|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
55-472 |
0e+00 |
|
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: 535.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 55 LYLGMDFGTSGGRFTVIDEQGEIKAQGKREYPPFMK--EESMGWASSWKATLFSLLEDIPVTVR-SLVSSISLDGTSATT 131
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPgpGWVEQDPEDWWEALRSLLRELPAELRpRRVVAIAVDGTSGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 132 LILNSEsGEVLCQPYLYNQSCPDALPEV-----KSIAPANHTVCSGTSTLCKLVSWWNTEvPN--RESAVLLHQADWLLW 204
Cdd:cd07783 81 VLVDRE-GEPLRPAIMYNDARAVAEAEElaeaaGAVAPRTGLAVSPSSSLAKLLWLKRHE-PEvlAKTAKFLHQADWLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 205 LLHGRLGVSDYNNALKVGYDPESESYPSWLLGQP--YSQLLPKVQAPGTSIGNLKESFTRQFGFPDDCIVCTGTTDSIAA 282
Cdd:cd07783 159 RLTGDRGVTDYNNALKLGYDPETGRWPSWLLALLgiPPDLLPRVVAPGTVIGTLTAEAAEELGLPAGTPVVAGTTDSIAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 283 FLAARATEPGKAVTSLGSTLAIKLLSTKRVDDARYGVYSHRL-DDKWLVGGASNTGGAILRQLFSDEQLERLSQEINPMV 361
Cdd:cd07783 239 FLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGVYSHRHgDGYWLVGGASNTGGAVLRWFFSDDELAELSAQADPPG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 362 GSPLDYYPLQSSGERFPIADPNLAPRLLPRPESDVEFLHGILESIARIEGKGYKLLKELGATEAEEVLTAGGGAKNDKWI 441
Cdd:cd07783 319 PSGLIYYPLPLRGERFPFWDPDARGFLLPRPHDRAEFLRALLEGIAFIERLGYERLEELGAPPVEEVRTAGGGARNDLWN 398
|
410 420 430
....*....|....*....|....*....|.
gi 30681377 442 KIRQRVLGLPVKKAVHTEASYGASLLALKGA 472
Cdd:cd07783 399 QIRADVLGVPVVIAEEEEAALGAALLAAAGL 429
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
54-472 |
5.48e-56 |
|
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: 193.90 E-value: 5.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 54 KLYLGMDFGTSGGRFTVIDEQGEIKAQGKREYPPFMKEEsmGWA-----SSWKATLFS---LLEDIPVTVRSlVSSISLD 125
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHP--GWAeqdpeDWWEAVVEAireLLAKAGVDPEE-IAAIGVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 126 GTSATTLILNsESGEVLCQPYLYNQSCpdALPEVK---------SIAPANHTVCSGTSTLCKLVsWWNTEVPN--RESAV 194
Cdd:COG1070 78 GQMHGLVLLD-ADGEPLRPAILWNDTR--AAAEAAelreelgeeALYEITGNPLHPGFTAPKLL-WLKENEPEifARIAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 195 LLHQADWLLWLLHGRLgVSDYNNA-LKVGYDPESESYPSWLL---GQPYSQLlPKVQAPGTSIGNLKESFTRQFGFPDDC 270
Cdd:COG1070 154 VLLPKDYLRYRLTGEF-VTDYSDAsGTGLLDVRTRDWSDELLealGIDRELL-PELVPPGEVAGTLTAEAAAETGLPAGT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 271 IVCTGTTDSIAAFLAARATEPGKAVTSLGSTLAIKLLSTKRVDDARYGV--YSHRLDDKWLVGGASNTGGAIL---RQLF 345
Cdd:COG1070 232 PVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVhtFCHAVPGRWLPMGATNNGGSALrwfRDLF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 346 SD------EQLERLSQEINPmvGS-PLDYYP-LqsSGERFPIADPNLAPRL--LPRPESDVEFLHGILESIARIEGKGYK 415
Cdd:COG1070 312 ADgelddyEELNALAAEVPP--GAdGLLFLPyL--SGERTPHWDPNARGAFfgLTLSHTRAHLARAVLEGVAFALRDGLE 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 30681377 416 LLKELGaTEAEEVLTAGGGAKNDKWIKIRQRVLGLPVKK-AVHTEASYGASLLALKGA 472
Cdd:COG1070 388 ALEEAG-VKIDRIRATGGGARSPLWRQILADVLGRPVEVpEAEEGGALGAALLAAVGL 444
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
55-468 |
2.24e-55 |
|
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: 189.31 E-value: 2.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 55 LYLGMDFGTSGGRFTVIDEQGEIKAQGKREYPPFMKEEsmGWA----SSW----KATLFSLLEDIPVTVRSlVSSISLDG 126
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQP--GWAeqdpEDWwqavVEAIREVLAKAGIDPSD-IAAIGISG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 127 TSATTLILNSEsGEVLCQPYLYNQSCpdalpevksiapanhtvcsgtstlcklvswwntevpnresAVLLHQADWLLWLL 206
Cdd:cd00366 78 QMPGVVLVDAD-GNPLRPAIIWLDRR----------------------------------------AKFLQPNDYIVFRL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 207 HGRLgVSDYNNALKVG-YDPESESypsW------LLGQPYSqLLPKVQAPGTSIGNLKESFTRQFGFPDDCIVCTGTTDS 279
Cdd:cd00366 117 TGEF-AIDYSNASGTGlYDIKTGD---WseelldALGIPRE-KLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGGDT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 280 IAAFLAARATEPGKAVTSLG-STLAIKLLSTKRVDDARYGVYSHRLDDKWLVGGASNTGGAILRQL-----------FSD 347
Cdd:cd00366 192 AAAALGAGVVEPGDAVDSTGtSSVLSVCTDEPVPPDPRLLNRCHVVPGLWLLEGAINTGGASLRWFrdefgeeedsdAEY 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 348 EQLERLSQEINPmvGS-PLDYYP-LqsSGERFPIADPNLAPRL--LPRPESDVEFLHGILESIARIEGKGYKLLKELGAt 423
Cdd:cd00366 272 EGLDELAAEVPP--GSdGLIFLPyL--SGERSPIWDPAARGVFfgLTLSHTRAHLIRAVLEGVAYALRDNLEILEELGV- 346
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 30681377 424 EAEEVLTAGGGAKNDKWIKIRQRVLGLPVKKAVHTE-ASYGASLLA 468
Cdd:cd00366 347 KIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEgAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
55-472 |
1.06e-40 |
|
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: 152.31 E-value: 1.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 55 LYLGMDFGTSGGRFTVIDEQGEIKAQGKREYPPFMKEEsmGWASS-----WKATLFS---LLEDIPVTVRSlVSSISLDG 126
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKP--GWAEQdpedwWQATKEAlreLLAKAGISPSD-IAAIGLTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 127 tSATTLILNSESGEVLCQPYLYN-----QSCP---DALPEVKSIAPANHtvCSGTSTLCKLVsWWNT---EVPNRESAVL 195
Cdd:cd07808 78 -QMHGLVLLDKNGRPLRPAILWNdqrsaAECEeleARLGDEILIITGNP--PLPGFTLPKLL-WLKEnepEIFARIRKIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 196 LHQaDWLLWLLHGRLGvSDYNNAlkVG---YDPESESypsW------LLGQPYSqLLPKVQAPGTSIGNLKESFTRQFGF 266
Cdd:cd07808 154 LPK-DYLRYRLTGELA-TDPSDA--SGtllFDVEKRE---WseelleALGLDPS-ILPPIVESTEIVGTLTPEAAEELGL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 267 PDDCIVCTGTTDSIAAFLAARATEPGKAVTSLGSTLAIKLLSTKRVDDARYGV--YSHRLDDKWLVGGASNTGGAIL--- 341
Cdd:cd07808 226 PEGTPVVAGAGDNAAAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLhtFPHAVPGKWYAMGVTLSAGLSLrwl 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 342 RQLFSD-----EQLERLSQEINPmvGS-PLDYYP-LqsSGERFPIADPNLapR-----LlpRPESD-VEFLHGILESIA- 407
Cdd:cd07808 306 RDLFGPdresfDELDAEAAKVPP--GSeGLLFLPyL--SGERTPYWDPNA--RgsffgL--SLSHTrAHLARAVLEGVAf 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30681377 408 --RIegkGYKLLKELGAtEAEEVLTAGGGAKNDKWIKIRQRVLGLPVKK-AVHTEASYGASLLALKGA 472
Cdd:cd07808 378 slRD---SLEVLKELGI-KVKEIRLIGGGAKSPLWRQILADVLGVPVVVpAEEEGSAYGAALLAAVGA 441
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
55-472 |
1.63e-39 |
|
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: 148.12 E-value: 1.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 55 LYLGMDFGTSGGRFTVIDEQGEIKAQGKREYPPFMKEEsmGWA-----SSWKATLfSLLEDI-----PVTVRSL-VSSIs 123
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGP--GWAeldpeELWEAVK-EAIREAaaqagPDPIAAIsVSSQ- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 124 ldgtsATTLILNSESGEVLCQPYLYnqSCPDALPEVKSIAPA-------NHT--VCSGTSTLCKLVsWWNTEVP--NRES 192
Cdd:cd07773 77 -----GESGVPVDRDGEPLGPAIVW--FDPRGKEEAEELAERigaeelyRITglPPSPMYSLAKLL-WLREHEPeiFAKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 193 AVLLHQADWLLWLLHGRLgVSDYNNALKVG-YDPESESYPSWLL---GQPySQLLPKVQAPGTSIGNLKESFTRQFGFPD 268
Cdd:cd07773 149 AKWLSVADYIAYRLTGEP-VTDYSLASRTMlFDIRKRTWSEELLeaaGID-ASLLPELVPSGTVIGTVTPEAAEELGLPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 269 DCIVCTGTTDSIAAFLAARATEPGKAVTSLGSTLAIKLLSTKRVDDARYG-----VYSHRLDDKWLVGGASNTGGAI--L 341
Cdd:cd07773 227 GTPVVVGGHDHLCAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLDEMLAegglsYGHHVPGGYYYLAGSLPGGALLewF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 342 RQLF-----SDEQLERLSQEINPMVGSPLDYYPLQSSGERFPIADPNLAPRLLPRPESDVEFLHGILESIARIEGKGYKL 416
Cdd:cd07773 307 RDLFggdesDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEA 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 30681377 417 LKELGaTEAEEVLTAGGGAKNDKWIKIRQRVLGLPVKKAVHTEA-SYGASLLALKGA 472
Cdd:cd07773 387 LEKAG-IPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEAtALGAALLAGVGA 442
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
55-478 |
3.87e-34 |
|
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: 133.84 E-value: 3.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 55 LYLGMDFGTSGGRFTVIDEQGEIKAQGKREYPPFMKEEsmGWASS-----WKATLFSLLEDIPVTVRSLVSSISLDGTsA 129
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEP--GWAEQdpeeiLEAVLEALKEVLAKLGGGEVDAIGFSSA-M 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 130 TTLILNSESGEVLCQPYLYNQSCPDALPEVKSIAPANHTV--CSGT-----STLCKLVsWWNTEVPNRESAV--LLHQAD 200
Cdd:cd07770 78 HSLLGVDEDGEPLTPVITWADTRAAEEAERLRKEGDGSELyrRTGCpihpmYPLAKLL-WLKEERPELFAKAakFVSIKE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 201 WLLWLLHGRLgVSDYNNA--------LKVGYDPEsesypsWL--LGQPYSQLlPKVQAPGTSIGNLKESFTRQFGFPDDC 270
Cdd:cd07770 157 YLLYRLTGEL-VTDYSTAsgtgllniHTLDWDEE------ALelLGIDEEQL-PELVDPTEVLPGLKPEFAERLGLLAGT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 271 IVCTGTTDSIAAFLAARATEPGKAVTSLGSTLAIKLLSTKRVDDARYGVYSHRLDDK-WLVGGASNTGGAIL---RQLF- 345
Cdd:cd07770 229 PVVLGASDGALANLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPGRLWCYRLDENrWLVGGAINNGGNVLdwlRDTLl 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 346 ----SDEQLERLSQEINPmvGSP-LDYYP-LqsSGERFPIADPN-------LaprllpRPESD-VEFLHGILESIA---- 407
Cdd:cd07770 309 lsgdDYEELDKLAEAVPP--GSHgLIFLPyL--AGERAPGWNPDargaffgL------TLNHTrADILRAVLEGVAfnlk 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30681377 408 RIegkgYKLLKELGAtEAEEVLTAGGGAKNDKWIKIRQRVLGLPVKKAVHTEAS-YGASLLALKGAKQNSGL 478
Cdd:cd07770 379 SI----YEALEELAG-PVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASaLGAALLALEALGLISSL 445
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
55-473 |
1.22e-30 |
|
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: 123.40 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 55 LYLGMDFGTSGGRFTVIDEQGEIKAQGKREYPpfMKEESMGWASSW--------KATLFSLLEDIPVTVRSlVSSISLDG 126
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHD--LLTPKPGWAEHDpevwwgavCEIIRELLAKAGISPKE-IAAIGVSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 127 TSATTLILNsESGEVLCQPYLYNqscpD--ALPEVKSI----------APANHTVCSGtSTLCKLVswWnteVPNRESAV 194
Cdd:cd07804 78 LVPALVPVD-ENGKPLRPAILYG----DrrATEEIEWLnenigedrifEITGNPLDSQ-SVGPKLL--W---IKRNEPEV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 195 ------LLHQADWLLWLLHGRLGVsDYNNALKVG--YDPESESypsW------LLGQPySQLLPKVQAPGTSIGNLKESF 260
Cdd:cd07804 147 fkktrkFLGAYDYIVYKLTGEYVI-DYSSAGNEGglFDIRKRT---WdeelleALGID-PDLLPELVPSTEIVGEVTKEA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 261 TRQFGFPDDCIVCTGTTDSIAAFLAARATEPGKAVTSLGSTLAIKLLSTKRVDDARYGVYSHRLDDKWLVGGASNTGGAI 340
Cdd:cd07804 222 AEETGLAEGTPVVAGTVDAAASALSAGVVEPGDLLLMLGTAGDIGVVTDKLPTDPRLWLDYHDIPGTYVLNGGMATSGSL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 341 LR----QLFSDE-------------QLERLSQEINPmvGSP----LDYYplqsSGERFPIADPN-------LAPRllprp 392
Cdd:cd07804 302 LRwfrdEFAGEEveaeksggdsaydLLDEEAEKIPP--GSDglivLPYF----MGERTPIWDPDargvifgLTLS----- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 393 esdveflHG-------ILESIARIEGKGYKLLKELGATEaEEVLTAGGGAKNDKWIKIRQRVLGLPVK-KAVHTEASYGA 464
Cdd:cd07804 371 -------HTrahlyraLLEGVAYGLRHHLEVIREAGLPI-KRLVAVGGGAKSPLWRQIVADVTGVPQEyVKDTVGASLGD 442
|
....*....
gi 30681377 465 SLLALKGAK 473
Cdd:cd07804 443 AFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
57-472 |
7.53e-28 |
|
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: 115.31 E-value: 7.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 57 LGMDFGTSGGRFTVIDEQGEIKAQGKREYPPFMKEEsmGW----ASSWKATLFS----LLEDIPVTVRSLVSsISLDGTS 128
Cdd:cd07779 3 LGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEP--GWveqdPDDWWDALCEalkeAVAKAGVDPEDIAA-IGLTSQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 129 ATTLILNsESGEVLCqpylynqscpdalpevksiaPAnhtvcsgtstlcklVSWWNTevpnRESAVLLHQaDWLLWLLHG 208
Cdd:cd07779 80 STFVPVD-EDGRPLR--------------------PA--------------ISWQDK----RTAKFLTVQ-DYLLYRLTG 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 209 RLgVSDYNNALKVG--------YDPESEsypsWLLGQPySQLLPKVQAPGTSIGNLKESFTRQFGFPDDCIVCTGTTDSI 280
Cdd:cd07779 120 EF-VTDTTSASRTGlpdirtrdWSDDLL----DAFGID-RDKLPELVPPGTVIGTLTKEAAEETGLPEGTPVVAGGGDQQ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 281 AAFLAARATEPGKAVTSLGSTLAIKLLSTKRVDDA--RYGVYSHRLDDKWLVGGASNTGGAILR----QLFSDEQLERLS 354
Cdd:cd07779 194 CAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPerRIPCNPSAVPGKWVLEGSINTGGSAVRwfrdEFGQDEVAEKEL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 355 -----QEINPMVGSPldyyPLQSSGerfPIADPNLAPRLLPRPESDVE--FL-----HG-------ILESIArIEGK-GY 414
Cdd:cd07779 274 gvspyELLNEEAAKS----PPGSDG---LLFLPYLAGAGTPYWNPEARgaFIgltlsHTrahlaraILEGIA-FELRdNL 345
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 30681377 415 KLLKELGaTEAEEVLTAGGGAKNDKWIKIRQRVLGLPVKKAVHTEAS-YGASLLALKGA 472
Cdd:cd07779 346 EAMEKAG-VPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATaLGAAILAAVGA 403
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
55-473 |
4.23e-27 |
|
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: 113.09 E-value: 4.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 55 LYLGMDFGTSGGRFTVIDEQGEIKAQGKREyPPFMKEESMGWASSWKATLFslLEDIPVTVRSL----------VSSISL 124
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYRE-WEYYTDDDYPDAKEFDPEEL--WEKICEAIREAlkkagispedISAVSS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 125 DGTSATTLILNSESGEVLCQPYLYNQscpdALPEVKSIAPAN-----HTVCSGTSTL---CKLVsWWNTEVP---NRESA 193
Cdd:cd07798 78 TSQREGIVFLDKDGRELYAGPNIDAR----GVEEAAEIDDEFgeeiyTTTGHWPTELfpaARLL-WFKENRPeifERIAT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 194 VLLhQADWLLWLLHGRLgVSDYNNALKVG-YDPESESYpSW----LLGQPYSqLLPKVQAPGTSIGNLKESFTRQFGFPD 268
Cdd:cd07798 153 VLS-ISDWIGYRLTGEL-VSEPSQASETQlFDIKKREW-SQelleALGLPPE-ILPEIVPSGTVLGTVSEEAARELGLPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 269 DCIVCTGTTDSIAAFLAARATEPGKAVTSLGSTLAIKLLSTKRVDDARYGVYS--HRLDDKWLV-GGASNTGGAI--LRQ 343
Cdd:cd07798 229 GTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTgcHLVPGKWVLeSNAGVTGLNYqwLKE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 344 LFSD------EQLERLSQEINPmvGSPLDYyplQSSGERFPIADPNLAPR---LLPRPESDVE-----FLHGILESIA-R 408
Cdd:cd07798 309 LLYGdpedsyEVLEEEASEIPP--GANGVL---AFLGPQIFDARLSGLKNggfLFPTPLSASEltrgdFARAILENIAfA 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30681377 409 IEGKgYKLLKELGATEAEEVLTAGGGAKNDKWIKIRQRVLGLPVKKAVHTEAS-YGASLLALKGAK 473
Cdd:cd07798 384 IRAN-LEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASaLGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
57-472 |
3.84e-26 |
|
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: 110.69 E-value: 3.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 57 LGMDFGTSGGRFTVIDEQGEIKAQGKREYPPFMKEEsmGWA----SSW----KATLFSLLEDIPVTVRSlVSSISLDGTS 128
Cdd:cd07805 3 LAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKP--GWAeqdpEDWwdavCRATRALLEKSGIDPSD-IAAIAFSGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 129 ATTLILNsESGEVLCQPYLYNqscpD--ALPEVKSIAPA-----------NHTVcSGTSTLCKLVsWWNTEVPN--RESA 193
Cdd:cd07805 80 QGVVPVD-KDGNPLRNAIIWS----DtrAAEEAEEIAGGlggiegyrlggGNPP-SGKDPLAKIL-WLKENEPEiyAKTH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 194 VLLHQADWLLWLLHGRLgVSDYNNALKVG-YDPESESYPSWLL---GQPYSqLLPKVQAPGTSIGNLKESFTRQFGFPDD 269
Cdd:cd07805 153 KFLDAKDYLNFRLTGRA-ATDPSTASTTGlMDLRKRRWSEELLraaGIDPD-KLPELVPSTEVVGELTPEAAAELGLPAG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 270 CIVCTGTTDSIAAFLAARATEPGKAVTSLGSTLAIKLLSTKRVDDARYGVYS--HRLDDKWLVGGASNTGGAIL----RQ 343
Cdd:cd07805 231 TPVVGGGGDAAAAALGAGAVEEGDAHIYLGTSGWVAAHVPKPKTDPDHGIFTlaSADPGRYLLAAEQETAGGALewarDN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 344 LFSDEQ--------LERLSQEINPMVGSPLdYYP-LQssGERFPIADPNLaprllpR-------PESD-VEFLHGILESI 406
Cdd:cd07805 311 LGGDEDlgaddyelLDELAAEAPPGSNGLL-FLPwLN--GERSPVEDPNA------RgafiglsLEHTrADLARAVLEGV 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30681377 407 A---RIegkGYKLLKELGATeAEEVLTAGGGAKNDKWIKIRQRVLGLPVKKAVHTE--ASYGASLLALKGA 472
Cdd:cd07805 382 AfnlRW---LLEALEKLTRK-IDELRLVGGGARSDLWCQILADVLGRPVEVPENPQeaGALGAALLAAVGL 448
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
55-472 |
3.28e-20 |
|
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: 93.37 E-value: 3.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 55 LYLGMDFGTSGGRFTVIDEQ-GEIKAQGKREYPPFMKEESMGWASS-----WKATLFSL---LEDIPVTvRSLVSSISLD 125
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDLAdGEELASAVVPYPTGYIPPRPGWAEQnpadyWEALEEAVrgaLAEAGVD-PEDVVGIGVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 126 GTSATTLILNsESGEVLCQPYL------YNQScpDALPEV-KSIAPANHTVCSGTST----LCKLVsWW---NTEVPNRe 191
Cdd:cd07781 80 TTSSTVVPVD-EDGNPLAPAILwmdhraQEEA--AEINETaHPALEYYLAYYGGVYSsewmWPKAL-WLkrnAPEVYDA- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 192 SAVLLHQADWLLWLLHGRLGVSDYNNALKVGYDPEsESYPSW--------LLGQPYSQLLPKVQAPGTSIGNLKESFTRQ 263
Cdd:cd07781 155 AYTIVEACDWINARLTGRWVRSRCAAGHKWMYNEW-GGGPPReflaaldpGLLKLREKLPGEVVPVGEPAGTLTAEAAER 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 264 FGFPDDCIVCTGTTDSIAAFLAARATEPGKAVTSLG-STLaiKLLSTKRVDDAR--YGVY-SHRLDDKWLV-GGASNTGG 338
Cdd:cd07781 234 LGLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGtSTC--HLMVSPKPVDIPgiCGPVpDAVVPGLYGLeAGQSAVGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 339 AI--LRQLF-------SDEQLERLSQE---INPmvGSP----LDYYplqsSGERFPIADPNLapR-------LLPRPEsd 395
Cdd:cd07781 312 IFawFVRLFvppaeerGDSIYALLSEEaakLPP--GESglvaLDWF----NGNRTPLVDPRL--RgaivgltLGTTPA-- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 396 vEFLHGILESIA--------RIEGKGYKLlkelgateaEEVLTAGGGA-KNDKWIKIRQRVLGLPVKKAVHTEAS-YGAS 465
Cdd:cd07781 382 -HIYRALLEATAfgtraiieRFEEAGVPV---------NRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAPaLGAA 451
|
....*..
gi 30681377 466 LLALKGA 472
Cdd:cd07781 452 ILAAVAA 458
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
55-469 |
1.45e-17 |
|
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: 84.91 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 55 LYLGMDFGTSGGRFTVID-EQGEIKAQGKREYPPFmkEESMGWASS-----WKA--TLFS-LLEDIPVTVRSLVS-SIS- 123
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENI--LIDPGWAEQdpedwWDAlqAAFAqLLKDAGAELRDVAAiGISg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 124 -------LDgtsattlilnsESGEVLCQPYLYNQS--------------CPDALpEVKSIAPANHTVCsgtstlcKLVsw 182
Cdd:cd07809 79 qmhglvaLD-----------ADGKVLRPAKLWCDTrtapeaeeltealgGKKCL-LVGLNIPARFTAS-------KLL-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 183 WNTEvpNRESAV-------LLHqaDWLLWLLHGRLgVSDYNNALKVGY-DPESESY---------PSWLLgqpySQLLPK 245
Cdd:cd07809 138 WLKE--NEPEHYariakilLPH--DYLNWKLTGEK-VTGLGDASGTFPiDPRTRDYdaellaaidPSRDL----RDLLPE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 246 VQAPGTSIGNLKESFTRQFGFPDDCIVCTGTTDSIAAFLAARATEPGKAVTSLGSTLAIKLLSTKRVDDARYGV--YSHR 323
Cdd:cd07809 209 VLPAGEVAGRLTPEGAEELGLPAGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSDPHGRVatFCDS 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 324 LDDK-WLVGGAS--NTGGAILRQLF--SDEQLERLSQEINPmvGSP----LDYYplqsSGERFPiADPNLAPRLLPRPES 394
Cdd:cd07809 289 TGGMlPLINTTNclTAWTELFRELLgvSYEELDELAAQAPP--GAGglllLPFL----NGERTP-NLPHGRASLVGLTLS 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 395 DVE---FLHGILESIA---RIegkGYKLLKELGAtEAEEVLTAGGGAKNDKWIKIRQRVLGLPVKKAVHTE-ASYGASLL 467
Cdd:cd07809 362 NFTranLARAALEGATfglRY---GLDILRELGV-EIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEgGALGAALQ 437
|
..
gi 30681377 468 AL 469
Cdd:cd07809 438 AA 439
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
196-472 |
2.82e-14 |
|
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: 74.51 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 196 LHQADWLLWLLHGRLGvSDYNNALKVGYDPESESYP----SWLLGQPYSQLLPKVQAPGTSIGNLKESFTRQFGFPDDCI 271
Cdd:cd07802 154 LFCKDWIRYRLTGEIS-TDYTDAGSSLLDLDTGEYDdellDLLGIEELKDKLPPLVPSTEIAGRVTAEAAALTGLPEGTP 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 272 VCTGTTDSIAAFLAARATEPGKAVTSLGSTLAIKLLSTKRVDDARYGVYS-HRLDDKWLVGGASNTGGA----ILRQLFS 346
Cdd:cd07802 233 VAAGAFDVVASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDSVGSNSlHADPGLYLIVEASPTSASnldwFLDTLLG 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 347 DE--QLERLSQEINPMVGSpldyYPLQSSGERF-P-IADPNLAPRL------LpRPESDV-EFLHGILESIA-----RIE 410
Cdd:cd07802 313 EEkeAGGSDYDELDELIAA----VPPGSSGVIFlPyLYGSGANPNArggffgL-TAWHTRaHLLRAVYEGIAfshrdHLE 387
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30681377 411 gkgyKLLKelgATEAEEVLTAGGGAKNDKWIKIRQRVLGLPVKKAVHTEA-SYGASLLALKGA 472
Cdd:cd07802 388 ----RLLV---ARKPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELgALGAAICAAVAA 443
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
294-472 |
1.56e-10 |
|
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: 60.42 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 294 AVTSLG-STLAIKLLSTKRVD-DARYGVY-SHRLDDKWLVGGASNTGGAIL---------RQLFSDEQLERLSQEINPMV 361
Cdd:pfam02782 1 LAISAGtSSFVLVETPEPVLSvHGVWGPYtNEMLPGYWGLEGGQSAAGSLLawllqfhglREELRDAGNVESLAELAALA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 362 GSP----LDYYPlQSSGERFPIADPNlAPRL---LPRPESDVEFLHGILESIA---RIegkGYKLLKELGATEAEEVLTA 431
Cdd:pfam02782 81 AVApaggLLFYP-DFSGNRAPGADPG-ARGSitgLSSPTTLAHLYRAILESLAlqlRQ---ILEALTKQEGHPIDTIHVS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 30681377 432 GGGAKNDKWIKIRQRVLGLPVKKAVHTEA-SYGASLLALKGA 472
Cdd:pfam02782 156 GGGSRNPLLLQLLADALGLPVVVPGPDEAtALGAALLAAVAA 197
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
56-478 |
1.68e-09 |
|
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: 59.85 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 56 YLGMDFGTSGGRF---TVIDEQGEIKAQGKREYPPFMKEESMGWasswkaTLFSLLEDIpvtVRSL---------VSSIS 123
Cdd:cd07771 2 YLAVDLGASSGRVilgSLDGGKLELEEIHRFPNRPVEINGHLYW------DIDRLFDEI---KEGLkkaaeqggdIDSIG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 124 LDGTSATTLILNsESGEVLCQPYLYNQSCPDALPE-VKSIAPANH------TVCSGTSTLCKLVSW-WNTEVPNRESAVL 195
Cdd:cd07771 73 IDTWGVDFGLLD-KNGELLGNPVHYRDPRTEGMMEeLFEKISKEElyertgIQFQPINTLYQLYALkKEGPELLERADKL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 196 LHQADWLLWLLHGRLgVSDYNNA----LkvgYDPESESypsW------LLGQPySQLLPKVQAPGTSIGNLKESFTRQFG 265
Cdd:cd07771 152 LMLPDLLNYLLTGEK-VAEYTIAsttqL---LDPRTKD---WseelleKLGLP-RDLFPPIVPPGTVLGTLKPEVAEELG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 266 FPDDCIVCTGTTDSIAAFLAARATEPGKAVTSLGSTLAIKLLSTKRVddarygvyshrLDDKWLVGGASNTGGA------ 339
Cdd:cd07771 224 LKGIPVIAVASHDTASAVAAVPAEDEDAAFISSGTWSLIGVELDEPV-----------ITEEAFEAGFTNEGGAdgtirl 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 340 --------ILRQLfsdeqLERLSQEinpmvGSPLDYYPL-----QSSGERFPIaDPNlAPRLL----------------- 389
Cdd:cd07771 293 lknitglwLLQEC-----RREWEEE-----GKDYSYDELvalaeEAPPFGAFI-DPD-DPRFLnpgdmpeairaycretg 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 390 -PRPESDVEFLHGILESIARIEGKGYKLLKELGATEAEEVLTAGGGAKND---KWIKirqRVLGLPVkKAVHTEAS-YGA 464
Cdd:cd07771 361 qPVPESPGEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNAllcQLTA---DATGLPV-IAGPVEATaIGN 436
|
490
....*....|....
gi 30681377 465 SLLALKGAKQNSGL 478
Cdd:cd07771 437 LLVQLIALGEIKSL 450
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
190-469 |
2.59e-09 |
|
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: 59.18 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 190 RESAVLLHQADWLLWLLHGRLgVSDYNNALKVGYDPESESYPSWLLG----QPYSQLLPKVQAPGTSIGNLKESFTRQFG 265
Cdd:cd24121 148 ERARTALHCKDWLFYKLTGEI-ATDPSDASLTFLDFRTRQYDDEVLDllglEELRHLLPPIRPGTEVIGPLTPEAAAATG 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 266 FPDDCIVCTGTTDSIAAFLAARATEPGKAVTSLGSTLaIKLLSTKRVDDARYGV---YSHRLDDKWLVGGASNTGGA--- 339
Cdd:cd24121 227 LPAGTPVVLGPFDVVATALGSGAIEPGDACSILGTTG-VHEVVVDEPDLEPEGVgytICLGVPGRWLRAMANMAGTPnld 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 340 -ILRQLFSDEQ-------------LERLSQEINPmvGSP-LDYYP-LQSSGERFPIADPN-------LAPRllprpesdv 396
Cdd:cd24121 306 wFLRELGEVLKegaepagsdlfqdLEELAASSPP--GAEgVLYHPyLSPAGERAPFVNPNaraqftgLSLE--------- 374
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30681377 397 eflHGILESI-ARIEGKGYKLL---KELGATEAEEVLTaGGGAKNDKWIKIRQRVLGLPVKKAVHTEA-SYGASLLAL 469
Cdd:cd24121 375 ---HTRADLLrAVYEGVALAMRdcyEHMGEDPGELRLS-GGGARSDTWCQILADALGVPVRVPAGEEFgARGAAMNAA 448
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
55-472 |
4.60e-09 |
|
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466794 [Multi-domain] Cd Length: 492 Bit Score: 58.50 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 55 LYLGMDFGTSGGRFTVIDEQGEIKAQGKRE--------YPPFMKEEsmgWASSWKaTLFSLLEDIPVTVRSLVSSISldG 126
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREwrhkevpdVPGSMDFD---TEKNWK-LICECIREALKKAGIAPKSIA--A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 127 TSATT----LILNSESGEVLcqpylynQSCPD----ALPEVKSIAPANHTV------CSG-TSTLCKL--VSWWNTEVPN 189
Cdd:cd07775 75 ISTTSmregIVLYDNEGEEI-------WACANvdarAAEEVSELKELYNTLeeevyrISGqTFALGAIprLLWLKNNRPE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 190 --RESAVLLHQADWLLWLLHGRLGVSDYN-------NALKVGYDPESESypswLLGQPySQLLPKVQAPGTSIGNLKESF 260
Cdd:cd07775 148 iyRKAAKITMLSDWIAYKLSGELAVEPSNgsttglfDLKTRDWDPEILE----MAGLK-ADILPPVVESGTVIGKVTKEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 261 TRQFGFPDDCIVCTGTTDSIAAFLAARATEPGKAVTSLGSTLAIKLLSTKRVDD--ARYGVYSHRLDDKWLVGGASNTGG 338
Cdd:cd07775 223 AEETGLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDpaMNIRVNCHVIPDMWQAEGISFFPG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 339 AILR----QLFSDEQ-------------LERLSQEINPmvGS----PLDYYPLQSSGERFPiadpnlAP-----RLLPRP 392
Cdd:cd07775 303 LVMRwfrdAFCAEEKeiaerlgidaydlLEEMAKDVPP--GSygimPIFSDVMNYKNWRHA------APsflnlDIDPEK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 393 ESDVEFLHGILESIARIEGKGYKLLKELGATEAEEVLTAGGGAKNDKWIKIRQRVLGLPVKKAVHTEAS-YGASLLALKG 471
Cdd:cd07775 375 CNKATFFRAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATaLGAAIAAGVG 454
|
.
gi 30681377 472 A 472
Cdd:cd07775 455 A 455
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
55-284 |
8.17e-08 |
|
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: 53.11 E-value: 8.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 55 LYLGMDFGTSGGRFTVIDEQGEIKAQGKREYPpfMKEESMGWASS-----WKAT---LFSLLEDIPVTVrSLVSSISLDG 126
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENP--QITPHPGWAEQdpdeiWQAVaqcIAKTLSQLGISL-KQIKGIGISN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 127 TSATTLILNSESgevlcQPyLYNQ---SCPDALPEV---------KSIAPANHTVCSGTSTLCKLvSWWNTEVPNR---- 190
Cdd:pfam00370 78 QGHGTVLLDKND-----KP-LYNAilwKDRRTAEIVenlkeegnnQKLYEITGLPIWPGFTLSKL-RWIKENEPEVfeki 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 191 ESAVLLHqaDWLLWLLHGRLgVSDYNNALKVG--------YDPESESYpswlLGQPYSQlLPKVQAPGTSIGNLKESFTR 262
Cdd:pfam00370 151 HKFLTIH--DYLRWRLTGVF-VTDHTNASRSMmfnihkldWDPELLAA----LGIPRDH-LPPLVESSEIYGELNPELAA 222
|
250 260
....*....|....*....|..
gi 30681377 263 QFGFPDDCIVCTGTTDSIAAFL 284
Cdd:pfam00370 223 MWGLDEGVPVVGGGGDQQAAAF 244
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
56-474 |
1.56e-07 |
|
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: 53.78 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 56 YLGMDFGTSGGRFTVID-EQGEIKAQGKREYPPF-MKEESMGWASS---WKATLFSLLEdipVTVRSLVSSISLD--GTS 128
Cdd:cd07768 2 GIGVDVGTSSARAGVYDlYAGLEMAQEPVPYYQDsSKKSWKFWQKSteiIKALQKCVQK---LNIREGVDAYEVKgcGVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 129 AT-TLILNSESGEVLCQPYLYNqscpdalPEVKSIAPANH---TVCSGTSTLC----------KLVSWWNT--------E 186
Cdd:cd07768 79 ATcSLAIFDREGTPLMALIPYP-------NEDNVIFWMDHsavNEAQWINMQCpqqlldylggKISPEMGVpklkyfldE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 187 VPNRESAV--LLHQADWLLWLLHGRLGVSDYNNALKVGYDPEsESYPS---------WLLGQPYSQLLPKVQAPGTSIGN 255
Cdd:cd07768 152 YSHLRDKHfhIFDLHDYIAYELTRLYEWNICGLLGKENLDGE-ESGWSssffknidpRLEHLTTTKNLPSNVPIGTTSGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 256 LKESFTRQFGFPDDCIVCTGTTDSIAAFLA-ARATEPGKAVTSLGSTLAIKLLSTK--RVDDARYGVYSHRLDDKWLVGG 332
Cdd:cd07768 231 ALPEMAEKMGLHPGTAVVVSCIDAHASWFAvASPHLETSLFMIAGTSSCHMYGTTIsdRIPGVWGPFDTIIDPDYSVYEA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 333 ASNTGGAILRQLFS--------DEQLER-------LSQEINPMVGSP--------LDYYplqsSGERFPIADPNLAPRLL 389
Cdd:cd07768 311 GQSATGKLIEHLFEshpcarkfDEALKKgadiyqvLEQTIRQIEKNNglsihiltLDMF----FGNRSEFADPRLKGSFI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 390 -----PRPESDVEFLHGILESIA--------RIEGKGYkllkelgatEAEEVLTAGGGAKNDKWIKIRQRVLGLPVKKAV 456
Cdd:cd07768 387 gesldTSMLNLTYKYIAILEALAfgtrliidTFQNEGI---------HIKELRASGGQAKNERLLQLIALVTNVAIIKPK 457
|
490 500
....*....|....*....|.
gi 30681377 457 HTEAS-YGASLLA--LKGAKQ 474
Cdd:cd07768 458 ENMMGiLGAAVLAkvAAGKKQ 478
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
240-471 |
2.37e-07 |
|
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: 52.95 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 240 SQLLPKVQAPGTSIGNLKESFTRQFGFPDDCIVCTGTTDSIAAFLAARAtEPGKAVTSLGS--TLaikLLSTKRVDDARY 317
Cdd:cd07776 235 KEKLGELVPSSTVAGGISSYFVERYGFSPDCLVVAFTGDNPASLAGLGL-EPGDVAVSLGTsdTV---FLVLDEPKPGPE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 318 G-VYSHRLDDKWLVGGASNTGGAILRQ------------LFsDEQLER-------------LSQEINPmvgspldyyPLQ 371
Cdd:cd07776 311 GhVFANPVDPGSYMAMLCYKNGSLARErvrdryaggsweKF-NELLEStppgnngnlglyfDEPEITP---------PVP 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 372 SSGERFPIADPNLAprlLPRPESDVEflhGILESIA-----RIEGKGYKllkelgaTEAEEVLTAGGGAKNDkwiKIRQR 446
Cdd:cd07776 381 GGGRRFFGDDGVDA---FFDPAVEVR---AVVESQFlsmrlHAERLGSD-------IPPTRILATGGASANK---AILQV 444
|
250 260
....*....|....*....|....*....
gi 30681377 447 ---VLGLPVKKAVHTE-ASYGASLLALKG 471
Cdd:cd07776 445 ladVFGAPVYTLDVANsAALGAALRAAHG 473
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
152-472 |
3.31e-07 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 52.72 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 152 CPDALPEVKSIA----PANHTVCSGT-----STLCKLVsWWNTEVPNresavLLHQAD-WLLW--LLHGRL--------- 210
Cdd:PRK10331 102 CPRTAAVMENIEryisAQQLQQISGVgafsfNTLYKLV-WLKENHPQ-----LLEQAHaWLFIssLINHRLtgefttdit 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 211 --GVSDYNNALKVGYDPESESYpswlLGQPySQLLPKVQAPGTSIGNLKESFTRQFGFPDDCIVCTGTTDSIAAFLAARA 288
Cdd:PRK10331 176 maGTSQMLDIQQRDFSPEILQA----TGLS-RRLFPRLVEAGEQIGTLQPSAAALLGLPVGIPVISAGHDTQFALFGSGA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 289 TEpGKAVTSLGsTLAIKLLSTKRVD--------------DARYGVYSHRLddKWLvggASntgGAI--LRQLFSdeqler 352
Cdd:PRK10331 251 GQ-NQPVLSSG-TWEILMVRSAQVDtsllsqyagstcelDSQSGLYNPGM--QWL---AS---GVLewVRKLFW------ 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 353 lsqeinpmvgSPLDYYP-LQSSGERFPI-ADP-NLAPRLLPRPESDVE--FLHGILESIAR--IEGKGYKL------LKE 419
Cdd:PRK10331 315 ----------TAETPYQtMIEEARAIPPgADGvKMQCDLLACQNAGWQgvTLNTTRGHFYRaaLEGLTAQLkrnlqvLEK 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 30681377 420 LGATEAEEVLTAGGGAKNDKWIKIRQRVLGLPVKKAVHTEASY-GASLLALKGA 472
Cdd:PRK10331 385 IGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVaGAAMFGWYGV 438
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
195-301 |
1.72e-06 |
|
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: 50.34 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681377 195 LLHQADWLL-------WLLHGRLgVSDYNNalkVG-----YDPESESYPSWLLGQPYSQLLPKVQAPGTSIGNLKESFTR 262
Cdd:cd07772 139 LFARAKTILplpqywaWRLTGKA-ASEITS---LGchtdlWDFEKNEYSSLVKKEGWDKLFPPLRKAWEVLGPLRPDLAR 214
|
90 100 110
....*....|....*....|....*....|....*....
gi 30681377 263 QFGFPDDCIVCTGTTDSIAAFLAARATEPGKAVtsLGST 301
Cdd:cd07772 215 RTGLPKDIPVGCGIHDSNAALLPYLAAGKEPFT--LLST 251
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
415-472 |
3.34e-03 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 39.99 E-value: 3.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 30681377 415 KLLKELGATEAEEVLTAGGGAKNDKWIKIRQRVLGLPVKKAVHTEA-SYGASLLALKGA 472
Cdd:PRK10939 400 QQIAAFSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEAtALGCAIAAGVGA 458
|
|
| |
