|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
7-461 |
0e+00 |
|
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: 599.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 7 RHIAIDLGASGGRVALGAVEGGRLSFDILHRFPNRAVPLGASLYWDMLELWREIRHGLRIASGQG-PVASIGVTTWGVDY 85
Cdd:cd07771 1 NYLAVDLGASSGRVILGSLDGGKLELEEIHRFPNRPVEINGHLYWDIDRLFDEIKEGLKKAAEQGgDIDSIGIDTWGVDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 86 ALFDADALPIGMVHSHRDRRTEGVIDTLDETMPRADLYQATGVQFLPINTLPQLLAAKRASPDLFSRATRFLMLPDLIHY 165
Cdd:cd07771 81 GLLDKNGELLGNPVHYRDPRTEGMMEELFEKISKEELYERTGIQFQPINTLYQLYALKKEGPELLERADKLLMLPDLLNY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 166 WLCGVVACEHTNASTTQLYDPVRRDWSNTVLTAFGIPRAMFPDLVEPGTILGPLLPAIAADTGLVGTIVIAPATHDTASA 245
Cdd:cd07771 161 LLTGEKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPEVAEELGLKGIPVIAVASHDTASA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 246 IAAIPAEaGEDWAYISSGTWCLAGIERPRPLISEAARRANITNEQGIAGTTRLLKNTSGLFILQECLRAWG----DPPIE 321
Cdd:cd07771 241 VAAVPAE-DEDAAFISSGTWSLIGVELDEPVITEEAFEAGFTNEGGADGTIRLLKNITGLWLLQECRREWEeegkDYSYD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 322 PILQDAA-ALCSDVAIDPTEPEFAHPGvTMPDRILRWCAARGIVLDPAPAVITRAVLRGLAASVAASLAEIDQVANHQTR 400
Cdd:cd07771 320 ELVALAEeAPPFGAFIDPDDPRFLNPG-DMPEAIRAYCRETGQPVPESPGEIARCIYESLALKYAKTIEELEELTGKRID 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1232321867 401 RIHIVGGGSRIDLLCQAIADCTNATVIAGPVEATTAGNLLVQAASLGVIE-HNAIRTVMRAT 461
Cdd:cd07771 399 RIHIVGGGSRNALLCQLTADATGLPVIAGPVEATAIGNLLVQLIALGEIKsLEEGRELVRNS 460
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
26-471 |
2.31e-107 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 326.68 E-value: 2.31e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 26 EGGRLSFDILHRFPNRAVPLGASLYWDMLELWREIRHGLRIASGQG-PVASIGVTTWGVDYALFDADALPIGMVHSHRDR 104
Cdd:PRK10640 8 ECRSLTLREIHRFNNGLHSQDGFDTWDVDSLESAIRLGLNKVCEEGiRIDSIGIDTWGVDYVLLDKQGQRVGLPVSYRDS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 105 RTEGVIDTLDETMPRADLYQATGVQFLPINTLPQLLAAKRASPDLFSRATRFLMLPDLIHYWLCGVVACEHTNASTTQLY 184
Cdd:PRK10640 88 RTDGVMAQAQQQLGKRDIYRRSGIQFLPFNTLYQLRALTEQQPELIAQVAHALLIPDYFSYRLTGKMNWEYTNATTTQLV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 185 DPVRRDWSNTVLTAFGIPRAMFPDLVEPGTILG----PLLPAIAadtglvgtiVIAPATHDTASAIAAIPAeAGEDWAYI 260
Cdd:PRK10640 168 NINSDDWDESLLAWSGAPKAWFGRPTHPGNVIGhwicPQGNEIP---------VVAVASHDTASAVIASPL-NDSDAAYL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 261 SSGTWCLAGIERPRPLISEAARRANITNEQGIAGTTRLLKNTSGLFILQECLRAWGDPPIEPILQDAAAL--CSDVaIDP 338
Cdd:PRK10640 238 SSGTWSLMGFESQTPFTNDTALAANITNEGGAEGRYRVLKNIMGLWLLQRVLQERQITDLPALIAATAALpaCRFL-INP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 339 TEPEFAHPgVTMPDRILRWCAARGIVLDPAPAVITRAVLRGLAASVAASLAEIDQVANHQTRRIHIVGGGSRIDLLCQAI 418
Cdd:PRK10640 317 NDDRFINP-PSMCSEIQAACRETAQPVPESDAELARCIFDSLALLYADVLHELAQLRGEPFSQLHIVGGGCQNALLNQLC 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1232321867 419 ADCTNATVIAGPVEATTAGNLLVQAASLGVIEH-NAIRTVMRATADLRCFIPKT 471
Cdd:PRK10640 396 ADACGIRVIAGPVEASTLGNIGIQLMTLDELNNvDDFRQVVSTNFPLTTFTPNP 449
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
9-437 |
3.35e-55 |
|
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: 190.11 E-value: 3.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 9 IAIDLGASGGRVALGAVEGGRLSfdiLHRFPNRAVPLGAS-LYWDMLELWREIRHGLRIASGQ---GPVASIGVTTWGVD 84
Cdd:cd07773 3 LGIDIGTTNVKAVLFDEDGRILA---SASRETPLIHPGPGwAELDPEELWEAVKEAIREAAAQagpDPIAAISVSSQGES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 85 YALFDADALPIGMVHSHRDRRTEGVIDTLDETMPRADLYQATGVQFLPINTLPQLLAAKRASPDLFSRATRFLMLPDLIH 164
Cdd:cd07773 80 GVPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAKWLSVADYIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 165 YWLCGVVACEHTNASTTQLYDPVRRDWSNTVLTAFGIPRAMFPDLVEPGTILGPLLPAIAADTGLVGTIVIAPATHD-TA 243
Cdd:cd07773 160 YRLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEELGLPAGTPVVVGGHDhLC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 244 SAIAAIPAEAGEdwAYISSGTW-CLAGIeRPRPLISEAARRANITNEQGIAGT-TRLLKNTSGLFILQECLRAWGDPPIE 321
Cdd:cd07773 240 AALGAGVIEPGD--VLDSTGTAeALLAV-VDEPPLDEMLAEGGLSYGHHVPGGyYYLAGSLPGGALLEWFRDLFGGDESD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 322 PILQDAAAlcSDVAIDPTE----PEFAHPGVTMPDRILRWcAARGIVLDPAPAVITRAVLRGLAASVAASLAEIDQvANH 397
Cdd:cd07773 317 LAAADELA--EAAPPGPTGllflPHLSGSGTPDFDPDARG-AFLGLTLGTTRADLLRAILEGLAFELRLNLEALEK-AGI 392
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1232321867 398 QTRRIHIVGGGSRIDLLCQAIADCTNATVIAGPV-EATTAG 437
Cdd:cd07773 393 PIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVpEATALG 433
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
9-450 |
2.04e-49 |
|
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: 175.79 E-value: 2.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 9 IAIDLGASGGRVALGAVEG-----GRLSFDILHRFPNRAVplgaslyWDMLELWREIRHGLRIASGQGP-----VASIGV 78
Cdd:COG1070 4 LGIDIGTTSVKAVLFDADGevvasASAEYPLSSPHPGWAE-------QDPEDWWEAVVEAIRELLAKAGvdpeeIAAIGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 79 TTWGVDYALFDADALPIGMVHSHRDRRTEGVIDTLDETMPRADLYQATGVQFLPINTLPQLLAAKRASPDLFSRATRFLM 158
Cdd:COG1070 77 SGQMHGLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAKVLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 159 LPDLIHYWLCGVVACEHTNASTTQLYDPVRRDWSNTVLTAFGIPRAMFPDLVEPGTILGPLLPAIAADTGLVGTIVIAPA 238
Cdd:COG1070 157 PKDYLRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAAETGLPAGTPVVAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 239 THDT-ASAIAAIPAEAGEdwAYISSGTWCLAGIERPRPLISEAARRANIT--------NEQGIAGTTRLLKNTSGLFilq 309
Cdd:COG1070 237 AGDNaAAALGAGAVEPGD--AAVSLGTSGVVFVVSDKPLPDPEGRVHTFChavpgrwlPMGATNNGGSALRWFRDLF--- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 310 eclrAWGDPPIEPILQDAAAlcsDVAIDPTEPEFaHP---GvtmpDRILRWCA-ARGIV--LDPA--PAVITRAVLRGLA 381
Cdd:COG1070 312 ----ADGELDDYEELNALAA---EVPPGADGLLF-LPylsG----ERTPHWDPnARGAFfgLTLShtRAHLARAVLEGVA 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 382 ASVAASLAEIDQvANHQTRRIHIVGGGSRIDLLCQAIADCTNATVIAGPVEATTA-GNLLVQAASLGVIE 450
Cdd:COG1070 380 FALRDGLEALEE-AGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGAlGAALLAAVGLGLYD 448
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
9-245 |
5.15e-39 |
|
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: 141.32 E-value: 5.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 9 IAIDLGASGGRVALGAVEG-----GRLSFDILHRFPNRAVplgaslyWDMLELWREIRHGLRIA------SGQGPVAsIG 77
Cdd:pfam00370 3 LGIDCGTTSTKAILFNEQGkiiavAQLENPQITPHPGWAE-------QDPDEIWQAVAQCIAKTlsqlgiSLKQIKG-IG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 78 VTTWGVDYALFDADALPIGMVHSHRDRRTEGVIDTLDETMPRADLYQATGVQFLPINTLPQLLAAKRASPDLFSRATRFL 157
Cdd:pfam00370 75 ISNQGHGTVLLDKNDKPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 158 MLPDLIHYWLCGVVACEHTNASTTQLYDPVRRDWSNTVLTAFGIPRAMFPDLVEPGTILGPLLPAIAADTGLVGTIVIAP 237
Cdd:pfam00370 155 TIHDYLRWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMWGLDEGVPVVG 234
|
....*...
gi 1232321867 238 ATHDTASA 245
Cdd:pfam00370 235 GGGDQQAA 242
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
9-447 |
2.33e-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: 139.28 E-value: 2.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 9 IAIDLGASGGRVALGAVEGGRLSFDilhRFPNRAVPLGA---SLYWDMLELWREIRHGLRIA---SGQGPVASIGVTTWG 82
Cdd:cd07798 3 LVIDIGTGGGRCALVDSEGKIVAIA---YREWEYYTDDDypdAKEFDPEELWEKICEAIREAlkkAGISPEDISAVSSTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 83 VDYA--LFDAD-----ALPigmvhsHRDRRTEGVIDTLDETMpRADLYQATGVQFLPINTLPQLLAAKRASPDLFSRATR 155
Cdd:cd07798 80 QREGivFLDKDgrelyAGP------NIDARGVEEAAEIDDEF-GEEIYTTTGHWPTELFPAARLLWFKENRPEIFERIAT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 156 FLMLPDLIHYWLCGVVACEHTNASTTQLYDPVRRDWSNTVLTAFGIPRAMFPDLVEPGTILGPLLPAIAADTGL-VGTIV 234
Cdd:cd07798 153 VLSISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAARELGLpEGTPV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 235 IAPAThDTASAIAAIPAEAGEDwAYISSGTWCLAGIERPRPLISEAAR---RANITNEQGI----AGTT----RLLKNts 303
Cdd:cd07798 233 VVGGA-DTQCALLGSGAIEPGD-IGIVAGTTTPVQMVTDEPIIDPERRlwtGCHLVPGKWVlesnAGVTglnyQWLKE-- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 304 glfILQEClrawGDPPIEPILQDAAalcsdvAIDPTEPE---------------------FAHPGVTMPDRILRWCAARG 362
Cdd:cd07798 309 ---LLYGD----PEDSYEVLEEEAS------EIPPGANGvlaflgpqifdarlsglknggFLFPTPLSASELTRGDFARA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 363 IVLDPAPAVitRAVLRglaasvaaslaEIDQVANHQTRRIHIVGGGSRIDLLCQAIADCTNATVI-AGPVEATTAGNLLV 441
Cdd:cd07798 376 ILENIAFAI--RANLE-----------QLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLvPEGREASALGAAIC 442
|
....*.
gi 1232321867 442 QAASLG 447
Cdd:cd07798 443 AAVGAG 448
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
51-437 |
7.47e-36 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 138.24 E-value: 7.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 51 WDMLELW-------REIRHGLRiasgQGPVASIGVTTWGVDYALFDADALPIGMVHSHRDRRTEGVIDTLDETMPRADLY 123
Cdd:PRK10331 47 WSLDAILqrfadccRQINSELT----ECHIRGITVTTFGVDGALVDKQGNLLYPIISWKCPRTAAVMENIERYISAQQLQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 124 QATGVQFLPINTLPQLLAAKRASPDLFSRATRFLMLPDLIHYWLCGVVACEHTNASTTQLYDPVRRDWSNTVLTAFGIPR 203
Cdd:PRK10331 123 QISGVGAFSFNTLYKLVWLKENHPQLLEQAHAWLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 204 AMFPDLVEPGTILGPLLPAIAADTGL-VGTIVIApATHDTASAIAAipAEAGEDWAYISSGTWCLAGIERPRPLISEAAR 282
Cdd:PRK10331 203 RLFPRLVEAGEQIGTLQPSAAALLGLpVGIPVIS-AGHDTQFALFG--SGAGQNQPVLSSGTWEILMVRSAQVDTSLLSQ 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 283 RANITNEqgiagttrlLKNTSGLF--ILQ-------ECLRA--WGDPPIEPILQDAAAlcsdvAIDPtepefAHPGVTMP 351
Cdd:PRK10331 280 YAGSTCE---------LDSQSGLYnpGMQwlasgvlEWVRKlfWTAETPYQTMIEEAR-----AIPP-----GADGVKMQ 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 352 DRILR-----WCaarGIVLDPAPAVITRAVLRGLAASVAASLAEIDQVANHQTRRIHIVGGGSRIDLLCQAIADCTNATV 426
Cdd:PRK10331 341 CDLLAcqnagWQ---GVTLNTTRGHFYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPI 417
|
410
....*....|..
gi 1232321867 427 -IAGPVEATTAG 437
Cdd:PRK10331 418 kVLDDAETTVAG 429
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
9-436 |
5.78e-34 |
|
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: 131.53 E-value: 5.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 9 IAIDLGASGGRVALGAVEG-----GRLSFDILHRFPNRAvplgaslYWDMLELWREIRHGLRIASGQGP-----VASIGV 78
Cdd:cd00366 3 LGIDIGTTSVKAALFDEDGnlvasASREYPLIYPQPGWA-------EQDPEDWWQAVVEAIREVLAKAGidpsdIAAIGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 79 TTWGVDYALFDADALPIGMVHSHRDRRTegvidtldetmpradlyqatgvqflpintlpqllaakraspdlfsratRFLM 158
Cdd:cd00366 76 SGQMPGVVLVDADGNPLRPAIIWLDRRA------------------------------------------------KFLQ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 159 LPDLIHYWLCGVVACEHTNASTTQLYDPVRRDWSNTVLTAFGIPRAMFPDLVEPGTILGPLLPAIAADTGL-VGTIVIAp 237
Cdd:cd00366 108 PNDYIVFRLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAAEETGLpAGTPVVA- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 238 ATHDTASAIAAIPA-EAGEdwAYISSGTWCLAGIERPRPLISEaarrANITNEQ-GIAGTTRLLKNTS-GLFILQECLRA 314
Cdd:cd00366 187 GGGDTAAAALGAGVvEPGD--AVDSTGTSSVLSVCTDEPVPPD----PRLLNRChVVPGLWLLEGAINtGGASLRWFRDE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 315 WGDPPIEPILQ---DAAALCSDVAIDptepefahpGVT-----MPDRILRW-CAAR----GIVLDPAPAVITRAVLRGLA 381
Cdd:cd00366 261 FGEEEDSDAEYeglDELAAEVPPGSD---------GLIflpylSGERSPIWdPAARgvffGLTLSHTRAHLIRAVLEGVA 331
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1232321867 382 ASVAASLAEIDQvANHQTRRIHIVGGGSRIDLLCQAIADCTNATVIAGPVEATTA 436
Cdd:cd00366 332 YALRDNLEILEE-LGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAA 385
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
9-437 |
9.97e-33 |
|
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: 128.88 E-value: 9.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 9 IAIDLGASGGRVALGAVEGGRLSFDiLHRFPNRAVPLG-----ASLYWDML-ELWREIRHGLRIAsgqgPVASIGVT-TW 81
Cdd:cd07783 3 LGIDLGTSGVRAVVVDEDGTVLASA-SEPYPTSRPGPGwveqdPEDWWEALrSLLRELPAELRPR----RVVAIAVDgTS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 82 GVdYALFDADALPIGMVHSHRDRRTEGVIDTLDETMPRAdlYQATGVQFLPINTLPQLLAAKRASPDLFSRATRFLMLPD 161
Cdd:cd07783 78 GT-LVLVDREGEPLRPAIMYNDARAVAEAEELAEAAGAV--APRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFLHQAD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 162 LIHYWLCGVVAC-EHTNASTTqLYDPVRRDWSNTVLTAFGIPRAMFPDLVEPGTILGPLLPAIAADTGL-VGTIVIAPAT 239
Cdd:cd07783 155 WLAGRLTGDRGVtDYNNALKL-GYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLpAGTPVVAGTT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 240 HDTASAIAAIPAEAGEdwAYISSGT-WCLAGIeRPRPLISEAARRANITNEQGI---AGTTrllkNTSGlfilqECLRAW 315
Cdd:cd07783 234 DSIAAFLASGAVRPGD--AVTSLGTtLVLKLL-SDKRVPDPGGGVYSHRHGDGYwlvGGAS----NTGG-----AVLRWF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 316 GDppiepiLQDAAALCSDVAIDPTEPEFAHPGVTMPDRILRWCAARGIVLDPAP---AVITRAVLRGLAASVAASLAEID 392
Cdd:cd07783 302 FS------DDELAELSAQADPPGPSGLIYYPLPLRGERFPFWDPDARGFLLPRPhdrAEFLRALLEGIAFIERLGYERLE 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1232321867 393 QVANHQTRRIHIVGGGSRIDLLCQAIADCTNATVIAGPVEATTAG 437
Cdd:cd07783 376 ELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEAALG 420
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
9-264 |
2.64e-32 |
|
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: 128.43 E-value: 2.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 9 IAIDLGASGGRVALGAVEGGRL-----SFDILHRFPNRAV--PlgaSLYWD-MLELWREIRHGLRIASGQgpVASIGVT- 79
Cdd:cd07808 3 LGIDLGTSSVKAVLVDEDGRVLasasaEYPTSSPKPGWAEqdP---EDWWQaTKEALRELLAKAGISPSD--IAAIGLTg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 80 -TWGVdyALFDADALPIGMVHSHRDRRTEGVIDTLDETMPrADLYQATGVQFLPINTLPQLLAAKRASPDLFSRATRFLM 158
Cdd:cd07808 78 qMHGL--VLLDKNGRPLRPAILWNDQRSAAECEELEARLG-DEILIITGNPPLPGFTLPKLLWLKENEPEIFARIRKILL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 159 LPDLIHYWLCGVVACEHTNASTTQLYDPVRRDWSNTVLTAFGIPRAMFPDLVEPGTILGPLLPAIAADTGL-VGTIVIAP 237
Cdd:cd07808 155 PKDYLRYRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAAEELGLpEGTPVVAG 234
|
250 260
....*....|....*....|....*..
gi 1232321867 238 ATHDTASAIAAIPAEAGEdwAYISSGT 264
Cdd:cd07808 235 AGDNAAAALGAGVVEPGD--ALISLGT 259
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
152-436 |
1.48e-31 |
|
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: 125.71 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 152 RATRFLMLPDLIHYWLCGVVACEHTNASTTQLYDPVRRDWSNTVLTAFGIPRAMFPDLVEPGTILGPLLPAIAADTGL-V 230
Cdd:cd07779 102 RTAKFLTVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAAEETGLpE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 231 GTIVIApATHDTA-SAIAAIPAEAGEdwAYISSGTWCLAGIERPRPLisEAARRANITN----------EQGIAGTTRLL 299
Cdd:cd07779 182 GTPVVA-GGGDQQcAALGAGVLEPGT--ASLSLGTAAVVIAVSDKPV--EDPERRIPCNpsavpgkwvlEGSINTGGSAV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 300 KNTSGLFILQECLRAWGDPPIEPILQDAAAlcsdvAIDP------TEPEFAHPGVTMPDrilrwCAARGIV--LDPA--P 369
Cdd:cd07779 257 RWFRDEFGQDEVAEKELGVSPYELLNEEAA-----KSPPgsdgllFLPYLAGAGTPYWN-----PEARGAFigLTLShtR 326
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1232321867 370 AVITRAVLRGLAASVAASLAEIDQvANHQTRRIHIVGGGSRIDLLCQAIADCTNATVIAGPVEATTA 436
Cdd:cd07779 327 AHLARAILEGIAFELRDNLEAMEK-AGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATA 392
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
9-450 |
3.22e-30 |
|
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: 122.63 E-value: 3.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 9 IAIDLGASGGRVALGAVEGGRL-----SFDILHRFPNRAV--PlgaSLYWD-MLELWREIRHGLRIASGQgpVASIGVTT 80
Cdd:cd07805 3 LAIDLGTSGVKAALVDLDGELVasafaPYPTYYPKPGWAEqdP---EDWWDaVCRATRALLEKSGIDPSD--IAAIAFSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 81 WGVDYALFDADALPIGMVHSHRDRRTEGVIDTLDETMPRADLYQATGVQFL-PINTLPQLLAAKRASPDLFSRATRFLML 159
Cdd:cd07805 78 QMQGVVPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLGGGNPPsGKDPLAKILWLKENEPEIYAKTHKFLDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 160 PDLIHYWLCGVVACEHTNASTTQLYDPVRRDWSNTVLTAFGIPRAMFPDLVEPGTILGPLLPAIAADTGLV-GTIVIAPA 238
Cdd:cd07805 158 KDYLNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAAAELGLPaGTPVVGGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 239 THDTASAIAAIPAEAGEDWAYISSGTWcLAGIeRPRPLISEAARRANI----------TNEQGIAGTTrllkntsglfiL 308
Cdd:cd07805 238 GDAAAAALGAGAVEEGDAHIYLGTSGW-VAAH-VPKPKTDPDHGIFTLasadpgryllAAEQETAGGA-----------L 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 309 QECLRAWGDPPIEPIlqDAAALCSDVAidPTEPEFAHpGVT-----MPDRILRW-CAARG----IVLDPAPAVITRAVLR 378
Cdd:cd07805 305 EWARDNLGGDEDLGA--DDYELLDELA--AEAPPGSN-GLLflpwlNGERSPVEdPNARGafigLSLEHTRADLARAVLE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 379 GlaasvaaslaeidqVA-------------NHQTRRIHIVGGGSRIDLLCQAIADCTNATVI--AGPVEATTAGNLLVQA 443
Cdd:cd07805 380 G--------------VAfnlrwllealeklTRKIDELRLVGGGARSDLWCQILADVLGRPVEvpENPQEAGALGAALLAA 445
|
....*..
gi 1232321867 444 ASLGVIE 450
Cdd:cd07805 446 VGLGLLK 452
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
52-436 |
4.21e-28 |
|
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: 116.11 E-value: 4.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 52 DMLELW-------REIRHGLRIASGQgpVASIGVTTWGVDYALFDADALPIGMVHSHRDRRTEGVIDTLDETMPRADLYQ 124
Cdd:cd07802 44 DMDELWqataeaiRELLEKSGVDPSD--IAGVGVTGHGNGLYLVDKDGKPVRNAILSNDSRAADIVDRWEEDGTLEKVYP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 125 ATGVQFLPINTLPQLLAAKRASPDLFSRATRFLMLPDLIHYWLCGVVACEHTNASTTqLYDPVRRDWSNTVLTAFGIP-- 202
Cdd:cd07802 122 LTGQPLWPGQPVALLRWLKENEPERYDRIRTVLFCKDWIRYRLTGEISTDYTDAGSS-LLDLDTGEYDDELLDLLGIEel 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 203 RAMFPDLVEPGTILGPLLPAIAADTGL-VGTIVIAPAtHD-TASAIAAIPAEAGEdwAYISSGTWCLAGIERPRPLISEA 280
Cdd:cd07802 201 KDKLPPLVPSTEIAGRVTAEAAALTGLpEGTPVAAGA-FDvVASALGAGAVDEGQ--LCVILGTWSINEVVTDEPVVPDS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 281 ARRanitNEQGIAGTTRLLKNTSGL------FILQECLRAWGDPPiEPILQDAAALCSDVAIDPTEPEF--------AHP 346
Cdd:cd07802 278 VGS----NSLHADPGLYLIVEASPTsasnldWFLDTLLGEEKEAG-GSDYDELDELIAAVPPGSSGVIFlpylygsgANP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 347 GvtmpdrilrwcaAR----GIVLDPAPAVITRAVLRGLAASVAASLAEIDQvaNHQTRRIHIVGGGSRIDLLCQAIADCT 422
Cdd:cd07802 353 N------------ARggffGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLV--ARKPETIRLTGGGARSPVWAQIFADVL 418
|
410
....*....|....
gi 1232321867 423 NATVIAGPVEATTA 436
Cdd:cd07802 419 GLPVEVPDGEELGA 432
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
10-237 |
1.92e-24 |
|
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: 105.88 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 10 AIDLGASGGR----------VALGAVEGGRLSFdilHRFPnravplgASLYWDMLELW----REIRHGLRIASGQGP-VA 74
Cdd:cd07775 4 ALDAGTGSGRavifdlegnqIAVAQREWRHKEV---PDVP-------GSMDFDTEKNWklicECIREALKKAGIAPKsIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 75 SIGVTTWGVDYALFDADALPIGMVHSHRDRRTEGVIDtLDETMP--RADLYQATGvQFLPINTLPQLLAAKRASPDLFSR 152
Cdd:cd07775 74 AISTTSMREGIVLYDNEGEEIWACANVDARAAEEVSE-LKELYNtlEEEVYRISG-QTFALGAIPRLLWLKNNRPEIYRK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 153 ATRFLMLPDLIHYWLCGVVACEHTNASTTQLYDPVRRDWSNTVLTAFGIPRAMFPDLVEPGTILGPLLPAIAADTGL-VG 231
Cdd:cd07775 152 AAKITMLSDWIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEAAEETGLkEG 231
|
....*.
gi 1232321867 232 TIVIAP 237
Cdd:cd07775 232 TPVVVG 237
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
57-433 |
4.18e-24 |
|
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: 104.53 E-value: 4.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 57 WREIRHGLRIASGQGPV-----ASIGVTTWGVDYALFDADALPIGMVHSHRDRRTEGVIDTLDETMPRADLYQATGVQFL 131
Cdd:cd07804 49 WGAVCEIIRELLAKAGIspkeiAAIGVSGLVPALVPVDENGKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLD 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 132 PINTLPQLLAAKRASPDLFSRATRFLMLPDLIHYWLCGVVACEHTNAS-TTQLYDPVRRDWSNTVLTAFGIPRAMFPDLV 210
Cdd:cd07804 129 SQSVGPKLLWIKRNEPEVFKKTRKFLGAYDYIVYKLTGEYVIDYSSAGnEGGLFDIRKRTWDEELLEALGIDPDLLPELV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 211 EPGTILGPLLPAIAADTGLV-GTIVIAPATHDTASAIAAIPAEAGEDWAYI-SSGTWcLAGIERPRPLISEAARRANITN 288
Cdd:cd07804 209 PSTEIVGEVTKEAAEETGLAeGTPVVAGTVDAAASALSAGVVEPGDLLLMLgTAGDI-GVVTDKLPTDPRLWLDYHDIPG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 289 EQGIAGTTrllkNTSG----------LFILQECLRAWGDPPIEPILQDAAALCsdvaidptepefahPG----VTMP--- 351
Cdd:cd07804 288 TYVLNGGM----ATSGsllrwfrdefAGEEVEAEKSGGDSAYDLLDEEAEKIP--------------PGsdglIVLPyfm 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 352 -------DRIlrwcaARGIV----LDPAPAVITRAVLRGLAASVAASLAEIDQvANHQTRRIHIVGGGSRIDLLCQAIAD 420
Cdd:cd07804 350 gertpiwDPD-----ARGVIfgltLSHTRAHLYRALLEGVAYGLRHHLEVIRE-AGLPIKRLVAVGGGAKSPLWRQIVAD 423
|
410
....*....|....*
gi 1232321867 421 CTNATV--IAGPVEA 433
Cdd:cd07804 424 VTGVPQeyVKDTVGA 438
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
52-268 |
4.66e-23 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466792 [Multi-domain] Cd Length: 424 Bit Score: 101.18 E-value: 4.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 52 DMLELWREIRHGLRIASGQGPVASIGVTTWGVDYALFDAD---ALPigmvhshrdrrtegVIDTLDETMP--RADLYQAT 126
Cdd:cd07772 43 DVEAIWEWLLDSLAELAKRHRIDAINFTTHGATFALLDENgelALP--------------VYDYEKPIPDeiNEAYYAER 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 127 GvQFLPINTLP---------QLLAAKRASPDLFSRATRFLMLPDLIHYWLCGVVACEHTNAST-TQLYDPVRRDWSnTVL 196
Cdd:cd07772 109 G-PFEETGSPPlpgglnlgkQLYWLKREKPELFARAKTILPLPQYWAWRLTGKAASEITSLGChTDLWDFEKNEYS-SLV 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1232321867 197 TAFGIpRAMFPDLVEPGTILGPLLPAIAADTGLVGTIVIAPATHDTASAIAAIPAEAGEDWAYISSGTWCLA 268
Cdd:cd07772 187 KKEGW-DKLFPPLRKAWEVLGPLRPDLARRTGLPKDIPVGCGIHDSNAALLPYLAAGKEPFTLLSTGTWCIA 257
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
9-449 |
6.64e-23 |
|
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: 101.09 E-value: 6.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 9 IAIDLGASGGRVALGAVEGgrlsfDILHRFPNR---AVPLGASLYWDMLELWREIRHGLRIA---SGQGPVASIGVTTwg 82
Cdd:cd07770 3 LGIDIGTTSTKAVLFDEDG-----RVVASSSAEyplIRPEPGWAEQDPEEILEAVLEALKEVlakLGGGEVDAIGFSS-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 83 vdyALF-----DADALPIGMVHSHRDRRTEGVIDTLDETMPRADLYQATGVQFLPINTLPQLLAAKRASPDLFSRATRFL 157
Cdd:cd07770 76 ---AMHsllgvDEDGEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAAKFV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 158 MLPDLIHYWLCGVVACEHTNASTTQLYDPVRRDWSNTVLTAFGIPRAMFPDLVEPGTILGPLLPAIAADTGL-VGTIVIA 236
Cdd:cd07770 153 SIKEYLLYRLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAERLGLlAGTPVVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 237 PAThD---------------------TASAIAAIPAEAGEDwayISSGTWCLAGIERpRPLISEAarraniTNEQGIAgt 295
Cdd:cd07770 233 GAS-DgalanlgsgaldpgraaltvgTSGAIRVVSDRPVLD---PPGRLWCYRLDEN-RWLVGGA------INNGGNV-- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 296 TRLLKNTSGLFilqeclrawgdppiEPILQDAAALCSDVAIDPTEPEFaHPGVTmPDRILRWCA-ARGIV--LDPA--PA 370
Cdd:cd07770 300 LDWLRDTLLLS--------------GDDYEELDKLAEAVPPGSHGLIF-LPYLA-GERAPGWNPdARGAFfgLTLNhtRA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 371 VITRAVLRGLAASVAASLAEIDQVAnHQTRRIHIVGGGSRIDLLCQAIADCTNATVIAGPV-EATTAGNLLVQAASLGVI 449
Cdd:cd07770 364 DILRAVLEGVAFNLKSIYEALEELA-GPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEeEASALGAALLALEALGLI 442
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
258-446 |
6.02e-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: 93.16 E-value: 6.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 258 AYISSGTWCLAGIERPRPLISEAARRANITNEQ-----GIAGTTRLLKNTSGLFILQ-ECLRAWGDPPIEPILQ-----D 326
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSVHGVWGPYTNEMlpgywGLEGGQSAAGSLLAWLLQFhGLREELRDAGNVESLAelaalA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 327 AAALCSDVAIDPTEPEFAHPGVtMPDRIlrwCAARGIVLDPAPAVITRAVLRGLAASVAASLAEIDQVANHQTRRIHIVG 406
Cdd:pfam02782 81 AVAPAGGLLFYPDFSGNRAPGA-DPGAR---GSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1232321867 407 GGSRIDLLCQAIADCTNATV-IAGPVEATTAGNLLVQAASL 446
Cdd:pfam02782 157 GGSRNPLLLQLLADALGLPVvVPGPDEATALGAALLAAVAA 197
|
|
| XylB |
TIGR01312 |
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ... |
103-264 |
1.76e-21 |
|
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of carbohydrate kinases. The member from Klebsiella pneumoniae, designated DalK (see , was annotated erroneously in GenBank as D-arabinitol kinase but is authentic D-xylulose kinase. D-xylulose kinase (XylB) generally is found with xylose isomerase (XylA) and acts in xylose utilization. [Energy metabolism, Sugars]
Pssm-ID: 273550 [Multi-domain] Cd Length: 481 Bit Score: 97.00 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 103 DRRTEGVIDTLDETMPRADLYQATGVQFLPINTLPQLLAAKRASPDLFSRaTRFLMLP-DLIHYWLCGVVACEHTNASTT 181
Cdd:TIGR01312 98 DTRTAQECEELEAELGDERVLEITGNLALPGFTAPKLLWVRKHEPEVFAR-IAKVMLPkDYLRYRLTGEYVTEYSDASGT 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 182 QLYDPVRRDWSNTVLTAFGIPRAMFPDLVEPGTILGPLLPAIAADTGL-VGTIVIAPATHDTASAIAAIPAEAGEdwAYI 260
Cdd:TIGR01312 177 GWFDVAKRAWSKELLDALDLPESQLPELIESSEKAGTVRPEVAARLGLsAGVPVAAGGGDNAAGAIGTGTVDPGD--AMM 254
|
....
gi 1232321867 261 SSGT 264
Cdd:TIGR01312 255 SLGT 258
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
87-236 |
2.07e-21 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 97.00 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 87 LFDADALPIGMVHSHRDRRTEGVIDtLDETMP--RADLYQATGvQFLPINTLPQLLAAKRASPDLFSRATRFLMLPDLIH 164
Cdd:PRK10939 89 LYDRNGTEIWACANVDARASREVSE-LKELHNnfEEEVYRCSG-QTLALGALPRLLWLAHHRPDIYRQAHTITMISDWIA 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1232321867 165 YWLCGVVACEHTNASTTQLYDPVRRDWSNTVLTAFGIPRAMFPDLVEPGTILGPLLPAIAADTGL-VGTIVIA 236
Cdd:PRK10939 167 YMLSGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAKAAAETGLrAGTPVVM 239
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
9-447 |
1.89e-16 |
|
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: 81.52 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 9 IAIDLGASGGRVALGAVEGGRLSFdilHRFPNRAVPLGASLY-WDMLELWREIRHGLR-----IASGQGPVASIGVT--- 79
Cdd:cd24121 3 IGIDAGTSVVKAVAFDLDGRELAV---AARRNAVLYPQPGWAeQDMNETWQAVVATIRevvakLDVLPDRVAAIGVTgqg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 80 --TWgvdyaLFDADALPIGMVHSHRDRRTEGVIDTLDETmPRAD-LYQATGVQFLPINTLPQLLAAKRASPDLFSRATRF 156
Cdd:cd24121 80 dgTW-----LVDEDGRPVRDAILWLDGRAADIVERWQAD-GIAEaVFEITGTGLFPGSQAAQLAWLKENEPERLERARTA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 157 LMLPDLIHYWLCGVVACEHTNASTTqLYDPVRRDWSNTVLTAFGIP--RAMFPDLVEPGTILGPLLPAIAADTGL-VGTI 233
Cdd:cd24121 154 LHCKDWLFYKLTGEIATDPSDASLT-FLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAAAATGLpAGTP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 234 VIAPATHDTASAIAAIPAEAGEDWAYIssGTWCLAGIERPRPLISeaARRANITNEQGIAGT-TRLLKNTSG-------L 305
Cdd:cd24121 233 VVLGPFDVVATALGSGAIEPGDACSIL--GTTGVHEVVVDEPDLE--PEGVGYTICLGVPGRwLRAMANMAGtpnldwfL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 306 FILQECLRAWGDPPIEPILQDAAALCSDVAIDpTEPEFAHP-----G----VTMPDrilrwcaAR----GIVLDPAPAVI 372
Cdd:cd24121 309 RELGEVLKEGAEPAGSDLFQDLEELAASSPPG-AEGVLYHPylspaGerapFVNPN-------ARaqftGLSLEHTRADL 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1232321867 373 TRAVLRGLAASVAASLAEIDQVANhqtrRIHIVGGGSRIDLLCQAIADCTNATV--IAGPvEATTAGNLLVQAASLG 447
Cdd:cd24121 381 LRAVYEGVALAMRDCYEHMGEDPG----ELRLSGGGARSDTWCQILADALGVPVrvPAGE-EFGARGAAMNAAVALG 452
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
8-264 |
1.24e-15 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 78.86 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 8 HIAIDLGASGGRVALGAVEGGRLSFDILHRFPNRAVPLgaslywdmlelWREirhglriasgQGP-----VASIGVTTWG 82
Cdd:PRK15027 2 YIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPL-----------WSE----------QDPeqwwqATDRAMKALG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 83 VDYALFDADALPI-GMVH-------SHR---------DRRTEGVIDTLDETMPRADlyQATGVQFLPINTLPQLLAAKRA 145
Cdd:PRK15027 61 DQHSLQDVKALGIaGQMHgatlldaQQRvlrpailwnDGRCAQECALLEARVPQSR--VITGNLMMPGFTAPKLLWVQRH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 146 SPDLFSRATRFLMLPDLIHYWLCGVVACEHTNASTTQLYDPVRRDWSNTVLTAFGIPRAMFPDLVEPGTILGPLLPAIAA 225
Cdd:PRK15027 139 EPEIFRQIDKVLLPKDYLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAK 218
|
250 260 270
....*....|....*....|....*....|....*....
gi 1232321867 226 DTGLVGTIVIAPATHDTASAIAAIPAEAGEdwAYISSGT 264
Cdd:PRK15027 219 AWGMATVPVVAGGGDNAAGAVGVGMVDANQ--AMLSLGT 255
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
7-264 |
1.78e-14 |
|
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: 75.34 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 7 RHIAIDLGASggRVALGAVEGGrlSFDILH--RFPNRAVPLGASLY---WDMLELWREIRHGLR--IASGQGPVASIGVT 79
Cdd:cd07777 1 NVLGIDIGTT--SIKAALLDLE--SGRILEsvSRPTPAPISSDDPGrseQDPEKILEAVRNLIDelPREYLSDVTGIGIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 80 TW--GVdyALFDADALPIGMVHSHRDRRT-----EGVIDTLDETMPRADLYQATGvqfLPINTLPQLLAAKraspDLFSR 152
Cdd:cd07777 77 GQmhGI--VLWDEDGNPVSPLITWQDQRCseeflGGLSTYGEELLPKSGMRLKPG---YGLATLFWLLRNG----PLPSK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 153 ATRFLMLPDLIHYWLCG--VVACEHTNASTTQLYDPVRRDWSNTVLTAFGIPRAMFPDLVEPGTILGPLLPAIAADtglv 230
Cdd:cd07777 148 ADRAGTIGDYIVARLTGlpKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLSSALPKG---- 223
|
250 260 270
....*....|....*....|....*....|....*
gi 1232321867 231 gtIVIAPATHDT-ASAIAAIPAEAGEdwAYISSGT 264
Cdd:cd07777 224 --IPVYVALGDNqASVLGSGLNEEND--AVLNIGT 254
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
135-426 |
2.00e-11 |
|
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: 65.65 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 135 TLPQLLAAKRASPDLFSRaTRFLMLP-DLIHYWLCGVVACEHTNASTTQLYDPVRRDWSNTVLTAF---GIPRAMFPDLV 210
Cdd:cd07809 132 TASKLLWLKENEPEHYAR-IAKILLPhDYLNWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAIdpsRDLRDLLPEVL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 211 EPGTILGPLLPAIAADTGLVGTIVIAPATHDTA-SAIAAIPAEAGEdwAYISSGT-WCLAGIeRPRPLISEAARRA---- 284
Cdd:cd07809 211 PAGEVAGRLTPEGAEELGLPAGIPVAPGEGDNMtGALGTGVVNPGT--VAVSLGTsGTAYGV-SDKPVSDPHGRVAtfcd 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 285 ---------NITNEQgiagtTRLLKNTSGLFilqeclrAWGDPPIEPILQDAAALCSdvaidptepefahpGVTM-P--- 351
Cdd:cd07809 288 stggmlpliNTTNCL-----TAWTELFRELL-------GVSYEELDELAAQAPPGAG--------------GLLLlPfln 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 352 -DRILRWCAARGIV--LDPA---PAVITRAVLRGlAASVAASLAEIDQVANHQTRRIHIVGGGSRIDLLCQAIADCTNAT 425
Cdd:cd07809 342 gERTPNLPHGRASLvgLTLSnftRANLARAALEG-ATFGLRYGLDILRELGVEIDEIRLIGGGSKSPVWRQILADVFGVP 420
|
.
gi 1232321867 426 V 426
Cdd:cd07809 421 V 421
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
9-248 |
5.53e-08 |
|
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: 54.85 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 9 IAIDLGASGGRVALGAVEGGR-LSFDIlHRFPNRAVPLGASL-------YWDMLElwREIRHGLRIASGQGP-VASIGVT 79
Cdd:cd07781 3 IGIDFGTQSVRAGLVDLADGEeLASAV-VPYPTGYIPPRPGWaeqnpadYWEALE--EAVRGALAEAGVDPEdVVGIGVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 80 TWGVDYALFDADALPIGMV---HSHRDRRTEGVIDTLDETMPRADLYQATGvqflPINT---LPQLLAAKRASPDLFSRA 153
Cdd:cd07781 80 TTSSTVVPVDEDGNPLAPAilwMDHRAQEEAAEINETAHPALEYYLAYYGG----VYSSewmWPKALWLKRNAPEVYDAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 154 TRFLMLPDLIHYWLCGVVACEHTNASTTQLYDPVRRDWSNTVLTAFG-----IPRAMFPDLVEPGTILGPLLPAIAADTG 228
Cdd:cd07781 156 YTIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGGPPREFLAALDpgllkLREKLPGEVVPVGEPAGTLTAEAAERLG 235
|
250 260
....*....|....*....|.
gi 1232321867 229 LVGTIVIAPATHDT-ASAIAA 248
Cdd:cd07781 236 LPAGIPVAQGGIDAhMGAIGA 256
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
172-228 |
2.45e-07 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 53.14 E-value: 2.45e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1232321867 172 ACEHTNASTTQLYDPVRRDWSNTVLTAFGIPRAMFPDlVEP-----GTILGPLLPA---IAADTG 228
Cdd:COG0554 179 VTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPE-VRPssevfGETDPDLFGAeipIAGIAG 242
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
166-210 |
1.84e-06 |
|
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: 50.16 E-value: 1.84e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1232321867 166 WLC------GVVACEHTNASTTQLYDPVRRDWSNTVLTAFGIPRAMFPDLV 210
Cdd:cd07769 164 WLIwkltggKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVR 214
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| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
9-249 |
3.59e-06 |
|
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: 49.16 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 9 IAIDLGASGGRVALGAVEGGRLSFDilHRFPNRA-VPLGASLYWDM-LELWREIRHGLRIASGQGPVASIGVTTWGVDY- 85
Cdd:cd07768 3 IGVDVGTSSARAGVYDLYAGLEMAQ--EPVPYYQdSSKKSWKFWQKsTEIIKALQKCVQKLNIREGVDAYEVKGCGVDAt 80
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 86 ---ALFDADALPIGMVHSHR---------DRRTEGVIDTLDETMPRAdLYQATGVQFLPINTLPQLLAAKRASPDLFSRA 153
Cdd:cd07768 81 cslAIFDREGTPLMALIPYPnednvifwmDHSAVNEAQWINMQCPQQ-LLDYLGGKISPEMGVPKLKYFLDEYSHLRDKH 159
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 154 TRFLMLPDLIHYWLCGVVACEHTNASTTQLYDPVRRDWSNTVLTAFGI------PRAMFPDLVEPGTILGPLLPAIAADT 227
Cdd:cd07768 160 FHIFDLHDYIAYELTRLYEWNICGLLGKENLDGEESGWSSSFFKNIDPrlehltTTKNLPSNVPIGTTSGVALPEMAEKM 239
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250 260
....*....|....*....|..
gi 1232321867 228 GLVGTIVIAPATHDTASAIAAI 249
Cdd:cd07768 240 GLHPGTAVVVSCIDAHASWFAV 261
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| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
172-223 |
7.73e-06 |
|
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: 48.33 E-value: 7.73e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1232321867 172 ACEHTNASTTQLYDPVRRDWSNTVLTAFGIPRAMFPDLVEPGTILGPLLPAI 223
Cdd:cd07793 192 ATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFGSTDPSI 243
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| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
172-231 |
1.33e-04 |
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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: 44.40 E-value: 1.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1232321867 172 ACEHTNASTTQLYDPVRRDWSNTVLTAFGIPRAMFPDLVEP----GTILGPLLPAIAADTGLVG 231
Cdd:cd07786 176 ATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSsevfGYTDPDLLGAEIPIAGIAG 239
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| glpK |
PRK00047 |
glycerol kinase GlpK; |
176-208 |
7.80e-04 |
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glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 41.73 E-value: 7.80e-04
10 20 30
....*....|....*....|....*....|...
gi 1232321867 176 TNASTTQLYDPVRRDWSNTVLTAFGIPRAMFPD 208
Cdd:PRK00047 185 TNASRTMLFNIHTLDWDDELLELLDIPRSMLPE 217
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| PLN02295 |
PLN02295 |
glycerol kinase |
103-210 |
4.93e-03 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 39.30 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232321867 103 DRRTEGVIDTLDETMP--RADLYQATGvqfLPINT-------------LPQLLAAKRASPDLFSRATRFLmlpdlIHYWL 167
Cdd:PLN02295 105 DSRTSSICRRLEKELSggRKHFVETCG---LPISTyfsatkllwllenVDAVKEAVKSGDALFGTIDSWL-----IWNLT 176
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90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1232321867 168 CGVVACEH----TNASTTQLYDPVRRDWSNTVLTAFGIPRAMFPDLV 210
Cdd:PLN02295 177 GGASGGVHvtdvTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIV 223
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