|
Name |
Accession |
Description |
Interval |
E-value |
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
5-295 |
2.12e-155 |
|
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.
Pssm-ID: 238914 [Multi-domain] Cd Length: 290 Bit Score: 435.68 E-value: 2.12e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 5 QILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFVLDDLRRYSVDLR 84
Cdd:cd01939 1 AVLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 85 YtVFQTTGSVPIATVIINEASGSRTILYYDRSLPDVSATDFEKVDLTQFKWIHIEGRNASEQVKMLQRIDAHNTRQPpEQ 164
Cdd:cd01939 81 H-CYRKDIDEPASSYIIRSRAGGRTTIVNDNNLPEVTYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNNRRP-EI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 165 KIRVSVEVEKPQEELFQLFGYGDVVFVSKDVAKHLGFQSAGEALRGLYGRVRKGAVLVCAWAEEGADALGPDGKLIHSDA 244
Cdd:cd01939 159 RITISVEVEKPREELLELAAYCDVVFVSKDWAQSRGYKSPEECLRGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSPA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 109102319 245 FPPPRVVDTLGAGDTFNASVIFSLSQG-RSVQEALRFGCQVAGKKCGQQGFD 295
Cdd:cd01939 239 HKPIRVVDTLGAGDTFNAAVIYALNKGpDDLSEALDFGNRVASQKCTGVGFD 290
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
5-293 |
4.02e-44 |
|
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440290 [Multi-domain] Cd Length: 301 Bit Score: 152.35 E-value: 4.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 5 QILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFVLDDLRRYSVDLR 84
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 85 YTVFQTTGSVPIATVIINEaSGSRTILYYDRSLPDVSATDFEKVDLTQFKWIHIEG------RNASEQVKMLQRIDAHNt 158
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDP-DGERTIVFYRGANAELTPEDLDEALLAGADILHLGGitlasePPREALLAALEAARAAG- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 159 rqppeqkIRVSVEV-------EKPQEELFQLFGYGDVVFVSKDVAKHL-GFQSAGEALRGLYGRVRKGAVLVCawAEEGA 230
Cdd:COG0524 159 -------VPVSLDPnyrpalwEPARELLRELLALVDILFPNEEEAELLtGETDPEEAAAALLARGVKLVVVTL--GAEGA 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109102319 231 DALGpDGKLIHSDAFpPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKKCGQQG 293
Cdd:COG0524 230 LLYT-GGEVVHVPAF-PVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPG 290
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
5-296 |
2.17e-33 |
|
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time. .
Pssm-ID: 238920 [Multi-domain] Cd Length: 284 Bit Score: 123.56 E-value: 2.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 5 QILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFVLDDLRRYSVDLR 84
Cdd:cd01945 1 RVLGVGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 85 YTVfQTTGSVPIATVIINEASGSRTILYYDRsLPDVSATDFEKVDLTQFKWIHIEGRNASEQVKMLQRIDAHNTRQPpeq 164
Cdd:cd01945 81 FIV-VAPGARSPISSITDITGDRATISITAI-DTQAAPDSLPDAILGGADAVLVDGRQPEAALHLAQEARARGIPIP--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 165 kIRVSVEVEKPQEELFQLfgyGDVVFVSKDVAKHLGFQSAGEALRGLYGRVRKgAVLVCAwAEEGADALGPDGKLIHSDA 244
Cdd:cd01945 156 -LDLDGGGLRVLEELLPL---ADHAICSENFLRPNTGSADDEALELLASLGIP-FVAVTL-GEAGCLWLERDGELFHVPA 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 109102319 245 FpPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKKCgqQGFDG 296
Cdd:cd01945 230 F-PVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKC--RGLGG 278
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
6-293 |
2.40e-27 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 107.81 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 6 ILCVGLVVLDVISLVDKYPKEDSEIRCLSQRwqRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFVLDDLRRYSVDLRY 85
Cdd:pfam00294 2 VVVIGEANIDLIGNVEGLPGELVRVSTVEKG--PGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 86 TVFQTTGSVPIATVIINEAsGSRTILYYDRSLPDVSATDFEKV--DLTQFKWIHIEG------RNASEQvKMLQRIDAHN 157
Cdd:pfam00294 80 VVIDEDTRTGTALIEVDGD-GERTIVFNRGAAADLTPEELEENedLLENADLLYISGslplglPEATLE-ELIEAAKNGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 158 TRQPpeqkiRVSVEVEKPQEELFQLFGYGDVVFVSKDVAKHLGFQSAG---EALRGLYGRVRKGA-VLVCAWAEEGADAL 233
Cdd:pfam00294 158 TFDP-----NLLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLDdieEALAALHKLLAKGIkTVIVTLGADGALVV 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 234 GPDGKLIHsDAFPPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKKCGQQG 293
Cdd:pfam00294 233 EGDGEVHV-PAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSG 291
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
5-293 |
8.89e-25 |
|
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.
Pssm-ID: 238571 [Multi-domain] Cd Length: 294 Bit Score: 100.73 E-value: 8.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 5 QILCVGLVVLDVislvdkYPKEDSEIRClSQRWQR--GGNASNSCTVLSLLGAPCAFMGSMAPGHVADFVLDDLRRYSVD 82
Cdd:cd01166 1 DVVTIGEVMVDL------SPPGGGRLEQ-ADSFRKffGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 83 LRYTVfqTTGSVPIATVII-NEASGSRTILYY--DRSLPDVSATDFEKVDLTQFKWIHIEG----RNASEQVKMLQRIda 155
Cdd:cd01166 74 TSHVR--VDPGRPTGLYFLeIGAGGERRVLYYraGSAASRLTPEDLDEAALAGADHLHLSGitlaLSESAREALLEAL-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 156 hntRQPPEQKIRVSVEV---------EKPQEELFQLFGYGDVVFVSK-DVAKHLGFQSAGEALRGLYGRVRKGAVLVCAW 225
Cdd:cd01166 150 ---EAAKARGVTVSFDLnyrpklwsaEEAREALEELLPYVDIVLPSEeEAEALLGDEDPTDAAERALALALGVKAVVVKL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109102319 226 AEEGADALGPDGkLIHSDAFPPPrVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKKCGQQG 293
Cdd:cd01166 227 GAEGALVYTGGG-RVFVPAYPVE-VVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPG 292
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
3-293 |
2.72e-23 |
|
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.
Pssm-ID: 238573 [Multi-domain] Cd Length: 312 Bit Score: 97.30 E-value: 2.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 3 EKQILCVGLVVLDVISLVDKYP------KEDSEIRCLSQRWQR-----------GGNASNSCTVLSLLGAPCAFMGSMAP 65
Cdd:cd01168 1 RYDVLGLGNALVDILAQVDDAFleklglKKGDMILADMEEQEEllaklpvkyiaGGSAANTIRGAAALGGSAAFIGRVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 66 GHVADFVLDDLRRYSVDLRYTV--FQTTGSvpiATVIINEaSGSRTILYYDRSLPDVSATDFEKVDLTQFKWIHIEG--R 141
Cdd:cd01168 81 DKLGDFLLKDLRAAGVDTRYQVqpDGPTGT---CAVLVTP-DAERTMCTYLGAANELSPDDLDWSLLAKAKYLYLEGylL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 142 NASEQVKMLQRIDAHntrqppEQKIRVSV------EVEKPQEELFQLFGYGDVVFVSKDVAKHLGFQSAGE----ALRGL 211
Cdd:cd01168 157 TVPPEAILLAAEHAK------ENGVKIALnlsapfIVQRFKEALLELLPYVDILFGNEEEAEALAEAETTDdleaALKLL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 212 YGRVRKGAVLVCAwaeEGAdALGPDGKLIHSDAFPPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKKCGQ 291
Cdd:cd01168 231 ALRCRIVVITQGA---KGA-VVVEGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQ 306
|
..
gi 109102319 292 QG 293
Cdd:cd01168 307 LG 308
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
6-288 |
2.70e-21 |
|
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238917 [Multi-domain] Cd Length: 279 Bit Score: 91.22 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 6 ILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSMApghvADF----VLDDLRRYSV 81
Cdd:cd01942 2 VAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVG----EDFhgrlYLEELREEGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 82 DLRYTVFQTTGSVPIAtVIINEASGSRTILYY----DRSLPDVSATDFEKVDLtqfkwIHIEGRnaseqvkmlqRIDAHN 157
Cdd:cd01942 78 DTSHVRVVDEDSTGVA-FILTDGDDNQIAYFYpgamDELEPNDEADPDGLADI-----VHLSSG----------PGLIEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 158 TRQPPEQKIRVS-----VEVEKPQEELFQLFGYGDVVFVSKDVAKHLgFQSAGEALRGLYGRVRkgaVLVCAWAEEGADA 232
Cdd:cd01942 142 ARELAAGGITVSfdpgqELPRLSGEELEEILERADILFVNDYEAELL-KERTGLSEAELASGVR---VVVVTLGPKGAIV 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 109102319 233 LGPDGKlIHSDAFPPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKK 288
Cdd:cd01942 218 FEDGEE-VEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLK 272
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
5-293 |
3.91e-17 |
|
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.
Pssm-ID: 238572 [Multi-domain] Cd Length: 295 Bit Score: 79.60 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 5 QILCVGLVVLDVISlvDKYPKEDSEIRCLsqrwqrGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFVLDDLRRYSVDLR 84
Cdd:cd01167 1 KVVCFGEALIDFIP--EGSGAPETFTKAP------GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 85 YTVFQTTGSVPIATVIINeASGSRTILYYDRSLPDVSA-TDFEKVDLTQFKWIH------IEGRNASEQVKMLQRIDAH- 156
Cdd:cd01167 73 GIQFDPAAPTTLAFVTLD-ADGERSFEFYRGPAADLLLdTELNPDLLSEADILHfgsialASEPSRSALLELLEAAKKAg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 157 -------NTRQPPEQKIRVSVEVEKPqeelfqLFGYGDVVFVSKDVAKHL---GFQSAGEALRGLYGRvrkgAVLVCAWA 226
Cdd:cd01167 152 vlisfdpNLRPPLWRDEEEARERIAE------LLELADIVKLSDEELELLfgeEDPEEIAALLLLFGL----KLVLVTRG 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109102319 227 EEGADALGPDGKLIHSDafPPPRVVDTLGAGDTFNASVIFSLSQG-------RSVQEALRFGCQVAGKKCGQQG 293
Cdd:cd01167 222 ADGALLYTKGGVGEVPG--IPVEVVDTTGAGDAFVAGLLAQLLSRgllaldeDELAEALRFANAVGALTCTKAG 293
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
19-293 |
1.46e-16 |
|
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.
Pssm-ID: 238915 [Multi-domain] Cd Length: 264 Bit Score: 77.78 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 19 LVDKYPKEDseirclsqRWQRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFVLDDLRRYSVDLRYtVFQTTGSVPIAT 98
Cdd:cd01940 9 VVDKYLHLG--------KMYPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISH-CRVKEGENAVAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 99 VIINEasGSRTILYYD-----RSLPDvsATDFEKvdLTQFKWIHIegrNASEQVKMLQRidahNTRQPPEQKIRVSVEVE 173
Cdd:cd01940 80 VELVD--GDRIFGLSNkggvaREHPF--EADLEY--LSQFDLVHT---GIYSHEGHLEK----ALQALVGAGALISFDFS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 174 -KPQEELFQL-FGYGDVVFVSkdvAKHLGFQSAGEALRGLYGRvrkGAVLVCAwaeegadALGPDGKLIHSDAF---PPP 248
Cdd:cd01940 147 dRWDDDYLQLvCPYVDFAFFS---ASDLSDEEVKAKLKEAVSR---GAKLVIV-------TRGEDGAIAYDGAVfysVAP 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 109102319 249 R---VVDTLGAGDTFNASVIFSLSQGR-SVQEALRFGCQVAGKKCGQQG 293
Cdd:cd01940 214 RpveVVDTLGAGDSFIAGFLLSLLAGGtAIAEAMRQGAQFAAKTCGHEG 262
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
6-286 |
1.11e-12 |
|
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.
Pssm-ID: 238579 [Multi-domain] Cd Length: 292 Bit Score: 66.80 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 6 ILCVGLVVLDVISLVDKYPK-------EDSEIRClsqrwqrGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFVLDDLRR 78
Cdd:cd01174 2 VVVVGSINVDLVTRVDRLPKpgetvlgSSFETGP-------GGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 79 YSVDLRYtVFQTTGsVPIATVIIN-EASGSRTILYY-------DRSLPDVSATDFEKVD--LTQFKwIHIEgrnASEQVk 148
Cdd:cd01174 75 EGIDVSY-VEVVVG-APTGTAVITvDESGENRIVVVpgangelTPADVDAALELIAAADvlLLQLE-IPLE---TVLAA- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 149 mLQRIDAHNTR--------QPPEQKIRVSVEVEKPQE-ELFQLFGygdvvfvskdvAKHLGFQSAGEALRGLYGRVRKGA 219
Cdd:cd01174 148 -LRAARRAGVTvilnpapaRPLPAELLALVDILVPNEtEAALLTG-----------IEVTDEEDAEKAARLLLAKGVKNV 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109102319 220 VLvcawaeegadALGPDGKLIHSD----AFPPPRV--VDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAG 286
Cdd:cd01174 216 IV----------TLGAKGALLASGgeveHVPAFKVkaVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAA 278
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
10-285 |
1.68e-11 |
|
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose catabolism. The rbsK gene encoding ribokinase typically is found with ribose transport genes. Ribokinase belongs to the carbohydrate kinase pfkB family (pfam00294). In the wide gulf between the current trusted (360 bit) and noise (100 bit) cutoffs are a number of sequences, few of which are clustered with predicted ribose transport genes but many of which are currently annotated as if having ribokinase activity. Most likely some have this function and others do not. [Energy metabolism, Sugars]
Pssm-ID: 274000 [Multi-domain] Cd Length: 293 Bit Score: 63.39 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 10 GLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFVLDDLRRYSVDLRYTVF- 88
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 89 --QTTGSVPI--------ATVIINEASGSRTILYYDRSLPDVSATDFEkvdLTQFKwIHIEGrnASEQVKMLQRID---- 154
Cdd:TIGR02152 81 kdTPTGTAFItvddtgenRIVVVAGANAELTPEDIDAAEALIAESDIV---LLQLE-IPLET--VLEAAKIAKKHGvkvi 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 155 ---AHNTRQPPEQKIRVsVEVEKPQE-ELFQLFGygdvVFVSKdvakhlgFQSAGEALRGLYGRVRKGAVLvcawaeega 230
Cdd:TIGR02152 155 lnpAPAIKDLDDELLSL-VDIITPNEtEAEILTG----IEVTD-------EEDAEKAAEKLLEKGVKNVII--------- 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109102319 231 dALGPDGKLIHSDA----FPPPRV--VDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVA 285
Cdd:TIGR02152 214 -TLGSKGALLVSKDesklIPAFKVkaVDTTAAGDTFNGAFAVALAEGKSLEDAIRFANAAA 273
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
6-293 |
4.06e-10 |
|
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238922 [Multi-domain] Cd Length: 265 Bit Score: 59.35 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 6 ILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFVLDDLRrySVDLRY 85
Cdd:cd01947 2 IAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELE--SGGDKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 86 TVFQTTGSVPIATVIInEASGSRTILYYDRSLPDvsatDFEKVDLTQFKWIHIegrNASEQVKMLQRIDAHNTRQPPEQK 165
Cdd:cd01947 80 TVAWRDKPTRKTLSFI-DPNGERTITVPGERLED----DLKWPILDEGDGVFI---TAAAVDKEAIRKCRETKLVILQVT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 166 IRVSVEVEKPQEELFqlfgygDVVFVSKDVAKHLGFQSAgEALRGLygrvrkgAVLVCAWAEEGAdALGPDGKLIHSDAF 245
Cdd:cd01947 152 PRVRVDELNQALIPL------DILIGSRLDPGELVVAEK-IAGPFP-------RYLIVTEGELGA-ILYPGGRYNHVPAK 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 109102319 246 PPPrVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKKCGQQG 293
Cdd:cd01947 217 KAK-VPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFG 263
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
14-281 |
1.22e-09 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 58.22 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 14 LDVISLVDKyPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAP---CAFMGsmapGHVADFVLDDLRRYSVDLRYtvFQT 90
Cdd:COG1105 10 LDRTYEVDE-LEPGEVNRASEVRLDPGGKGINVARVLKALGVDvtaLGFLG----GFTGEFIEELLDEEGIPTDF--VPI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 91 TGSVPIATVIINEASGSRTILYyDRSlPDVSATDFEKV------DLTQFKWIHIEG---RNASEQ--VKMLQRIDAHNTR 159
Cdd:COG1105 83 EGETRINIKIVDPSDGTETEIN-EPG-PEISEEELEALlerleeLLKEGDWVVLSGslpPGVPPDfyAELIRLARARGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 160 -------QPPEQKIRVSVEVEKP-QEELFQLFGY-----GDVVfvskdvakhlgfqsagEALRGLygrVRKGAVLVCAwa 226
Cdd:COG1105 161 vvldtsgEALKAALEAGPDLIKPnLEELEELLGRpletlEDII----------------AAAREL---LERGAENVVV-- 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109102319 227 eegadALGPDG-------KLIHSDAfPPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFG 281
Cdd:COG1105 220 -----SLGADGallvtedGVYRAKP-PKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLA 275
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
3-285 |
9.07e-09 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 55.51 E-value: 9.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 3 EKQILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSMapGHVADFV--LDDLRRYS 80
Cdd:PTZ00292 15 EPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMV--GTDGFGSdtIKNFKRNG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 81 VDLRYTVFQTTGSVPIATVIINEASGSRTIL-------YYDRSLPDVSATDFE---KVDLTQFKwIHIEGR-NASEQVKM 149
Cdd:PTZ00292 93 VNTSFVSRTENSSTGLAMIFVDTKTGNNEIViipgannALTPQMVDAQTDNIQnicKYLICQNE-IPLETTlDALKEAKE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 150 LQRIDAHNTRQPPEQkirVSVEVEKPqeelfqLFGYGDVVFVSKDVAKhlgfQSAGEALRGLYGRVRKGAVLVCAWAEEG 229
Cdd:PTZ00292 172 RGCYTVFNPAPAPKL---AEVEIIKP------FLKYVSLFCVNEVEAA----LITGMEVTDTESAFKASKELQQLGVENV 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109102319 230 ADALGPDGKLIHSDAFPPP-------RVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVA 285
Cdd:PTZ00292 239 IITLGANGCLIVEKENEPVhvpgkrvKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIA 301
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
6-286 |
1.93e-08 |
|
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238919 [Multi-domain] Cd Length: 289 Bit Score: 54.35 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 6 ILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGnASNSCTVLSLLGAPCAFMGSMAPGHVADFVLDDLRRYSVDLRY 85
Cdd:cd01944 2 VLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEILL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 86 TVFQTTGSVPIATVIinEASGSRTILYYDRSLPDVSATDFEKVDLTQFKWIHIEG-----RNASEQVkMLQRIDAHNTRQ 160
Cdd:cd01944 81 PPRGGDDGGCLVALV--EPDGERSFISISGAEQDWSTEWFATLTVAPYDYVYLSGytlasENASKVI-LLEWLEALPAGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 161 P----PEQKIRvsvevEKPQEELFQLFGYGDVVFVSKDVAKHL---GFQSAGEALRGLYGRVRkgAVLVCAWAEEGADAL 233
Cdd:cd01944 158 TlvfdPGPRIS-----DIPDTILQALMAKRPIWSCNREEAAIFaerGDPAAEASALRIYAKTA--APVVVRLGSNGAWIR 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 109102319 234 GPDGKLIHSDAFPPpRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAG 286
Cdd:cd01944 231 LPDGNTHIIPGFKV-KAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAA 282
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
31-281 |
2.15e-08 |
|
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.
Pssm-ID: 238570 [Multi-domain] Cd Length: 289 Bit Score: 54.46 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 31 RCLSQRWQRGG---NASNsctVLSLLGAPCAFMGsMAPGHVADFVLDDLRRYSVDLRYtvFQTTGSVPIaTVIINEASGS 107
Cdd:cd01164 27 RVSSTRKDAGGkgiNVAR---VLKDLGVEVTALG-FLGGFTGDFFEALLKEEGIPDDF--VEVAGETRI-NVKIKEEDGT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 108 RTILyyDRSLPDVSATDFEKVdLTQFK-------WIHIEG---RNASEQ--VKMLQRIDAHNTR-------QPPEQKIRV 168
Cdd:cd01164 100 ETEI--NEPGPEISEEELEAL-LEKLKallkkgdIVVLSGslpPGVPADfyAELVRLAREKGARvildtsgEALLAALAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 169 SVEVEKP-QEELFQLFGygdvvfvskdvAKHLGFQSAGEALRGLygrVRKGA--VLVcawaeegadALGPDGKL-IHSDA 244
Cdd:cd01164 177 KPFLIKPnREELEELFG-----------RPLGDEEDVIAAARKL---IERGAenVLV---------SLGADGALlVTKDG 233
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 109102319 245 F-----PPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFG 281
Cdd:cd01164 234 VyraspPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLA 275
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
20-293 |
3.42e-08 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 53.59 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 20 VDKYPKEDseirclsqRWQRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFVLDDLRRYSVDLRYTvfqTTGSVPIATV 99
Cdd:PRK09813 11 VDIYPQLG--------KAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHV---HTKHGVTAQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 100 IINEASGSRtIL--YYDRSLPDVSATDFEKVDLTQFKWIH--IEGrNASEQvkmLQRIDAHNTRqppeqkirVSVE-VEK 174
Cdd:PRK09813 80 QVELHDNDR-VFgdYTEGVMADFALSEEDYAWLAQYDIVHaaIWG-HAEDA---FPQLHAAGKL--------TAFDfSDK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 175 PQEELFQ-LFGYGDVVFVSKDvakhlgfQSAGEALRGLYGRVRKGA-VLVCAWAEEGAdaLGPDGKLIHSDAFPPPRVVD 252
Cdd:PRK09813 147 WDSPLWQtLVPHLDYAFASAP-------QEDEFLRLKMKAIVARGAgVVIVTLGENGS--IAWDGAQFWRQAPEPVTVVD 217
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 109102319 253 TLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKKCGQQG 293
Cdd:PRK09813 218 TMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
5-291 |
2.55e-07 |
|
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238916 [Multi-domain] Cd Length: 288 Bit Score: 51.16 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 5 QILCVGLVVLDVISLVDK-YPKEDS---EIRCLSqrwqrGGNASNSCTVLSLLGAPCAFM---GSMAPGHVadfVLDDLR 77
Cdd:cd01941 1 EIVVIGAANIDLRGKVSGsLVPGTSnpgHVKQSP-----GGVGRNIAENLARLGVSVALLsavGDDSEGES---ILEESE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 78 RYSVDLRYTVF--QTTGSVpiaTVIINE------------ASGSRTILYYDRSLPDVSATDFEKVDLtqfkwihiegrNA 143
Cdd:cd01941 73 KAGLNVRGIVFegRSTASY---TAILDKdgdlvvaladmdIYELLTPDFLRKIREALKEAKPIVVDA-----------NL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 144 SEQVkmLQRIdahnTRQPPEQKIRVSVE---VEKPQEeLFQLFGYGDVVFVSKDVAKHLgfqsAGEALRGLYGRVRKGAV 220
Cdd:cd01941 139 PEEA--LEYL----LALAAKHGVPVAFEptsAPKLKK-LFYLLHAIDLLTPNRAELEAL----AGALIENNEDENKAAKI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 221 LVCAWAEEGADALGPDGKLIHSDA-------FPPP---RVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGcQVAGKKCG 290
Cdd:cd01941 208 LLLPGIKNVIVTLGAKGVLLSSREggvetklFPAPqpeTVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFA-QAAAALTL 286
|
.
gi 109102319 291 Q 291
Cdd:cd01941 287 E 287
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
6-268 |
3.30e-07 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 49.79 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 6 ILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGsmapghvadfvlddlrrysvdlry 85
Cdd:cd00287 2 VLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG------------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 86 tvfqttgsvpiatviineasgsrtilyydrslpdvsatdfekvdltqFKWIHIEGRNASEQVkMLQRIDAHNTRQPPeqk 165
Cdd:cd00287 58 -----------------------------------------------ADAVVISGLSPAPEA-VLDALEEARRRGVP--- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 166 irVSVE-----VEKPQEELFQLFGYGDVVFVSKDVAKHLGFQ---SAGEALRGLYGRVRKGAVLVCAWAEEGADALGPDG 237
Cdd:cd00287 87 --VVLDpgpraVRLDGEELEKLLPGVDILTPNEEEAEALTGRrdlEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRG 164
|
250 260 270
....*....|....*....|....*....|.
gi 109102319 238 KLIHSDAFPPPRVVDTLGAGDTFNASVIFSL 268
Cdd:cd00287 165 GTEVHVPAFPVKVVDTTGAGDAFLAALAAGL 195
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
204-293 |
4.98e-06 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 47.11 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 204 AGEALRGLYGRvrkGAVLVCAwAEEGADALGPDGKLIHSDAFPPPrVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQ 283
Cdd:COG2870 226 AAAELLERLGL---EALLVTR-GEEGMTLFDADGPPHHLPAQARE-VFDVTGAGDTVIATLALALAAGASLEEAAELANL 300
|
90
....*....|
gi 109102319 284 VAGKKCGQQG 293
Cdd:COG2870 301 AAGIVVGKLG 310
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
237-281 |
1.11e-05 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 46.02 E-value: 1.11e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 109102319 237 GKLIhsdafPPPRV--VDTLGAGDTFNASVIFSLSQGRSVQEALRFG 281
Cdd:PRK11142 235 GQRV-----PGFRVqaVDTIAAGDTFNGALVTALLEGKPLPEAIRFA 276
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
191-293 |
1.12e-04 |
|
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.
Pssm-ID: 238577 [Multi-domain] Cd Length: 304 Bit Score: 42.93 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 191 VSKDVAKHLGFQSAGEALRGLYGRvrkGAVLVcAWAEEGADALGPDGKLIHSDAFPPPrVVDTLGAGDTFNASVIFSLSQ 270
Cdd:cd01172 196 LGDEINDDDELEAAGEKLLELLNL---EALLV-TLGEEGMTLFERDGEVQHIPALAKE-VYDVTGAGDTVIATLALALAA 270
|
90 100
....*....|....*....|...
gi 109102319 271 GRSVQEALRFGCQVAGKKCGQQG 293
Cdd:cd01172 271 GADLEEAAFLANAAAGVVVGKVG 293
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
171-288 |
1.65e-04 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 42.39 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 171 EVEKPQEELFQLFGYGDVVFVSKDVAKHLgfQSAGEALRGLygRVRKGAVLVCAWAEEGADALgpDGKLIHSDAFPPPRV 250
Cdd:cd01937 141 RANQEKLIKCVILKLHDVLKLSRVEAEVI--STPTELARLI--KETGVKEIIVTDGEEGGYIF--DGNGKYTIPASKKDV 214
|
90 100 110
....*....|....*....|....*....|....*...
gi 109102319 251 VDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKK 288
Cdd:cd01937 215 VDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAKF 252
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
227-285 |
3.87e-03 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 38.52 E-value: 3.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 227 EEGADALGPDGKLIhsdAFPPP-RVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVA 285
Cdd:PRK09513 226 AEGALWVNASGEWI---AKPPAcDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVS 282
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
24-282 |
6.92e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 37.85 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 24 PKEDSEIRCLSqrwqrGGNASNSCTVLSL-LGAPCAFMGSMAPGHVADFVLDDLRRYSVDLryTVFQTTGSVPIATVIIN 102
Cdd:PLN02379 75 PDDLSPIKTMA-----GGSVANTIRGLSAgFGVSTGIIGACGDDEQGKLFVSNMGFSGVDL--SRLRAKKGPTAQCVCLV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 103 EASGSRTILYYDRSLPDVSATDFEKVDLTQFKWIHIegRNASEQVKMLQRIdAHNTRQppeQKIRVSVE------VEKPQ 176
Cdd:PLN02379 148 DALGNRTMRPCLSSAVKLQADELTKEDFKGSKWLVL--RYGFYNLEVIEAA-IRLAKQ---EGLSVSLDlasfemVRNFR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109102319 177 EELFQLFGYGDV--VFVSKDVAKHL--GFQSAG--EALRGLYGRvrkgavlvCAWAeegADALGPDG-------KLIHSD 243
Cdd:PLN02379 222 SPLLQLLESGKIdlCFANEDEARELlrGEQESDpeAALEFLAKY--------CNWA---VVTLGSKGciarhgkEVVRVP 290
|
250 260 270
....*....|....*....|....*....|....*....
gi 109102319 244 AFPPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGC 282
Cdd:PLN02379 291 AIGETNAVDATGAGDLFASGFLYGLIKGLSLEECCKVGA 329
|
|
| |
