|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
9-428 |
0e+00 |
|
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: 520.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 9 RVAVIDIGKTNAKVVVIDTgSGEEIASKKQANPVLRDGIYPHYDVEMLWRFILSTLQRFGQKPGFDAISITTHGASAALL 88
Cdd:cd07772 1 VIAVFDIGKTNKKLLLFDE-NGEVLAERSTPNPEIEEDGYPCEDVEAIWEWLLDSLAELAKRHRIDAINFTTHGATFALL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 89 DGNGDLVMPVLDYEHSYSAAIEEAYRNIRPDFAETGSPQLPAGLNLGAQIHFQKTAFPNDFARVRSIVTYPQYWAGRLTG 168
Cdd:cd07772 80 DENGELALPVYDYEKPIPDEINEAYYAERGPFEETGSPPLPGGLNLGKQLYWLKREKPELFARAKTILPLPQYWAWRLTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 169 IRATETTSLGCHTDLWNPRRKSFSSLVERLGIETLMAPVRSAFDVLGTIHQSLALETGLSPHMPVYCGIHDSNASLLPHL 248
Cdd:cd07772 160 KAASEITSLGCHTDLWDFEKNEYSSLVKKEGWDKLFPPLRKAWEVLGPLRPDLARRTGLPKDIPVGCGIHDSNAALLPYL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 249 LRRDGDFSVVSTGTWVVNFAIGGAAGA--LDPIRDTLLNVDAFGRPVPSSRFMGGREYEMLAQQFGE-AKDEAIDAALGG 325
Cdd:cd07772 240 AAGKEPFTLLSTGTWCIAMNPGNDLPLteLDLARDCLYNLDVFGRPVKTARFMGGREYERLVERIAKsFPQLPSLADLAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 326 VVARGMMLLPSVVSGSGPFPDKTAQWLSDKNATAAERHAATSLYLALMTEFSLSLIGR-KGPILVEGPFASNALYLKALA 404
Cdd:cd07772 320 LLARGTFALPSFAPGGGPFPGSGGRGVLSAFPSAEEAYALAILYLALMTDYALDLLGSgVGRIIVEGGFAKNPVFLRLLA 399
|
410 420
....*....|....*....|....*
gi 739227954 405 G-FAETDVTAVEGSTGTSAGAALLT 428
Cdd:cd07772 400 AlRPDQPVYLSDDSEGTALGAALLA 424
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
13-430 |
1.63e-32 |
|
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: 128.47 E-value: 1.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 13 IDIGKTNAKVVVIDTgSGEEIASKKQANPVLRDGI-YPHYDVEMLWRFILSTLQRFGQKPGFD---AISITTHGASAALL 88
Cdd:cd07773 5 IDIGTTNVKAVLFDE-DGRILASASRETPLIHPGPgWAELDPEELWEAVKEAIREAAAQAGPDpiaAISVSSQGESGVPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 89 DGNGDLVMPVLD-YEHSYSAAIEEAYRNIRPD--FAETG---SPQLPAglnlgAQIHFQKTAFPNDFARVRSIVTYPQYW 162
Cdd:cd07773 84 DRDGEPLGPAIVwFDPRGKEEAEELAERIGAEelYRITGlppSPMYSL-----AKLLWLREHEPEIFAKAAKWLSVADYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 163 AGRLTGIRATETtSLGCHTDLWNPRRKSFSS-LVERLGIET-LMAPVRSAFDVLGTIHQSLALETGLSPHMPVYCGIHDS 240
Cdd:cd07773 159 AYRLTGEPVTDY-SLASRTMLFDIRKRTWSEeLLEAAGIDAsLLPELVPSGTVIGTVTPEAAEELGLPAGTPVVVGGHDH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 241 NASLLPHLLRRDGDFsVVSTGTWVVNFAIGGAAGALDPIRDTLLNVdafGRPVPSSRFM------GGREYEMLAQQFG-- 312
Cdd:cd07773 238 LCAALGAGVIEPGDV-LDSTGTAEALLAVVDEPPLDEMLAEGGLSY---GHHVPGGYYYlagslpGGALLEWFRDLFGgd 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 313 EAKDEAIDAALGGVV--ARGMMLLPSVVSGSGPFPDKTAQW----LSDkNATAAERHAATSLYLALMTEFSLSLIGRKG- 385
Cdd:cd07773 314 ESDLAAADELAEAAPpgPTGLLFLPHLSGSGTPDFDPDARGaflgLTL-GTTRADLLRAILEGLAFELRLNLEALEKAGi 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 739227954 386 ---PILVEGPFASNALYLKALAGFAETDVTAVEGSTGTSAGAALLTGI 430
Cdd:cd07773 393 pidEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGV 440
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
10-430 |
7.80e-31 |
|
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: 124.17 E-value: 7.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 10 VAVIDIGKTNAKVVVIDTgSGEEIASKKQANPVlrdgIYPH-----YDVEMLWRFILSTLQRFGQKPGFD-----AISIT 79
Cdd:COG1070 3 VLGIDIGTTSVKAVLFDA-DGEVVASASAEYPL----SSPHpgwaeQDPEDWWEAVVEAIRELLAKAGVDpeeiaAIGVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 80 THGASAALLDGNGDLVMPVLdyehSYS-----AAIEEAYRNIRPD--FAETGSPQLPAglNLGAQIHFQKTAFPNDFARV 152
Cdd:COG1070 78 GQMHGLVLLDADGEPLRPAI----LWNdtraaAEAAELREELGEEalYEITGNPLHPG--FTAPKLLWLKENEPEIFARI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 153 RSIVTYPQYWAGRLTGIRATETTSLGChTDLWNPRRKSFSS-LVERLGIET-LMAPVRSAFDVLGTIHQSLALETGLSPH 230
Cdd:COG1070 152 AKVLLPKDYLRYRLTGEFVTDYSDASG-TGLLDVRTRDWSDeLLEALGIDReLLPELVPPGEVAGTLTAEAAAETGLPAG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 231 MPVYCGIHDSNASLLPHLLRRDGDfSVVSTGTWVVNFAIGGAagaldPIRDTLLNVDAF-----GRPVPSSRFM-GGREY 304
Cdd:COG1070 231 TPVVAGAGDNAAAALGAGAVEPGD-AAVSLGTSGVVFVVSDK-----PLPDPEGRVHTFchavpGRWLPMGATNnGGSAL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 305 EMLAQQFGEAKD---EAIDAALGGVV--ARGMMLLPSvVSGSgPFPdktaqwLSDKNATAA-----ERHAATSLYLALMt 374
Cdd:COG1070 305 RWFRDLFADGELddyEELNALAAEVPpgADGLLFLPY-LSGE-RTP------HWDPNARGAffgltLSHTRAHLARAVL- 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739227954 375 E---FSLSLI-------GRK-GPILVEGPFASNALYLKALAGFAETDVTAVEGSTGTSAGAALLTGI 430
Cdd:COG1070 376 EgvaFALRDGlealeeaGVKiDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAV 442
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
9-263 |
4.61e-27 |
|
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: 113.01 E-value: 4.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 9 RVAVIDIGKTNAKVVV--IDTG--SGEEIasKKQAN-PVLRDGIYpHYDVEMLWRFILSTLQRFGQK-PGFDAISITTHG 82
Cdd:cd07771 1 NYLAVDLGASSGRVILgsLDGGklELEEI--HRFPNrPVEINGHL-YWDIDRLFDEIKEGLKKAAEQgGDIDSIGIDTWG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 83 ASAALLDGNGDLVMPVLDYEHSYSAAIEEAYRNIRPD---FAETGSPQLPagLNLGAQIHFQKTAFPNDFARVRSIVTYP 159
Cdd:cd07771 78 VDFGLLDKNGELLGNPVHYRDPRTEGMMEELFEKISKeelYERTGIQFQP--INTLYQLYALKKEGPELLERADKLLMLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 160 QYWAGRLTGIRATETTSLGcHTDLWNPRRKSFS-SLVERLGIET-LMAPVRSAFDVLGTIHQSLALETGLsPHMPV-YCG 236
Cdd:cd07771 156 DLLNYLLTGEKVAEYTIAS-TTQLLDPRTKDWSeELLEKLGLPRdLFPPIVPPGTVLGTLKPEVAEELGL-KGIPViAVA 233
|
250 260
....*....|....*....|....*..
gi 739227954 237 IHDSnASLLPHLLRRDGDFSVVSTGTW 263
Cdd:cd07771 234 SHDT-ASAVAAVPAEDEDAAFISSGTW 259
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
13-427 |
1.06e-23 |
|
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: 102.26 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 13 IDIGKTNAKVVVIDTgSGEEIASKKQANPVlrdgIYPH-----YDVEMLWRFILSTLQRFGQKPGFD-----AISITTHG 82
Cdd:cd00366 5 IDIGTTSVKAALFDE-DGNLVASASREYPL----IYPQpgwaeQDPEDWWQAVVEAIREVLAKAGIDpsdiaAIGISGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 83 ASAALLDGNGDLVMPVLDYehsysaaieeayrnirpdfaetgspqlpaglnlgaqihfqktafpNDfARVRsIVTYPQYW 162
Cdd:cd00366 80 PGVVLVDADGNPLRPAIIW---------------------------------------------LD-RRAK-FLQPNDYI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 163 AGRLTGIRATETTSLGChTDLWNPRRKSFSS-LVERLGIET-LMAPVRSAFDVLGTIHQSLALETGLSPHMPVYCGIHDS 240
Cdd:cd00366 113 VFRLTGEFAIDYSNASG-TGLYDIKTGDWSEeLLDALGIPReKLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGGDT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 241 NASLLPHLLRRDGDfSVVSTGTWVVNFAIGGAAGALDPirdTLLNVdafgRPVPSSRFM-------GGREYEMLAQQFGE 313
Cdd:cd00366 192 AAAALGAGVVEPGD-AVDSTGTSSVLSVCTDEPVPPDP---RLLNR----CHVVPGLWLlegaintGGASLRWFRDEFGE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 314 AKDEAID-------AALGGVVARGMMLLPSVVSGSGPFPDKTA----QWLSDkNATAAERHAA----TSLYLALMTEFSL 378
Cdd:cd00366 264 EEDSDAEyegldelAAEVPPGSDGLIFLPYLSGERSPIWDPAArgvfFGLTL-SHTRAHLIRAvlegVAYALRDNLEILE 342
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 739227954 379 SLIGRKGPILVEGPFASNALYLKALAGFAETDVTAVEGSTGTSAGAALL 427
Cdd:cd00366 343 ELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAIL 391
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
10-263 |
4.44e-21 |
|
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: 95.37 E-value: 4.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 10 VAVIDIGKTNAKVVVIDTgSGEEIASKKQANPVLRDGIYPH---YDVEMLWRFILS----TLQRFGQKPG-FDAISITTH 81
Cdd:cd07798 2 YLVIDIGTGGGRCALVDS-EGKIVAIAYREWEYYTDDDYPDakeFDPEELWEKICEaireALKKAGISPEdISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 82 GASAALLDGNGD--LVMPVLD-----YEHSYSAAIEEAYrnirpdfaETGSPQLPAGLNLGAQI-HFQKTAfPNDFARVR 153
Cdd:cd07798 81 REGIVFLDKDGRelYAGPNIDargveEAAEIDDEFGEEI--------YTTTGHWPTELFPAARLlWFKENR-PEIFERIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 154 SIVTYPQyWAG-RLTGIRATETTSlGCHTDLWNPRRKSFSS-LVERLGIETLMAP-VRSAFDVLGTIHQSLALETGLSPH 230
Cdd:cd07798 152 TVLSISD-WIGyRLTGELVSEPSQ-ASETQLFDIKKREWSQeLLEALGLPPEILPeIVPSGTVLGTVSEEAARELGLPEG 229
|
250 260 270
....*....|....*....|....*....|...
gi 739227954 231 MPVYCGIHDSNASLLPHLLRRDGDFSVVStGTW 263
Cdd:cd07798 230 TPVVVGGADTQCALLGSGAIEPGDIGIVA-GTT 261
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
10-245 |
4.54e-21 |
|
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: 94.98 E-value: 4.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 10 VAVIDIGKTNAKVVVIDTGsGEEIASKKQANPVLRDGIYPHY-DVEMLWRFILSTLQRFGQKPGFD---AISITTHGASA 85
Cdd:cd07783 2 FLGIDLGTSGVRAVVVDED-GTVLASASEPYPTSRPGPGWVEqDPEDWWEALRSLLRELPAELRPRrvvAIAVDGTSGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 86 ALLDGNGDLVMPVLDYEHSYSAAIEEAYRNIRPDFAETGSPQLPAGLNLgAQIHFQKTAFPNDFARVRSIVTYPQYWAGR 165
Cdd:cd07783 81 VLVDREGEPLRPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSPSSSL-AKLLWLKRHEPEVLAKTAKFLHQADWLAGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 166 LTGIR-ATETTSlgCHTDLWNPRRKSFSS-LVERLGI-ETLMAPVRSAFDVLGTIHQSLALETGLSPHMPVYCGIHDSNA 242
Cdd:cd07783 160 LTGDRgVTDYNN--ALKLGYDPETGRWPSwLLALLGIpPDLLPRVVAPGTVIGTLTAEAAEELGLPAGTPVVAGTTDSIA 237
|
...
gi 739227954 243 SLL 245
Cdd:cd07783 238 AFL 240
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
13-269 |
2.44e-20 |
|
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: 93.00 E-value: 2.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 13 IDIGKTNAKVVVIDTgSGEEIASKKQANPVlrdgIYPH-----YDVEMLWRFILSTLQRFGQKPGFD-----AISITTHG 82
Cdd:cd07802 5 IDNGTTNVKAVLFDL-DGREIAVASRPTPV----ISPRpgwaeRDMDELWQATAEAIRELLEKSGVDpsdiaGVGVTGHG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 83 ASAALLDGNGDLVMP-VLDYEHSYSAAIEEAYRNIRPD--FAETGSPqLPAGlNLGAQIHFQKTAFPNDFARVRSI---- 155
Cdd:cd07802 80 NGLYLVDKDGKPVRNaILSNDSRAADIVDRWEEDGTLEkvYPLTGQP-LWPG-QPVALLRWLKENEPERYDRIRTVlfck 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 156 --VTYpqywagRLTGIRATETTSLGchTDLWNPRRKSFS-SLVERLGIE---TLMAPVRSAFDVLGTIHQSLALETGLSP 229
Cdd:cd07802 158 dwIRY------RLTGEISTDYTDAG--SSLLDLDTGEYDdELLDLLGIEelkDKLPPLVPSTEIAGRVTAEAAALTGLPE 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 739227954 230 HMPVYCGIHDSNASLLPHLLRRDGDFSVVsTGTWVVNFAI 269
Cdd:cd07802 230 GTPVAAGAFDVVASALGAGAVDEGQLCVI-LGTWSINEVV 268
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
13-265 |
5.43e-20 |
|
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: 91.82 E-value: 5.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 13 IDIGKTNAKVVVIDTgSGEEIASKKQANPVlrdgIYPHY-----DVEMLWRFILSTLQRFGQKPGFD-----AISITTHG 82
Cdd:cd07804 5 IDIGTTGTKGVLVDE-DGKVLASASIEHDL----LTPKPgwaehDPEVWWGAVCEIIRELLAKAGISpkeiaAIGVSGLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 83 ASAALLDGNGDLVMPVLDYehSYSAA---IEEAYRNIRPD--FAETGSPqlpaglnLGAQIHFQKTAF-----PNDFARV 152
Cdd:cd07804 80 PALVPVDENGKPLRPAILY--GDRRAteeIEWLNENIGEDriFEITGNP-------LDSQSVGPKLLWikrnePEVFKKT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 153 RSIVTYPQYWAGRLTGIRATETTSLGCHTDLWNPRRKSFS-SLVERLGIET-LMAPVRSAFDVLGTIHQSLALETGLSPH 230
Cdd:cd07804 151 RKFLGAYDYIVYKLTGEYVIDYSSAGNEGGLFDIRKRTWDeELLEALGIDPdLLPELVPSTEIVGEVTKEAAEETGLAEG 230
|
250 260 270
....*....|....*....|....*....|....*..
gi 739227954 231 MPVYCGIHDSNASLLPHLLRRDGDFSVV--STGTWVV 265
Cdd:cd07804 231 TPVVAGTVDAAASALSAGVVEPGDLLLMlgTAGDIGV 267
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
10-245 |
1.17e-18 |
|
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: 88.35 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 10 VAVIDIGKTNAKVVVIDTgSGEEIASKKQANPVlrdgIYPH-----YDVEMLWRFILSTLQRFGQKPGFD-----AISIT 79
Cdd:cd07805 2 ILAIDLGTSGVKAALVDL-DGELVASAFAPYPT----YYPKpgwaeQDPEDWWDAVCRATRALLEKSGIDpsdiaAIAFS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 80 THGASAALLDGNGDLVMPVLdyehSYS---AAIEEAYRN---IRPDFAETGSPQLPAGLNLGAQIHFQKTAFPNDFARVR 153
Cdd:cd07805 77 GQMQGVVPVDKDGNPLRNAI----IWSdtrAAEEAEEIAgglGGIEGYRLGGGNPPSGKDPLAKILWLKENEPEIYAKTH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 154 SIVTYPQYWAGRLTGIRATETTSlGCHTDLWNPRRKSFS-SLVERLGIE-TLMAPVRSAFDVLGTIHQSLALETGLSPHM 231
Cdd:cd07805 153 KFLDAKDYLNFRLTGRAATDPST-ASTTGLMDLRKRRWSeELLRAAGIDpDKLPELVPSTEVVGELTPEAAAELGLPAGT 231
|
250
....*....|....
gi 739227954 232 PVYCGIHDSNASLL 245
Cdd:cd07805 232 PVVGGGGDAAAAAL 245
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
10-430 |
1.75e-16 |
|
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: 81.43 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 10 VAVIDIGKTNAKVVVIDTgSGEEIASKKQANPVlrdgIYPHY-----DVEMLWRFILSTLQRFGQKPGFD-----AISIT 79
Cdd:cd07808 2 LLGIDLGTSSVKAVLVDE-DGRVLASASAEYPT----SSPKPgwaeqDPEDWWQATKEALRELLAKAGISpsdiaAIGLT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 80 --THGAsaALLDGNGDLVMPVLDYEHSYSAA-IEEAYRNIRPDFAETG----SPQLPAglnlgAQIHFQKTAFPNDFARV 152
Cdd:cd07808 77 gqMHGL--VLLDKNGRPLRPAILWNDQRSAAeCEELEARLGDEILIITgnppLPGFTL-----PKLLWLKENEPEIFARI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 153 RSIVTYPQYWAGRLTGIRATETT-SLGchTDLWNPRRKSFSS-LVERLGI-ETLMAPVRSAFDVLGTIHQSLALETGLSP 229
Cdd:cd07808 150 RKILLPKDYLRYRLTGELATDPSdASG--TLLFDVEKREWSEeLLEALGLdPSILPPIVESTEIVGTLTPEAAEELGLPE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 230 HMPVYCGIHDSNASLLPHLLRRDGDFsVVSTGTWVVNFAIGGAagaldPIRDTLLNVDAFGRPVPSSRF-MG-----GRE 303
Cdd:cd07808 228 GTPVVAGAGDNAAAALGAGVVEPGDA-LISLGTSGVVFAPTDK-----PVPDPKGRLHTFPHAVPGKWYaMGvtlsaGLS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 304 YEMLAQQFGEAKD-------EAIDAALGgvvARGMMLLPsVVSGSGpfpdkTAQWlsDKNATAA-----ERHAATSLYLA 371
Cdd:cd07808 302 LRWLRDLFGPDREsfdeldaEAAKVPPG---SEGLLFLP-YLSGER-----TPYW--DPNARGSffglsLSHTRAHLARA 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 372 LMtE---FSL--------SLIGRKGPILVEGPFASNALYLKALAGFAETDVTAVEGSTGTSAGAALLTGI 430
Cdd:cd07808 371 VL-EgvaFSLrdslevlkELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAV 439
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
12-245 |
3.86e-16 |
|
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: 77.76 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 12 VIDIGKTNAKVVVIDTgSGEEIASKKQANPVlrdgIYPH-----YDVEMLWRFILSTLQRFGQKPGFD-----AISITTH 81
Cdd:pfam00370 4 GIDCGTTSTKAILFNE-QGKIIAVAQLENPQ----ITPHpgwaeQDPDEIWQAVAQCIAKTLSQLGISlkqikGIGISNQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 82 GASAALLDGNGDLVMPVLDYEHSYSAAI-EEAYRNIRPD--FAETGSPQLPagLNLGAQIHFQKTAFPNDFARVRSIVTY 158
Cdd:pfam00370 79 GHGTVLLDKNDKPLYNAILWKDRRTAEIvENLKEEGNNQklYEITGLPIWP--GFTLSKLRWIKENEPEVFEKIHKFLTI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 159 PQYWAGRLTGIRATETTSLGcHTDLWNPRRKSFS-SLVERLGI-ETLMAPVRSAFDVLGTIHQSLALETGLSPHMPVYCG 236
Cdd:pfam00370 157 HDYLRWRLTGVFVTDHTNAS-RSMMFNIHKLDWDpELLAALGIpRDHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGG 235
|
....*....
gi 739227954 237 IHDSNASLL 245
Cdd:pfam00370 236 GGDQQAAAF 244
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
10-349 |
5.52e-15 |
|
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: 76.79 E-value: 5.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 10 VAVIDIGKTNAKVVVIDTgSGEEIASKKQANPVL--RDGIYPHyDVEMLWRFILSTLQRFGQKPGFD-----AISITTHG 82
Cdd:cd07779 2 ILGIDVGTTSTRAIIFDL-DGNIVASGYREYPPYypEPGWVEQ-DPDDWWDALCEALKEAVAKAGVDpediaAIGLTSQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 83 ASAALLDGNGDLVMPVldyehsysaaieeayrnirpdfaetgspqlpaglnlgaqIHFQKTafpndfaRVRSIVTYPQYW 162
Cdd:cd07779 80 STFVPVDEDGRPLRPA---------------------------------------ISWQDK-------RTAKFLTVQDYL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 163 AGRLTGIRATETTSLGChTDLWNPRRKSFSS-LVERLGI-ETLMAPVRSAFDVLGTIHQSLALETGLSPHMPVYCGIHDS 240
Cdd:cd07779 114 LYRLTGEFVTDTTSASR-TGLPDIRTRDWSDdLLDAFGIdRDKLPELVPPGTVIGTLTKEAAEETGLPEGTPVVAGGGDQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 241 NASLLPHLLRRDGDfSVVSTGT-----------------------------WVVNFAIGGAAGALDPIRDTllnvdaFGR 291
Cdd:cd07779 193 QCAALGAGVLEPGT-ASLSLGTaavviavsdkpvedperripcnpsavpgkWVLEGSINTGGSAVRWFRDE------FGQ 265
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 739227954 292 PVPSSRFMGGREYEMLaqqfgeakDEAIDAALGGvvARGMMLLPSVVSGSGPFPDKTA 349
Cdd:cd07779 266 DEVAEKELGVSPYELL--------NEEAAKSPPG--SDGLLFLPYLAGAGTPYWNPEA 313
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
8-263 |
5.91e-13 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 70.44 E-value: 5.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 8 DRVAVIDIGKTNAKVVVIDTgSGEEIASKKQANPVLRDGIYPHY---DVEMLW-RFI---LSTLQRFGQKpGFDAISITT 80
Cdd:PRK10331 2 DVILVLDCGATNVRAIAVDR-QGKIVARASTPNASDIAAENSDWhqwSLDAILqRFAdccRQINSELTEC-HIRGITVTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 81 HGASAALLDGNGDLVMPVLDYEHSYSAAIEEA---YRNIRPDFAETGSPQLpaGLNLGAQIHFQKTAFPNDFAR------ 151
Cdd:PRK10331 80 FGVDGALVDKQGNLLYPIISWKCPRTAAVMENierYISAQQLQQISGVGAF--SFNTLYKLVWLKENHPQLLEQahawlf 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 152 VRSIVTYpqywagRLTGIRATETTSLGC------HTDLWNPrrksfsSLVERLGI-ETLMAPVRSAFDVLGTIHQSLALE 224
Cdd:PRK10331 158 ISSLINH------RLTGEFTTDITMAGTsqmldiQQRDFSP------EILQATGLsRRLFPRLVEAGEQIGTLQPSAAAL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 739227954 225 TGLSPHMPVYCGIHD-------SNASLlphllrrdgDFSVVSTGTW 263
Cdd:PRK10331 226 LGLPVGIPVISAGHDtqfalfgSGAGQ---------NQPVLSSGTW 262
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
10-239 |
1.68e-12 |
|
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: 69.12 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 10 VAVIDIGKTNAKVVVIDTgSGEEIASKKQANPVLRDGIYPHY-DVEMLWRFILSTLQRFGQKPGF---DAISITTHGASA 85
Cdd:cd07770 2 ILGIDIGTTSTKAVLFDE-DGRVVASSSAEYPLIRPEPGWAEqDPEEILEAVLEALKEVLAKLGGgevDAIGFSSAMHSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 86 ALLDGNGDLVMPVLDYEHSYSAAIEEAYRNiRPDFAE----TGSPQLPAglNLGAQIHFQKTAFPNDFARVRSIVTYPQY 161
Cdd:cd07770 81 LGVDEDGEPLTPVITWADTRAAEEAERLRK-EGDGSElyrrTGCPIHPM--YPLAKLLWLKEERPELFAKAAKFVSIKEY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 162 WAGRLTGIRATEtTSLGCHTDLWNPRRKSFSS-LVERLGI-ETLMAPVRSAFDVLGTIHQSLALETGLSPHMPVYCGIHD 239
Cdd:cd07770 158 LLYRLTGELVTD-YSTASGTGLLNIHTLDWDEeALELLGIdEEQLPELVDPTEVLPGLKPEFAERLGLLAGTPVVLGASD 236
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
13-264 |
2.06e-11 |
|
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: 65.71 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 13 IDIGKTNAKVVVIDTGSGEEIASKKQANPVLRDGIYPHY---DVEMLWRFILSTLQRFGQK--PGFDAISITT--HGasA 85
Cdd:cd07777 5 IDIGTTSIKAALLDLESGRILESVSRPTPAPISSDDPGRseqDPEKILEAVRNLIDELPREylSDVTGIGITGqmHG--I 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 86 ALLDGNGDlvmPVLDY----EHSYSAAIEEAYRNIRPDFAETGSPQLPAGL---NLGAQIHFQKtafpnDFARVRSIVTY 158
Cdd:cd07777 83 VLWDEDGN---PVSPLitwqDQRCSEEFLGGLSTYGEELLPKSGMRLKPGYglaTLFWLLRNGP-----LPSKADRAGTI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 159 PQYWAGRLTGIR--ATETT---SLGChtdlWNPRRKSFS-SLVERLGIETLMAP-VRSAFDVLGTIHQSlaletgLSPHM 231
Cdd:cd07777 155 GDYIVARLTGLPkpVMHPTnaaSWGL----FDLETGTWNkDLLEALGLPVILLPeIVPSGEIVGTLSSA------LPKGI 224
|
250 260 270
....*....|....*....|....*....|....
gi 739227954 232 PVYCGIHDSNASLLPHLLRRDGDFSV-VSTGTWV 264
Cdd:cd07777 225 PVYVALGDNQASVLGSGLNEENDAVLnIGTGAQL 258
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
13-266 |
1.50e-09 |
|
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: 60.04 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 13 IDIGKTNAKVVVIDTgSGEEIASKKQ-----ANPVLRDGIypHYDVEMLWRFILST----LQRFGQKPG-FDAISITTHG 82
Cdd:cd07775 5 LDAGTGSGRAVIFDL-EGNQIAVAQRewrhkEVPDVPGSM--DFDTEKNWKLICECireaLKKAGIAPKsIAAISTTSMR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 83 ASAALLDGNGDLVMPVLDYEhsySAAIEEAY--RNIRPDFAET---GSPQLPAgLNLGAQIHFQKTAFPNDFARVRSIVT 157
Cdd:cd07775 82 EGIVLYDNEGEEIWACANVD---ARAAEEVSelKELYNTLEEEvyrISGQTFA-LGAIPRLLWLKNNRPEIYRKAAKITM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 158 YPQYWAGRLTGIRATETtSLGCHTDLWNPRRKSFS-SLVERLGIE-TLMAPVRSAFDVLGTIHQSLALETGLSPHMPVYC 235
Cdd:cd07775 158 LSDWIAYKLSGELAVEP-SNGSTTGLFDLKTRDWDpEILEMAGLKaDILPPVVESGTVIGKVTKEAAEETGLKEGTPVVV 236
|
250 260 270
....*....|....*....|....*....|...
gi 739227954 236 GIHDSNASLLPHLLRRDGDFSVVSTGTW--VVN 266
Cdd:cd07775 237 GGGDVQLGCLGLGVVRPGQTAVLGGSFWqqEVN 269
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
13-427 |
1.81e-09 |
|
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: 59.49 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 13 IDIGKTNAKVVVIDTGSGEEIASkkqanpvlrdGIYPH-----------YDVEMLWRFILSTLQRFGQKPGFD-----AI 76
Cdd:cd07809 5 IDLGTQSIKAVLIDAETGRVVAS----------GSAPHenilidpgwaeQDPEDWWDALQAAFAQLLKDAGAElrdvaAI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 77 SIT--THGAsaALLDGNGDLVMPVLDYEHSYSAAI-EEAYRNIRPDFAETGSPQLPAGLNLgAQIHFQKTAFPNDFARVR 153
Cdd:cd07809 75 GISgqMHGL--VALDADGKVLRPAKLWCDTRTAPEaEELTEALGGKKCLLVGLNIPARFTA-SKLLWLKENEPEHYARIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 154 SIVTYPQYWAGRLTGIRATEttsLG--CHTDLWNPRRKSFSSLV-----ERLGIETLMAPVRSAFDVLGTIHQSLALETG 226
Cdd:cd07809 152 KILLPHDYLNWKLTGEKVTG---LGdaSGTFPIDPRTRDYDAELlaaidPSRDLRDLLPEVLPAGEVAGRLTPEGAEELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 227 LSPHMPVYCGIHDSNASLLPHLLRRDGDFsVVSTGTWVVNFAIGGAagaldPIRDTLLNVDAF----GRPVPSSRFMGG- 301
Cdd:cd07809 229 LPAGIPVAPGEGDNMTGALGTGVVNPGTV-AVSLGTSGTAYGVSDK-----PVSDPHGRVATFcdstGGMLPLINTTNCl 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 302 -REYEMLAQQFG---EAKDEAIDAALGGvvARGMMLLPSVVSGSGP-FPDKTAQW--LSDKNATAAE--RHAATSLYLAL 372
Cdd:cd07809 303 tAWTELFRELLGvsyEELDELAAQAPPG--AGGLLLLPFLNGERTPnLPHGRASLvgLTLSNFTRANlaRAALEGATFGL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 739227954 373 MteFSLSLIGRKG----PILVEGPFASNALYLKALAGFAETDVTAVEGSTGTSAGAALL 427
Cdd:cd07809 381 R--YGLDILRELGveidEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQ 437
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
13-262 |
1.06e-06 |
|
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: 51.00 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 13 IDIGKTNAKVVVIDTGSGEEIASKKQANPVLRDGIYPHY---DVEMLWRFILSTLQRFGQKPGFD-----AISITTHGAS 84
Cdd:cd07781 5 IDFGTQSVRAGLVDLADGEELASAVVPYPTGYIPPRPGWaeqNPADYWEALEEAVRGALAEAGVDpedvvGIGVDTTSST 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 85 AALLDGNGDLVMPVLDYEHSysAAIEEAyRNIrpdfAETGSPQLPAGLNLGAQI-----------HFQKTAfPNDFARVR 153
Cdd:cd07781 85 VVPVDEDGNPLAPAILWMDH--RAQEEA-AEI----NETAHPALEYYLAYYGGVyssewmwpkalWLKRNA-PEVYDAAY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 154 SIVTYPQYWAGRLTGIRATETTSLGCHTdLWNPRRKSFS-SLVERLGI------ETLMAPVRSAFDVLGTIHQSLALETG 226
Cdd:cd07781 157 TIVEACDWINARLTGRWVRSRCAAGHKW-MYNEWGGGPPrEFLAALDPgllklrEKLPGEVVPVGEPAGTLTAEAAERLG 235
|
250 260 270
....*....|....*....|....*....|....*.
gi 739227954 227 LSPHMPVYCGIHDSNASLLPHLLRRDGDFSVVsTGT 262
Cdd:cd07781 236 LPAGIPVAQGGIDAHMGAIGAGVVEPGTLALI-MGT 270
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
13-260 |
2.66e-06 |
|
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: 49.55 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 13 IDIGKTNAKVVVIDTgSGEEIASKKQANPVLR-DGIYPHYDVEMLWRFILSTLQRFGQKPGFD-----AISITTHGASAA 86
Cdd:cd24121 5 IDAGTSVVKAVAFDL-DGRELAVAARRNAVLYpQPGWAEQDMNETWQAVVATIREVVAKLDVLpdrvaAIGVTGQGDGTW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 87 LLDGNGDLVMPVLDYEHSYSAAIEEAYRN---IRPDFAETGSPQLPAglNLGAQIHFQKTAFPNDFARVRSIVTYPQYWA 163
Cdd:cd24121 84 LVDEDGRPVRDAILWLDGRAADIVERWQAdgiAEAVFEITGTGLFPG--SQAAQLAWLKENEPERLERARTALHCKDWLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 164 GRLTGIRATETTSlGCHTDLwNPRRKSFSS-LVERLGIET---LMAPVRSAFDVLGTIHQSLALETGLSPHMPVYCGIHD 239
Cdd:cd24121 162 YKLTGEIATDPSD-ASLTFL-DFRTRQYDDeVLDLLGLEElrhLLPPIRPGTEVIGPLTPEAAAATGLPAGTPVVLGPFD 239
|
250 260
....*....|....*....|..
gi 739227954 240 SNASLLPHLLRRDGD-FSVVST 260
Cdd:cd24121 240 VVATALGSGAIEPGDaCSILGT 261
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
13-251 |
3.17e-04 |
|
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: 43.00 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 13 IDIGKTNAKVVVIDTGSGEEIAskKQANPVLRDGIYPHYDVEM----LWRFILSTLQRFGQKPGFDAISITTHGASA--- 85
Cdd:cd07768 5 VDVGTSSARAGVYDLYAGLEMA--QEPVPYYQDSSKKSWKFWQksteIIKALQKCVQKLNIREGVDAYEVKGCGVDAtcs 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 86 -ALLDGNGDLVMPVLDYEHS-------YSAAIEEAYRnirpdFAETGSPQLPAGLN-------LGAQIHFQKTAFPNDFA 150
Cdd:cd07768 83 lAIFDREGTPLMALIPYPNEdnvifwmDHSAVNEAQW-----INMQCPQQLLDYLGgkispemGVPKLKYFLDEYSHLRD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227954 151 RVRSIVTYPQYWAGRLTGIRATETTSLGC------HTDLWNPR-RKSFSSLVERLGIETLMAPVRSAFDVLGTIHQSLAL 223
Cdd:cd07768 158 KHFHIFDLHDYIAYELTRLYEWNICGLLGkenldgEESGWSSSfFKNIDPRLEHLTTTKNLPSNVPIGTTSGVALPEMAE 237
|
250 260 270
....*....|....*....|....*....|..
gi 739227954 224 ETGLSPHMPVYCGIHDSNAS----LLPHLLRR 251
Cdd:cd07768 238 KMGLHPGTAVVVSCIDAHASwfavASPHLETS 269
|
|
| |
