|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
5-450 |
9.78e-178 |
|
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: 505.52 E-value: 9.78e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDLEGNVVCEGKGLLQPMHtPDADTAEHPDDDLWASLCFAGHDLMSQFAGNKEDIVGIGLGSIR 84
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYY-PEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 85 CCRALLKADGTPAAPLISWQDARVtrpyehtnpdvAYVTSFSGYLTHRLTGEF-KDNIANYFGQWPVDYKsWAWSEDaaV 163
Cdd:cd07779 80 STFVPVDEDGRPLRPAISWQDKRT-----------AKFLTVQDYLLYRLTGEFvTDTTSASRTGLPDIRT-RDWSDD--L 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 164 MDKFNIPRHMLFDVQMPGTVLGHITPQAALATHFPAGLPVVCTTSDKPVEALGAGLLDDETAVISLGTYIALMMNGKALP 243
Cdd:cd07779 146 LDAFGIDRDKLPELVPPGTVIGTLTKEAAEETGLPEGTPVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 244 KDPVAYWPIM-SSIPQTLLYEGYGIRkGMWTVSWLRDMLGESLIQdARAQDLSPEDLLNKKASCVPPGCNGLMTVLDWL- 321
Cdd:cd07779 226 EDPERRIPCNpSAVPGKWVLEGSINT-GGSAVRWFRDEFGQDEVA-EKELGVSPYELLNEEAAKSPPGSDGLLFLPYLAg 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 322 --TNPWEPYKRGIMIGFDSSMDYAWIYRSILESVALTLKNNYDNMCnEMNHFAKHVIITGGGSNSDLFMQIFADVFNLPA 399
Cdd:cd07779 304 agTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELRDNLEAME-KAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPV 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 16130683 400 RRNAINGCASLGAAINTAVGLGLYPDYATAVDNMVRVKDIFIPIESNAKRY 450
Cdd:cd07779 383 ERPETSEATALGAAILAAVGAGIYPDFEEAVKAMVRVTDTFEPDPENVAIY 433
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
5-414 |
1.41e-111 |
|
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: 335.69 E-value: 1.41e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDLEGNVVCEGKGLLqPMHTPDADTAEHPDDDLWASLCFAGHDLMSQFAGNKEDIVGIGLGSIR 84
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREY-PLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 85 CCRALLKADGTPAAPLISWQDARvtrpyehtnpdvAYVTSFSGYLTHRLTGEF-KDNIANYFGQWpVDYKSWAWSEDAAv 163
Cdd:cd00366 80 PGVVLVDADGNPLRPAIIWLDRR------------AKFLQPNDYIVFRLTGEFaIDYSNASGTGL-YDIKTGDWSEELL- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 164 mDKFNIPRHMLFDVQMPGTVLGHITPQAALATHFPAGLPVVCTTSDKPVEALGAGLLDDETAVISLGTYIALMMNGKALP 243
Cdd:cd00366 146 -DALGIPREKLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 244 KDPVAYWPIMSSIPQTLLYEGYgIRKGMWTVSWLRDMLGESLIQDARAQDlspedlLNKKASCVPPGCNGLMtVLDWLTN 323
Cdd:cd00366 225 PPDPRLLNRCHVVPGLWLLEGA-INTGGASLRWFRDEFGEEEDSDAEYEG------LDELAAEVPPGSDGLI-FLPYLSG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 324 ----PWEPYKRGIMIGFDSSMDYAWIYRSILESVALTLKNNYDNMCNEMNHFaKHVIITGGGSNSDLFMQIFADVFNLPA 399
Cdd:cd00366 297 erspIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEILEELGVKI-KEIRVTGGGAKSRLWNQIKADVLGVPV 375
|
410
....*....|....*
gi 16130683 400 RRNAINGCASLGAAI 414
Cdd:cd00366 376 VVPEVAEGAALGAAI 390
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
4-461 |
7.61e-97 |
|
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: 300.98 E-value: 7.61e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 4 KYIIGIDGGSQSTKVVMYDLEGNVVCEGKGLLqPMHTPDADTAEHPDDDLWASLCFAGHDLMSQFAGNKEDIVGIGLGSI 83
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEY-PLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 84 RCCRALLKADGTPAAPLISWQDAR-------------VTRPYEHT-NP----------------------DVAYVTSFSG 127
Cdd:COG1070 80 MHGLVLLDADGEPLRPAILWNDTRaaaeaaelreelgEEALYEITgNPlhpgftapkllwlkenepeifaRIAKVLLPKD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 128 YLTHRLTGEFKDNIANYFGQWPVDYKSWAWSEDaaVMDKFNIPRHMLFDVQMPGTVLGHITPQAALATHFPAGLPVVCTT 207
Cdd:COG1070 160 YLRYRLTGEFVTDYSDASGTGLLDVRTRDWSDE--LLEALGIDRELLPELVPPGEVAGTLTAEAAAETGLPAGTPVVAGA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 208 SDKPVEALGAGLLDDETAVISLGTYIALMMNGKALPKDP---VAYWPimSSIPQTLLYEGyGIRKGMWTVSWLRDMLGES 284
Cdd:COG1070 238 GDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPegrVHTFC--HAVPGRWLPMG-ATNNGGSALRWFRDLFADG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 285 liqdaraqDLSPEDLLNKKASCVPPGCNGLMtVLDWL----TNPWEPYKRGIMIGFDSSMDYAWIYRSILESVALTLKNN 360
Cdd:COG1070 315 --------ELDDYEELNALAAEVPPGADGLL-FLPYLsgerTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 361 YDNMcNEMNHFAKHVIITGGGSNSDLFMQIFADVFNLPARRNAINGCASLGAAINTAVGLGLYPDYATAVDNMVRVKDIF 440
Cdd:COG1070 386 LEAL-EEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMVRVGETI 464
|
490 500
....*....|....*....|.
gi 16130683 441 IPIESNAKRYDAMnKGIFKDL 461
Cdd:COG1070 465 EPDPENVAAYDEL-YERYREL 484
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
5-421 |
3.25e-71 |
|
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: 233.19 E-value: 3.25e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDLEGNVVCEGkGLLQPMHTPDADTAEHPDDDLWASLCFAGHDLMSQFAGNKEDIVGIGLGSIR 84
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASA-SIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 85 CCRALLKADGTPAAPLISWQDARVT-------------RPYEHTN-------------------PDV----AYVTSFSGY 128
Cdd:cd07804 80 PALVPVDENGKPLRPAILYGDRRATeeiewlnenigedRIFEITGnpldsqsvgpkllwikrnePEVfkktRKFLGAYDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 129 LTHRLTGEF---KDNIANYFGQWpvDYKSWAWSEDAavMDKFNIPRHMLFDVQMPGTVLGHITPQAALATHFPAGLPVVC 205
Cdd:cd07804 160 IVYKLTGEYvidYSSAGNEGGLF--DIRKRTWDEEL--LEALGIDPDLLPELVPSTEIVGEVTKEAAEETGLAEGTPVVA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 206 TTSDKPVEALGAGLLDDETAVISLGTYIALMMNGKALPKDPvAYWPIMSSIPQTLLYEGygirkGMWT----VSWLRDML 281
Cdd:cd07804 236 GTVDAAASALSAGVVEPGDLLLMLGTAGDIGVVTDKLPTDP-RLWLDYHDIPGTYVLNG-----GMATsgslLRWFRDEF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 282 GESLIQDARAQDLSPEDLLNKKASCVPPGCNGLMTVLDWL---TNPWEPYKRGIMIGFDSSMDYAWIYRSILESVALTLK 358
Cdd:cd07804 310 AGEEVEAEKSGGDSAYDLLDEEAEKIPPGSDGLIVLPYFMgerTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYGLR 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130683 359 NNYDNMcNEMNHFAKHVIITGGGSNSDLFMQIFADVFNLPARRNAINGCASLGAAINTAVGLG 421
Cdd:cd07804 390 HHLEVI-REAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
5-461 |
3.13e-68 |
|
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: 226.27 E-value: 3.13e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDLEGNVVCEGKGLLqPMHTPDADTAEHPDDDLWASLCFAGHDLMSQFAGNKEDIVGIGL---- 80
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEY-PTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLtgqm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 81 -GSIrccraLLKADGTPAAPLISWQDARVT------------RPYEHTN-------------------PDV----AYVTS 124
Cdd:cd07808 80 hGLV-----LLDKNGRPLRPAILWNDQRSAaeceelearlgdEILIITGnpplpgftlpkllwlkenePEIfariRKILL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 125 FSGYLTHRLTGEFKDNIANYFGQWPVDYKSWAWSEDaaVMDKFNIPRHMLFDVQMPGTVLGHITPQAALATHFPAGLPVV 204
Cdd:cd07808 155 PKDYLRYRLTGELATDPSDASGTLLFDVEKREWSEE--LLEALGLDPSILPPIVESTEIVGTLTPEAAEELGLPEGTPVV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 205 CTTSDKPVEALGAGLLDDETAVISLGTYIALMMNGKALPKDPVA-----------YWPIMSSIPQTllyeGYGIRkgmwt 273
Cdd:cd07808 233 AGAGDNAAAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGrlhtfphavpgKWYAMGVTLSA----GLSLR----- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 274 vsWLRDMLGEsliqdaraqDLSPEDLLNKKASCVPPGCNGLMTvLDWLT---NP-WEPYKRGIMIGFDSSMDYAWIYRSI 349
Cdd:cd07808 304 --WLRDLFGP---------DRESFDELDAEAAKVPPGSEGLLF-LPYLSgerTPyWDPNARGSFFGLSLSHTRAHLARAV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 350 LESVALTLKNNYDNMcNEMNHFAKHVIITGGGSNSDLFMQIFADVFNLPARRNAINGCASLGAAINTAVGLGLYPDYATA 429
Cdd:cd07808 372 LEGVAFSLRDSLEVL-KELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEA 450
|
490 500 510
....*....|....*....|....*....|..
gi 16130683 430 VDNMVRVKDIFIPIESNAKRYDAMNKgIFKDL 461
Cdd:cd07808 451 AAACIKIEKTIEPDPERHEAYDELYA-RYREL 481
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
5-453 |
5.22e-67 |
|
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Chromobacterium violaceum xylulose kinase (CvXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466807 [Multi-domain] Cd Length: 485 Bit Score: 223.17 E-value: 5.22e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDLEGNVVCEGKGLLqPMHTPDADTAEHPDDDLWASLCFAGHDLMSQFAGNKEDIVGIGLGSIR 84
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPY-PTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 85 CCRALLKADGTPAAPLISWQDAR--------------------VTRP-------------YEHTNPDVAYVTSF----SG 127
Cdd:cd07805 80 QGVVPVDKDGNPLRNAIIWSDTRaaeeaeeiagglggiegyrlGGGNppsgkdplakilwLKENEPEIYAKTHKfldaKD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 128 YLTHRLTGEFKDNIANYFGQWPVDYKSWAWSEDaaVMDKFNIPRHMLFDVQMPGTVLGHITPQAALATHFPAGLPVVCTT 207
Cdd:cd07805 160 YLNFRLTGRAATDPSTASTTGLMDLRKRRWSEE--LLRAAGIDPDKLPELVPSTEVVGELTPEAAAELGLPAGTPVVGGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 208 SDKPVEALGAGLLDDETAVISLGT--YIALmmngkALPKDPVAYWPIMSSIPqtllyegyGIRKGMW-----------TV 274
Cdd:cd07805 238 GDAAAAALGAGAVEEGDAHIYLGTsgWVAA-----HVPKPKTDPDHGIFTLA--------SADPGRYllaaeqetaggAL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 275 SWLRDMLGESLIQDARAqdlspEDLLNKKASCVPPGCNGLMtVLDWL----TNPWEPYKRGIMIGFDSSMDYAWIYRSIL 350
Cdd:cd07805 305 EWARDNLGGDEDLGADD-----YELLDELAAEAPPGSNGLL-FLPWLngerSPVEDPNARGAFIGLSLEHTRADLARAVL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 351 ESVALTLKNNYDNMcNEMNHFAKHVIITGGGSNSDLFMQIFADVFNLPARR--NAINgCASLGAAINTAVGLGLYPDYAt 428
Cdd:cd07805 379 EGVAFNLRWLLEAL-EKLTRKIDELRLVGGGARSDLWCQILADVLGRPVEVpeNPQE-AGALGAALLAAVGLGLLKSFD- 455
|
490 500
....*....|....*....|....*
gi 16130683 429 AVDNMVRVKDIFIPIESNAKRYDAM 453
Cdd:cd07805 456 EAKALVKVEKVFEPDPENRARYDRL 480
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
5-421 |
9.44e-58 |
|
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: 197.42 E-value: 9.44e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDLEGNVVCEGKgLLQPMHTPDADTAEHPDDDLWASLCFAGHDLMSQfaGNKEDIVGIGLGSIR 84
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASAS-RETPLIHPGPGWAELDPEELWEAVKEAIREAAAQ--AGPDPIAAISVSSQG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 85 CCRALLKADGTPAAPLISWQDARVT-------------RPYEHT-------------------NPDV----AYVTSFSGY 128
Cdd:cd07773 78 ESGVPVDRDGEPLGPAIVWFDPRGKeeaeelaerigaeELYRITglppspmyslakllwlrehEPEIfakaAKWLSVADY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 129 LTHRLTGEFK--DNIAN---YFgqwpvDYKSWAWSEDaaVMDKFNIPRHMLFDVQMPGTVLGHITPQAALATHFPAGLPV 203
Cdd:cd07773 158 IAYRLTGEPVtdYSLASrtmLF-----DIRKRTWSEE--LLEAAGIDASLLPELVPSGTVIGTVTPEAAEELGLPAGTPV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 204 VCTTSDKPVEALGAGLLDDETAVISLGTYIALMMNGKALPKDPVAYWPIMS---SIPQTLLYEGYGIRKGMwTVSWLRDM 280
Cdd:cd07773 231 VVGGHDHLCAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLDEMLAEGGLSyghHVPGGYYYLAGSLPGGA-LLEWFRDL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 281 LGESLIQDARAqdlspedllNKKASCVPPGCNGLMtVLDWL----TNPWEPYKRGIMIGFDSSMDYAWIYRSILESVALT 356
Cdd:cd07773 310 FGGDESDLAAA---------DELAEAAPPGPTGLL-FLPHLsgsgTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFE 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130683 357 LKNNYDNMCnEMNHFAKHVIITGGGSNSDLFMQIFADVFNLPARRNAINGCASLGAAINTAVGLG 421
Cdd:cd07773 380 LRLNLEALE-KAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
5-453 |
3.76e-56 |
|
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: 194.68 E-value: 3.76e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDLE-GNVVCEGKgllQPMHT----PDADTAEHPDDDLWASLCFAGHDLMSQFAGNKEDIVGIG 79
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDLAdGEELASAV---VPYPTgyipPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 80 LGSIRCCRALLKADGTPAAPLISWQDAR--------------VTRPYE--------------------HTNPDV----AY 121
Cdd:cd07781 78 VDTTSSTVVPVDEDGNPLAPAILWMDHRaqeeaaeinetahpALEYYLayyggvyssewmwpkalwlkRNAPEVydaaYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 122 VTSFSGYLTHRLTGEFKDNI------ANYF---GQWPVDYKSWAWSEDAAVMDKFniPRhmlfDVQMPGTVLGHITPQAA 192
Cdd:cd07781 158 IVEACDWINARLTGRWVRSRcaaghkWMYNewgGGPPREFLAALDPGLLKLREKL--PG----EVVPVGEPAGTLTAEAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 193 LATHFPAGLPVVCTTSDKPVEALGAGLLDDETAVISLGTYIALMMNGKAlPKDPVAYWPImssipqtllYEGyGIRKGMW 272
Cdd:cd07781 232 ERLGLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTCHLMVSPK-PVDIPGICGP---------VPD-AVVPGLY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 273 TV-----------SWLRDMLGEsliqDARAQDLSPEDLLNKKASCVPPGCNGLMtVLDWLT---NPW-EPYKRGIMIGFD 337
Cdd:cd07781 301 GLeagqsavgdifAWFVRLFVP----PAEERGDSIYALLSEEAAKLPPGESGLV-ALDWFNgnrTPLvDPRLRGAIVGLT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 338 SSMDYAWIYRSILESVALTLKNNYDNMcnEMNHFAKHVIITGGG--SNSDLFMQIFADVFNLPARRNAINGCASLGAAIN 415
Cdd:cd07781 376 LGTTPAHIYRALLEATAFGTRAIIERF--EEAGVPVNRVVACGGiaEKNPLWMQIYADVLGRPIKVPKSDQAPALGAAIL 453
|
490 500 510
....*....|....*....|....*....|....*...
gi 16130683 416 TAVGLGLYPDYATAVDNMVRVKDIFIPIESNAKRYDAM 453
Cdd:cd07781 454 AAVAAGVYADIEEAADAMVRVDRVYEPDPENHAVYEEL 491
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
5-461 |
1.88e-55 |
|
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: 192.39 E-value: 1.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDLEGNVVCEGKGLlQPMHTPDADTAEHPDDDLWASLCFAGHDLMSQFAGNKEDIVGIG--LGS 82
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAE-YPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVDAIGFSsaMHS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 83 IrccrALLKADGTPAAPLISWQDarvTRP----------------YEHT-------------------NPD----VAYVT 123
Cdd:cd07770 80 L----LGVDEDGEPLTPVITWAD---TRAaeeaerlrkegdgselYRRTgcpihpmyplakllwlkeeRPElfakAAKFV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 124 SFSGYLTHRLTGEfkdnianyfgqWPVDY-----------KSWAWSEDAavMDKFNIPRHMLFDVQMPGTVLGHITPQAA 192
Cdd:cd07770 153 SIKEYLLYRLTGE-----------LVTDYstasgtgllniHTLDWDEEA--LELLGIDEEQLPELVDPTEVLPGLKPEFA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 193 LATHFPAGLPVVCTTSDKPVEALGAGLLDDETAVISLGTYIALMMngkalpkdpvaywpiMSSIPQTLLYEG---YGIRK 269
Cdd:cd07770 220 ERLGLLAGTPVVLGASDGALANLGSGALDPGRAALTVGTSGAIRV---------------VSDRPVLDPPGRlwcYRLDE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 270 GMW-----------TVSWLRDMLGESliqdaraqDLSPEDLlNKKASCVPPGCNGLmTVLDWLT---NP-WEPYKRGIMI 334
Cdd:cd07770 285 NRWlvggainnggnVLDWLRDTLLLS--------GDDYEEL-DKLAEAVPPGSHGL-IFLPYLAgerAPgWNPDARGAFF 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 335 GFDSSMDYAWIYRSILESVALTLKNNYDNMCnEMNHFAKHVIITGGGSNSDLFMQIFADVFNLPARRNAINGCASLGAAI 414
Cdd:cd07770 355 GLTLNHTRADILRAVLEGVAFNLKSIYEALE-ELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAAL 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 16130683 415 NTAVGLGLYPDYatAVDNMVRVKDIFIPIESNAKRYDAMnKGIFKDL 461
Cdd:cd07770 434 LALEALGLISSL--EADELVKIGKVVEPDPENHAIYAEL-YERFKKL 477
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
5-421 |
9.44e-51 |
|
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466805 [Multi-domain] Cd Length: 444 Bit Score: 178.90 E-value: 9.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDLEGNVV-CEGKGLlqPMHTPDADTAEHPDDDLWASLCFAGHDLMSQFAGNKEDIVGIGL--- 80
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIaVASRPT--PVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVtgh 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 81 --GSIrccraLLKADGTPAAPLISWQDARVT-------------RPYEHT-------------------NPDV----AYV 122
Cdd:cd07802 79 gnGLY-----LVDKDGKPVRNAILSNDSRAAdivdrweedgtleKVYPLTgqplwpgqpvallrwlkenEPERydriRTV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 123 TSFSGYLTHRLTGEFKDNIANyFGQWPVDYKSWAWSEDaaVMDKFNIP--RHMLFDVQMPGTVLGHITPQAALATHFPAG 200
Cdd:cd07802 154 LFCKDWIRYRLTGEISTDYTD-AGSSLLDLDTGEYDDE--LLDLLGIEelKDKLPPLVPSTEIAGRVTAEAAALTGLPEG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 201 LPVVCTTSDKPVEALGAGLLDDETAVISLGTYIalmMNGKALPKDPVAYWPIMSS---IPQTLLYEgYGIRKGMWTVSWL 277
Cdd:cd07802 231 TPVAAGAFDVVASALGAGAVDEGQLCVILGTWS---INEVVTDEPVVPDSVGSNSlhaDPGLYLIV-EASPTSASNLDWF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 278 RDMLGEsliqDARAQDLSPEDLLNKKASCVPPGCNGLMtVLDWL-TNPWEPYKRGIMIGFDSSMDYAWIYRSILESVALT 356
Cdd:cd07802 307 LDTLLG----EEKEAGGSDYDELDELIAAVPPGSSGVI-FLPYLyGSGANPNARGGFFGLTAWHTRAHLLRAVYEGIAFS 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130683 357 LKNNYDNMCNEMNhfAKHVIITGGGSNSDLFMQIFADVFNLPARRNAINGCASLGAAINTAVGLG 421
Cdd:cd07802 382 HRDHLERLLVARK--PETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
5-453 |
5.67e-48 |
|
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: 172.52 E-value: 5.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDLEGNVVCEGKGLLQpmHTPDADTAEHPDDDL---WASLCFAGHDLMSQFAGNKEDIVGIGLG 81
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREWR--HKEVPDVPGSMDFDTeknWKLICECIREALKKAGIAPKSIAAISTT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 82 SIRCCRALLKADGTP----------------------------------------AAPLISWqdarvtrpYEHTNPDV-- 119
Cdd:cd07775 79 SMREGIVLYDNEGEEiwacanvdaraaeevselkelyntleeevyrisgqtfalgAIPRLLW--------LKNNRPEIyr 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 120 --AYVTSFSGYLTHRLTGEFKDNIANYFGQWPVDYKSWAWSEDaaVMDKFNIPRHMLFDVQMPGTVLGHITPQAALATHF 197
Cdd:cd07775 151 kaAKITMLSDWIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPE--ILEMAGLKADILPPVVESGTVIGKVTKEAAEETGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 198 PAGLPVVCTTSDKPVEALGAGLLDDETAVISLGTYIALMMNGKALPKDPVAYWPIM-SSIPQTLLYEGYGIRKGMwTVSW 276
Cdd:cd07775 229 KEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMNIRVNcHVIPDMWQAEGISFFPGL-VMRW 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 277 LRDMLGESLIQDARAQDLSPEDLLNKKASCVPPGCNGLMTVLDWLTN--PWE---PYKRGIMIGFDSSMDYAwIYRSILE 351
Cdd:cd07775 308 FRDAFCAEEKEIAERLGIDAYDLLEEMAKDVPPGSYGIMPIFSDVMNykNWRhaaPSFLNLDIDPEKCNKAT-FFRAIME 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 352 SVALTLKNNYDNMCNEMNHFAKHVIITGGGSNSDLFMQIFADVFNLPARRNAINGCASLGAAINTAVGLGLYPDYATAVD 431
Cdd:cd07775 387 NAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAGIYSSLEEAVE 466
|
490 500
....*....|....*....|..
gi 16130683 432 NMVRVKDIFIPIESNAKRYDAM 453
Cdd:cd07775 467 SLVKWEREYLPNPENHEVYQDL 488
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
5-420 |
1.11e-38 |
|
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: 145.83 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDLEGNVVCEGKGLLqPMHTPDADTAEHPDDDLWASLCFAGHDLMSQFAGNkeDIVGIGLGSIR 84
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPY-PTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPR--RVVAIAVDGTS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 85 CCRALLKADGTPAAPLISWQDARVT--------RPYEHTNPDVAYVTSFSG--------------------------YLT 130
Cdd:cd07783 78 GTLVLVDREGEPLRPAIMYNDARAVaeaeelaeAAGAVAPRTGLAVSPSSSlakllwlkrhepevlaktakflhqadWLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 131 HRLTGEFkdnianyfgqWPVDY----------KSWAWSEDaaVMDKFNIPRHMLFDVQMPGTVLGHITPQAALATHFPAG 200
Cdd:cd07783 158 GRLTGDR----------GVTDYnnalklgydpETGRWPSW--LLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLPAG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 201 LPVVCTTSDKPVEALGAGLLDDETAVISLGTYIALMMNGKALPKDPVAYwpimssIPQTLLYEGYgirkgmwtvsWL--- 277
Cdd:cd07783 226 TPVVAGTTDSIAAFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGG------VYSHRHGDGY----------WLvgg 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 278 -RDMLGESLIQDARAQDLspeDLLNKKAScvPPGCNGLmTVLDWLTN-----PWEPYKRGIMIGFDSsmDYAWIYRSILE 351
Cdd:cd07783 290 aSNTGGAVLRWFFSDDEL---AELSAQAD--PPGPSGL-IYYPLPLRgerfpFWDPDARGFLLPRPH--DRAEFLRALLE 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130683 352 SVALTLKNNYDNMCNEMNHFAKHVIITGGGSNSDLFMQIFADVFNLPARRNAINGcASLGAAINTAVGL 420
Cdd:cd07783 362 GIAFIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEE-AALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
5-421 |
6.45e-37 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 141.15 E-value: 6.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDLE-GNVVCEGKGLLQPMhTPDADTAEHPDDDLWASLCFAGHDLMSQFAGNKEDIVGIGL--- 80
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDAEtGRVVASGSAPHENI-LIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGIsgq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 81 --GSIrccraLLKADGTPAAPLISWQDAR-----------------------------------VTRPYEHTNPDVAYVT 123
Cdd:cd07809 80 mhGLV-----ALDADGKVLRPAKLWCDTRtapeaeeltealggkkcllvglniparftaskllwLKENEPEHYARIAKIL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 124 SFSGYLTHRLTGEFKDNIANYFGQWPVDYKSWAWSED-AAVMDKFNIPRHMLFDVQMPGTVLGHITPQAALATHFPAGLP 202
Cdd:cd07809 155 LPHDYLNWKLTGEKVTGLGDASGTFPIDPRTRDYDAElLAAIDPSRDLRDLLPEVLPAGEVAGRLTPEGAEELGLPAGIP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 203 VVCTTSDKPVEALGAGLLDDETAVISLGTYIalmmngkalpkdpVAYwpimsSIPQTLLYEGYGIRKGMW--TVSWL--R 278
Cdd:cd07809 235 VAPGEGDNMTGALGTGVVNPGTVAVSLGTSG-------------TAY-----GVSDKPVSDPHGRVATFCdsTGGMLplI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 279 DMLGE--SLIQDARAQDLSPEDLLNKKASCVPPGCNGLmTVLDWLT---NPWEPYKRGIMIGF-DSSMDYAWIYRSILES 352
Cdd:cd07809 297 NTTNCltAWTELFRELLGVSYEELDELAAQAPPGAGGL-LLLPFLNgerTPNLPHGRASLVGLtLSNFTRANLARAALEG 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130683 353 VALTLKNNYDNMcNEMNHFAKHVIITGGGSNSDLFMQIFADVFNLPARRNAINGCASLGAAINTAVGLG 421
Cdd:cd07809 376 ATFGLRYGLDIL-RELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
5-421 |
2.78e-36 |
|
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: 139.67 E-value: 2.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDLEGNVVCEGKgllQP--MHTPDADtaehPD------DDLWASLCFAGHDLMSQFAGNKEDIV 76
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAY---REweYYTDDDY----PDakefdpEELWEKICEAIREALKKAGISPEDIS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 77 GIGLGSIRCCRALLKADGTP--AAPLIswqDAR----------------VTRPYEHTNPD-------------------V 119
Cdd:cd07798 74 AVSSTSQREGIVFLDKDGRElyAGPNI---DARgveeaaeiddefgeeiYTTTGHWPTELfpaarllwfkenrpeiferI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 120 AYVTSFSGYLTHRLTGEFKDNIANYFGQWPVDYKSWAWSEDaaVMDKFNIPRHMLFDVQMPGTVLGHITPQAALATHFPA 199
Cdd:cd07798 151 ATVLSISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQE--LLEALGLPPEILPEIVPSGTVLGTVSEEAARELGLPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 200 GLPVVCTTSDKPVEALGAGLLDDETAVISLGTYIALMMngkaLPKDPVAywpimssIPQTLLYEGYGIRKGMWTV----- 274
Cdd:cd07798 229 GTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQM----VTDEPII-------DPERRLWTGCHLVPGKWVLesnag 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 275 ------SWLRDMLgesliqdARAQDLSPEDLlNKKASCVPPGCNGlmtVLDWLTnPWEPYKRGIMI---GF-------DS 338
Cdd:cd07798 298 vtglnyQWLKELL-------YGDPEDSYEVL-EEEASEIPPGANG---VLAFLG-PQIFDARLSGLkngGFlfptplsAS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 339 SMDYAWIYRSILESVALTLKNNYDNMCNEMNHFAKHVIITGGGSNSDLFMQIFADVFNLPARRNAINGCASLGAAINTAV 418
Cdd:cd07798 366 ELTRGDFARAILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAV 445
|
...
gi 16130683 419 GLG 421
Cdd:cd07798 446 GAG 448
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
3-452 |
8.64e-36 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 139.48 E-value: 8.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 3 KKYIIGIDGGSQSTKVVMYDLE-----GNVVCE----GKGLLQPmhtPDADTAEHPDDDLWASLCFAGHDLMSQFAGNKE 73
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDAAdgeelASAVHPyprwVIGLYLP---PPPDQARQHPLDYLEALEAAVREALAQAGVDPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 74 DIVGIGLGSIRCCRALLKADGTPAAPL-----------ISWQD-------ARVTRPYEHTNPDV-AYV------------ 122
Cdd:COG1069 78 DVVGIGVDATGCTPVPVDADGTPLALLpefaenphamvILWKDhtaqeeaERINELAKARGEDYlRYVggiissewfwpk 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 123 ---------------TSF---SGYLTHRLTGEFKDNI------ANY---FGQWPvdykswawSED--AAVMDKFNIPRHM 173
Cdd:COG1069 158 ilhllredpevyeaaDSFvelCDWITWQLTGSLKRSRctaghkALWhahEGGYP--------SEEffAALDPLLDGLADR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 174 LF-DVQMPGTVLGHITPQAALATHFPAGLPVVCTTSDKPVEALGAGLLDDETAVISLGTYIALMMNGKalpkDPVA---- 248
Cdd:COG1069 230 LGtEIYPLGEPAGTLTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGVEPGTLVKVMGTSTCHMLVSP----EERFvpgi 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 249 ---YWPIMssIPQTLLYEG--------YGirkgmwtvsWLRDML--GESLIQDARAQDLSPEDLLNKKASCVPPGCNGLm 315
Cdd:COG1069 306 cgqVDGSI--VPGMWGYEAgqsavgdiFA---------WFVRLLvpPLEYEKEAEERGISLHPLLTEEAAKLPPGESGL- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 316 TVLDW-------LTNPwepYKRGIMIGFDSSMDYAWIYRSILESVALTLKNNYDNMcNEMNHFAKHVIITGGGS-NSDLF 387
Cdd:COG1069 374 HALDWfngnrspLADQ---RLKGVILGLTLGTDAEDIYRALVEATAFGTRAIIERF-EEEGVPIDEIIACGGIAtKNPLV 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130683 388 MQIFADVFNLP---ARrnAINGCAsLGAAINTAVGLGLYPDYATAVDNMVRVKD-IFIPIESNAKRYDA 452
Cdd:COG1069 450 MQIYADVTGRPikvAA--SEQACA-LGAAMFAAVAAGAYPDVEEAMAAMGSGFDkVYTPDPENVAVYDA 515
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
5-421 |
4.78e-35 |
|
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: 136.22 E-value: 4.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDLEGNVV-CEGKGLlqPMHTPDADTAEHPDDDLWASLCFAGHDLMSQFAGNKEDIVGIGLGSI 83
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELaVAARRN--AVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 84 RCCRALLKADGTPAAPLISWQDARVT-------------RPYE-------------------HTNPDV----AYVTSFSG 127
Cdd:cd24121 79 GDGTWLVDEDGRPVRDAILWLDGRAAdiverwqadgiaeAVFEitgtglfpgsqaaqlawlkENEPERleraRTALHCKD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 128 YLTHRLTGEF----KDNIANYFgqwpvDYKSWAWSEDaaVMDKFNIP--RHMLFDVqMPGTVLGH-ITPQAALATHFPAG 200
Cdd:cd24121 159 WLFYKLTGEIatdpSDASLTFL-----DFRTRQYDDE--VLDLLGLEelRHLLPPI-RPGTEVIGpLTPEAAAATGLPAG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 201 LPVVCTTSDKPVEALGAGLLDDETAVISLGTYIALMMngkalpkdpvaywpIMSSIPQTLLYEGYGI---RKGMWT---- 273
Cdd:cd24121 231 TPVVLGPFDVVATALGSGAIEPGDACSILGTTGVHEV--------------VVDEPDLEPEGVGYTIclgVPGRWLrama 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 274 -------VSWLRDMLGESLIQDARAQDLSPEDLLNKKASCVPPGCNGLMtVLDWLTNPWE------PYKRGIMIGFDSSM 340
Cdd:cd24121 297 nmagtpnLDWFLRELGEVLKEGAEPAGSDLFQDLEELAASSPPGAEGVL-YHPYLSPAGErapfvnPNARAQFTGLSLEH 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 341 DYAWIYRSILESVALTLKNNYDNMcnemNHFAKHVIITGGGSNSDLFMQIFADVFNLPARRNAINGCASLGAAINTAVGL 420
Cdd:cd24121 376 TRADLLRAVYEGVALAMRDCYEHM----GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVAL 451
|
.
gi 16130683 421 G 421
Cdd:cd24121 452 G 452
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
2-453 |
1.02e-28 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 118.96 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 2 SKKYIIGIDGGSQSTKVVMYDLEGNVVCEGKGllQPMHTPDADTAEHPDDDL---WASLCFAGHDLMSQFAGNKEDIVGI 78
Cdd:PRK10939 1 SMSYLMALDAGTGSIRAVIFDLNGNQIAVGQA--EWRHLAVPDVPGSMEFDLeknWQLACQCIRQALQKAGIPASDIAAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 79 GLGSIRCCRALLKADGTPAaplisWQ----DARVTRP---------------YE------------------HTNPDV-- 119
Cdd:PRK10939 79 SATSMREGIVLYDRNGTEI-----WAcanvDARASREvselkelhnnfeeevYRcsgqtlalgalprllwlaHHRPDIyr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 120 --AYVTSFSGYLTHRLTGEFKDNIANYFGQWPVDYKSWAWSEDAAvmDKFNIPRHMLFDVQMPGTVLGHITPQAALATHF 197
Cdd:PRK10939 154 qaHTITMISDWIAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALL--EMAGLRADILPPVKETGTVLGHVTAKAAAETGL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 198 PAGLPVVCTTSDKPVEALGAGLLD-DETAVISlGTYIALMMNgkaLPKDpvAYWPIMS------SIPQTLLYEGYGIRKG 270
Cdd:PRK10939 232 RAGTPVVMGGGDVQLGCLGLGVVRpGQTAVLG-GTFWQQVVN---LPAP--VTDPNMNirinphVIPGMVQAESISFFTG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 271 MwTVSWLRDMLGESLIQDARAQDLSPEDLLNKKASCVPPGCNGLMTVldwltnpwepykrgimigFDSSMDY-AW----- 344
Cdd:PRK10939 306 L-TMRWFRDAFCAEEKLLAERLGIDAYSLLEEMASRVPVGSHGIIPI------------------FSDVMRFkSWyhaap 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 345 ----------------IYRSILESVALTLKNNYDNMCNEMNHFAKHVIITGGGSNSDLFMQIFADVFNLPARRNAINGCA 408
Cdd:PRK10939 367 sfinlsidpekcnkatLFRALEENAAIVSACNLQQIAAFSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEAT 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 16130683 409 SLGAAINTAVGLGLYPDYATAVDNMVRVKDIFIPIESNAKRYDAM 453
Cdd:PRK10939 447 ALGCAIAAGVGAGIYSSLAETGERLVRWERTFEPNPENHELYQEA 491
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
5-449 |
1.63e-24 |
|
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: 106.01 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDLEGNVVCEG-KGLLQpmHTPDADTAEHPDDDLWASLCFAGHDLMSQFAGNKEDIVGIGlgsI 83
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAqKEHEQ--IYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIG---I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 84 RCCR--ALL--KADGTPAAPLISWQDARvTRPYEHT---NPDVAYVTS---------FSG-------------------- 127
Cdd:cd07769 76 TNQRetTVVwdKKTGKPLYNAIVWQDRR-TADICEElkaKGLEERIREktglpldpyFSAtkikwildnvpgareraerg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 128 ---------YLTHRLTGEFK---D----------NIANyfGQWpvdykswawseDAAVMDKFNIPRHMLFDVQMPGTVLG 185
Cdd:cd07769 155 ellfgtidtWLIWKLTGGKVhvtDvtnasrtmlfNIHT--LEW-----------DDELLELFGIPRSMLPEVRPSSEVFG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 186 HITPqaalaTHFPAGLPVVCTTSDKPVEALGAGLLDDETAVISLGTYIALMMN--GKALPKDP-----VAYwpimsSIPQ 258
Cdd:cd07769 222 YTDP-----EGLGAGIPIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNtgEKPVPSKNgllttIAW-----QIGG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 259 TLLY--EGyGIRKGMWTVSWLRDMLGesLIQDARaqDLspEDLLNKKAS----CVPPGCNGLMTvldwltnP-WEPYKRG 331
Cdd:cd07769 292 KVTYalEG-SIFIAGAAIQWLRDNLG--LIEDAA--ET--EELARSVEDnggvYFVPAFSGLGA-------PyWDPDARG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 332 IMIGFDSSMDYAWIYRSILESVALTLKNNYDNMCNEMNHFAKHVIITGGGSNSDLFMQIFADVFNLPARRNAINGCASLG 411
Cdd:cd07769 358 AIVGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALG 437
|
490 500 510
....*....|....*....|....*....|....*...
gi 16130683 412 AAINTAVGLGLYPDYATAVDNMvRVKDIFIPIESNAKR 449
Cdd:cd07769 438 AAYLAGLAVGFWKDLDELASLW-QVDKRFEPSMDEEER 474
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
5-429 |
2.96e-22 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 99.33 E-value: 2.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDLEGNVVCEGkgllqpmHTPDADT--AEHPD------DDLWASLCFAGHDLMSQFAGnkEDIV 76
Cdd:PRK10331 3 VILVLDCGATNVRAIAVDRQGKIVARA-------STPNASDiaAENSDwhqwslDAILQRFADCCRQINSELTE--CHIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 77 GIGLGSIRCCRALLKADGTPAAPLISWQDARvTRP---------------------------------YEHTNPDV-AYV 122
Cdd:PRK10331 74 GITVTTFGVDGALVDKQGNLLYPIISWKCPR-TAAvmenieryisaqqlqqisgvgafsfntlyklvwLKENHPQLlEQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 123 TSF---SGYLTHRLTGEFKDNIANYFGQWPVDYKSWAWSEDaaVMDKFNIPRHMLFDVQMPGTVLGHITPQAALATHFPA 199
Cdd:PRK10331 153 HAWlfiSSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPE--ILQATGLSRRLFPRLVEAGEQIGTLQPSAAALLGLPV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 200 GLPVVCTTSDKPVEALGAGLLDDEtAVISLGTYIALMmngkalpkdpvaywpIMSSIPQTLL---YEGYGI----RKGMW 272
Cdd:PRK10331 231 GIPVISAGHDTQFALFGSGAGQNQ-PVLSSGTWEILM---------------VRSAQVDTSLlsqYAGSTCeldsQSGLY 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 273 T--VSWLrdmlGESLIQDARAQDLSPE---DLLNKKASCVPPGCNGLMTVLDWLTNpwepyKRGIMIGFDSSMDYAWIYR 347
Cdd:PRK10331 295 NpgMQWL----ASGVLEWVRKLFWTAEtpyQTMIEEARAIPPGADGVKMQCDLLAC-----QNAGWQGVTLNTTRGHFYR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 348 SILESVALTLKNNYDnMCNEMNHF-AKHVIITGGGSNSDLFMQIFADVFNLPARRNAINGCASLGAAINTAVGLGLYPDY 426
Cdd:PRK10331 366 AALEGLTAQLKRNLQ-VLEKIGHFkASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSP 444
|
...
gi 16130683 427 ATA 429
Cdd:PRK10331 445 EQA 447
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
225-420 |
3.21e-22 |
|
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: 94.31 E-value: 3.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 225 AVISLGTYIALMMNGK-ALPKDPVAYWPIMSSI-PQTLLYEGyGIRKGMWTVSWLRDMLGEsLIQDARAQDLSPEDLLNK 302
Cdd:pfam02782 1 LAISAGTSSFVLVETPePVLSVHGVWGPYTNEMlPGYWGLEG-GQSAAGSLLAWLLQFHGL-REELRDAGNVESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 303 KASCVPPGcnGLMTVLDWLTN---PWEPYKRGIMIGFDSSMDYAWIYRSILESVALTLKNNYDNMCNEMNHFAKHVIITG 379
Cdd:pfam02782 79 LAAVAPAG--GLLFYPDFSGNrapGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16130683 380 GGSNSDLFMQIFADVFNLPARRNAINGCASLGAAINTAVGL 420
Cdd:pfam02782 157 GGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVAA 197
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
5-455 |
3.22e-22 |
|
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: 99.56 E-value: 3.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDLEGNVVCEGKGLLQPMHtPDADTAEHPDDDLWASLCFAGHDLMSQFAGNKEDIVGIGLGSIR 84
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLY-PEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 85 CCRALLKAD-GTPAAPLISWQDAR--------------------------VTRpyeHTNPDVAYVTSFS-GYLTHRL--- 133
Cdd:cd07793 80 NTFLTWDKKtGKPLHNFITWQDLRaaelceswnrslllkalrggskflhfLTR---NKRFLAASVLKFStAHVSIRLlwi 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 134 ---TGEFKDNIAN---YFG---QWPV-----------DYkSWA------------WSEdaAVMDKFNIPRHMLFDVQMPG 181
Cdd:cd07793 157 lqnNPELKEAAEKgelLFGtidTWLLwkltggkvhatDY-SNAsatglfdpftleWSP--ILLSLFGIPSSILPEVKDTS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 182 TVLGHITPQAalathFPAGLPVVCTTSDKPVEALGAGLLDDETAVISLGTYIALMMN-GKALPKD-----PVAYWPIMSS 255
Cdd:cd07793 234 GDFGSTDPSI-----FGAEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINtGSKPHASvkglyPLVGWKIGGE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 256 IpqTLLYEGYGIRKGMwTVSWLRDMLGESliqdaraqdlSPEDLlNKKASCVPPgCNGLMTV--LDWLTNP-WEPYKRGI 332
Cdd:cd07793 309 I--TYLAEGNASDTGT-VIDWAKSIGLFD----------DPSET-EDIAESVED-TNGVYFVpaFSGLQAPyNDPTACAG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 333 MIGFDSSMDYAWIYRSILESVALTLKNNYDNMCNEMNHFAKHVIITGGGSNSDLFMQIFADVFNLPARRNAINGCASLGA 412
Cdd:cd07793 374 FIGLTPSTTKAHLVRAILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGA 453
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 16130683 413 AINTAVGLGLYpDYATAVDNMVRVKDIFIPIESNAKRYDAMNK 455
Cdd:cd07793 454 AFLAGLASGIW-KSKEELKKLRKIEKIFEPKMDNEKREELYKN 495
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
5-450 |
6.86e-20 |
|
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: 92.30 E-value: 6.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDL-EGNVVCEGKGLLQPMHTPDADTAEHPDDDLWASLCFAGHDLMSQFAGNKEDIVGIGLgSI 83
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDLyAGLEMAQEPVPYYQDSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGV-DA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 84 RCCRALLKADGTPAAPLIS---------WQDAR-----------------------------------VTRPYEHTNPDV 119
Cdd:cd07768 80 TCSLAIFDREGTPLMALIPypnednvifWMDHSavneaqwinmqcpqqlldylggkispemgvpklkyFLDEYSHLRDKH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 120 AYVTSFSGYLTHRLTGEFKDNIANYFGQWPVDYKSWAWS----EDAAVMDKFNIPRHMLFDVQMPGTVLGHITPQAALAT 195
Cdd:cd07768 160 FHIFDLHDYIAYELTRLYEWNICGLLGKENLDGEESGWSssffKNIDPRLEHLTTTKNLPSNVPIGTTSGVALPEMAEKM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 196 HFPAGLPVV--CTTSDKPVEALGAGLLDDETAVISlGTYIALMMNGKALPKDPVAYWPIMSSI-PQTLLYEGygirkGMW 272
Cdd:cd07768 240 GLHPGTAVVvsCIDAHASWFAVASPHLETSLFMIA-GTSSCHMYGTTISDRIPGVWGPFDTIIdPDYSVYEA-----GQS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 273 TVSWLRDMLGESLIQdARAQDLSPED------LLNKKASCV---PPGCNGLMTVLDWLTNPWE---PYKRGIMIGF--DS 338
Cdd:cd07768 314 ATGKLIEHLFESHPC-ARKFDEALKKgadiyqVLEQTIRQIeknNGLSIHILTLDMFFGNRSEfadPRLKGSFIGEslDT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 339 SM-DYAWIYRSILESVALTLKNNYDNMCNEMNHFaKHVIITGGGSNSDLFMQIFADVFNLPARRNAINGCASLGAAINTA 417
Cdd:cd07768 393 SMlNLTYKYIAILEALAFGTRLIIDTFQNEGIHI-KELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAAVLAK 471
|
490 500 510
....*....|....*....|....*....|....*.
gi 16130683 418 VGLG---LYPDYATAVDNMVRVKDIFIPIESNAKRY 450
Cdd:cd07768 472 VAAGkkqLADSITEADISNDRKSETFEPLAYRLGAD 507
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
2-449 |
8.02e-20 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 92.05 E-value: 8.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 2 SKKYIIGIDGGSQSTKVVMYDLEGNVVCEGkgllQ---PMHTPDADTAEHPDDDLWASLCFAGHDLMSQFAGNKEDIVGI 78
Cdd:COG0554 1 MKKYILAIDQGTTSTRAILFDRDGNIVAVA----QrefTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 79 GLGSIR--CcraLL--KADGTPAAPLISWQDARvTRPY--------------EHTN--PDvAYvtsFSG----------- 127
Cdd:COG0554 77 GITNQRetT---VVwdRKTGKPLYNAIVWQDRR-TADIceelkadgledlirEKTGlvLD-PY---FSAtkikwildnvp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 128 ------------------YLTHRLTGE---------------FkdNIANyfGQWpvdykswawseDAAVMDKFNIPRHML 174
Cdd:COG0554 149 gareraeagellfgtidsWLIWKLTGGkvhvtdvtnasrtmlF--NIHT--LDW-----------DDELLELFGIPRSML 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 175 FDVQMPGTVLGHITPqaalaTHFPAGLPVV----------------------CT----------TSDKPVEAlGAGLLdd 222
Cdd:COG0554 214 PEVRPSSEVFGETDP-----DLFGAEIPIAgiagdqqaalfgqacfepgmakNTygtgcfllmnTGDEPVRS-KNGLL-- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 223 etavislgTYIALMMNGK---ALpkdpvaywpimssipqtllyEGyGIRKGMWTVSWLRDMLGesLIQDAraQDLspEDL 299
Cdd:COG0554 286 --------TTIAWGLGGKvtyAL--------------------EG-SIFVAGAAVQWLRDGLG--LIDSA--AES--EAL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 300 lnkkASCVPPgCNGLMTVldwltnP---------WEPYKRGIMIGFDSSMDYAWIYRSILESVALTLKNNYDNMCNEMNH 370
Cdd:COG0554 331 ----ARSVED-NGGVYFV------PaftglgapyWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADSGI 399
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130683 371 FAKHVIITGGGSNSDLFMQIFADVFNLPARRNAINGCASLGAAINTAVGLGLYPDYATAVDNMvRVKDIFIPIESNAKR 449
Cdd:COG0554 400 PLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEELAALW-KVDRRFEPQMDEEER 477
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
176-452 |
1.60e-19 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 91.45 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 176 DVQMPGTVLGHITPQAALATHFPAGLPVVCTTSDKPVEALGAGLLDDE-TAVIslGTYIALMMNGkalpkdpvaywPIMS 254
Cdd:PRK04123 241 ETWTAGEPAGTLTAEWAQRLGLPEGVAVSVGAFDAHMGAVGAGAEPGTlVKVM--GTSTCDILLA-----------DKQR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 255 SIP----QTllyEGyGIRKGMWTV-----------SWLRDMLG-ESLIQDARAQDLSPEDLLNKKASCVPPGCNGLMtVL 318
Cdd:PRK04123 308 AVPgicgQV---DG-SIVPGLIGYeagqsavgdifAWFARLLVpPEYKDEAEARGKQLLELLTEAAAKQPPGEHGLV-AL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 319 DWLTNPWEPYK----RGIMIGFDSSMDYAWIYRSILESVALTLKNNYDNMcnEMNHFAKHVIITGGG--SNSDLFMQIFA 392
Cdd:PRK04123 383 DWFNGRRTPLAdqrlKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECF--EDQGVPVEEVIAAGGiaRKNPVLMQIYA 460
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130683 393 DVFNLPARRNAINGCASLGAAINTAVGLGLYPDYATAVDNMVRVKD-IFIPIESNAKRYDA 452
Cdd:PRK04123 461 DVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEAQQAMASPVEkTYQPDPENVARYEQ 521
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
5-461 |
2.55e-19 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 90.53 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDLEGNVVCEGKgLLQPMHTPDADTAEHPDDDLWASL--CFA---------GHDLMSqfagnke 73
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYDRDARPVASHQ-VEFTQIYPQAGWVEHDPMEILESVltCIAkalekaaakGHNVDS------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 74 DIVGIGLGSIR-CCRALLKADGTPAAPLISWQDARvTRP------YEHTNPDVAYV--------TSFSG----------- 127
Cdd:PLN02295 73 GLKAIGITNQReTTVAWSKSTGRPLYNAIVWMDSR-TSSicrrleKELSGGRKHFVetcglpisTYFSAtkllwllenvd 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 128 ------------------YLTHRLTG-----EFKDNIANYFGQWPVDYKSWAWseDAAVMDKFNIPRHMLFDVQMPGTVL 184
Cdd:PLN02295 152 avkeavksgdalfgtidsWLIWNLTGgasggVHVTDVTNASRTMLMNLKTLDW--DKPTLEALGIPAEILPKIVSNSEVI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 185 GHITPQAALAthfpaGLPVVCTTSDKPVEALGAGLLDDEtAVISLGTYIALMMN--GKALPKD-----PVAYwPIMSSIP 257
Cdd:PLN02295 230 GTIAKGWPLA-----GVPIAGCLGDQHAAMLGQRCRPGE-AKSTYGTGCFILLNtgEEVVPSKhglltTVAY-KLGPDAP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 258 QTLLYEGyGIRKGMWTVSWLRDMLGesLIQDARaqdlSPEDLlnkkASCVP--------PGCNGLMTvldwltnP-WEPY 328
Cdd:PLN02295 303 TNYALEG-SVAIAGAAVQWLRDNLG--IIKSAS----EIEAL----AATVDdtggvyfvPAFSGLFA-------PrWRDD 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 329 KRGIMIGFDSSMDYAWIYRSILESVALTLKNNYDNM----CNEMNH---FAKHViiTGGGSNSDLFMQIFADVFNLPARR 401
Cdd:PLN02295 365 ARGVCVGITRFTNKAHIARAVLESMCFQVKDVLDAMrkdaGEEKSHkglFLLRV--DGGATANNLLMQIQADLLGSPVVR 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130683 402 NAINGCASLGAAINTAVGLGLYPDYATAVDNMVRVKDIFIP---IESNAKRYDAMNKGIFKDL 461
Cdd:PLN02295 443 PADIETTALGAAYAAGLAVGLWTEEEIFASEKWKNTTTFRPkldEEERAKRYASWCKAVERSF 505
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
5-216 |
5.81e-19 |
|
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: 86.24 E-value: 5.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDLEGNVVceGKGLLQ-PMHTPDADTAEHPDDDLWASLCFAGHDLMSQFAGNKEDIVGIGLGSI 83
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKII--AVAQLEnPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 84 RCCRALLKADGTPAAPLISWQDAR-------------VTRPYEHTN-------------------PDVA-----YVTSfS 126
Cdd:pfam00370 79 GHGTVLLDKNDKPLYNAILWKDRRtaeivenlkeegnNQKLYEITGlpiwpgftlsklrwikenePEVFekihkFLTI-H 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 127 GYLTHRLTGEFKDNIANYFGQWPVDYKSWAWSEDaaVMDKFNIPRHMLFDVQMPGTVLGHITPQAALATHFPAGLPVVCT 206
Cdd:pfam00370 158 DYLRWRLTGVFVTDHTNASRSMMFNIHKLDWDPE--LLAALGIPRDHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGG 235
|
250
....*....|
gi 16130683 207 TSDKPVEALG 216
Cdd:pfam00370 236 GGDQQAAAFG 245
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
3-455 |
6.35e-19 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 89.26 E-value: 6.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 3 KKYIIGIDGGSQSTKVVMYDLEGNVVCEgKGLLQPMHTPDADTAEHPDDDLWASLCFAGHDLMSQFAGNKE--DIVGIGL 80
Cdd:PTZ00294 1 MKYIGSIDQGTTSTRFIIFDEKGNVVSS-HQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKGPsfKIKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 81 GSIR-CCRALLKADGTPAAPLISWQDAR----VTRPYEHTNPDVAYV--------TSFSGY------------------- 128
Cdd:PTZ00294 80 TNQReTVVAWDKVTGKPLYNAIVWLDTRtydiVNELTKKYGGSNFFQkitglpisTYFSAFkirwmlenvpavkdavkeg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 129 ----------LTHRLTGE--FKDNIANYFGQWPVDYKSWAWSEDaaVMDKFNIPRHMLFDVQMPGTVLGHITPQAALATH 196
Cdd:PTZ00294 160 tllfgtidtwLIWNLTGGksHVTDVTNASRTFLMNIKTLKWDEE--LLNKFGIPKETLPEIKSSSENFGTISGEAVPLLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 197 fpaGLPVVCTTSDKPVEALGAGLLDDETAVISLGTYIALMMNgkalpkdpVAYWPIMSS--IPQTLLY------------ 262
Cdd:PTZ00294 238 ---GVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMN--------TGTEIVFSKhgLLTTVCYqlgpngptvyal 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 263 EGyGIRKGMWTVSWLRDMLGesLIQDARAQDLSPEDLLNKKASCVPPGCNGLMTvldwltnP-WEPYKRGIMIGFDSSMD 341
Cdd:PTZ00294 307 EG-SIAVAGAGVEWLRDNMG--LISHPSEIEKLARSVKDTGGVVFVPAFSGLFA-------PyWRPDARGTIVGMTLKTT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 342 YAWIYRSILESVALTLKNNYDNMCNEMNHFAKHVIITGGGSNSDLFMQIFADVFNLPARRNAINGCASLGAAINTAVGLG 421
Cdd:PTZ00294 377 RAHIVRAALEAIALQTNDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVG 456
|
490 500 510
....*....|....*....|....*....|....*
gi 16130683 422 LYPDyATAVDNMVRVKD-IFIPIESNAKRYDAMNK 455
Cdd:PTZ00294 457 VWKS-LEEVKKLIRRSNsTFSPQMSAEERKAIYKE 490
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
5-449 |
1.10e-18 |
|
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: 88.70 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDLEGNVVCEG-KGLLQpmHTPDADTAEHPDDDLWASLCFAGHDLMSQfAGNK-EDIVGIGLGS 82
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAqREFTQ--IYPKPGWVEHDPEEIWESQLAVAREALAK-AGIRaSDIAAIGITN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 83 IRCCrALL--KADGTPAAPLISWQDARvTRPY--------------EHTN--PDvAYvtsFSG----------------- 127
Cdd:cd07786 78 QRET-TVVwdRETGKPVYNAIVWQDRR-TADIceelkaegheemirEKTGlvLD-PY---FSAtkirwildnvpgarera 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 128 ------------YLTHRLTGefkdnianyfGQWPV-DY-----------KSWAWSEDaaVMDKFNIPRHMLFDVQMPGTV 183
Cdd:cd07786 152 ergelafgtidsWLIWKLTG----------GKVHAtDVtnasrtmlfniHTLEWDDE--LLELFGIPASMLPEVKPSSEV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 184 LGHITPqaalaTHFPAGLPVVCTTSDKPVEALGAGLLDDETAVISLGTYIALMMN-GKALPKDP------VAYwpimsSI 256
Cdd:cd07786 220 FGYTDP-----DLLGAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMNtGEKPVRSKngllttIAW-----QL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 257 PQTLLY--EGyGIRKGMWTVSWLRDMLGesLIQDARAQdlspEDLlnkkASCVPPGcNGLMTV--LDWLTNP-WEPYKRG 331
Cdd:cd07786 290 GGKVTYalEG-SIFIAGAAVQWLRDGLG--LIESAAET----EAL----ARSVPDN-GGVYFVpaFTGLGAPyWDPDARG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 332 IMIGFDSSMDYAWIYRSILESVALTLKNNYDNMCNEMNHFAKHVIITGGGSNSDLFMQIFADVFNLPARRNAINGCASLG 411
Cdd:cd07786 358 AIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALG 437
|
490 500 510
....*....|....*....|....*....|....*...
gi 16130683 412 AAINTAVGLGLYPDYAtAVDNMVRVKDIFIPIESNAKR 449
Cdd:cd07786 438 AAYLAGLAVGLWKSLD-ELAKLWQVDRRFEPSMSEEER 474
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
5-464 |
2.78e-17 |
|
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: 84.51 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDLEGNVVCEGkglLQP--MHTPDADTAEHPDDDLWASLCFAGHDLMSQFAGNKEDIVGIGLGS 82
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATA---SQPitTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 83 iRCCRALLKADGTPAAP---------LISWQDARVTRPYEHTNPDVAYVTSFSG-------------------------- 127
Cdd:cd07782 78 -TCSLVVLDAEGKPVSVspsgddernVILWMDHRAVEEAERINATGHEVLKYVGgkispemeppkllwlkenlpetwaka 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 128 --------YLTHRLTG---------------EFKDNIAnyfGQWPVDYkswaWS----EDAAVMDKFNIPRHmlfdVQMP 180
Cdd:cd07782 157 ghffdlpdFLTWKATGsltrslcslvckwtyLAHEGSE---GGWDDDF----FKeiglEDLVEDNFAKIGSV----VLPP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 181 GTVLGH-ITPQAALATHFPAGLPVvcTTSdkPVEA-------LGAGLLDDETAVISLGTYIALM-------MngkALPKD 245
Cdd:cd07782 226 GEPVGGgLTAEAAKELGLPEGTPV--GVS--LIDAhagglgtLGADVGGLPCEADPLTRRLALIcgtsschM---AVSPE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 246 PVA-------YWPIMssIPqtllyegygirkGMW--------TVSWLRDML-----GESLIQDARAQDLSPEDLLN---- 301
Cdd:cd07782 299 PVFvpgvwgpYYSAM--LP------------GLWlneggqsaTGALLDHIIethpaYPELKEEAKAAGKSIYEYLNerle 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 302 --KKASCVPPGC--NGLMTVLDWLTN--PW-EPYKRGIMIG--FDSSM-DYAWIYRSILESVALTLKNNYDNMcNEMNHF 371
Cdd:cd07782 365 qlAEEKGLPLAYltRDLHVLPDFHGNrsPLaDPTLRGMISGltLDTSLdDLALLYLATLQALAYGTRHIIEAM-NAAGHK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 372 AKHVIITGGGSNSDLFMQIFADVFNLPARRNAINGCASLGAAINTAVGLGLYPDYATAVDNMVRVKDIFIPIESNAKRYD 451
Cdd:cd07782 444 IDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDAMAAMSGPGKVVEPNEELKKYHD 523
|
570
....*....|...
gi 16130683 452 AMNKgIFKDLTKH 464
Cdd:cd07782 524 RKYE-VFLKMYED 535
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
128-427 |
1.86e-16 |
|
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: 81.42 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 128 YLTHRLTGEfKDN---IANYFGQwpVDYKSWAWSEDaaVMDKFNIPRHMLFDVQMPGTVLGHITPQAALATHFPaGLPVV 204
Cdd:cd07771 157 LLNYLLTGE-KVAeytIASTTQL--LDPRTKDWSEE--LLEKLGLPRDLFPPIVPPGTVLGTLKPEVAEELGLK-GIPVI 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 205 CTTS-DKPVEALGAGLLDDETAVISLGTYiALMmnGKALPKdpvaywPIMSsiPQTLLYE-----GYG--IRK-----GM 271
Cdd:cd07771 231 AVAShDTASAVAAVPAEDEDAAFISSGTW-SLI--GVELDE------PVIT--EEAFEAGftnegGADgtIRLlknitGL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 272 WtvswlrdmlgesLIQDARAQ------DLSPEDLLNKKASCVPPGC-------------NGLMTVLDWL--TNPWEPYKR 330
Cdd:cd07771 300 W------------LLQECRREweeegkDYSYDELVALAEEAPPFGAfidpddprflnpgDMPEAIRAYCreTGQPVPESP 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 331 GImigfdssmdyawIYRSILESVALTLKNNYDNMCNEMNHFAKHVIITGGGSNSDLFMQIFADVFNLPARRNAINgCASL 410
Cdd:cd07771 368 GE------------IARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAGPVE-ATAI 434
|
330
....*....|....*..
gi 16130683 411 GAAINTAVGLGLYPDYA 427
Cdd:cd07771 435 GNLLVQLIALGEIKSLE 451
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
5-414 |
7.29e-16 |
|
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: 79.57 E-value: 7.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDLEGNVVCEgkglLQPMHTPDADTAEHPDDDLW--ASLCFAGHDLMSQFAGN-KEDIVGIGLg 81
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLESGRILE----SVSRPTPAPISSDDPGRSEQdpEKILEAVRNLIDELPREyLSDVTGIGI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 82 sirCCR----ALLKADGTPAAPLISWQDARVTRPYE-------------------------------HTNPDVAYVTSFS 126
Cdd:cd07777 76 ---TGQmhgiVLWDEDGNPVSPLITWQDQRCSEEFLgglstygeellpksgmrlkpgyglatlfwllRNGPLPSKADRAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 127 ---GYLTHRLTGEFKDNI----ANYFGQWPVDYKSWawseDAAVMDKFNIPRHMLFDVQMPGTVLGHITPQAalathfPA 199
Cdd:cd07777 153 tigDYIVARLTGLPKPVMhptnAASWGLFDLETGTW----NKDLLEALGLPVILLPEIVPSGEIVGTLSSAL------PK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 200 GLPVVCTTSDKPVEALGAGLLDDETAVISLGT--YIALMMNGKALPkDPVAYWP--------IMSSIPqtllyegygirk 269
Cdd:cd07777 223 GIPVYVALGDNQASVLGSGLNEENDAVLNIGTgaQLSFLTPKFELS-GSVEIRPffdgryllVAASLP------------ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 270 GMWTVSWLRDMLgESLIQDArAQDLSPEDLLNKKASCVPPGCNGLMTV-LDWLTNPWEPYKRGIMIGFDSSM-DYAWIYR 347
Cdd:cd07777 290 GGRALAVLVDFL-REWLREL-GGSLSDDEIWEKLDELAESEESSDLSVdPTFFGERHDPEGRGSITNIGESNfTLGNLFR 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130683 348 SILESVALTLKNNYDNMCnEMNHFAKHVIITGGGSN-SDLFMQIFADVFNLPARRNAINGCASLGAAI 414
Cdd:cd07777 368 ALCRGIAENLHEMLPRLD-LDLSGIERIVGSGGALRkNPVLRRIIEKRFGLPVVLSEGSEEAAVGAAL 434
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
4-449 |
1.51e-13 |
|
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: 72.56 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 4 KYIIGIDGGSQSTKVVMYDLEGNVVCEgKGLLQPMHTPDADTAEHPDDDLWASL--CFAG-HDLMSQFAGNKEDIVGIGL 80
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFDSTGELVAS-HQVEHKQIYPKPGWVEHDPMEILESVyeCIEEaVEKLKALGISPSDIKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 81 GSIRccRALL---KADGTPAAPLISWQDAR----VTRPYEHTNPDVAYV---------TSFSGY---------------- 128
Cdd:cd07792 80 TNQR--ETTVvwdKSTGKPLYNAIVWLDTRtsdtVEELSAKTPGGKDHFrkktglpisTYFSAVklrwlldnvpevkkav 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 129 -------------LTHRLTGEFKD----------------NIANyfGQWpvdykswawseDAAVMDKFNIPRHMLFDVQM 179
Cdd:cd07792 158 ddgrllfgtvdswLIWNLTGGKNGgvhvtdvtnasrtmlmNLRT--LQW-----------DPELCEFFGIPMSILPEIRS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 180 PGTVLGHITpqaalATHFpAGLPVVCTTSDKPVEALGAGLLDDETAVISLGTYIALMMN-----------------GKAL 242
Cdd:cd07792 225 SSEVYGKIA-----SGPL-AGVPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNtgeepvfskhgllttvaYKLG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 243 PKDPVAYwpimssipqTLlyEGYGIRKGMwTVSWLRDMLGesLIQDAraQDLspEDLlnkkASCVP--------PGCNGL 314
Cdd:cd07792 299 PDAPPVY---------AL--EGSIAIAGA-AVQWLRDNLG--IISSA--SEV--ETL----AASVPdtggvyfvPAFSGL 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 315 MTvldwltnP-WEPYKRGIMIGFDSSMDYAWIYRSILESVALTLKNNYDNMCNEMNHFAKHVIITGGGSNSDLFMQIFAD 393
Cdd:cd07792 357 FA-------PyWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQAD 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130683 394 VFNLPARRNAINGCASLGAAINTAVGLGLYPDYATAVDNMVRVKDIFIPIESNAKR 449
Cdd:cd07792 430 ILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSLNEGGRTVFEPQISEEER 485
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
151-453 |
2.00e-12 |
|
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: 69.12 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 151 DYKSWAWSEDAavMDKFNIP--RHMLFDVQMPGTVLGHITPQAALATHFPAGLPVVCTTSDKPVEALGAGLLDDEtAVIS 228
Cdd:cd07776 215 DIRSRKWSPEL--LDAATAPdlKEKLGELVPSSTVAGGISSYFVERYGFSPDCLVVAFTGDNPASLAGLGLEPGD-VAVS 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 229 LGTYIALMMNGKALPKDPVAYwpIMSSIPQTLLYEGYGIRK-GMWTVSWLRDMLGEsliqdaraQDLspeDLLNKKASCV 307
Cdd:cd07776 292 LGTSDTVFLVLDEPKPGPEGH--VFANPVDPGSYMAMLCYKnGSLARERVRDRYAG--------GSW---EKFNELLEST 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 308 PPGCNG-LMTVLDwltnPWE--PYKRGIMIGF------DSSMDYAWIYRSILESVALTLKNNYDNMcnEMNHFAKHVIIT 378
Cdd:cd07776 359 PPGNNGnLGLYFD----EPEitPPVPGGGRRFfgddgvDAFFDPAVEVRAVVESQFLSMRLHAERL--GSDIPPTRILAT 432
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130683 379 GGGSNSDLFMQIFADVFNLPARRNAINGCASLGAAINTAVGL----GLYPDYATAVDNMVRVKDIFIPIESNAKRYDAM 453
Cdd:cd07776 433 GGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLlcagSGDFSPEFVVFSAEEPKLVAEPDPEAAEVYDKL 511
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
7-413 |
9.88e-10 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 60.75 E-value: 9.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 7 IGIDGGSQSTKVVMYDLEGNVVCEGKGLLQpMHTPDADTAEHPDDDLWASLCFAGHDLMSQFAGNkeDIVGIGLGSIRCC 86
Cdd:PRK15027 3 IGIDLGTSGVKVILLNEQGEVVASQTEKLT-VSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQ--DVKALGIAGQMHG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 87 RALLKADGTPAAPLISWQDARV--------------------------TRP----YEHTNPD----VAYVTSFSGYLTHR 132
Cdd:PRK15027 80 ATLLDAQQRVLRPAILWNDGRCaqecallearvpqsrvitgnlmmpgfTAPkllwVQRHEPEifrqIDKVLLPKDYLRLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 133 LTGEFKDNIANYFGQWPVDYKSWAWSEdaAVMDKFNIPRHmlfdvQMPG-----TVLGHITPQAALATHFPAgLPVVCTT 207
Cdd:PRK15027 160 MTGEFASDMSDAAGTMWLDVAKRDWSD--VMLQACHLSRD-----QMPAlyegsEITGALLPEVAKAWGMAT-VPVVAGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 208 SDKPVEALGAGLLDDETAVISLGT---YIALMMNGKALPKDPV--------AYWPIMSSipqtllyegygIRKGMWTVSW 276
Cdd:PRK15027 232 GDNAAGAVGVGMVDANQAMLSLGTsgvYFAVSEGFLSKPESAVhsfchalpQRWHLMSV-----------MLSAASCLDW 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 277 LRDMLGE----SLIQDARAQDLSPEdllnkkASCVPPGCNGLMTVLDwltnpwEPYKRGIMIGFDSSMDYAWIYRSILES 352
Cdd:PRK15027 301 AAKLTGLsnvpALIAAAQQADESAE------PVWFLPYLSGERTPHN------NPQAKGVFFGLTHQHGPNELARAVLEG 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130683 353 VALTLKNNYDnMCNEMNHFAKHVIITGGGSNSDLFMQIFADV--FNLPARRNAINGCAsLGAA 413
Cdd:PRK15027 369 VGYALADGMD-VVHACGIKPQSVTLIGGGARSEYWRQMLADIsgQQLDYRTGGDVGPA-LGAA 429
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
1-413 |
1.25e-07 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 54.06 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 1 MSKKYIIGIDGGSQSTKVVMYDLEGNVVCEGkgllQPMHT---PDADTAEHPDDDLWASLCFAGHDLMSQFAGNKEDIVG 77
Cdd:PRK00047 2 MMKKYILALDQGTTSSRAIIFDHDGNIVSVA----QKEFTqifPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 78 IGLGSIRCCRALL-KADGTPAAPLISWQDARvTRPY--------------EHTN--PDvAYvtsFSG------------- 127
Cdd:PRK00047 78 IGITNQRETTVVWdKETGRPIYNAIVWQDRR-TADIceelkrdgyedyirEKTGlvID-PY---FSGtkikwildnvega 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 128 ----------------YLTHRLTGefkdnianyfGQWPV-DY-----------KSWAWSEDaaVMDKFNIPRHMLFDVQ- 178
Cdd:PRK00047 153 reraekgellfgtidtWLVWKLTG----------GKVHVtDYtnasrtmlfniHTLDWDDE--LLELLDIPRSMLPEVRp 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 179 --------MPGTVLGHITP--------QAALATH--FPAGLpVVCT----------TSDKPVEAlGAGLLddetavislg 230
Cdd:PRK00047 221 ssevygktNPYGFFGGEVPiagiagdqQAALFGQlcFEPGM-AKNTygtgcfmlmnTGEKAVKS-ENGLL---------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 231 TYIALMMNGK---ALpkdpvaywpimssipqtllyEGyGIRKGMWTVSWLRDMLGesLIQDARAQdlspEDLLNKKASC- 306
Cdd:PRK00047 289 TTIAWGIDGKvvyAL--------------------EG-SIFVAGSAIQWLRDGLK--IISDASDS----EALARKVEDNd 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 307 ---VPPGCNGLMTvldwltnP-WEPYKRGIMIGFDSSMDYAWIYRSILESVALTLKNNYDNMCNEMNHFAKHVIITGGGS 382
Cdd:PRK00047 342 gvyVVPAFTGLGA-------PyWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADSGIRLKELRVDGGAV 414
|
490 500 510
....*....|....*....|....*....|.
gi 16130683 383 NSDLFMQIFADVFNLPARRNAINGCASLGAA 413
Cdd:PRK00047 415 ANNFLMQFQADILGVPVERPVVAETTALGAA 445
|
|
| ASKHA_NBD_MurK-like |
cd24084 |
nucleotide-binding domain (NBD) of Clostridium acetobutylicum N-acetylmuramic acid ... |
4-82 |
8.27e-05 |
|
nucleotide-binding domain (NBD) of Clostridium acetobutylicum N-acetylmuramic acid/N-acetylglucosamine kinase (MurK) and similar proteins; The family includes a group of uncharacterized proteins similar to Clostridium acetobutylicum N-acetylmuramic acid/N-acetylglucosamine kinase (MurK; EC 2.7.1.-/EC 2.7.1.59), also known MurNAc/GlcNAc kinase, or murein sugar kinase. It catalyzes the ATP-dependent phosphorylation of both cell wall (peptidoglycan) amino sugars, N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), at the 6-hydroxyl group. Neither the non-N-acetylated forms of the cell wall sugars, i.e., glucosamine and/or muramic acid, nor epimeric hexoses or 1,6-anhydro-MurNAc are substrates for the enzyme. MurK may have a role in the rescue of the murein sugars GlcNAc and MurNAc released from muropeptides during cell wall turnover in C.acetobutylicum.
Pssm-ID: 466934 [Multi-domain] Cd Length: 302 Bit Score: 44.66 E-value: 8.27e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130683 4 KYIIGIDGGSQSTKVVMYDLEGNVVCEGKGLLQPMHTPDADTAEHPDDDLWASLCfaghdlmSQFAGNKEDIVGIGLGS 82
Cdd:cd24084 1 KYVIGIDGGGTKTHLKITDLNGNVVGEGFGGSSNLESNSLETVRENLKELFQDFY-------EQLGKSLKECGSICLGT 72
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
4-81 |
7.61e-04 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 41.41 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 4 KYIIGIDGGSQSTKVVMYDLEGNVVCEGKGL-LQPMHtpdadtaeHPDDDLWASLcfagHDLMSQF---AGNKEDIVGIG 79
Cdd:COG2971 1 PYILGVDGGGTKTRAVLVDADGEVLGRGRAGgANPQS--------VGLEEALASL----REALEEAlaaAGDPADIEAVG 68
|
..
gi 16130683 80 LG 81
Cdd:COG2971 69 FG 70
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-82 |
1.36e-03 |
|
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: 40.65 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 1 MSKKYIIGIDGGSQSTKVVMYDLEGNVVCEGKgllqpMHTPDADTAEHPDDDLWASLcfagHDLMSQFAGNKEDIVGIGL 80
Cdd:COG1940 2 PDAGYVIGIDIGGTKIKAALVDLDGEVLARER-----IPTPAGAGPEAVLEAIAELI----EELLAEAGISRGRILGIGI 72
|
..
gi 16130683 81 GS 82
Cdd:COG1940 73 GV 74
|
|
| ASKHA_NBD_GspK-like |
cd24082 |
nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar ... |
5-93 |
2.41e-03 |
|
nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar proteins; The family includes a group of uncharacterized proteins similar to Vibrio cholerae glucosamine kinase GspK (EC 2.7.1.8), also called GlcN kinase. It acts as ATP-dependent kinase, which is specific for glucosamine. GspK does not show kinase activity with any other sugar.
Pssm-ID: 466932 [Multi-domain] Cd Length: 279 Bit Score: 39.82 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 5 YIIGIDGGSQSTKVVMYDLEGNVVCEGKGllqpmhTP-----DADTAehpdddlWASLC----FAGHDLMSQFAGNKEDI 75
Cdd:cd24082 1 YFIGIDGGGTKCRARLADADGTVLGEATG------GPanlssDLDQA-------WASILaaikQALAQAGLDAAALSDLH 67
|
90 100
....*....|....*....|.
gi 16130683 76 VGIGL---GSIRCCRALLKAD 93
Cdd:cd24082 68 AGLGLagaNVPEARAAFLAAL 88
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
346-424 |
3.11e-03 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 39.73 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 346 YRSILESVALTLKNNydnmcNEMNHFAKHVIITGGGSNSDLFMQIFADVFNLPARRNAINGCASLGAAIN-----TAVGL 420
Cdd:COG0849 297 VEEIFELVRKELKRS-----GYEEKLPAGVVLTGGGSQLPGLVELAEEILGLPVRIGRPDGIGGLPEAVRdpayaTAVGL 371
|
....
gi 16130683 421 GLYP 424
Cdd:COG0849 372 LLYA 375
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
117-236 |
3.71e-03 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 39.70 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130683 117 PDVAYVTSFSGYLTHRLTGEFKDNIANYFGQWPVDYKSWAWseDAAVMDKFNIPRHMLFDVQMPGTVLGH-ITPQAalat 195
Cdd:PRK10640 134 AQVAHALLIPDYFSYRLTGKMNWEYTNATTTQLVNINSDDW--DESLLAWSGAPKAWFGRPTHPGNVIGHwICPQG---- 207
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 16130683 196 hfpAGLPVVCTTS-DKPVEALGAGLLDDETAVISLGTYiALM 236
Cdd:PRK10640 208 ---NEIPVVAVAShDTASAVIASPLNDSDAAYLSSGTW-SLM 245
|
|
| ASKHA_NBD_eukNAGK-like |
cd24007 |
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ... |
6-33 |
9.59e-03 |
|
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) family; The eukaryotic-type NAGK-like family includes a group of proteins similar to eukaryotic N-acetyl-D-glucosamine kinases, such as Vibrio cholerae glucosamine kinase GspK, Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK), Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase (KdgK) and Clostridium acetobutylicum N-acetylmuramic acid/N-acetylglucosamine kinase (MurK). NAGK (EC 2.7.1.59), also called GlcNAc kinase, converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. It is involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. NAGK also has ManNAc kinase activity. GspK (EC 2.7.1.8), also called GlcN kinase, acts as ATP-dependent kinase, which is specific for glucosamine. StHK is a novel hexokinase that can phosphorylate not only glucose but also GlcNAc, glucosamine, and mannose. KdgK (EC 2.7.1.45), also called 2-keto-3-deoxy-D-gluconate kinase, or KDG kinase, catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). It is specific for KDG. MurK (EC 2.7.1.-/EC 2.7.1.59), also known MurNAc/GlcNAc kinase, or murein sugar kinase, catalyzes the ATP-dependent phosphorylation of both cell wall (peptidoglycan) amino sugars, N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), at the 6-hydroxyl group. The eukaryotic-type N-acetylglucosamine kinase (NAGK) 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: 466857 [Multi-domain] Cd Length: 295 Bit Score: 38.05 E-value: 9.59e-03
10 20
....*....|....*....|....*...
gi 16130683 6 IIGIDGGSQSTKVVMYDLEGNVVCEGKG 33
Cdd:cd24007 1 VLGVDGGGTKTRAVLADEDGKILGRGKG 28
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