|
Name |
Accession |
Description |
Interval |
E-value |
| XylB |
TIGR01312 |
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ... |
3-478 |
0e+00 |
|
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of carbohydrate kinases. The member from Klebsiella pneumoniae, designated DalK (see , was annotated erroneously in GenBank as D-arabinitol kinase but is authentic D-xylulose kinase. D-xylulose kinase (XylB) generally is found with xylose isomerase (XylA) and acts in xylose utilization. [Energy metabolism, Sugars]
Pssm-ID: 273550 [Multi-domain] Cd Length: 481 Bit Score: 689.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 3 LGIDLGTSEVKALVIDENNEIVATHSAPLTIQRPHPHWSEQSPQAWWEATEYLMSTLREKCGHHWQAIKAIGLSGQMHGA 82
Cdd:TIGR01312 1 LGIDLGTSGVKALLVDEQGEVIASGSAPHTVISPHPGWSEQDPEDWWDATEEAIKELLEQASEMGQDIKGIGISGQMHGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 83 VLLDEKGEAIRPAILWNDTRSAQECAELEEIAPE--LHQVAGNLAMPGFTAPKLLWVRRHEPQHFARISTVLLPKDYLRF 160
Cdd:TIGR01312 81 VLLDANGEVLRPAILWNDTRTAQECEELEAELGDerVLEITGNLALPGFTAPKLLWVRKHEPEVFARIAKVMLPKDYLRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 161 KMTGQKISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSATLSPEVASRWGLTSSVVVAGGGGDNAVS 240
Cdd:TIGR01312 161 RLTGEYVTEYSDASGTGWFDVAKRAWSKELLDALDLPESQLPELIESSEKAGTVRPEVAARLGLSAGVPVAAGGGDNAAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 241 AIGVGAVSPGDAFISLGTSGVLFVVTDAYRPAPQSAVHAFCHVLPNLWHQMSVMLSAASCLQWFCRLVGVTETELLEEIA 320
Cdd:TIGR01312 241 AIGTGTVDPGDAMMSLGTSGVVYAVTDKPLPDPAGAVHGFCHALPGGWLPMGVTLSATSSLEWFRELFGKEDVEALNELA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 321 QLSDADkASAPMFLPYLSGERTPHNDPHARGLFWALTHSSQRALMGYAVLEGVSFGIADGLRVL-QESGTAIEQCSLVGG 399
Cdd:TIGR01312 321 EQSPPG-AEGVTFLPYLNGERTPHLDPQARGSFIGLTHNTTRADLTRAVLEGVTFALRDSLDILrEAGGIPIQSIRLIGG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 400 GARSPFWAQLLADILDMPVVTHKgGETGGALGAARLACLAAG-KPLAAVCEKPEIFKTWRSDP--ERHNALMQRYQQFTA 476
Cdd:TIGR01312 400 GAKSPAWRQMLADIFGTPVDVPE-GEEGPALGAAILAAWALGeKDLAALCSEAVVKQTESVLPiaENVEAYEELYERYKK 478
|
..
gi 446202723 477 LY 478
Cdd:TIGR01312 479 LY 480
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
1-480 |
0e+00 |
|
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: 626.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 1 MYLGIDLGTSEVKALVIDENNEIVATHSAPLTIQRPHPHWSEQSPQAWWEATEYLMSTLREKCGHHWQAIKAIGLSGQMH 80
Cdd:COG1070 2 YVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQMH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 81 GAVLLDEKGEAIRPAILWNDTRSAQECAELEEI--APELHQVAGNLAMPGFTAPKLLWVRRHEPQHFARISTVLLPKDYL 158
Cdd:COG1070 82 GLVLLDADGEPLRPAILWNDTRAAAEAAELREElgEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAKVLLPKDYL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 159 RFKMTGQKISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSATLSPEVASRWGLTSSVVVAGGGGDNA 238
Cdd:COG1070 162 RYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAAETGLPAGTPVVAGAGDNA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 239 VSAIGVGAVSPGDAFISLGTSGVLFVVTDAYRPAPQSAVHAFCHVLPNLWHQMSVMLSAASCLQWFCRLVGVTET---EL 315
Cdd:COG1070 242 AAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAVPGRWLPMGATNNGGSALRWFRDLFADGELddyEE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 316 LEEIAQLSDADkASAPMFLPYLSGERTPHNDPHARGLFWALTHSSQRALMGYAVLEGVSFGIADGLRVLQESGTAIEQCS 395
Cdd:COG1070 322 LNALAAEVPPG-ADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEALEEAGVKIDRIR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 396 LVGGGARSPFWAQLLADILDMPVVTHKGGEtGGALGAARLACLAAGK---PLAAVCEKPEIFKTWRSDPERHNALMQRYQ 472
Cdd:COG1070 401 ATGGGARSPLWRQILADVLGRPVEVPEAEE-GGALGAALLAAVGLGLyddLEEAAAAMVRVGETIEPDPENVAAYDELYE 479
|
....*...
gi 446202723 473 QFTALYHN 480
Cdd:COG1070 480 RYRELYPA 487
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
1-478 |
0e+00 |
|
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: 623.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 1 MYLGIDLGTSEVKALVIDENNEIVATHSAPLTIQRPHPHWSEQSPQAWWEATEYLMSTLREKCGHHWQAIKAIGLSGQMH 80
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 81 GAVLLDEKGEAIRPAILWNDTRSAQECAELEE-IAPELHQVAGNLAMPGFTAPKLLWVRRHEPQHFARISTVLLPKDYLR 159
Cdd:cd07808 81 GLVLLDKNGRPLRPAILWNDQRSAAECEELEArLGDEILIITGNPPLPGFTLPKLLWLKENEPEIFARIRKILLPKDYLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 160 FKMTGQKISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSATLSPEVASRWGLTSSVVVAGGGGDNAV 239
Cdd:cd07808 161 YRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAAEELGLPEGTPVVAGAGDNAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 240 SAIGVGAVSPGDAFISLGTSGVLFVVTDAYRPAPQSAVHAFCHVLPNLWHQMSVMLSAASCLQWFCRLVGvTETELLEEI 319
Cdd:cd07808 241 AALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLHTFPHAVPGKWYAMGVTLSAGLSLRWLRDLFG-PDRESFDEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 320 AQLSDADKASA--PMFLPYLSGERTPHNDPHARGLFWALTHSSQRALMGYAVLEGVSFGIADGLRVLQESGTAIEQCSLV 397
Cdd:cd07808 320 DAEAAKVPPGSegLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVLKELGIKVKEIRLI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 398 GGGARSPFWAQLLADILDMPVVTHKGGEtGGALGAARLACLAAG--KPLAAVCEK-PEIFKTWRSDPERHNALMQRYQQF 474
Cdd:cd07808 400 GGGAKSPLWRQILADVLGVPVVVPAEEE-GSAYGAALLAAVGAGvfDDLEEAAAAcIKIEKTIEPDPERHEAYDELYARY 478
|
....
gi 446202723 475 TALY 478
Cdd:cd07808 479 RELY 482
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
1-478 |
0e+00 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 583.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 1 MYLGIDLGTSEVKALVIDENNEIVATHSAPLTIQRPHPHWSEQSPQAWWEATEYLMSTLREKcgHHWQAIKAIGLSGQMH 80
Cdd:PRK15027 1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQ--HSLQDVKALGIAGQMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 81 GAVLLDEKGEAIRPAILWNDTRSAQECAELEEIAPELHQVAGNLAMPGFTAPKLLWVRRHEPQHFARISTVLLPKDYLRF 160
Cdd:PRK15027 79 GATLLDAQQRVLRPAILWNDGRCAQECALLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 161 KMTGQKISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSATLSPEVASRWGLTSSVVVAgGGGDNAVS 240
Cdd:PRK15027 159 RMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAKAWGMATVPVVA-GGGDNAAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 241 AIGVGAVSPGDAFISLGTSGVLFVVTDAYRPAPQSAVHAFCHVLPNLWHQMSVMLSAASCLQWFCRLVGVTETELLEEIA 320
Cdd:PRK15027 238 AVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWAAKLTGLSNVPALIAAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 321 QLSDaDKASAPMFLPYLSGERTPHNDPHARGLFWALTHSSQRALMGYAVLEGVSFGIADGLRVLQESGTAIEQCSLVGGG 400
Cdd:PRK15027 318 QQAD-ESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTLIGGG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 401 ARSPFWAQLLADILDMPVVTHKGGETGGALGAARLACLAAG--KPLAAVCEKPEIFKTWRSDPERHNALMQRYQQFTALY 478
Cdd:PRK15027 397 ARSEYWRQMLADISGQQLDYRTGGDVGPALGAARLAQIAANpeKSLIELLPQLPLEQSHLPDAQRYAAYQPRRETFRRLY 476
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
3-474 |
3.63e-148 |
|
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: 432.33 E-value: 3.63e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 3 LGIDLGTSEVKALVIDENNEIVATHSAPLTIQRPHPHWSEQSPQAWWEATEYLMSTLREKCGHHWQAIKAIGLSGQMHGA 82
Cdd:cd07805 3 LAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 83 VLLDEKGEAIRPAILWNDTRSAQECAELEEIAPELHQVA---GNLAMPGFTAPKLLWVRRHEPQHFARISTVLLPKDYLR 159
Cdd:cd07805 83 VPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRlggGNPPSGKDPLAKILWLKENEPEIYAKTHKFLDAKDYLN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 160 FKMTGQKISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSATLSPEVASRWGLTSSVVVAGGGGDNAV 239
Cdd:cd07805 163 FRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAAAELGLPAGTPVVGGGGDAAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 240 SAIGVGAVSPGDAFISLGTSGVLFVVTDAYRPAPQSAVHAFCHVLPNLWHQMSVMLSAASCLQWFCRLVGVTET------ 313
Cdd:cd07805 243 AALGAGAVEEGDAHIYLGTSGWVAAHVPKPKTDPDHGIFTLASADPGRYLLAAEQETAGGALEWARDNLGGDEDlgaddy 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 314 ELLEEIAQLSDAdKASAPMFLPYLSGERTPHNDPHARGLFWALTHSSQRALMGYAVLEGVSFGIADGLRVLQESGTAIEQ 393
Cdd:cd07805 323 ELLDELAAEAPP-GSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWLLEALEKLTRKIDE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 394 CSLVGGGARSPFWAQLLADILDMPVVTHKGGETGGALGAARLACLAAG--KPLAAVCEKPEIFKTWRSDPERHNALMQRY 471
Cdd:cd07805 402 LRLVGGGARSDLWCQILADVLGRPVEVPENPQEAGALGAALLAAVGLGllKSFDEAKALVKVEKVFEPDPENRARYDRLY 481
|
...
gi 446202723 472 QQF 474
Cdd:cd07805 482 EVF 484
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
1-441 |
1.53e-143 |
|
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: 418.88 E-value: 1.53e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 1 MYLGIDLGTSEVKALVID-ENNEIVATHSAPLTIQRPHPHWSEQSPQAWWEATEYLMSTLREKCGHHWQAIKAIGLSGQM 79
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 80 HGAVLLDEKGEAIRPAILWNDTRSAQECAEL-EEIAPELHQVAGNLAMPGFTAPKLLWVRRHEPQHFARISTVLLPKDYL 158
Cdd:cd07809 81 HGLVALDADGKVLRPAKLWCDTRTAPEAEELtEALGGKKCLLVGLNIPARFTASKLLWLKENEPEHYARIAKILLPHDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 159 RFKMTGQKISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRAN---MPELVEGCDVSATLSPEVASRWGLTSSVVVAGGGG 235
Cdd:cd07809 161 NWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAIDPSRDLrdlLPEVLPAGEVAGRLTPEGAEELGLPAGIPVAPGEG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 236 DNAVSAIGVGAVSPGDAFISLGTSGVLFVVTDAYRPAPQSAVHAFCHVLPNLWHQMSVMLSAASCLQWFCRLVGVTETEL 315
Cdd:cd07809 241 DNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSDPHGRVATFCDSTGGMLPLINTTNCLTAWTELFRELLGVSYEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 316 LEEIAQlsDADKASAPMFLPYLSGERTPHNdPHARGLFWALTHSS-QRALMGYAVLEGVSFGIADGLRVLQESGTAIEQC 394
Cdd:cd07809 321 DELAAQ--APPGAGGLLLLPFLNGERTPNL-PHGRASLVGLTLSNfTRANLARAALEGATFGLRYGLDILRELGVEIDEI 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 446202723 395 SLVGGGARSPFWAQLLADILDMPVVTHKGGEtGGALGAARLACLAAG 441
Cdd:cd07809 398 RLIGGGSKSPVWRQILADVFGVPVVVPETGE-GGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
1-436 |
5.42e-130 |
|
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: 382.30 E-value: 5.42e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 1 MYLGIDLGTSEVKALVIDENNEIVATHSAPLTIQRPHPHWSEQSPQAWWEAteyLMSTLREKCGHH---WQAIKAIGLSG 77
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQA---VVEAIREVLAKAgidPSDIAAIGISG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 78 QMHGAVLLDEKGEAIRPAILWNDTRSaqecaeleeiapelhqvagnlampgftapkllwvrrhepqhfarisTVLLPKDY 157
Cdd:cd00366 78 QMPGVVLVDADGNPLRPAIIWLDRRA----------------------------------------------KFLQPNDY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 158 LRFKMTGQKISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSATLSPEVASRWGLTSSVVVAGGGGDN 237
Cdd:cd00366 112 IVFRLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGGDT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 238 AVSAIGVGAVSPGDAFISLGTSGVLFVVTDAYRPaPQSAVHAFCHVLPNLWHQMSVMLSAASCLQWFCRLVGVTETELLE 317
Cdd:cd00366 192 AAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVP-PDPRLLNRCHVVPGLWLLEGAINTGGASLRWFRDEFGEEEDSDAE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 318 EIAQLSDADKASAP----MFLPYLSGERTPHNDPHARGLFWALTHSSQRALMGYAVLEGVSFGIADGLRVLQESGTAIEQ 393
Cdd:cd00366 271 YEGLDELAAEVPPGsdglIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEILEELGVKIKE 350
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 446202723 394 CSLVGGGARSPFWAQLLADILDMPVVTHKGGEtGGALGAARLA 436
Cdd:cd00366 351 IRVTGGGAKSRLWNQIKADVLGVPVVVPEVAE-GAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
1-441 |
5.30e-127 |
|
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: 376.87 E-value: 5.30e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 1 MYLGIDLGTSEVKALVIDENNEIVATHSAPLTIQRPHPHWSEQSPQAWWEATEYLMSTLREKCGHHWQAIKAIGLSGqMH 80
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSG-LV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 81 GA-VLLDEKGEAIRPAILWNDTRSAQECAELEEIAPE--LHQVAGNLAMPGFTAPKLLWVRRHEPQHFARISTVLLPKDY 157
Cdd:cd07804 80 PAlVPVDENGKPLRPAILYGDRRATEEIEWLNENIGEdrIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRKFLGAYDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 158 LRFKMTGQKISDMSDSA--GTLWlDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSATLSPEVASRWGLTSSVVVAGGGG 235
Cdd:cd07804 160 IVYKLTGEYVIDYSSAGneGGLF-DIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEAAEETGLAEGTPVVAGTV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 236 DNAVSAIGVGAVSPGDAFISLGTSGVLFVVTDAYRPAPQSAVHAfcHVLPNLWHQMSVMLSAASCLQWFCRLVGVTETEL 315
Cdd:cd07804 239 DAAASALSAGVVEPGDLLLMLGTAGDIGVVTDKLPTDPRLWLDY--HDIPGTYVLNGGMATSGSLLRWFRDEFAGEEVEA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 316 LEEIA----QLSDADKASAP------MFLPYLSGERTPHNDPHARGLFWALTHSSQRALMGYAVLEGVSFGIADGLRVLQ 385
Cdd:cd07804 317 EKSGGdsayDLLDEEAEKIPpgsdglIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYGLRHHLEVIR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446202723 386 ESGTAIEQCSLVGGGARSPFWAQLLADILDMPVVTHKGGeTGGALGAARLACLAAG 441
Cdd:cd07804 397 EAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDT-VGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
1-441 |
4.37e-124 |
|
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: 369.22 E-value: 4.37e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 1 MYLGIDLGTSEVKALVIDENNEIVATHSAPLTIQRPHPHWSEQSPQAWWEATEYLMSTLREKCGHHwqAIKAIGLSGQMH 80
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGPD--PIAAISVSSQGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 81 GAVLLDEKGEAIRPAILWNDTRSAQECAELEEI--APELHQVAGNLAMPGFTAPKLLWVRRHEPQHFARISTVLLPKDYL 158
Cdd:cd07773 79 SGVPVDRDGEPLGPAIVWFDPRGKEEAEELAERigAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAKWLSVADYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 159 RFKMTGQKISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSATLSPEVASRWGLTSSVVVAGGGGDNA 238
Cdd:cd07773 159 AYRLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEELGLPAGTPVVVGGHDHL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 239 VSAIGVGAVSPGDAFISLGTSGVLFVVTDAYRP--APQSAVHAFCHVLPNLWHQMSVMLSAASCLQWFCRLVGVTETELL 316
Cdd:cd07773 239 CAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLdeMLAEGGLSYGHHVPGGYYYLAGSLPGGALLEWFRDLFGGDESDLA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 317 EEIAQLSDA-DKASAPMFLPYLSGERTPHNDPHARGLFWALTHSSQRALMGYAVLEGVSFGIADGLRVLQESGTAIEQCS 395
Cdd:cd07773 319 AADELAEAApPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEALEKAGIPIDEIR 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 446202723 396 LVGGGARSPFWAQLLADILDMPVVTHKGGETgGALGAARLACLAAG 441
Cdd:cd07773 399 AVGGGARSPLWLQLKADILGRPIEVPEVPEA-TALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
2-441 |
1.65e-122 |
|
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: 365.34 E-value: 1.65e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 2 YLGIDLGTSEVKALVIDENNEIVATHSAPLTIQRPHPHWSEQSPQAWWEATEYLMSTLREKCGHHWQAIKAIGLSGQMHG 81
Cdd:cd07802 2 LLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 82 AVLLDEKGEAIRPAILWNDTRSAQECAELEE--IAPELHQVAGNLAMPGFTAPKLLWVRRHEPQHFARISTVLLPKDYLR 159
Cdd:cd07802 82 LYLVDKDGKPVRNAILSNDSRAADIVDRWEEdgTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRIRTVLFCKDWIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 160 FKMTGQKISDMSDsAGTLWLDVEKRDWSDSLLEKCGLT--RANMPELVEGCDVSATLSPEVASRWGLTSSVVVAGGGGDN 237
Cdd:cd07802 162 YRLTGEISTDYTD-AGSSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVTAEAAALTGLPEGTPVAAGAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 238 AVSAIGVGAVSPGDAFISLGTSGVLFVVTDAYRPAPQSAVHaFCHVLPNLWHQMSVMLSAASCLQWFCRLVGVTET---- 313
Cdd:cd07802 241 VASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDSVGSN-SLHADPGLYLIVEASPTSASNLDWFLDTLLGEEKeagg 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 314 ----ELLEEIAQLSDAdkASAPMFLPYLSGERTphnDPHARGLFWALTHSSQRALMGYAVLEGVSFGIADGLRVLQESGt 389
Cdd:cd07802 320 sdydELDELIAAVPPG--SSGVIFLPYLYGSGA---NPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLVAR- 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 446202723 390 AIEQCSLVGGGARSPFWAQLLADILDMPVVTHKGGETgGALGAARLACLAAG 441
Cdd:cd07802 394 KPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEEL-GALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
1-478 |
4.28e-120 |
|
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: 360.33 E-value: 4.28e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 1 MYLGIDLGTSEVKALVIDENNEIVATHSAPLTIQRPHPHWSEQSPQAWWEATEYLMSTLREKCGHHwqAIKAIGLSGQMH 80
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGG--EVDAIGFSSAMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 81 GAVLLDEKGEAIRPAILWNDTRSAQECAEL--EEIAPELHQVAGNLAMPGFTAPKLLWVRRHEPQHFARISTVLLPKDYL 158
Cdd:cd07770 79 SLLGVDEDGEPLTPVITWADTRAAEEAERLrkEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAAKFVSIKEYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 159 RFKMTGQKISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSATLSPEVASRWGLTSSVVVAGGGGDNA 238
Cdd:cd07770 159 LYRLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAERLGLLAGTPVVLGASDGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 239 VSAIGVGAVSPGDAFISLGTSGVLFVVTDAYRPAPQSAVhaFCHVLP-NLWhqmsvmLS------AASCLQWFCRLVG-- 309
Cdd:cd07770 239 LANLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPGRL--WCYRLDeNRW------LVggainnGGNVLDWLRDTLLls 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 310 VTETELLEEIAQLSDADkASAPMFLPYLSGERTPHNDPHARGLFWALTHSSQRALMGYAVLEGVSFGIADGLRVLQESGT 389
Cdd:cd07770 311 GDDYEELDKLAEAVPPG-SHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEALEELAG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 390 AIEQCSLVGGGARSPFWAQLLADILDMPVVTHKGGEtGGALGAARLACLAAGK-PLAAVCEKPEIFKTWRSDPERHNALM 468
Cdd:cd07770 390 PVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEE-ASALGAALLALEALGLiSSLEADELVKIGKVVEPDPENHAIYA 468
|
490
....*....|
gi 446202723 469 QRYQQFTALY 478
Cdd:cd07770 469 ELYERFKKLY 478
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
1-436 |
5.50e-120 |
|
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: 358.07 E-value: 5.50e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 1 MYLGIDLGTSEVKALVIDENNEIVATHSAPLTIQRPHPHWSEQSPQAWWEATEYLMSTLREKCGhhWQAIKAIGLSGQMH 80
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELR--PRRVVAIAVDGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 81 GAVLLDEKGEAIRPAILWNDTRSAQECAELEEIAPELHQVAGNLAMPGFTAPKLLWVRRHEPQHFARISTVLLPKDYLRF 160
Cdd:cd07783 79 TLVLVDREGEPLRPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFLHQADWLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 161 KMTGQK-ISDMSdSAGTLWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSATLSPEVASRWGLTSSVVVAGGGGDNAV 239
Cdd:cd07783 159 RLTGDRgVTDYN-NALKLGYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLPAGTPVVAGTTDSIA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 240 SAIGVGAVSPGDAFISLGTSGVLFVVTDAYRPAPQSAVHafCHVLP-NLWhqmsvMLSAAS-----CLQWFcrlvgvTET 313
Cdd:cd07783 238 AFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGVY--SHRHGdGYW-----LVGGASntggaVLRWF------FSD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 314 ELLEEIAQLSDADKASAPMFLPY-LSGERTPHNDPHARGLFWALTHSsqRALMGYAVLEGVSFGIADGLRVLQESG-TAI 391
Cdd:cd07783 305 DELAELSAQADPPGPSGLIYYPLpLRGERFPFWDPDARGFLLPRPHD--RAEFLRALLEGIAFIERLGYERLEELGaPPV 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 446202723 392 EQCSLVGGGARSPFWAQLLADILDMPVVTHKggETGGALGAARLA 436
Cdd:cd07783 383 EEVRTAGGGARNDLWNQIRADVLGVPVVIAE--EEEAALGAALLA 425
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
1-441 |
3.21e-115 |
|
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: 346.04 E-value: 3.21e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 1 MYLGIDLGTSEVKALVIDENNEIVATHSAPLTIQRPHPHWSEQSPQAWWEATEYLMSTLREKCGHHWQAIKAIGLSGQMH 80
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 81 GAVLLDEKGEAIRPAILWNDTRSAqecaeleeiapelhqvagnlampgftapkllwvrrhepqhfarisTVLLPKDYLRF 160
Cdd:cd07779 81 TFVPVDEDGRPLRPAISWQDKRTA---------------------------------------------KFLTVQDYLLY 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 161 KMTGQKISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSATLSPEVASRWGLTSSVVVAGGGGDNAVS 240
Cdd:cd07779 116 RLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAAEETGLPEGTPVVAGGGDQQCA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 241 AIGVGAVSPGDAFISLGTSGVLFVVTDAYRPAPQSAVHAFCHVLPNLWHQMSVMLSAASCLQWFCRLVGVTET------- 313
Cdd:cd07779 196 ALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWVLEGSINTGGSAVRWFRDEFGQDEVaekelgv 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 314 ---ELLEEIAQLSDADkASAPMFLPYLSGERTPHNDPHARGLFWALTHSSQRALMGYAVLEGVSFGIADGLRVLQESGTA 390
Cdd:cd07779 276 spyELLNEEAAKSPPG-SDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELRDNLEAMEKAGVP 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 446202723 391 IEQCSLVGGGARSPFWAQLLADILDMPVVTHKGGETgGALGAARLACLAAG 441
Cdd:cd07779 355 IEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEA-TALGAAILAAVGAG 404
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
1-441 |
5.71e-104 |
|
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: 318.03 E-value: 5.71e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 1 MYLGIDLGTSEVKALVIDENNEIVATHSAPLTIQRPHPHWSEQSPQAWWEATEYLMSTLREKCGHHWQAIKAIGLSGQMH 80
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 81 GAVLLDEKGEAIRPAILWNDTRSAQECAELEE--IAPELHQVAGNLAMPGFTAPKLLWVRRHEPQHFARISTVLLPKDYL 158
Cdd:cd24121 81 GTWLVDEDGRPVRDAILWLDGRAADIVERWQAdgIAEAVFEITGTGLFPGSQAAQLAWLKENEPERLERARTALHCKDWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 159 RFKMTGQKISDMSDSAGTlWLDVEKRDWSDSLLEKCGLT--RANMPELVEGCDVSATLSPEVASRWGLTSSVVVAGGGGD 236
Cdd:cd24121 161 FYKLTGEIATDPSDASLT-FLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAAAATGLPAGTPVVLGPFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 237 NAVSAIGVGAVSPGDAFISLGTSGVLFVVTDAYRPAPQSAVHAFCHVLPNLWHQMSVMLSAASCLQWFCRLVGVTETE-- 314
Cdd:cd24121 240 VVATALGSGAIEPGDACSILGTTGVHEVVVDEPDLEPEGVGYTICLGVPGRWLRAMANMAGTPNLDWFLRELGEVLKEga 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 315 --LLEEIAQLSDADKASAP------MFLPYLS--GERTPHNDPHARGLFWALTHSSQRALMGYAVLEGVSFGIADglrVL 384
Cdd:cd24121 320 epAGSDLFQDLEELAASSPpgaegvLYHPYLSpaGERAPFVNPNARAQFTGLSLEHTRADLLRAVYEGVALAMRD---CY 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 446202723 385 QESGTAIEQCSLVGGGARSPFWAQLLADILDMPVVTHKGGETgGALGAARLACLAAG 441
Cdd:cd24121 397 EHMGEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEF-GARGAAMNAAVALG 452
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
1-243 |
4.93e-87 |
|
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: 266.90 E-value: 4.93e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 1 MYLGIDLGTSEVKALVIDENNEIVATHSAPLTIQRPHPHWSEQSPQAWWEAteyLMSTLREKCGHHW---QAIKAIGLSG 77
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQA---VAQCIAKTLSQLGislKQIKGIGISN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 78 QMHGAVLLDEKGEAIRPAILWNDTRSAQECAELEE--IAPELHQVAGNLAMPGFTAPKLLWVRRHEPQHFARISTVLLPK 155
Cdd:pfam00370 78 QGHGTVLLDKNDKPLYNAILWKDRRTAEIVENLKEegNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 156 DYLRFKMTGQKISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSATLSPEVASRWGLTSSVVVAGGGG 235
Cdd:pfam00370 158 DYLRWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGG 237
|
....*...
gi 446202723 236 DNAVSAIG 243
Cdd:pfam00370 238 DQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
2-478 |
4.64e-82 |
|
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: 262.86 E-value: 4.64e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 2 YLGIDLGTSEVKALVIDENN-EIVATHSAPLTI--QRPHPHWSEQSPQAWWEATEYLMSTLREKCGHHWQAIKAIGLSGQ 78
Cdd:cd07781 2 VIGIDFGTQSVRAGLVDLADgEELASAVVPYPTgyIPPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 79 MHGAVLLDEKGEAIRPAILWNDTRSAQECAELEEIAPELHQVAGNLAMPGFTA----PKLLWVRRHEPQHFARISTVLLP 154
Cdd:cd07781 82 SSTVVPVDEDGNPLAPAILWMDHRAQEEAAEINETAHPALEYYLAYYGGVYSSewmwPKALWLKRNAPEVYDAAYTIVEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 155 KDYLRFKMTGQKISDMSdSAGTLWL-DVEKRDWSDSLLEKCGL----TRANMPELVEGCDVSA-TLSPEVASRWGLTSSV 228
Cdd:cd07781 162 CDWINARLTGRWVRSRC-AAGHKWMyNEWGGGPPREFLAALDPgllkLREKLPGEVVPVGEPAgTLTAEAAERLGLPAGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 229 VVAGGGGDNAVSAIGVGAVSPGDAFISLGTSGVLFVVTDAYRPAPqsavhAFC-----HVLPNLWhqmsvML-----SAA 298
Cdd:cd07781 241 PVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTCHLMVSPKPVDIP-----GICgpvpdAVVPGLY-----GLeagqsAVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 299 SCLQWFCRLVGVTETELLEEI-AQLSDADKASAP-----MFLPYLSGERTPHNDPHARGLFWALTHSSQRALMGYAVLEG 372
Cdd:cd07781 311 DIFAWFVRLFVPPAEERGDSIyALLSEEAAKLPPgesglVALDWFNGNRTPLVDPRLRGAIVGLTLGTTPAHIYRALLEA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 373 VSFGIADGLRVLQESGTAIEQCSLVGGGA-RSPFWAQLLADILDMPVVTHKGGETgGALGAARLACLAAG--KPLAAVCE 449
Cdd:cd07781 391 TAFGTRAIIERFEEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQA-PALGAAILAAVAAGvyADIEEAAD 469
|
490 500 510
....*....|....*....|....*....|
gi 446202723 450 K-PEIFKTWRSDPERHNALMQRYQQFTALY 478
Cdd:cd07781 470 AmVRVDRVYEPDPENHAVYEELYALYKELY 499
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
2-441 |
5.99e-73 |
|
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: 237.51 E-value: 5.99e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 2 YLGIDLGTSEVKALVIDENNEIVATHSAPLTIQRP--HPHWSEQSPQAWWEATEYLMSTLREKCGHHWQAIKAIGLSGQM 79
Cdd:cd07798 2 YLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDddYPDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTSQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 80 HGAVLLDEKGEAIR--PAIlwnDTRSAQECAEL-EEIAPELHQVAGNLAMPGFTAPKLLWVRRHEPQHFARISTVLLPKD 156
Cdd:cd07798 82 EGIVFLDKDGRELYagPNI---DARGVEEAAEIdDEFGEEIYTTTGHWPTELFPAARLLWFKENRPEIFERIATVLSISD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 157 YLRFKMTGQKISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSATLSPEVASRWGLTSSVVVAGGGGD 236
Cdd:cd07798 159 WIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAARELGLPEGTPVVVGGAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 237 NAVSAIGVGAVSPGDAFISLGTSGVLFVVTDAYRPAPQSAVHAFCHVLPNLWHQMSVMLSAASCLQWFCRLVGVTET--- 313
Cdd:cd07798 239 TQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTGCHLVPGKWVLESNAGVTGLNYQWLKELLYGDPEdsy 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 314 ELLEEIAQLSD--ADKASA---PMFLPYLSGERTPHndpharGLFW---ALTHSSQRALMGYAVLEGVSFGIADGLRVLQ 385
Cdd:cd07798 319 EVLEEEASEIPpgANGVLAflgPQIFDARLSGLKNG------GFLFptpLSASELTRGDFARAILENIAFAIRANLEQLE 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 446202723 386 E-SGTAIEQCSLVGGGARSPFWAQLLADILDMPVVTHKGGEtGGALGAARLACLAAG 441
Cdd:cd07798 393 EvSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGRE-ASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
3-472 |
4.25e-59 |
|
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: 201.93 E-value: 4.25e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 3 LGIDLGTSEVKALVIDENNEIVATHSAPLTIQRPHPHWSEQSPQAWWEATEYLMSTLREKCGHHWQAIKAIGLSGQMHGA 82
Cdd:cd07769 3 LAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRETT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 83 VLLDEK-GEAIRPAILWNDTRSAQECAELEE--IAPELHQVAGNLAMPGFTAPKLLWVRRHEPQHFARIS-------TVl 152
Cdd:cd07769 83 VVWDKKtGKPLYNAIVWQDRRTADICEELKAkgLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAErgellfgTI- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 153 lpkD-YLRFKMTGQK--ISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSATLSPEvasrwGLTSSVV 229
Cdd:cd07769 162 ---DtWLIWKLTGGKvhVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTDPE-----GLGAGIP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 230 VAGGGGDNAVSAIGVGAVSPGDAFISLGTSGVLFVVTDAYRPAPQSAV---------HAFCHVLpnlwhQMSVMlSAASC 300
Cdd:cd07769 234 IAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLlttiawqigGKVTYAL-----EGSIF-IAGAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 301 LQWFCRLVG----VTETellEEIA-QLSDADKAsapMFLPYLSGERTPHNDPHARGLFWALTHSSQRALMGYAVLEGVSF 375
Cdd:cd07769 308 IQWLRDNLGliedAAET---EELArSVEDNGGV---YFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 376 GIADGLRVLQE-SGTAIEqcSL-VGGGA-RSPFWAQLLADILDMPVVTHKGGETgGALGAARLACLAAG--KPLAAVCEK 450
Cdd:cd07769 382 QTRDVLEAMEKdSGIKLK--ELrVDGGAtANNFLMQFQADILGVPVVRPKVAET-TALGAAYLAGLAVGfwKDLDELASL 458
|
490 500
....*....|....*....|....
gi 446202723 451 PEIFKTWRS--DPERHNALMQRYQ 472
Cdd:cd07769 459 WQVDKRFEPsmDEEERERLYRGWK 482
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
1-436 |
2.32e-55 |
|
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: 190.90 E-value: 2.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 1 MYLGIDLGTSEVKALVID-ENNEIVATHSAP--LTIQRPHPHWSEQSPQAWWEATEYLMSTLrekCGHHWQAIKAIGLSG 77
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDlESGRILESVSRPtpAPISSDDPGRSEQDPEKILEAVRNLIDEL---PREYLSDVTGIGITG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 78 QMHGAVLLDEKGEAIRPAILWNDTR-SAQECAELEEIAPEL-HQVAGNLAmPGFTAPKLLWVRRH--EPQHFARISTVLl 153
Cdd:cd07777 78 QMHGIVLWDEDGNPVSPLITWQDQRcSEEFLGGLSTYGEELlPKSGMRLK-PGYGLATLFWLLRNgpLPSKADRAGTIG- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 154 pkDYLRFKMTGQK--ISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSATLSPEvasrwgLTSSVVVA 231
Cdd:cd07777 156 --DYIVARLTGLPkpVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLSSA------LPKGIPVY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 232 GGGGDNAVSAIGVGAVSPGDAFISLGTSGVLFVVTDA--------YRPAPQSAvhaFCHV---LP--NLWHQMSVMLsaA 298
Cdd:cd07777 228 VALGDNQASVLGSGLNEENDAVLNIGTGAQLSFLTPKfelsgsveIRPFFDGR---YLLVaasLPggRALAVLVDFL--R 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 299 SCLQWFCrlVGVTETELLEEIAQLSDADKASAPMFLPYLSGERTphnDPHARGLFWALTHS--SQRALMgYAVLEGVSFG 376
Cdd:cd07777 303 EWLRELG--GSLSDDEIWEKLDELAESEESSDLSVDPTFFGERH---DPEGRGSITNIGESnfTLGNLF-RALCRGIAEN 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446202723 377 IADGLRVLQESGTAIEQCSLVGGGAR-SPFWAQLLADILDMPVVTHKGGEtGGALGAARLA 436
Cdd:cd07777 377 LHEMLPRLDLDLSGIERIVGSGGALRkNPVLRRIIEKRFGLPVVLSEGSE-EAAVGAALLA 436
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
3-473 |
1.84e-51 |
|
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: 181.54 E-value: 1.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 3 LGIDLGTSEVKALVIDENNEIVATHSAPLTIQRPHPHWSEQSPQAWWEATEYLMSTLREKCGHHWQAIKAIGLSGQMHGA 82
Cdd:cd07786 3 LAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRETT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 83 VLLDEK-GEAIRPAILWNDTRSAQECAELEE--IAPELHQVAGNLAMPGFTAPKLLWVRRHEPQHFARIS-------TVl 152
Cdd:cd07786 83 VVWDREtGKPVYNAIVWQDRRTADICEELKAegHEEMIREKTGLVLDPYFSATKIRWILDNVPGARERAErgelafgTI- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 153 lpkD-YLRFKMTGQK--ISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSATLSPEvasrwGLTSSVV 229
Cdd:cd07786 162 ---DsWLIWKLTGGKvhATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDPD-----LLGAEIP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 230 VAGGGGDNAVSAIGVGAVSPGDAFISLGTSGVLFVVTDAYRPAPQSAvhafchVLPNLWHQM----------SVMlSAAS 299
Cdd:cd07786 234 IAGIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNG------LLTTIAWQLggkvtyalegSIF-IAGA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 300 CLQWF---CRLVGVT-ETELLEEiaQLSDADKAsapMFLPYLSGERTPHNDPHARGLFWALTHSSQRALMGYAVLEGVSF 375
Cdd:cd07786 307 AVQWLrdgLGLIESAaETEALAR--SVPDNGGV---YFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 376 GIADGLRVLQE-SGTAIEQCSLVGGGARSPFWAQLLADILDMPVVTHKGGETgGALGAARLACLAAG--KPLAAVCEKPE 452
Cdd:cd07786 382 QTRDLLEAMEAdSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTET-TALGAAYLAGLAVGlwKSLDELAKLWQ 460
|
490 500
....*....|....*....|...
gi 446202723 453 IFKTWRS--DPERHNALMQRYQQ 473
Cdd:cd07786 461 VDRRFEPsmSEEEREALYAGWKK 483
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
2-474 |
8.09e-50 |
|
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: 177.52 E-value: 8.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 2 YLGIDLGTSEVKALVIDENNEIVATHsapltiQRPHPHWSEQS-PQA----WWEATEYLMSTLRE---KCGHHWQAIKAI 73
Cdd:cd07775 2 LLALDAGTGSGRAVIFDLEGNQIAVA------QREWRHKEVPDvPGSmdfdTEKNWKLICECIREalkKAGIAPKSIAAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 74 GLSGQMHGAVLLDEKGEAIrpailWN----DTRSAQECAELEEIAPELHQVAGNLAMPGFT---APKLLWVRRHEPQHFA 146
Cdd:cd07775 76 STTSMREGIVLYDNEGEEI-----WAcanvDARAAEEVSELKELYNTLEEEVYRISGQTFAlgaIPRLLWLKNNRPEIYR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 147 RISTVLLPKDYLRFKMTGQKISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSATLSPEVASRWGLTS 226
Cdd:cd07775 151 KAAKITMLSDWIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEAAEETGLKE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 227 SVVVAGGGGDNAVSAIGVGAVSPGDAFISLGTSGVLFVVTDAYRPAPQSAVHAFCHVLPNLWHQMSVMLSAASCLQWF-- 304
Cdd:cd07775 231 GTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMNIRVNCHVIPDMWQAEGISFFPGLVMRWFrd 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 305 ---CRLV------GVTETELLEEIAQL------------SDAD-----KASAPMFLPY-LSGERTphndphARGLFWalt 357
Cdd:cd07775 311 afcAEEKeiaerlGIDAYDLLEEMAKDvppgsygimpifSDVMnyknwRHAAPSFLNLdIDPEKC------NKATFF--- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 358 hssqRALMGYAVLegVSFGiaDGLRVLQESGTAIEQCSLVGGGARSPFWAQLLADILDMPVVTHKGGETgGALGAARLAC 437
Cdd:cd07775 382 ----RAIMENAAI--VSAG--NLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEA-TALGAAIAAG 452
|
490 500 510
....*....|....*....|....*....|....*..
gi 446202723 438 LAAGKpLAAVCEKPEIFKTWRSDPERHNALMQRYQQF 474
Cdd:cd07775 453 VGAGI-YSSLEEAVESLVKWEREYLPNPENHEVYQDL 488
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
3-441 |
8.06e-48 |
|
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: 172.36 E-value: 8.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 3 LGIDLGTSEVKALVIDENNEIVATHSAPLTIQRPHPHWSEQSPQAWWEATEYLMSTLREKCGHHWQAIKAIGLSGQMHGA 82
Cdd:cd07793 3 LAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQRNTF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 83 VLLDEK-GEAIRPAILWNDTRSAQECAE---------LEEIAPELHQVAGN---LA------MPGFTAPKLLWVRRHEPQ 143
Cdd:cd07793 83 LTWDKKtGKPLHNFITWQDLRAAELCESwnrslllkaLRGGSKFLHFLTRNkrfLAasvlkfSTAHVSIRLLWILQNNPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 144 hfARIstvLLPKDYLRF---------KMTGQK--ISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSA 212
Cdd:cd07793 163 --LKE---AAEKGELLFgtidtwllwKLTGGKvhATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 213 TLSPEVasrwgLTSSVVVAGGGGDNAVSAIGVGAVSPGDAFISLGTSGVLFVVTDayrpapqSAVHAFCHVLPNL--WH- 289
Cdd:cd07793 238 STDPSI-----FGAEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTG-------SKPHASVKGLYPLvgWKi 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 290 ----------QMSvmlSAASCLQWFCRLVGVTETELLEEIA-QLSDADKASapmFLPYLSGERTPHNDPHARGLFWALTH 358
Cdd:cd07793 306 ggeitylaegNAS---DTGTVIDWAKSIGLFDDPSETEDIAeSVEDTNGVY---FVPAFSGLQAPYNDPTACAGFIGLTP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 359 SSQRALMGYAVLEGVSFGIADGLR-VLQESGTAIEQCSLVGGGARSPFWAQLLADILDMPVVTHKGGETgGALGAARLAC 437
Cdd:cd07793 380 STTKAHLVRAILESIAFRVKQLLEtMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEM-SALGAAFLAG 458
|
....
gi 446202723 438 LAAG 441
Cdd:cd07793 459 LASG 462
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
2-486 |
6.79e-47 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 170.30 E-value: 6.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 2 YLGIDLGTSEVKALVIDENN-EIVATHSAPLTIQR------PHPHWSEQSPQAWWEATEYLMSTLREKCGHHWQAIKAIG 74
Cdd:COG1069 4 VIGVDFGTDSVRAVVVDAADgEELASAVHPYPRWViglylpPPPDQARQHPLDYLEALEAAVREALAQAGVDPADVVGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 75 LSGQMHGAVLLDEKGE--AIRP---------AILWNDTRSAQECAELEEIAPE-----LHQVAGNLAMPGFTaPKLLWVR 138
Cdd:COG1069 84 VDATGCTPVPVDADGTplALLPefaenphamVILWKDHTAQEEAERINELAKArgedyLRYVGGIISSEWFW-PKILHLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 139 RHEPQHFARI-STVLLPkDYLRFKMTGqkisDMSDSAGT-----LWLDVEKRDWSDSLLEKCGLT----RANMPELVEGC 208
Cdd:COG1069 163 REDPEVYEAAdSFVELC-DWITWQLTG----SLKRSRCTaghkaLWHAHEGGYPSEEFFAALDPLldglADRLGTEIYPL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 209 DVSA-TLSPEVASRWGLTSSVVVAGGGGDNAVSAIGVGAVSPGDAFISLGTSGVLFVVTDAYRPAP------QSAVhafc 281
Cdd:COG1069 238 GEPAgTLTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGVEPGTLVKVMGTSTCHMLVSPEERFVPgicgqvDGSI---- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 282 hvLPNLW----HQmsvmlSAA-SCLQWFCRLVgVTETELLEEIAQLSD------ADKASA-------PMFLPYLSGERTP 343
Cdd:COG1069 314 --VPGMWgyeaGQ-----SAVgDIFAWFVRLL-VPPLEYEKEAEERGIslhpllTEEAAKlppgesgLHALDWFNGNRSP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 344 HNDPHARGLFWALTHSSQRALMGYAVLEGVSFG---IADglrVLQESGTAIEQCSLVGGGAR-SPFWAQLLADILDMPVV 419
Cdd:COG1069 386 LADQRLKGVILGLTLGTDAEDIYRALVEATAFGtraIIE---RFEEEGVPIDEIIACGGIATkNPLVMQIYADVTGRPIK 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446202723 420 THKGGETGgALGAARLACLAAGK------PLAAVCEKPEifKTWRSDPERHNALMQRYQQFTALYHNDLNYRN 486
Cdd:COG1069 463 VAASEQAC-ALGAAMFAAVAAGAypdveeAMAAMGSGFD--KVYTPDPENVAVYDALYAEYLQLHDYFGRGRN 532
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
3-441 |
2.95e-43 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 159.75 E-value: 2.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 3 LGIDLGTSEVKALVIDENNEIVATHSAPLTIQRPHPHWSEQSPQAWWEATEYLMSTLREKCGHHWQA--IKAIGLSGQMH 80
Cdd:PTZ00294 5 GSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKGPSfkIKAIGITNQRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 81 GAVLLDEK-GEAIRPAILWNDTRSAQECAELEEIAPE---LHQVAGNLAMPGFTAPKLLWVRRHEPQ----------HFA 146
Cdd:PTZ00294 85 TVVAWDKVtGKPLYNAIVWLDTRTYDIVNELTKKYGGsnfFQKITGLPISTYFSAFKIRWMLENVPAvkdavkegtlLFG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 147 RISTVLLpkdylrFKMTGQK--ISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSATLSPEVAsrwGL 224
Cdd:PTZ00294 165 TIDTWLI------WNLTGGKshVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTISGEAV---PL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 225 TSSVVVAGGGGDNAVSAIGVGAVSPGDAFISLGTsGVLFVVTDAYRPapqsaVHAFCHVLPNLWHQM------------S 292
Cdd:PTZ00294 236 LEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGT-GCFLLMNTGTEI-----VFSKHGLLTTVCYQLgpngptvyalegS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 293 VMlSAASCLQWFCRLVGVTETelLEEIAQLSDADKASAPM-FLPYLSGERTPHNDPHARGLFWALTHSSQRALMGYAVLE 371
Cdd:PTZ00294 310 IA-VAGAGVEWLRDNMGLISH--PSEIEKLARSVKDTGGVvFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALE 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446202723 372 GVSFGIADGLRVLQE-SGTAIEQCSLVGGGARSPFWAQLLADILDMPVVTHKGGETgGALGAARLACLAAG 441
Cdd:PTZ00294 387 AIALQTNDVIESMEKdAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAET-TALGAALLAGLAVG 456
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
3-478 |
1.25e-40 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 152.85 E-value: 1.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 3 LGIDLGTSEVKALVIDEN-NEIVATHSAPLTIQRPH-PHWSEQSPQAWWEATEYLMSTLREKCGHHWQAIKAIGLSGQMH 80
Cdd:PRK10939 6 MALDAGTGSIRAVIFDLNgNQIAVGQAEWRHLAVPDvPGSMEFDLEKNWQLACQCIRQALQKAGIPASDIAAVSATSMRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 81 GAVLLDEKGEAIrpailWN----DTRSAQECAELEEIAP----ELHQVAGN-LAMPGFtaPKLLWVRRHEPQHFARISTV 151
Cdd:PRK10939 86 GIVLYDRNGTEI-----WAcanvDARASREVSELKELHNnfeeEVYRCSGQtLALGAL--PRLLWLAHHRPDIYRQAHTI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 152 LLPKDYLRFKMTGQKISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSATLSPEVASRWGLTSSVVVA 231
Cdd:PRK10939 159 TMISDWIAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAKAAAETGLRAGTPVV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 232 GGGGDNAVSAIGVGAVSPGDAFISLGTSGVLFVVTDAYRPAPQSAVHAFCHVLPNLWHQMSVMLSAASCLQWF----CRL 307
Cdd:PRK10939 239 MGGGDVQLGCLGLGVVRPGQTAVLGGTFWQQVVNLPAPVTDPNMNIRINPHVIPGMVQAESISFFTGLTMRWFrdafCAE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 308 -------VGVTETELLEEIAQ------------LSDADKAS-----APMFLPyLSgertphNDPHArglfwalthsSQRA 363
Cdd:PRK10939 319 ekllaerLGIDAYSLLEEMASrvpvgshgiipiFSDVMRFKswyhaAPSFIN-LS------IDPEK----------CNKA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 364 LMGYAVLEGVSFGIADGL-RVLQESGTAIEQCSLVGGGARSPFWAQLLADILDMPVVTHKGGEtGGALGAARLACLAAG- 441
Cdd:PRK10939 382 TLFRALEENAAIVSACNLqQIAAFSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKE-ATALGCAIAAGVGAGi 460
|
490 500 510
....*....|....*....|....*....|....*....
gi 446202723 442 -KPLAAVCEKPEIF-KTWRSDPERHNALMQRYQQFTALY 478
Cdd:PRK10939 461 ySSLAETGERLVRWeRTFEPNPENHELYQEAKEKWQAVY 499
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
1-436 |
2.38e-40 |
|
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: 151.94 E-value: 2.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 1 MYLGIDLGTSEVKALVIDENNEIVATHSAPLTIQRPH------------PHWSEQSPQAWWEATEYLMSTLREKcGHHWQ 68
Cdd:cd07776 1 LYLGLDLSTQSLKAVVIDSDLKVVAEESVNFDSDLPEygtkggvhrdgdGGEVTSPVLMWVEALDLLLEKLKAA-GFDFS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 69 AIKAIGLSGQMHGAVLLDEKGEAIRP---------AIL-----------WNDTRSAQECAELEEI---APELHQVAGNLA 125
Cdd:cd07776 80 RVKAISGSGQQHGSVYWSKGAESALAnldpskslaEQLegafsvpdspiWMDSSTTKQCRELEKAvggPEALAKLTGSRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 126 MPGFTAPKLLWVRRHEPQHF---ARISTV------LLPKDYlrfkmtgQKIsDMSDSAGTLWLDVEKRDWSDSLLEKC-- 194
Cdd:cd07776 160 YERFTGPQIAKIAQTDPEAYentERISLVssflasLLLGRY-------API-DESDGSGMNLMDIRSRKWSPELLDAAta 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 195 -GLtRANMPELVEGCDVSATLSPEVASRWGLTSSVVVAGGGGDNAVSAIGVGaVSPGDAFISLGTSGVLFVVTDAYRPAP 273
Cdd:cd07776 232 pDL-KEKLGELVPSSTVAGGISSYFVERYGFSPDCLVVAFTGDNPASLAGLG-LEPGDVAVSLGTSDTVFLVLDEPKPGP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 274 QSavHAFCH-VLPNLWhqMSvMLsaasCL-------QWFCRLVGVTE----TELLEEIAQLSDadkasAPMFLPYLSGER 341
Cdd:cd07776 310 EG--HVFANpVDPGSY--MA-ML----CYkngslarERVRDRYAGGSwekfNELLESTPPGNN-----GNLGLYFDEPEI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 342 TPHNDP------HARGLFWALTHSSQ-------RALMGYAVLEGVSFGIaDGLRVLqesgtaieqcsLVGGGARSPFWAQ 408
Cdd:cd07776 376 TPPVPGggrrffGDDGVDAFFDPAVEvravvesQFLSMRLHAERLGSDI-PPTRIL-----------ATGGASANKAILQ 443
|
490 500
....*....|....*....|....*...
gi 446202723 409 LLADILDMPVVTHKGGEtGGALGAARLA 436
Cdd:cd07776 444 VLADVFGAPVYTLDVAN-SAALGAALRA 470
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
2-441 |
1.80e-38 |
|
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: 146.51 E-value: 1.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 2 YLG-IDLGTSEVKALVIDENNEIVATHSAPLTIQRPHPHWSEQSPQAWWEATEYLMSTLREKC---GHHWQAIKAIGLSG 77
Cdd:cd07792 2 LVGaIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLkalGISPSDIKAIGITN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 78 QMHGAVLLDEK-GEAIRPAILWNDTRSAQECAELEEIAP----ELHQVAGNLAMPGFTAPKLLWVRRHEP-------QHF 145
Cdd:cd07792 82 QRETTVVWDKStGKPLYNAIVWLDTRTSDTVEELSAKTPggkdHFRKKTGLPISTYFSAVKLRWLLDNVPevkkavdDGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 146 ARISTVllpkD-YLRFKMTGQK-----ISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVsatlspeva 219
Cdd:cd07792 162 LLFGTV----DsWLIWNLTGGKnggvhVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEV--------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 220 srWGLTSS-----VVVAGGGGDNAVSAIGVGAVSPGDAFISLGTSGVLFVVTDayrpapQSAVHAFCHVLPNLWHQM--- 291
Cdd:cd07792 229 --YGKIASgplagVPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTG------EEPVFSKHGLLTTVAYKLgpd 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 292 ---------SVMLsAASCLQWFCRLVGVTETEllEEIAQLSDADKASAPM-FLPYLSGERTPHNDPHARGLFWALTHSSQ 361
Cdd:cd07792 301 appvyalegSIAI-AGAAVQWLRDNLGIISSA--SEVETLAASVPDTGGVyFVPAFSGLFAPYWRPDARGTIVGLTQFTT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 362 RALMGYAVLEGVSFGIADGLRVL-QESGTAIEQCSLVGGGARSPFWAQLLADILDMPVVTHKGGETgGALGAARLACLAA 440
Cdd:cd07792 378 KAHIARAALEAVCFQTREILDAMnKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVET-TALGAAIAAGLAV 456
|
.
gi 446202723 441 G 441
Cdd:cd07792 457 G 457
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
2-420 |
2.96e-36 |
|
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: 139.59 E-value: 2.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 2 YLGIDLGTSEVKALV--IDEN----NEIvatHSAPLTIQRPHPHWseqspqaWWEaTEYLMSTLRE---KCGHHWQAIKA 72
Cdd:cd07771 2 YLAVDLGASSGRVILgsLDGGklelEEI---HRFPNRPVEINGHL-------YWD-IDRLFDEIKEglkKAAEQGGDIDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 73 IGLSGqmHGA--VLLDEKGEAIRPAILWNDTRSAQECAELEEIAP--ELHQVAGNLAMPGFTAPKLLWVRRHEPQHFARI 148
Cdd:cd07771 71 IGIDT--WGVdfGLLDKNGELLGNPVHYRDPRTEGMMEELFEKISkeELYERTGIQFQPINTLYQLYALKKEGPELLERA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 149 STVLLPKDYLRFKMTGQKISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSATLSPEVASRWGLTSSV 228
Cdd:cd07771 149 DKLLMLPDLLNYLLTGEKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPEVAEELGLKGIP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 229 VVAGGGGDNAvSAI-GVGAVSPGDAFISLGTSGVLFVVTDAYRPAPQSAVHAF---CHV---------LPNLWhqmsvML 295
Cdd:cd07771 229 VIAVASHDTA-SAVaAVPAEDEDAAFISSGTWSLIGVELDEPVITEEAFEAGFtneGGAdgtirllknITGLW-----LL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 296 SaaSCL-QWFCRLVGVTETELLEEIAQLSDADKA---SAPMFLP----------YL--SGERTPHNDPH-ARglfwalth 358
Cdd:cd07771 303 Q--ECRrEWEEEGKDYSYDELVALAEEAPPFGAFidpDDPRFLNpgdmpeairaYCreTGQPVPESPGEiAR-------- 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446202723 359 ssqralmgyAVLEGVSFGIADGLRVLQE-SGTAIEQCSLVGGGARSPFWAQLLADILDMPVVT 420
Cdd:cd07771 373 ---------CIYESLALKYAKTIEELEElTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIA 426
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
2-485 |
8.99e-36 |
|
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: 139.59 E-value: 8.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 2 YLGIDLGTSEVKALVIDENNEIVATHSAPLTIQRPHPHWSEQSPQAWWEATEYLMSTLREKCGHHWQAIKAIG------L 75
Cdd:cd07782 2 YIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGfdatcsL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 76 sgqmhgaVLLDEK---------GEAIRPAILWNDTRSAQECAELEEIAPELHQVAGNLAMPGFTAPKLLWVRRHEPQHFA 146
Cdd:cd07782 82 -------VVLDAEgkpvsvspsGDDERNVILWMDHRAVEEAERINATGHEVLKYVGGKISPEMEPPKLLWLKENLPETWA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 147 RISTVL-LPkDYLRFKMTGqkisDMSDSAGTL---WL----DVEKRDWSDSLLEKCGLtranmPELVE------GCDVSA 212
Cdd:cd07782 155 KAGHFFdLP-DFLTWKATG----SLTRSLCSLvckWTylahEGSEGGWDDDFFKEIGL-----EDLVEdnfakiGSVVLP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 213 -------TLSPEVASRWGLTSSVVVAGGGGDNAVSAIG-VGAVSPGD-----------AFISlGTSGVLFVVTDA----- 268
Cdd:cd07782 225 pgepvggGLTAEAAKELGLPEGTPVGVSLIDAHAGGLGtLGADVGGLpceadpltrrlALIC-GTSSCHMAVSPEpvfvp 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 269 -----YRPAP----------QSAVHAFC-HVLPNlwHqmsvmlSAASCLQWFCRLVGVTETELLEEI-AQLSDADKASAP 331
Cdd:cd07782 304 gvwgpYYSAMlpglwlneggQSATGALLdHIIET--H------PAYPELKEEAKAAGKSIYEYLNERlEQLAEEKGLPLA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 332 M------FLPYLSGERTPHNDPHARGLFWALT-HSSQR--ALMGYAVLEGVSFGIADGLRVLQESGTAIEQCSLVGGGAR 402
Cdd:cd07782 376 YltrdlhVLPDFHGNRSPLADPTLRGMISGLTlDTSLDdlALLYLATLQALAYGTRHIIEAMNAAGHKIDTIFMCGGLSK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 403 SPFWAQLLADILDMPVVTHKGGETgGALGAARLACLAAG--KPLAAVCEK---PEifKTWRSDPER---HNAlmqRYQQF 474
Cdd:cd07782 456 NPLFVQLHADVTGCPVVLPKEPEA-VLLGAAILGAVASGdfPSLWDAMAAmsgPG--KVVEPNEELkkyHDR---KYEVF 529
|
570
....*....|.
gi 446202723 475 TALYHNDLNYR 485
Cdd:cd07782 530 LKMYEDQREYR 540
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
252-440 |
2.20e-34 |
|
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: 127.83 E-value: 2.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 252 AFISLGTSGVLFVVTdayrPAPQSAVHAFCHVLPNLWHQMSVML-----SAASCLQWFCRLVGVTE-------TELLEEI 319
Cdd:pfam02782 1 LAISAGTSSFVLVET----PEPVLSVHGVWGPYTNEMLPGYWGLeggqsAAGSLLAWLLQFHGLREelrdagnVESLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 320 AQLSDADKASAPMFLPYLSGERTPHNDPHARGLFWALTHSSQRALMGYAVLEGVSFGIADGLRVL-QESGTAIEQCSLVG 398
Cdd:pfam02782 77 AALAAVAPAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALtKQEGHPIDTIHVSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446202723 399 GGARSPFWAQLLADILDMPVVTHKGGEtGGALGAARLACLAA 440
Cdd:pfam02782 157 GGSRNPLLLQLLADALGLPVVVPGPDE-ATALGAALLAAVAA 197
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
3-441 |
6.45e-33 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 130.53 E-value: 6.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 3 LGIDLGTSEVKALVIDENNEIVATHSAP----LTIQRPHPH-WS-EQSPQAWWEATEYLMSTLREkcghhwQAIKAIGLS 76
Cdd:PRK10331 5 LVLDCGATNVRAIAVDRQGKIVARASTPnasdIAAENSDWHqWSlDAILQRFADCCRQINSELTE------CHIRGITVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 77 G-QMHGAvLLDEKGEAIRPAILWNDTRSAQECAELE-EIAPE-LHQVAGNLAMPGFTAPKLLWVRRHEPQHFARISTVLL 153
Cdd:PRK10331 79 TfGVDGA-LVDKQGNLLYPIISWKCPRTAAVMENIErYISAQqLQQISGVGAFSFNTLYKLVWLKENHPQLLEQAHAWLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 154 PKDYLRFKMTGQKISDMSdSAGT-LWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSATLSPEVASRWGLTSSVVVAG 232
Cdd:PRK10331 158 ISSLINHRLTGEFTTDIT-MAGTsQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPSAAALLGLPVGIPVIS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 233 GGGDNAVSAIGVGAvSPGDAFISLGTSGVLFVVTdayrPAPQSAVHAfchvlpnLWHQMSVMLSAASCL-----QWFCRl 307
Cdd:PRK10331 237 AGHDTQFALFGSGA-GQNQPVLSSGTWEILMVRS----AQVDTSLLS-------QYAGSTCELDSQSGLynpgmQWLAS- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 308 vGVTE--TELL---EEIAQLSDADKASAPmflPYLSGER-TPHNDPHARGLFWALTHSSQRALMGYAVLEGVSFGIADGL 381
Cdd:PRK10331 304 -GVLEwvRKLFwtaETPYQTMIEEARAIP---PGADGVKmQCDLLACQNAGWQGVTLNTTRGHFYRAALEGLTAQLKRNL 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446202723 382 RVLQE-SGTAIEQCSLVGGGARSPFWAQLLADILDMPVVTHKGGETgGALGAARLACLAAG 441
Cdd:PRK10331 380 QVLEKiGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAET-TVAGAAMFGWYGVG 439
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
3-473 |
1.25e-32 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 129.94 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 3 LGIDLGTSEVKALVIDENNEIVATHSAPLTIQRPHPHWSEQSPQAWWEATEYLMSTLREKCGHHWQAIKAIGLSGQMHGA 82
Cdd:PRK00047 8 LALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGITNQRETT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 83 VLLD-EKGEAIRPAILWNDTRSAQECAELEE--IAPELHQVAGNLAMPGFTAPKLLWVRRHEPQH----------FARIS 149
Cdd:PRK00047 88 VVWDkETGRPIYNAIVWQDRRTADICEELKRdgYEDYIREKTGLVIDPYFSGTKIKWILDNVEGAreraekgellFGTID 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 150 TVLLpkdylrFKMTGQK--ISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSAtlspEVASRWGLTSS 227
Cdd:PRK00047 168 TWLV------WKLTGGKvhVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYG----KTNPYGFFGGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 228 VVVAGGGGDNAVSAIGVGAVSPGDA--------FISLGT--------SGVLfvVTDAYRPaPQSAVHAFchvlpnlwhQM 291
Cdd:PRK00047 238 VPIAGIAGDQQAALFGQLCFEPGMAkntygtgcFMLMNTgekavkseNGLL--TTIAWGI-DGKVVYAL---------EG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 292 SVMLsAASCLQWF---CRLV-GVTETELLEEiaQLSDADKAsapMFLPYLSGERTPHNDPHARGLFWALTHSSQRALMGY 367
Cdd:PRK00047 306 SIFV-AGSAIQWLrdgLKIIsDASDSEALAR--KVEDNDGV---YVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIR 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 368 AVLEGVSFGIADGLRVLQE-SGTAIEQCSLVGGGARSPFWAQLLADILDMPVVTHKGGETgGALGAARLACLAAG--KPL 444
Cdd:PRK00047 380 ATLESIAYQTRDVLDAMQAdSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAET-TALGAAYLAGLAVGfwKDL 458
|
490 500 510
....*....|....*....|....*....|.
gi 446202723 445 AAVCEKPEIFKTWRS--DPERHNALMQRYQQ 473
Cdd:PRK00047 459 DELKEQWKIDRRFEPqmDEEEREKLYAGWKK 489
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
2-479 |
1.28e-29 |
|
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: 121.58 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 2 YLGIDLGTSEVKALVID-ENNEIVATHSAPLT-IQRPHPHWSEQSPQAWWEATEYLMSTLREKCGHHWQAIKAIGLSGQM 79
Cdd:cd07768 2 GIGVDVGTSSARAGVYDlYAGLEMAQEPVPYYqDSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVDATC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 80 HGAVLlDEKGEAI------RP---AILWNDTRSAQECAELEEIAPE-LHQVAGNLAMPGFTAPKLLWVRRHEPQHFARIS 149
Cdd:cd07768 82 SLAIF-DREGTPLmalipyPNednVIFWMDHSAVNEAQWINMQCPQqLLDYLGGKISPEMGVPKLKYFLDEYSHLRDKHF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 150 TVLLPKDYLRFKMTGqKISDMSDSAGTLW-LDVEKRDWSDSLLEKCGL------TRANMPELVEGCDVSATLSPEVASRW 222
Cdd:cd07768 161 HIFDLHDYIAYELTR-LYEWNICGLLGKEnLDGEESGWSSSFFKNIDPrlehltTTKNLPSNVPIGTTSGVALPEMAEKM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 223 GLTSSVVVAGGGGDNAVSAIGVG-AVSPGDAFISLGTS--------------GVLFVVTDAYRP------APQSAVHAFc 281
Cdd:cd07768 240 GLHPGTAVVVSCIDAHASWFAVAsPHLETSLFMIAGTSschmygttisdripGVWGPFDTIIDPdysvyeAGQSATGKL- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 282 hvlpnLWHQMSVMLSAASCLQwfCRLVGVTETELLEEIA-QLSDADKASAPMF-LPYLSGERTPHNDPHARGLFWALTHS 359
Cdd:cd07768 319 -----IEHLFESHPCARKFDE--ALKKGADIYQVLEQTIrQIEKNNGLSIHILtLDMFFGNRSEFADPRLKGSFIGESLD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 360 SQRALMGY---AVLEGVSFGIADGLRVLQESGTAIEQCSLVGGGARSPFWAQLLADILDMPVVTHKGGETgGALGAARLA 436
Cdd:cd07768 392 TSMLNLTYkyiAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMM-GILGAAVLA 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 446202723 437 CLAAG-KPLAAVCEKPEIF-----KTWRSDPERHNALMQR-YQQFTALYH 479
Cdd:cd07768 471 KVAAGkKQLADSITEADISndrksETFEPLAYRLGADYILlYKLLCVKYH 520
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
5-455 |
1.17e-28 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 118.65 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 5 IDLGTSEVKALVIDENNEIVATHSAPLTIQRPHPHWSEQSPQAWWEATEYLMSTLREKC---GHH-WQAIKAIGLSGQMH 80
Cdd:PLN02295 5 IDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAaakGHNvDSGLKAIGITNQRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 81 GAVLLDEK-GEAIRPAILWNDTRSAQECAELEEIAPE----LHQVAGNLAMPGFTAPKLLWVRRHEPQ----------HF 145
Cdd:PLN02295 85 TTVAWSKStGRPLYNAIVWMDSRTSSICRRLEKELSGgrkhFVETCGLPISTYFSATKLLWLLENVDAvkeavksgdaLF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 146 ARISTVLLpkdylrFKMTGQK-----ISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRANMPELVEGCDVSATLSPEvas 220
Cdd:PLN02295 165 GTIDSWLI------WNLTGGAsggvhVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIAKG--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 221 rwGLTSSVVVAGGGGDNAVSAIGVGAvSPGDA--------FISLGTS--------GVLfvVTDAYRPAPQSAvhafchvl 284
Cdd:PLN02295 236 --WPLAGVPIAGCLGDQHAAMLGQRC-RPGEAkstygtgcFILLNTGeevvpskhGLL--TTVAYKLGPDAP-------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 285 PNLWHQMSVMLSAAScLQWFCRLVGVTETEllEEIAQLSDADKASAPM-FLPYLSGERTPHNDPHARGLFWALTHSSQRA 363
Cdd:PLN02295 303 TNYALEGSVAIAGAA-VQWLRDNLGIIKSA--SEIEALAATVDDTGGVyFVPAFSGLFAPRWRDDARGVCVGITRFTNKA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 364 LMGYAVLEGVSFGIADGL------RVLQESGTAIEQCSLVGGGARSPFWAQLLADILDMPVVTHKGGETgGALGAARLAC 437
Cdd:PLN02295 380 HIARAVLESMCFQVKDVLdamrkdAGEEKSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIET-TALGAAYAAG 458
|
490
....*....|....*...
gi 446202723 438 LAAGkplaaVCEKPEIFK 455
Cdd:PLN02295 459 LAVG-----LWTEEEIFA 471
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
3-473 |
2.10e-24 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 106.08 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 3 LGIDLGTSEVKALVID-ENNEIVATHSAP---LTIQR---PHPHWSEQSPQAWWEATEYLMSTLREKCGHHWQAIKAIGL 75
Cdd:PRK04123 6 IGLDFGTDSVRALLVDcATGEELATAVVEyphWVKGRyldLPPNQALQHPLDYIESLEAAIPAVLKEAGVDPAAVVGIGV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 76 ---SGQM-----HGAVLLDEKGEAIRP---AILWNDTRSAQECAELEEIAPELHQVA------GNLAMPGFTApKLLWVR 138
Cdd:PRK04123 86 dftGSTPapvdaDGTPLALLPEFAENPhamVKLWKDHTAQEEAEEINRLAHERGEADlsryigGIYSSEWFWA-KILHVL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 139 RHEPQHFARISTVLLPKDYLRFKMTGQKI-SDMSDSAGT-----LWLDvekrDWS-----------DSLLEKcgLTRANM 201
Cdd:PRK04123 165 REDPAVYEAAASWVEACDWVVALLTGTTDpQDIVRSRCAaghkaLWHE----SWGglpsadffdalDPLLAR--GLRDKL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 202 PELVEGCDVSA-TLSPEVASRWGLTSSVVVAGGGGDNAVSAIGVGAvSPGDAFISLGTSGVLFVVTDAyrpapQSAVHAF 280
Cdd:PRK04123 239 FTETWTAGEPAgTLTAEWAQRLGLPEGVAVSVGAFDAHMGAVGAGA-EPGTLVKVMGTSTCDILLADK-----QRAVPGI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 281 C-----HVLPNLWHqmsvmLSAA-SC----LQWFCRLVGvtETELLEEIAQLSD------ADKASA-------PMFLPYL 337
Cdd:PRK04123 313 CgqvdgSIVPGLIG-----YEAGqSAvgdiFAWFARLLV--PPEYKDEAEARGKqllellTEAAAKqppgehgLVALDWF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 338 SGERTPHNDPHARGLF--WALTHSSQ---RALmgyavLEGVSFG---IADGLRvlqESGTAIEQCSLVGGGAR-SPFWAQ 408
Cdd:PRK04123 386 NGRRTPLADQRLKGVItgLTLGTDAPdiyRAL-----IEATAFGtraIMECFE---DQGVPVEEVIAAGGIARkNPVLMQ 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446202723 409 LLADILDMPVVTHkGGETGGALGAARLACLAAGK----PLAAVCEKPEIFKTWRSDPERH---NALMQRYQQ 473
Cdd:PRK04123 458 IYADVLNRPIQVV-ASDQCPALGAAIFAAVAAGAypdiPEAQQAMASPVEKTYQPDPENVaryEQLYQEYKQ 528
|
|
| PLN02669 |
PLN02669 |
xylulokinase |
1-286 |
8.58e-24 |
|
xylulokinase
Pssm-ID: 178274 [Multi-domain] Cd Length: 556 Bit Score: 104.47 E-value: 8.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 1 MYLGIDLGTSEVKALVIDENNEIVATHSAPLTIQRPH----------PHWSEQ--SPQAWW-EATEYLMSTL-REKCGHH 66
Cdd:PLN02669 9 LFLGFDSSTQSLKATVLDSNLRIVASEIVHFDSDLPHygtkdgvyrdPKVNGRivSPTLMWvEALDLLLQKLaKEKFPFH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 67 wqAIKAIGLSGQMHGAV------------------LLDEKGEA--IRPAILWNDTRSAQECAELEEI---APELHQVAGN 123
Cdd:PLN02669 89 --KVVAISGSGQQHGSVywrkgasavlksldpsksLVAQLQDAfsTKDSPIWMDSSTTKQCREIEEAvggAAELSKLTGS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 124 LAMPGFTAPKLLWVRRHEPQHFARISTVLLPKDYLRFKMTGQKIS-DMSDSAGTLWLDVEKRDWSDSLLEkcgltrANMP 202
Cdd:PLN02669 167 RAYERFTGPQIRKIYETQPEVYHDTERISLVSSFMASLLVGDYASiDETDGAGMNLMDIEKRCWSKAALE------ATAP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 203 ELVE-------GCDVSATLSPEVASRWGLTSSVVVAGGGGDNAVSAIGVGAVSPGDAFISLGTSGVLFVVTDAYRPAPQS 275
Cdd:PLN02669 241 GLEEklgklapAHAVAGKIHPYFVQRFGFSSNCLVVQWSGDNPNSLAGLTLSTPGDLAISLGTSDTVFGITREPQPSLEG 320
|
330
....*....|.
gi 446202723 276 avhafcHVLPN 286
Cdd:PLN02669 321 ------HVFPN 325
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
5-238 |
7.91e-19 |
|
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: 88.47 E-value: 7.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 5 IDLGTSEVKALVIDENNEIVATHSAPLTIQRPHPHWSEQSPQAWweatEYLMSTLREKCGHHwqAIKAIGLSGqmHGA-- 82
Cdd:cd07772 5 FDIGKTNKKLLLFDENGEVLAERSTPNPEIEEDGYPCEDVEAIW----EWLLDSLAELAKRH--RIDAINFTT--HGAtf 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 83 VLLDEKGEAIRPAILWNDTRSAQECAELEEIAPELHQvAGNLAMPGFT--APKLLWVRRHEPQHFARISTVL-LPkDYLR 159
Cdd:cd07772 77 ALLDENGELALPVYDYEKPIPDEINEAYYAERGPFEE-TGSPPLPGGLnlGKQLYWLKREKPELFARAKTILpLP-QYWA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 160 FKMTGQKISDMSdSAGT---LWlDVEKRDWSdSLLEKCGLTRAnMPELVEGCDVSATLSPEVASRWGLTSSVVVAGGGGD 236
Cdd:cd07772 155 WRLTGKAASEIT-SLGChtdLW-DFEKNEYS-SLVKKEGWDKL-FPPLRKAWEVLGPLRPDLARRTGLPKDIPVGCGIHD 230
|
...
gi 446202723 237 -NA 238
Cdd:cd07772 231 sNA 233
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
2-454 |
3.25e-13 |
|
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: 71.67 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 2 YLGIDLGTSEVKALVIDENNEIVATHSAPLT-IQRPHPHWS-EQSPQAWWEATEYLMSTLREKCGHHwqAIKAIGLSGQM 79
Cdd:cd07778 2 GIGIDVGSTSVRIGIFDYHGTLLATSERPISyKQDPKDLWFvTQSSTEIWKAIKTALKELIEELSDY--IVSGIGVSATC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 80 HGAVL-LDEKGEAIRP-------------AILWNDTRSAQECAELEEIAPE--LHQVAGNLaMPGFTAPKLLWVRRHEPQ 143
Cdd:cd07778 80 SMVVMqRDSDTSYLVPynviheksnpdqdIIFWMDHRASEETQWLNNILPDdiLDYLGGGF-IPEMAIPKLKYLIDLIKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 144 HFARISTVLLPKDYLRFKMTGQKI--------SDMSDSAGtlwLDVEKRDWSDSLLEKCGL----------TRANMPELV 205
Cdd:cd07778 159 DTFKKLEVFDLHDWISYMLATNLGhsnivpvnAPPSIGIG---IDGSLKGWSKDFYSKLKIstkvcnvgntFKEAPPLPY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 206 EGCDVsATLSPEVASRWGLTSSVVVAGGGGDNAVSAIGVGA---VSPGDAFISLGTSGVLFVVTDAYRPAPQSAVHA-FC 281
Cdd:cd07778 236 AGIPI-GKVNVILASYLGIDKSTVVGHGCIDCYAGWFSTFAaakTLDTTLFMVAGTSTCFLYATSSSQVGPIPGIWGpFD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 282 HVLPNLW-------------------HQMSVMLSAASCLQWfcrlvgvtetELLEEiaQLSDADKASAP----MFLPYL- 337
Cdd:cd07778 315 QLLKNYSvyeggqsatgklieklfnsHPAIIELLKSDANFF----------ETVEE--KIDKYERLLGQsihyLTRHMFf 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 338 ----SGERTPHNDPHARGLFWALTHSSQR---ALMGYAVLEGVSFGIADGLRVLQESGTAIEQCSLVGGGARSPFWAQLL 410
Cdd:cd07778 383 ygdyLGNRTPYNDPNMSGSFIGESTDSSLtdlVLKYILILEFLAFQTKLIIDNFQKEKIIIQKVVISGSQAKNARLLQLL 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 446202723 411 ADILDMPVVthKGGETGGALGAARLACLaAGKPLAAVCEKPEIF 454
Cdd:cd07778 463 STVLSKIHI--IVPLSDSKYAVVKGAAL-LGKAAFLHNQSIEER 503
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-100 |
5.44e-07 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 51.44 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 1 MYLGIDLGTSEVKALVIDENNEIVATHSAPLTiqrphphwSEQSPQAWWEATEYLMSTLREKCGHHWQAIKAIGLSgqMH 80
Cdd:COG1940 6 YVIGIDIGGTKIKAALVDLDGEVLARERIPTP--------AGAGPEAVLEAIAELIEELLAEAGISRGRILGIGIG--VP 75
|
90 100
....*....|....*....|...
gi 446202723 81 GAVllD-EKGEAIRPAIL--WND 100
Cdd:COG1940 76 GPV--DpETGVVLNAPNLpgWRG 96
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
83-419 |
6.81e-07 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 51.64 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 83 VLLDEKGEAIRPAILWNDTRS----AQECAELEEiaPELHQVAGNLAMPGFTAPKLLWVRRHEPQHFARISTVLLPKDYL 158
Cdd:PRK10640 69 VLLDKQGQRVGLPVSYRDSRTdgvmAQAQQQLGK--RDIYRRSGIQFLPFNTLYQLRALTEQQPELIAQVAHALLIPDYF 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 159 RFKMTGQKISDMSDSAGTLWLDVEKRDWSDSLLEKCGLTRANMPelvegcdvSATLSPEVASRWGLTSSV---VVAGGGG 235
Cdd:PRK10640 147 SYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGAPKAWFG--------RPTHPGNVIGHWICPQGNeipVVAVASH 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 236 DNAVSAIGVGAVSPGDAFISLGT-SGVLFVVTDAY-RPAPQSA-------VHAFCHVLPNLwhqMSVMLsaascLQWFCR 306
Cdd:PRK10640 219 DTASAVIASPLNDSDAAYLSSGTwSLMGFESQTPFtNDTALAAnitneggAEGRYRVLKNI---MGLWL-----LQRVLQ 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 307 LVGVTETELLeeiaqLSDADKASAPMFLPYLSGERTPHNDPHARGLFWALTHSSQ-----RALMGYAVLEGVSFGIADGL 381
Cdd:PRK10640 291 ERQITDLPAL-----IAATAALPACRFLINPNDDRFINPPSMCSEIQAACRETAQpvpesDAELARCIFDSLALLYADVL 365
|
330 340 350
....*....|....*....|....*....|....*....
gi 446202723 382 RVLQE-SGTAIEQCSLVGGGARSPFWAQLLADILDMPVV 419
Cdd:PRK10640 366 HELAQlRGEPFSQLHIVGGGCQNALLNQLCADACGIRVI 404
|
|
| ASKHA_NBD_BcrAD_BadFG_HgdC_HadI |
cd24036 |
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and ... |
2-30 |
2.46e-04 |
|
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and HgdC/HadI family includes BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins which are subunits of benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also contains some dehydratase activators, such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). Uncharacterized proteins, such as Escherichia coli protein YjiL and Methanocaldococcus jannaschii protein MJ0800, are also included in this family.
Pssm-ID: 466886 [Multi-domain] Cd Length: 250 Bit Score: 42.53 E-value: 2.46e-04
10 20
....*....|....*....|....*....
gi 446202723 2 YLGIDLGTSEVKALVIDENNEIVATHSAP 30
Cdd:cd24036 1 FAGIDVGSTTTKAVILDDKGKILGKAVIR 29
|
|
| ASKHA_NBD_O66634-like_rpt1 |
cd24034 |
nucleotide-binding domain (NBD) of the first repeat of Aquifex aeolicus hypothetical protein ... |
2-27 |
1.04e-03 |
|
nucleotide-binding domain (NBD) of the first repeat of Aquifex aeolicus hypothetical protein O66634 and similar proteins; The family includes a group of uncharacterized proteins similar to Aquifex aeolicus hypothetical protein O66634, which contains two copies of the BcrAD/BadFG-like domain, suggesting that the family may structurally dimerize. The model corresponds to the first copy of the BcrAD/BadFG-like domain.
Pssm-ID: 466884 [Multi-domain] Cd Length: 258 Bit Score: 40.65 E-value: 1.04e-03
10 20
....*....|....*....|....*.
gi 446202723 2 YLGIDLGTSEVKALVIDENNEIVATH 27
Cdd:cd24034 1 YLGIDIGSTTVKAVVLDEKGNIVFSD 26
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
3-100 |
4.98e-03 |
|
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family corresponds to a group of proteins including sugar kinases, transcriptional repressors, and yet uncharacterized open reading frames. ROK family sugar kinases phosphorylate a range of structurally distinct hexoses including the key carbon source D-glucose, various glucose epimers, and several acetylated hexosamines. The sugar kinases include N-acetyl-D-glucosamine kinase (NAGK; EC 2.7.1.59), polyphosphate glucokinase (PPGK; EC 2.7.1.63/EC 2.7.1.2), glucokinase (GLK; EC 2.7.1.2), fructokinase (FRK; EC 2.7.1.4), hexokinase (HK; EC 2.7.1.1), D-allose kinase (AlsK; EC 2.7.1.55), bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE; EC 3.2.1.183/EC 2.7.1.60), N-acetylmannosamine kinase (NanK; EC 2.7.1.60), beta-glucoside kinase (BglK; EC 2.7.1.85), and N-acetylglucosamine kinase (EC 2.7.1.59). The family also contains the repressor proteins, such as N-acetylglucosamine repressor (NagC), xylose repressor (XylR), cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and protein Mlc. ROK kinases harbor a conserved N-terminal ATP binding motif of sequence DxGxT, while ROK repressors possess a N-terminal extension that contains a canonical helix-turn-helix DNA binding motif. The ROK family proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466849 [Multi-domain] Cd Length: 239 Bit Score: 38.60 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446202723 3 LGIDLGTSEVKALVIDENNEIVATHSAPLTiqrphphwSEQSPQAWWEATEYLMSTLREKCGhHWQAIKAIGLSgqMHGA 82
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTP--------AEEGPEAVLDRIAELIEELLAEAG-VRERILGIGIG--VPGP 69
|
90 100
....*....|....*....|.
gi 446202723 83 VllD-EKGEAIRPAIL--WND 100
Cdd:cd23763 70 V--DpETGIVLFAPNLpwWKN 88
|
|
| ASKHA_NBD_benz_CoA_BcrD_BadG |
cd24105 |
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit D (BcrD/BadG) and similar ... |
3-30 |
8.42e-03 |
|
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit D (BcrD/BadG) and similar proteins; benzoyl-CoA reductase (EC 1.3.7.8), also called benzoyl-CoA reductase (dearomatizing), or 3-hydroxybenzoyl-CoA reductase, catalyzes the anaerobic reduction of benzoyl-CoA and 3-hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme also reduces other benzoyl-CoA analogs with small substituents at the aromatic ring. The model corresponds to subunit D of benzoyl-CoA reductase.
Pssm-ID: 466955 Cd Length: 256 Bit Score: 37.95 E-value: 8.42e-03
10 20
....*....|....*....|....*...
gi 446202723 3 LGIDLGTSEVKALVIDENNEIVATHSAP 30
Cdd:cd24105 2 AGIDVGSGYTKAVIMDDGEKILAKRVER 29
|
|
| |
