAVICGTSSCHMGISKDPI--FVPGVWGPyFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKAT 222
Cdd:cd07778 275 -AAAKTLDTTLFMVAGTSTCFLYATSSSQvgPIPGIWGP-FDQLLKNYSVYEGGQSATGKLIEKLFNSHPAIIELLKSDA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 223 arcqSIYAYLNSHLDLI--KKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATVQAIALG 300
Cdd:cd07778 353 ----NFFETVEEKIDKYerLLGQSIHYLTRHMFFYGDYLGNRTPYNDPNMSGSFIGESTDSSLTDLVLKYILILEFLAFQ 428
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184725761 301 TRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVV---LSQEVESVLVGAAVLGACAS 363
Cdd:cd07778 429 TKLIIDNFQKEKIIIQKVVISGSQAKNARLLQLLSTVLSKIHIivpLSDSKYAVVKGAALLGKAAF 494
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
2-401 |
2.44e-41 |
|
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: 152.29 E-value: 2.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 2 PRVLWLfwissfthyqstRKNLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLED 80
Cdd:cd07805 135 AKILWL------------KENEPEI-YAKTHKFLDAKDYLNFRLTGRAATDPSTASTTGLMDLRKRrWSEELLRAAGIDP 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 81 fvadnySKIgNQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGViGADVRGHGLICegqpvtsrlaviCG 160
Cdd:cd07805 202 ------DKL-PELVPSTEVVG-ELTPEAAAELGLPAGTPVVGGGGDAAAAALGA-GAVEEGDAHIY------------LG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 161 TSS---CHmgiSKDPIFVPGvwGPYFS--AMVPGFWLNEGGQSVTGKLIDHMVQgHAAFPELQVKatarcqSIYAYLNsh 235
Cdd:cd07805 261 TSGwvaAH---VPKPKTDPD--HGIFTlaSADPGRYLLAAEQETAGGALEWARD-NLGGDEDLGA------DDYELLD-- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 236 lDLIKKAQP----VGFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEAA 311
Cdd:cd07805 327 -ELAAEAPPgsngLLFL-------PWLNGERSPVEDPNARGAFIGLSLEHTRADLA---RAVLEGVAFNLRWLLEALEKL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 312 GHSISTLFLCGGLSKNPLFVQMHADITGMPV-VLSQEVESVLVGAAVLGACASGDFASVQEAmAKMSKVGKVVFPRLQDK 390
Cdd:cd07805 396 TRKIDELRLVGGGARSDLWCQILADVLGRPVeVPENPQEAGALGAALLAAVGLGLLKSFDEA-KALVKVEKVFEPDPENR 474
|
410
....*....|.
gi 1184725761 391 KYYDKKYQVFL 401
Cdd:cd07805 475 ARYDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
1-403 |
2.43e-38 |
|
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: 144.22 E-value: 2.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 1 MPRVLWLfwissfthyqstRKNLREIcWDKAGHFFdLP-DFLSWKATGVTAR-------SLCslvckwtYSAEKG-WDDS 71
Cdd:cd07808 132 LPKLLWL------------KENEPEI-FARIRKIL-LPkDYLRYRLTGELATdpsdasgTLL-------FDVEKReWSEE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 72 FWKMIGLEdfvadnyskigNQVLPP---GASLGNGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEG 148
Cdd:cd07808 191 LLEALGLD-----------PSILPPiveSTEIVGTLTPEAAEELGLPEGTPVVAGAGDNAAAALGA--------GVVEPG 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 149 QPV----TSrlAVICGTSSCHMGISKDPIF-----VPGVW---GPYFSAmvpGF---WLNE--GGQSVTGKLIDHMVQGH 211
Cdd:cd07808 252 DALislgTS--GVVFAPTDKPVPDPKGRLHtfphaVPGKWyamGVTLSA---GLslrWLRDlfGPDRESFDELDAEAAKV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 212 AAfpelqvkatarcqsiyaylnshldlikKAQPVGFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAilyL 291
Cdd:cd07808 327 PP---------------------------GSEGLLFL-------PYLSGERTPYWDPNARGSFFGLSLSHTRAHLA---R 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 292 ATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQE 371
Cdd:cd07808 370 AVLEGVAFSLRDSLEVLKELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEE 449
|
410 420 430
....*....|....*....|....*....|..
gi 1184725761 372 AMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKL 403
Cdd:cd07808 450 AAAACIKIEKTIEPDPERHEAYDELYARYREL 481
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
29-359 |
6.47e-38 |
|
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466787 [Multi-domain] Cd Length: 392 Bit Score: 141.16 E-value: 6.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 29 DKAGHFFDLPDFLSWKATGVTA--RSLCSLVCKWTYsAEKGWDDSFWKMIGL-EDFVADnyskignqVLPPGASLGnGLT 105
Cdd:cd00366 100 DRRAKFLQPNDYIVFRLTGEFAidYSNASGTGLYDI-KTGDWSEELLDALGIpREKLPP--------IVESGEVVG-RVT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 106 PEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVtsrlaVICGTSSCHMGISKDPIFVPGVWGPYFSA 185
Cdd:cd00366 170 PEAAEETGLPAGTPVVAGGGDTAAAALGA--------GVVEPGDAV-----DSTGTSSVLSVCTDEPVPPDPRLLNRCHV 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 186 mVPGFWLNEGGQSVTGKLIDHMVQghaafpelqvkATARCQSIYAYLNSHLDLIKKAQP----VGFLtvdlhvwPDFHGN 261
Cdd:cd00366 237 -VPGLWLLEGAINTGGASLRWFRD-----------EFGEEEDSDAEYEGLDELAAEVPPgsdgLIFL-------PYLSGE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 262 RSPLADLTLKGMVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMP 341
Cdd:cd00366 298 RSPIWDPAARGVFFGLTLSHTRAHL---IRAVLEGVAYALRDNLEILEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVP 374
|
330
....*....|....*...
gi 1184725761 342 VVLSQEVESVLVGAAVLG 359
Cdd:cd00366 375 VVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
2-364 |
2.29e-34 |
|
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: 132.71 E-value: 2.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 2 PRVLWLfwissfthyqstRKNLREIcWDKAGHFFDLPDFLSWKATGVTARSLcSLVCKWTY--SAEKGWDDSFWKMIGLE 79
Cdd:cd07773 132 AKLLWL------------REHEPEI-FAKAAKWLSVADYIAYRLTGEPVTDY-SLASRTMLfdIRKRTWSEELLEAAGID 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 80 dfvADNYSkignQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVIC 159
Cdd:cd07773 198 ---ASLLP----ELVPSGTVIGT-VTPEAAEELGLPAGTPVVVGGHDHLCAALGA--------GVIEPGD-----VLDST 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 160 GTSSCHMGISKDPIFVPGVWGPYFS---AMVPGFWLNEGGQSvTGKLIDHMVQGHAAFPELQVKATARCQSIYAylnshl 236
Cdd:cd07773 257 GTAEALLAVVDEPPLDEMLAEGGLSyghHVPGGYYYLAGSLP-GGALLEWFRDLFGGDESDLAAADELAEAAPP------ 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 237 dlikKAQPVGFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSIS 316
Cdd:cd07773 330 ----GPTGLLFL-------PHLSGSGTPDFDPDARGAFLGLTLGTTRADL---LRAILEGLAFELRLNLEALEKAGIPID 395
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1184725761 317 TLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 364
Cdd:cd07773 396 EIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
2-364 |
1.64e-32 |
|
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: 127.64 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 2 PRVLWLfwissfthyqstRKNLREIcWDKAGHFFDLPDFLSWKATG--VTARSLCSLvckwtYS-----AEKGWDDSFWK 74
Cdd:cd07804 134 PKLLWI------------KRNEPEV-FKKTRKFLGAYDYIVYKLTGeyVIDYSSAGN-----EGglfdiRKRTWDEELLE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 75 MIGLEdfvadnySKIGNQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsr 154
Cdd:cd07804 196 ALGID-------PDLLPELVPSTEIVG-EVTKEAAEETGLAEGTPVVAGTVDAAASALSA--------GVVEPGD----- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 155 LAVICGTSSCHMGISKDPIFVPGVWGPYFSamVPGFWLNEGGQSVTGKLIDHMVQGHAafPELQVKATARCQSIYAYLNs 234
Cdd:cd07804 255 LLLMLGTAGDIGVVTDKLPTDPRLWLDYHD--IPGTYVLNGGMATSGSLLRWFRDEFA--GEEVEAEKSGGDSAYDLLD- 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 235 hldliKKAQ--PVGfltVD-LHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAA 311
Cdd:cd07804 330 -----EEAEkiPPG---SDgLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHL---YRALLEGVAYGLRHHLEVIREA 398
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1184725761 312 GHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 364
Cdd:cd07804 399 GLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
20-404 |
1.01e-30 |
|
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: 123.05 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 20 RKNLREIcWDKAGHFFDLPDFLSWKATG--VTARSLCSlvckWT---YSAEKGWDDSFWKMIGLEdfvADNYSKIgnqvL 94
Cdd:cd07770 138 KEERPEL-FAKAAKFVSIKEYLLYRLTGelVTDYSTAS----GTgllNIHTLDWDEEALELLGID---EEQLPEL----V 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 95 PPGASLGnGLTPEAARDLGLLPGIAVAASLIDahaGGLGVIGAdvrghGLICEGqpvtsRLAVICGTSschmG----ISK 170
Cdd:cd07770 206 DPTEVLP-GLKPEFAERLGLLAGTPVVLGASD---GALANLGS-----GALDPG-----RAALTVGTS----GairvVSD 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 171 DPIFVP--GVWgPYFSAmvPGFWL-----NEGGqSVTGKLIDHMVQGHAAFPELQVKATArcqsiyAYLNSHlDLIkkaq 243
Cdd:cd07770 268 RPVLDPpgRLW-CYRLD--ENRWLvggaiNNGG-NVLDWLRDTLLLSGDDYEELDKLAEA------VPPGSH-GLI---- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 244 pvgFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGG 323
Cdd:cd07770 333 ---FL-------PYLAGERAPGWNPDARGAFFGLTLNHTRADI---LRAVLEGVAFNLKSIYEALEELAGPVKEIRASGG 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 324 LSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEamAKMSKVGKVVFPRLQDKKYYDKKYQVFLKL 403
Cdd:cd07770 400 FLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSLEA--DELVKIGKVVEPDPENHAIYAELYERFKKL 477
|
.
gi 1184725761 404 V 404
Cdd:cd07770 478 Y 478
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
29-364 |
8.00e-30 |
|
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: 119.96 E-value: 8.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 29 DKAGHFFDLPDFLSWKATGVtarslcsLVCKWT-YSA------EKGWDDSFWKMIGLEDFvadnYSKIGnQVLPPGASLG 101
Cdd:cd07802 148 DRIRTVLFCKDWIRYRLTGE-------ISTDYTdAGSslldldTGEYDDELLDLLGIEEL----KDKLP-PLVPSTEIAG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 102 nGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGp 181
Cdd:cd07802 216 -RVTAEAAALTGLPEGTPVAAGAFDVVASALGA--------GAVDEGQ-----LCVILGTWSINEVVTDEPVVPDSVGS- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 182 YFSAMVPGFWLNEGGQSVTGKLIDHMVQghaafpELQVKATARCQSIYAYLNshlDLIKKAQPVG----FLtvdlhvwPD 257
Cdd:cd07802 281 NSLHADPGLYLIVEASPTSASNLDWFLD------TLLGEEKEAGGSDYDELD---ELIAAVPPGSsgviFL-------PY 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 258 FHGNRsplADLTLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEAAGHsISTLFLCGGLSKNPLFVQMHADI 337
Cdd:cd07802 345 LYGSG---ANPNARGGFFGLTAWHTRAHLL---RAVYEGIAFSHRDHLERLLVARK-PETIRLTGGGARSPVWAQIFADV 417
|
330 340
....*....|....*....|....*..
gi 1184725761 338 TGMPVVLSQEVESVLVGAAVLGACASG 364
Cdd:cd07802 418 LGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
1-360 |
1.15e-29 |
|
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: 119.25 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 1 MPRVLWLfwissfthyqstRKNLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLE 79
Cdd:cd07783 129 LAKLLWL------------KRHEPEV-LAKTAKFLHQADWLAGRLTGDRGVTDYNNALKLGYDPETGrWPSWLLALLGIP 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 80 dfvadnySKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVTSrlaviC 159
Cdd:cd07783 196 -------PDLLPRVVAPGTVIGT-LTAEAAEELGLPAGTPVVAGTTDSIAAFLAS--------GAVRPGDAVTS-----L 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 160 GTSSCHMGISKDPIFVPGVwGPYFSAMVPGFWLNEGGQSVTGKLIDHmvqghaAFPELQVKAtarcqsiyaylnshldLI 239
Cdd:cd07783 255 GTTLVLKLLSDKRVPDPGG-GVYSHRHGDGYWLVGGASNTGGAVLRW------FFSDDELAE----------------LS 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 240 KKAQPVGflTVDLHVWP-DFHGNRSPLADLTLKGMVTGLKlsqdlDDLAILYLATVQAIALGTRFIIEAMEAAGHS-IST 317
Cdd:cd07783 312 AQADPPG--PSGLIYYPlPLRGERFPFWDPDARGFLLPRP-----HDRAEFLRALLEGIAFIERLGYERLEELGAPpVEE 384
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1184725761 318 LFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLvGAAVLGA 360
Cdd:cd07783 385 VRTAGGGARNDLWNQIRADVLGVPVVIAEEEEAAL-GAALLAA 426
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
3-364 |
1.09e-22 |
|
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: 99.60 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 3 RVLWLfwissfthyqstRKNLREIcWDKAGHFFDLPDFLSWKATGVtarslcsLVCKWTYSAEKG--------WDDSFWK 74
Cdd:cd07798 135 RLLWF------------KENRPEI-FERIATVLSISDWIGYRLTGE-------LVSEPSQASETQlfdikkreWSQELLE 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 75 MIGLEDfvadnysKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsr 154
Cdd:cd07798 195 ALGLPP-------EILPEIVPSGTVLGT-VSEEAARELGLPEGTPVVVGGADTQCALLGS--------GAIEPGD----- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 155 LAVICGTSSCHMGISKDPIFVP--GVW-GPYfsaMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQvkatarcqsiYAY 231
Cdd:cd07798 254 IGIVAGTTTPVQMVTDEPIIDPerRLWtGCH---LVPGKWVLESNAGVTGLNYQWLKELLYGDPEDS----------YEV 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 232 LNSHLDLIKKAQP--VGFLTVDLhvwpdFHGNRSPLADLTLKGMVTGLKLSQDLDDLAIlylATVQAIALGTRFIIEAME 309
Cdd:cd07798 321 LEEEASEIPPGANgvLAFLGPQI-----FDARLSGLKNGGFLFPTPLSASELTRGDFAR---AILENIAFAIRANLEQLE 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1184725761 310 A-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 364
Cdd:cd07798 393 EvSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
33-364 |
5.63e-21 |
|
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: 94.54 E-value: 5.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 33 HFFDLP-DFLSWKATG--VTARSLCSLVckwtysaekGWDDSF-----WKMIGLEDFVADNYSKIGnQVLPPGASLGnGL 104
Cdd:cd07809 151 AKILLPhDYLNWKLTGekVTGLGDASGT---------FPIDPRtrdydAELLAAIDPSRDLRDLLP-EVLPAGEVAG-RL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 105 TPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVTSrlaviCGTSSCHMGISKDPIFVPgvwgpyfS 184
Cdd:cd07809 220 TPEGAEELGLPAGIPVAPGEGDNMTGALGT--------GVVNPGTVAVS-----LGTSGTAYGVSDKPVSDP-------H 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 185 AMVPGF--------WLNEG---GQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYlnshldlikkaqpvgfltvdlh 253
Cdd:cd07809 280 GRVATFcdstggmlPLINTtncLTAWTELFRELLGVSYEELDELAAQAPPGAGGLLLL---------------------- 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 254 vwPDFHGNRSP-LADLTlkGMVTGLKLSQDldDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQ 332
Cdd:cd07809 338 --PFLNGERTPnLPHGR--ASLVGLTLSNF--TRANLARAALEGATFGLRYGLDILRELGVEIDEIRLIGGGSKSPVWRQ 411
|
330 340 350
....*....|....*....|....*....|..
gi 1184725761 333 MHADITGMPVVLSQEVESVLVGAAVLGACASG 364
Cdd:cd07809 412 ILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
1-398 |
3.68e-18 |
|
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: 86.23 E-value: 3.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 1 MPRVLWLfwissfthyqstRKNLREIcWDKAGHFFDLPDFLSWKATGVTAR--SLCSLVCKWTySAEKGWDDSFWKMIGL 78
Cdd:cd07775 135 IPRLLWL------------KNNRPEI-YRKAAKITMLSDWIAYKLSGELAVepSNGSTTGLFD-LKTRDWDPEILEMAGL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 79 EDFvadnyskIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrlAVI 158
Cdd:cd07775 201 KAD-------ILPPVVESGTVIGK-VTKEAAEETGLKEGTPVVVGGGDVQLGCLGL--------GVVRPGQ------TAV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 159 CGTSSCHMGI-SKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQghAAFPELQVKATARCQSIYAYLNshld 237
Cdd:cd07775 259 LGGSFWQQEVnTAAPVTDPAMNIRVNCHVIPDMWQAEGISFFPGLVMRWFRD--AFCAEEKEIAERLGIDAYDLLE---- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 238 liKKAQ--PVGF-----LTVDL-------HVWPDFhgnrspladltlkgmvTGLKLSQDLDDLAILYLATVQAIALGTRF 303
Cdd:cd07775 333 --EMAKdvPPGSygimpIFSDVmnyknwrHAAPSF----------------LNLDIDPEKCNKATFFRAIMENAAIVSAG 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 304 IIEAMEAA-GHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKV 382
Cdd:cd07775 395 NLERIAEFsGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAGIYSSLEEAVESLVKWERE 474
|
410
....*....|....*.
gi 1184725761 383 VFPRLQDKKYYDKKYQ 398
Cdd:cd07775 475 YLPNPENHEVYQDLYE 490
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
256-405 |
3.69e-16 |
|
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466789 [Multi-domain] Cd Length: 486 Bit Score: 80.20 E-value: 3.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 256 PDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMH 334
Cdd:cd07769 341 PAFSGLGAPYWDPDARGAIVGLTRGTTKAHIV---RAALESIAYQTRDVLEAMEKdSGIKLKELRVDGGATANNFLMQFQ 417
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184725761 335 ADITGMPVVLSQEVESVLVGAAVLGACASGdFASVQEAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 405
Cdd:cd07769 418 ADILGVPVVRPKVAETTALGAAYLAGLAVG-FWKDLDELASLWQVDKRFEPSMDEEE-RERLYRGWKKAVE 486
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
292-405 |
1.58e-15 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466802 [Multi-domain] Cd Length: 499 Bit Score: 78.33 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 292 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 370
Cdd:cd07792 384 AALEAVCFQTREILDAMNKdSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLD 463
|
90 100 110
....*....|....*....|....*....|....*
gi 1184725761 371 EAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 405
Cdd:cd07792 464 ELKSLNEGGRTVFEPQISEEE-RERRYKRWKKAVE 497
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
271-405 |
1.63e-15 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 78.18 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 271 KGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVE 349
Cdd:COG0554 359 RGAIFGLTRGTTRAHIA---RAALESIAYQTRDVLDAMEAdSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTE 435
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1184725761 350 SVLVGAAVLGACASGDFASVQEaMAKMSKVGKVVFPRLqDKKYYDKKYQVFLKLVE 405
Cdd:COG0554 436 TTALGAAYLAGLAVGFWKSLEE-LAALWKVDRRFEPQM-DEEERERLYAGWKKAVE 489
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
292-405 |
1.18e-14 |
|
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases
Pssm-ID: 198361 [Multi-domain] Cd Length: 486 Bit Score: 75.61 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 292 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 370
Cdd:cd07786 374 AALESIAYQTRDLLEAMEAdSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLD 453
|
90 100 110
....*....|....*....|....*....|....*
gi 1184725761 371 EAmAKMSKVGKVVFPRLqDKKYYDKKYQVFLKLVE 405
Cdd:cd07786 454 EL-AKLWQVDRRFEPSM-SEEEREALYAGWKKAVK 486
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
292-392 |
1.36e-14 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 75.40 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 292 ATVQAIALGTRFIIEAME-AAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 370
Cdd:PTZ00294 383 AALEAIALQTNDVIESMEkDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLE 462
|
90 100
....*....|....*....|..
gi 1184725761 371 EAMAKMSKVGKVVFPRLQDKKY 392
Cdd:PTZ00294 463 EVKKLIRRSNSTFSPQMSAEER 484
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
104-364 |
2.58e-14 |
|
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: 74.20 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 104 LTPEAARDLGLLPGIAVAASLIDAHAGGLGViGADVRGHGLicegqpvtsrlaVICGTSSCHMGISKDPIFVPGVWGPYF 183
Cdd:cd24121 217 LTPEAAAATGLPAGTPVVLGPFDVVATALGS-GAIEPGDAC------------SILGTTGVHEVVVDEPDLEPEGVGYTI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 184 SAMVPGFWLNEGGqSVTGKL-IDHMVQ--GHAAFPELQVKATarcqSIYAYLNSHLdlikKAQPVGFLTVDLHVWPDFHG 260
Cdd:cd24121 284 CLGVPGRWLRAMA-NMAGTPnLDWFLRelGEVLKEGAEPAGS----DLFQDLEELA----ASSPPGAEGVLYHPYLSPAG 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 261 NRSPLADLTLKGMVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMeaaGHSISTLFLCGGLSKNPLFVQMHADITGM 340
Cdd:cd24121 355 ERAPFVNPNARAQFTGLSLEHTRADLL---RAVYEGVALAMRDCYEHM---GEDPGELRLSGGGARSDTWCQILADALGV 428
|
250 260
....*....|....*....|....
gi 1184725761 341 PVVLSQEVESVLVGAAVLGACASG 364
Cdd:cd24121 429 PVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
256-405 |
3.54e-13 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466803 [Multi-domain] Cd Length: 501 Bit Score: 71.05 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 256 PDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAIlylATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMH 334
Cdd:cd07793 356 PAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVR---AILESIAFRVKQLLETMEKeTSIKISSIRVDGGVSNNDFILQLI 432
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184725761 335 ADITGMPVVLSQEVESVLVGAAVLGACASGDFASVqEAMAKMSKVGKVVFPRlQDKKYYDKKYQVFLKLVE 405
Cdd:cd07793 433 ADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSK-EELKKLRKIEKIFEPK-MDNEKREELYKNWKKAVK 501
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
292-406 |
3.72e-12 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 67.93 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 292 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 370
Cdd:PRK00047 380 ATLESIAYQTRDVLDAMQAdSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLD 459
|
90 100 110
....*....|....*....|....*....|....*.
gi 1184725761 371 EaMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVEH 406
Cdd:PRK00047 460 E-LKEQWKIDRRFEPQMDEEE-REKLYAGWKKAVKR 493
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
289-392 |
2.34e-08 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 55.80 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 289 LYLATVQAIALGTRFIIEAMEAAGH-SISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFA 367
Cdd:PRK10331 363 FYRAALEGLTAQLKRNLQVLEKIGHfKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFS 442
|
90 100
....*....|....*....|....*
gi 1184725761 368 SVQEAMAKMSKVGKVVFPRLQDKKY 392
Cdd:PRK10331 443 SPEQARAQMKYQYRYFYPQTEPEFI 467
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
297-372 |
2.47e-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: 55.61 E-value: 2.47e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184725761 297 IALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSqEVESVLVGAAVLGACASGDFASVQEA 372
Cdd:cd07771 378 LALKYAKTIEELEElTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAG-PVEATAIGNLLVQLIALGEIKSLEEG 453
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
292-405 |
1.76e-07 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 53.16 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 292 ATVQAIALGTRFIIEAM------EAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGD 365
Cdd:PLN02295 384 AVLESMCFQVKDVLDAMrkdageEKSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGL 463
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1184725761 366 FASVQEAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 405
Cdd:PLN02295 464 WTEEEIFASEKWKNTTTFRPKLDEEE-RAKRYASWCKAVE 502
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
226-356 |
2.65e-07 |
|
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466796 [Multi-domain] Cd Length: 436 Bit Score: 52.61 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 226 QSIYAYLNShLDLIKKAQPvgfLTVDlhvwPDFHGNRSplaDLTLKGMVTGLklsqDLDDLAI--LYLATVQAIALGTRF 303
Cdd:cd07777 315 DEIWEKLDE-LAESEESSD---LSVD----PTFFGERH---DPEGRGSITNI----GESNFTLgnLFRALCRGIAENLHE 379
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1184725761 304 IIEAMEAAGHSISTLFLCGG-LSKNPLFVQMHADITGMPVVLSQEVESVLVGAA 356
Cdd:cd07777 380 MLPRLDLDLSGIERIVGSGGaLRKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAA 433
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
1-406 |
4.27e-07 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 51.93 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 1 MPRVLWLfwissfthyqstRKNLREIcWDKAGHFFDLPDFLSWKATGVTA--------RSLCSLVckwtysaEKGWDDSF 72
Cdd:PRK10939 138 LPRLLWL------------AHHRPDI-YRQAHTITMISDWIAYMLSGELAvdpsnagtTGLLDLV-------TRDWDPAL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 73 WKMIGLEDfvadnysKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvt 152
Cdd:PRK10939 198 LEMAGLRA-------DILPPVKETGTVLGH-VTAKAAAETGLRAGTPVVMGGGDVQLGCLGL--------GVVRPGQ--- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 153 srLAVICGT------------SSCHMGISKDPifvpgvwgpyfsAMVPGFWLNEGGQSVTGkLIdhMVQGHAAF-PELQV 219
Cdd:PRK10939 259 --TAVLGGTfwqqvvnlpapvTDPNMNIRINP------------HVIPGMVQAESISFFTG-LT--MRWFRDAFcAEEKL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 220 KATARCQSIYAYLNshldliKKAQ--PVGFLTV-----DL-------HVWPDFhgnrspladltlkgmvtgLKLSQDLD- 284
Cdd:PRK10939 322 LAERLGIDAYSLLE------EMASrvPVGSHGIipifsDVmrfkswyHAAPSF------------------INLSIDPEk 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 285 -DLAILYLATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACA 362
Cdd:PRK10939 378 cNKATLFRALEENAAIVSACNLQQIAAfSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVG 457
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1184725761 363 SGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKK-------YQVFLKLVEH 406
Cdd:PRK10939 458 AGIYSSLAETGERLVRWERTFEPNPENHELYQEAkekwqavYADQLGLVDH 508
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
7-358 |
1.12e-05 |
|
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: 47.25 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 7 LFWIssfthyQSTRKNLreicWDKAGHFFDLPDFLSWKATGVTARSLCSLVC--------KWTYS---AEKGWDDSFWKM 75
Cdd:cd07772 129 LYWL------KREKPEL----FARAKTILPLPQYWAWRLTGKAASEITSLGChtdlwdfeKNEYSslvKKEGWDKLFPPL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 76 igledfvadnyskignqvLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAgglgvigadvrghglicegqpvtSRL 155
Cdd:cd07772 199 ------------------RKAWEVLGP-LRPDLARRTGLPKDIPVGCGIHDSNA-----------------------ALL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 156 AvicgtsscHMGISKDPiFV---PGVWgpyFSAMVPGF-----WLNEG-----GQSVTGKLIdhmvqGHAAFP-----EL 217
Cdd:cd07772 237 P--------YLAAGKEP-FTllsTGTW---CIAMNPGNdlpltELDLArdclyNLDVFGRPV-----KTARFMggreyER 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 218 QVKataRCQSIYAYLNSHLDLIKkaqpvgFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLKLSQDLDDLAILYLATVQAI 297
Cdd:cd07772 300 LVE---RIAKSFPQLPSLADLAK------LLARGTFALPSFAPGGGPFPGSGGRGVLSAFPSAEEAYALAILYLALMTDY 370
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184725761 298 ALgtrfiieamEAAGHSISTLFLCGGLSKNPLFVQMHADI-TGMPVVLSQEVESVLVGAAVL 358
Cdd:cd07772 371 AL---------DLLGSGVGRIIVEGGFAKNPVFLRLLAALrPDQPVYLSDDSEGTALGAALL 423
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
312-395 |
1.39e-03 |
|
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466795 [Multi-domain] Cd Length: 514 Bit Score: 40.62 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725761 312 GHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKV----GKVVFPRL 387
Cdd:cd07776 423 DIPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVVFSaeepKLVAEPDP 502
|
....*...
gi 1184725761 388 QDKKYYDK 395
Cdd:cd07776 503 EAAEVYDK 510
|
|
| |
