|
Name |
Accession |
Description |
Interval |
E-value |
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
5-295 |
1.69e-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: 1.69e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 5 QILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFLVADFRRRGVDVS 84
Cdd:cd01939 1 AVLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 85 QVaWQSKGDTPSSCCIINNSNGNRTIVLHDTSLPDVSATDFEKVDLTQFKWIHIEGRNASEQVKMLQRIDAHNTRQPpEQ 164
Cdd:cd01939 81 HC-YRKDIDEPASSYIIRSRAGGRTTIVNDNNLPEVTYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNNRRP-EI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 165 KIRVSVEVEKPREELFQLFGYGDVVFVSKDVAKHLGFQSAEEALRGLYGRVRKGAVLVCAWAEEGADALGPDGKLLHSDA 244
Cdd:cd01939 159 RITISVEVEKPREELLELAAYCDVVFVSKDWAQSRGYKSPEECLRGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSPA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 816380035 245 FPPPRVVDTLGAGDTFNASVIFSLSQG-RSVQEALRFGCQVAGKKCGLQGFD 295
Cdd:cd01939 239 HKPIRVVDTLGAGDTFNAAVIYALNKGpDDLSEALDFGNRVASQKCTGVGFD 290
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
5-289 |
4.10e-45 |
|
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: 154.66 E-value: 4.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 5 QILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFLVADFRRRGVDVS 84
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 85 QVAwQSKGDTPSSCCIINNSNGNRTIVLHDTSLPDVSATDFEKVDLTQFKWIHIEG------RNASEQVKMLQRIDAHNt 158
Cdd:COG0524 81 GVR-RDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEALLAGADILHLGGitlasePPREALLAALEAARAAG- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 159 rqppeqkIRVSVEV-------EKPREELFQLFGYGDVVFVSKDVAKHL-GFQSAEEALRGLYGRVRKGAVLVCawAEEGA 230
Cdd:COG0524 159 -------VPVSLDPnyrpalwEPARELLRELLALVDILFPNEEEAELLtGETDPEEAAAALLARGVKLVVVTL--GAEGA 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 816380035 231 DALGpDGKLLHSDAFpPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKKC 289
Cdd:COG0524 230 LLYT-GGEVVHVPAF-PVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVV 286
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
5-296 |
2.12e-31 |
|
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: 118.17 E-value: 2.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 5 QILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFLVADFRRRGVDVS 84
Cdd:cd01945 1 RVLGVGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 85 QVawQSKGDTPSSCCIINNSNGNRTIVLHDTSLPDVSATDFEKVDLTQFKWIHIEGRNASEQVKMLQRIDAHNTRQPpeq 164
Cdd:cd01945 81 FI--VVAPGARSPISSITDITGDRATISITAIDTQAAPDSLPDAILGGADAVLVDGRQPEAALHLAQEARARGIPIP--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 165 kirVSVEVEKPR--EELFQLfgyGDVVFVSKDVAKHLGFQSAEEALRGLYGRVRKgAVLVCAwAEEGADALGPDGKLLHS 242
Cdd:cd01945 156 ---LDLDGGGLRvlEELLPL---ADHAICSENFLRPNTGSADDEALELLASLGIP-FVAVTL-GEAGCLWLERDGELFHV 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 816380035 243 DAFpPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKKCglQGFDG 296
Cdd:cd01945 228 PAF-PVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKC--RGLGG 278
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
6-293 |
8.72e-29 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 111.67 E-value: 8.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 6 ILCVGLVVLDVISLVDKYPKEDSEIRCLSQRwqRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFLVADFRRRGVDVSQ 85
Cdd:pfam00294 2 VVVIGEANIDLIGNVEGLPGELVRVSTVEKG--PGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 86 VawQSKGDTPSSCCII-NNSNGNRTIVLHDTSLPDVSATDFEKV--DLTQFKWIHIEG------RNASEQvKMLQRIDAH 156
Cdd:pfam00294 80 V--VIDEDTRTGTALIeVDGDGERTIVFNRGAAADLTPEELEENedLLENADLLYISGslplglPEATLE-ELIEAAKNG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 157 NTRQPpeqkiRVSVEVEKPREELFQLFGYGDVVFVSKDVAKHLGFQ---SAEEALRGLYGRVRKGA-VLVCAWAEEGADA 232
Cdd:pfam00294 157 GTFDP-----NLLDPLGAAREALLELLPLADLLKPNEEELEALTGAkldDIEEALAALHKLLAKGIkTVIVTLGADGALV 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 816380035 233 LGPDGKLLHsDAFPPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKKCGLQG 293
Cdd:pfam00294 232 VEGDGEVHV-PAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSG 291
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
5-293 |
1.20e-24 |
|
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: 100.34 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 5 QILCVGLVVLDVislvdkYPKEDSEIRClSQRWQR--GGNASNSCTVLSLLGAPCAFMGSMAPGHVADFLVADFRRRGVD 82
Cdd:cd01166 1 DVVTIGEVMVDL------SPPGGGRLEQ-ADSFRKffGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 83 VSQVAwQSKGDTPSSCCIINNSNGNRTiVLHD---TSLPDVSATDFEKVDLTQFKWIHIEG----RNASEQVKMLQRIda 155
Cdd:cd01166 74 TSHVR-VDPGRPTGLYFLEIGAGGERR-VLYYragSAASRLTPEDLDEAALAGADHLHLSGitlaLSESAREALLEAL-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 156 hntRQPPEQKIRVSVEV---------EKPREELFQLFGYGDVVFVSK-DVAKHLGFQSAEEALRGLYGRVRKGAVLVCAW 225
Cdd:cd01166 150 ---EAAKARGVTVSFDLnyrpklwsaEEAREALEELLPYVDIVLPSEeEAEALLGDEDPTDAAERALALALGVKAVVVKL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 816380035 226 AEEGADALGPDGkLLHSDAFPPPrVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKKCGLQG 293
Cdd:cd01166 227 GAEGALVYTGGG-RVFVPAYPVE-VVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPG 292
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
3-293 |
2.39e-24 |
|
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: 100.00 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 3 EKQILCVGLVVLDVISLVDKYP------KEDSEIRCLSQRWQR-----------GGNASNSCTVLSLLGAPCAFMGSMAP 65
Cdd:cd01168 1 RYDVLGLGNALVDILAQVDDAFleklglKKGDMILADMEEQEEllaklpvkyiaGGSAANTIRGAAALGGSAAFIGRVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 66 GHVADFLVADFRRRGVDVSqvaWQSKGDTPSSCCIIN-NSNGNRTIVLHDTSLPDVSATDFEKVDLTQFKWIHIEG--RN 142
Cdd:cd01168 81 DKLGDFLLKDLRAAGVDTR---YQVQPDGPTGTCAVLvTPDAERTMCTYLGAANELSPDDLDWSLLAKAKYLYLEGylLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 143 ASEQVKMLQRIDAHntrqppEQKIRVSV------EVEKPREELFQLFGYGDVVFVSKDVAKHLGFQ----SAEEALRGLY 212
Cdd:cd01168 158 VPPEAILLAAEHAK------ENGVKIALnlsapfIVQRFKEALLELLPYVDILFGNEEEAEALAEAettdDLEAALKLLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 213 GRVRKGAVLVCAwaeEGAdALGPDGKLLHSDAFPPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKKCGLQ 292
Cdd:cd01168 232 LRCRIVVITQGA---KGA-VVVEGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQL 307
|
.
gi 816380035 293 G 293
Cdd:cd01168 308 G 308
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
6-288 |
1.87e-23 |
|
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: 97.00 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 6 ILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSMApghvADF----LVADFRRRGV 81
Cdd:cd01942 2 VAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVG----EDFhgrlYLEELREEGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 82 DVSQVawqSKGDTPSS--CCIINNSNGNRTIVLH----DTSLPDVSATDFEKVDLtqfkwIHIEGRnaseqvkmlqRIDA 155
Cdd:cd01942 78 DTSHV---RVVDEDSTgvAFILTDGDDNQIAYFYpgamDELEPNDEADPDGLADI-----VHLSSG----------PGLI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 156 HNTRQPPEQKIRVS-----VEVEKPREELFQLFGYGDVVFVSKDVAKHLgfqsAEEALRGLYGRVRKGAVLVCAWAEEGA 230
Cdd:cd01942 140 ELARELAAGGITVSfdpgqELPRLSGEELEEILERADILFVNDYEAELL----KERTGLSEAELASGVRVVVVTLGPKGA 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 816380035 231 DALGPDGKLLHsDAFPPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKK 288
Cdd:cd01942 216 IVFEDGEEVEV-PAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLK 272
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
5-293 |
5.96e-18 |
|
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: 81.91 E-value: 5.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 5 QILCVGLVVLDVISlvDKYPKEDSEIRCLsqrwqrGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFLVADFRRRGVDVS 84
Cdd:cd01167 1 KVVCFGEALIDFIP--EGSGAPETFTKAP------GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 85 QVawQSKGDTPSSCCIIN-NSNGNRTIVLHDTSLPDVSA-TDFEKVDLTQFKWIH------IEGRNASEQVKMLQRIDAH 156
Cdd:cd01167 73 GI--QFDPAAPTTLAFVTlDADGERSFEFYRGPAADLLLdTELNPDLLSEADILHfgsialASEPSRSALLELLEAAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 157 --------NTRQPPEQKIrvsvevEKPREELFQLFGYGDVVFVSKDVAKHLGFQSAEEALRGLYGRVRKGAVLVcawaee 228
Cdd:cd01167 151 gvlisfdpNLRPPLWRDE------EEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLV------ 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 816380035 229 gadALGPDGKLLHSDAF------PPPRVVDTLGAGDTFNASVIFSLSQG-------RSVQEALRFGCQVAGKKCGLQG 293
Cdd:cd01167 219 ---TRGADGALLYTKGGvgevpgIPVEVVDTTGAGDAFVAGLLAQLLSRgllaldeDELAEALRFANAVGALTCTKAG 293
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
19-293 |
1.66e-17 |
|
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: 80.09 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 19 LVDKYPKEDseirclsqRWQRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFLVADFRRRGVDVSQVAwQSKGDTpsSC 98
Cdd:cd01940 9 VVDKYLHLG--------KMYPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCR-VKEGEN--AV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 99 CIINNSNGNRTIVLHDTS-----LPDvsATDFEKvdLTQFKWIHIegrNASEQVKMLQRidahNTRQPPEQKIRVSVEVE 173
Cdd:cd01940 78 ADVELVDGDRIFGLSNKGgvareHPF--EADLEY--LSQFDLVHT---GIYSHEGHLEK----ALQALVGAGALISFDFS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 174 KPR--EELFQLFGYGDVVFVSkdvAKHLGFQSAEEALRGLYGRvrkGAVLVCAwaeegadALGPDGKLLHSDAF---PPP 248
Cdd:cd01940 147 DRWddDYLQLVCPYVDFAFFS---ASDLSDEEVKAKLKEAVSR---GAKLVIV-------TRGEDGAIAYDGAVfysVAP 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 816380035 249 R---VVDTLGAGDTFNASVIFSLSQGR-SVQEALRFGCQVAGKKCGLQG 293
Cdd:cd01940 214 RpveVVDTLGAGDSFIAGFLLSLLAGGtAIAEAMRQGAQFAAKTCGHEG 262
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
6-286 |
6.11e-14 |
|
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: 70.66 E-value: 6.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 6 ILCVGLVVLDVISLVDKYPK-------EDSEIRClsqrwqrGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFLVADFRR 78
Cdd:cd01174 2 VVVVGSINVDLVTRVDRLPKpgetvlgSSFETGP-------GGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 79 RGVDVSQVawQSKGDTPSSCCIIN-NSNGNRTIVLH-------DTSLPDVSATDFEKVD--LTQFKwIHIEgrnASEQVk 148
Cdd:cd01174 75 EGIDVSYV--EVVVGAPTGTAVITvDESGENRIVVVpgangelTPADVDAALELIAAADvlLLQLE-IPLE---TVLAA- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 149 mLQRIDAHNTR--------QPPEQKIRVSVEVEKPRE-ELFQLFGygdvvfvskdvAKHLGFQSAEEALRGLYGRVRKGA 219
Cdd:cd01174 148 -LRAARRAGVTvilnpapaRPLPAELLALVDILVPNEtEAALLTG-----------IEVTDEEDAEKAARLLLAKGVKNV 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 816380035 220 VLvcawaeegadALGPDGKLLHSD----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 |
8.26e-14 |
|
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: 70.32 E-value: 8.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 10 GLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFLVADFRRRGVDVSQVawQ 89
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYV--G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 90 SKGDTPS-SCCIINNSNGNRTIVL----HDTSLPDV---SATDFEKVDLT--QFKwIHIEGrnASEQVKMLQRID----- 154
Cdd:TIGR02152 79 TVKDTPTgTAFITVDDTGENRIVVvagaNAELTPEDidaAEALIAESDIVllQLE-IPLET--VLEAAKIAKKHGvkvil 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 155 --AHNTRQPPEQKIRVsVEVEKPRE-ELFQLFGygdvVFVSKdvakhlgFQSAEEALRGLYGRVRKGAVLvcawaeegad 231
Cdd:TIGR02152 156 npAPAIKDLDDELLSL-VDIITPNEtEAEILTG----IEVTD-------EEDAEKAAEKLLEKGVKNVII---------- 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 232 ALGPDGKLLHSDA----FPPPRV--VDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVA 285
Cdd:TIGR02152 214 TLGSKGALLVSKDesklIPAFKVkaVDTTAAGDTFNGAFAVALAEGKSLEDAIRFANAAA 273
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
3-285 |
1.09e-11 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 64.37 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 3 EKQILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFLVADFRRRGVD 82
Cdd:PTZ00292 15 EPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 83 VSQVAWQSKGDTPSSCCIINNSNGNRTIVLHDTS-------LPDVSATDFE---KVDLTQFKwIHIEG-----RNASEQ- 146
Cdd:PTZ00292 95 TSFVSRTENSSTGLAMIFVDTKTGNNEIVIIPGAnnaltpqMVDAQTDNIQnicKYLICQNE-IPLETtldalKEAKERg 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 147 -VKMLQRIDAHNTRQPPEQK-IRVSVEVEKPRE-ELFQLFGyGDVV--FVSKDVAKHLGFQSAEEALRGLYGrvrKGavl 221
Cdd:PTZ00292 174 cYTVFNPAPAPKLAEVEIIKpFLKYVSLFCVNEvEAALITG-MEVTdtESAFKASKELQQLGVENVIITLGA---NG--- 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 816380035 222 vCAWAEEGADALGPDGKLLhsdafpppRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVA 285
Cdd:PTZ00292 247 -CLIVEKENEPVHVPGKRV--------KAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIA 301
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
6-286 |
1.92e-11 |
|
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: 63.21 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 6 ILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGnASNSCTVLSLLGAPCAFMGSMAPGHVADFLVADFRRRGVDVSQ 85
Cdd:cd01944 2 VLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEILL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 86 vawQSKGDTPSSCCI-INNSNGNRTIVLHDTSLPDVSATDFEKVDLTQFKWIHIEG-----RNASEQ--VKMLQRIDAhn 157
Cdd:cd01944 81 ---PPRGGDDGGCLVaLVEPDGERSFISISGAEQDWSTEWFATLTVAPYDYVYLSGytlasENASKVilLEWLEALPA-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 158 tRQP----PEQKIRvsvevEKPREELFQLFGYGDVVFVSKDVAKHL---GFQSAEEALRGLYGRVRkgAVLVCAWAEEGA 230
Cdd:cd01944 156 -GTTlvfdPGPRIS-----DIPDTILQALMAKRPIWSCNREEAAIFaerGDPAAEASALRIYAKTA--APVVVRLGSNGA 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 816380035 231 DALGPDGKLLHSDAFPPpRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAG 286
Cdd:cd01944 228 WIRLPDGNTHIIPGFKV-KAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAA 282
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
20-293 |
2.54e-11 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 62.45 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 20 VDKYPKEDseirclsqRWQRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFLVADFRRRGVDVSQVawqSKGDTPSSCC 99
Cdd:PRK09813 11 VDIYPQLG--------KAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHV---HTKHGVTAQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 100 IINNSNGNRtiVLHDTS---LPDVSATDFEKVDLTQFKWIH--IEGrNASEQvkmLQRIDAHNTRqppeqkirVSVE-VE 173
Cdd:PRK09813 80 QVELHDNDR--VFGDYTegvMADFALSEEDYAWLAQYDIVHaaIWG-HAEDA---FPQLHAAGKL--------TAFDfSD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 174 KPREELFQ-LFGYGDVVFVSKDvakhlgfQSAEEALRGLYGRVRKGA-VLVCAWAEEGAdaLGPDGKLLHSDAFPPPRVV 251
Cdd:PRK09813 146 KWDSPLWQtLVPHLDYAFASAP-------QEDEFLRLKMKAIVARGAgVVIVTLGENGS--IAWDGAQFWRQAPEPVTVV 216
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 816380035 252 DTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKKCGLQG 293
Cdd:PRK09813 217 DTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
31-281 |
5.68e-11 |
|
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: 61.78 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 31 RCLSQRWQRGG---NASNsctVLSLLGAPCAFMGsMAPGHVADFLVADFRRRGVDVSQVawQSKGDTPSSCCIINNSNgn 107
Cdd:cd01164 27 RVSSTRKDAGGkgiNVAR---VLKDLGVEVTALG-FLGGFTGDFFEALLKEEGIPDDFV--EVAGETRINVKIKEEDG-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 108 rtivlHDTSL----PDVSATDFEKVdLTQFK-------WIHIEG---RNASEQ--VKMLQRIDAHNTR-------QPPEQ 164
Cdd:cd01164 99 -----TETEInepgPEISEEELEAL-LEKLKallkkgdIVVLSGslpPGVPADfyAELVRLAREKGARvildtsgEALLA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 165 KIRVSVEVEKP-REELFQLFGygdvvfvskdvAKHLGFQSAEEALRGLygrVRKGA--VLVcawaeegadALGPDGKLL- 240
Cdd:cd01164 173 ALAAKPFLIKPnREELEELFG-----------RPLGDEEDVIAAARKL---IERGAenVLV---------SLGADGALLv 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 816380035 241 HSDAF-----PPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFG 281
Cdd:cd01164 230 TKDGVyraspPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLA 275
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
5-288 |
6.24e-11 |
|
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: 61.95 E-value: 6.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 5 QILCVGLVVLDVISLVDK-YPKEDS---EIRCLSqrwqrGGNASNSCTVLSLLGAPCAFM---GSMAPGHVadfLVADFR 77
Cdd:cd01941 1 EIVVIGAANIDLRGKVSGsLVPGTSnpgHVKQSP-----GGVGRNIAENLARLGVSVALLsavGDDSEGES---ILEESE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 78 RRGVDVSQVawQSKGDTPSSCCIINNSNGNRTIVLHDTSLPDVSATDFE---KVDLTQFKWIHIEGrNASEQVkmLQRId 154
Cdd:cd01941 73 KAGLNVRGI--VFEGRSTASYTAILDKDGDLVVALADMDIYELLTPDFLrkiREALKEAKPIVVDA-NLPEEA--LEYL- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 155 ahnTRQPPEQKIRVSVEVEK-PR-EELFQLFGYGDVVFVSKDVAKHLgfqsAEEALRGLYGRVRKGAVLVCAWAEEGADA 232
Cdd:cd01941 147 ---LALAAKHGVPVAFEPTSaPKlKKLFYLLHAIDLLTPNRAELEAL----AGALIENNEDENKAAKILLLPGIKNVIVT 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 816380035 233 LGPDGKLLHSDA-------FPPP---RVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGcQVAGKK 288
Cdd:cd01941 220 LGAKGVLLSSREggvetklFPAPqpeTVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFA-QAAAAL 284
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
14-281 |
1.04e-10 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 61.30 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 14 LDVISLVDKyPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAP---CAFMGsmapGHVADFLVADFRRRGVDVSQVawQS 90
Cdd:COG1105 10 LDRTYEVDE-LEPGEVNRASEVRLDPGGKGINVARVLKALGVDvtaLGFLG----GFTGEFIEELLDEEGIPTDFV--PI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 91 KGDTPSscCI-INNSNGNRTIVLHDTSlPDVSATDFEKV------DLTQFKWIHIEG---RNASEQ--VKMLQRIDAHNT 158
Cdd:COG1105 83 EGETRI--NIkIVDPSDGTETEINEPG-PEISEEELEALlerleeLLKEGDWVVLSGslpPGVPPDfyAELIRLARARGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 159 R-------QPPEQKIRVSVEVEKP-REELFQLFGygdvvfvsKDVAkhlGFQSAEEALRGLygrVRKGAVLVCAwaeega 230
Cdd:COG1105 160 KvvldtsgEALKAALEAGPDLIKPnLEELEELLG--------RPLE---TLEDIIAAAREL---LERGAENVVV------ 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 816380035 231 dALGPDG-------KLLHSDAfPPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFG 281
Cdd:COG1105 220 -SLGADGallvtedGVYRAKP-PKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLA 275
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
6-287 |
3.71e-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: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 6 ILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFLVADFRRRGVDVSq 85
Cdd:cd01947 2 IAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHT- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 86 VAWQSKGdTPSSCCIINNsNGNRTIVLHDTSLPDvsatDFEKVDLTQFKWIHIegrNASEQVKMLQRIDAHNTRQPPEQK 165
Cdd:cd01947 81 VAWRDKP-TRKTLSFIDP-NGERTITVPGERLED----DLKWPILDEGDGVFI---TAAAVDKEAIRKCRETKLVILQVT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 166 IRVSVEVekpREELFQLFgygDVVFVSKDVAKHLGFQSAEeALRGLygrvrkgAVLVCAWAEEGAdALGPDGKLLHSDAF 245
Cdd:cd01947 152 PRVRVDE---LNQALIPL---DILIGSRLDPGELVVAEKI-AGPFP-------RYLIVTEGELGA-ILYPGGRYNHVPAK 216
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 816380035 246 PPPrVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGK 287
Cdd:cd01947 217 KAK-VPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAI 257
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
6-268 |
4.11e-08 |
|
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: 52.48 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 6 ILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGsmapghvadflvadfrrrgvdvsq 85
Cdd:cd00287 2 VLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG------------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 86 vawqskgdtpsscciinnsngnrtivlhdtslpdvsatdfekvdltqFKWIHIEGRNASEQVkMLQRIDAHNTRQPPeqk 165
Cdd:cd00287 58 -----------------------------------------------ADAVVISGLSPAPEA-VLDALEEARRRGVP--- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 166 irVSVE-----VEKPREELFQLFGYGDVVFVSKDVAKHLGFQ---SAEEALRGLYGRVRKGAVLVCAWAEEGADALGPDG 237
Cdd:cd00287 87 --VVLDpgpraVRLDGEELEKLLPGVDILTPNEEEAEALTGRrdlEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRG 164
|
250 260 270
....*....|....*....|....*....|.
gi 816380035 238 KLLHSDAFPPPRVVDTLGAGDTFNASVIFSL 268
Cdd:cd00287 165 GTEVHVPAFPVKVVDTTGAGDAFLAALAAGL 195
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
24-282 |
6.43e-08 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 53.26 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 24 PKEDSEIRCLSqrwqrGGNASNSCTVLSL-LGAPCAFMGSMAPGHVADFLVADFRRRGVDVSQVAwQSKGDTPSSCCIIN 102
Cdd:PLN02379 75 PDDLSPIKTMA-----GGSVANTIRGLSAgFGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSRLR-AKKGPTAQCVCLVD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 103 NSnGNRTIVLHDTSLPDVSATDFEKVDLTQFKWIHIegRNASEQVKMLQRIdAHNTRQppeQKIRVSVE------VEKPR 176
Cdd:PLN02379 149 AL-GNRTMRPCLSSAVKLQADELTKEDFKGSKWLVL--RYGFYNLEVIEAA-IRLAKQ---EGLSVSLDlasfemVRNFR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 177 EELFQLFGYGDV--VFVSKDVAKHL--GFQSA--EEALRGLYGRvrkgavlvCAWAeegADALGPDG-------KLLHSD 243
Cdd:PLN02379 222 SPLLQLLESGKIdlCFANEDEARELlrGEQESdpEAALEFLAKY--------CNWA---VVTLGSKGciarhgkEVVRVP 290
|
250 260 270
....*....|....*....|....*....|....*....
gi 816380035 244 AFPPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGC 282
Cdd:PLN02379 291 AIGETNAVDATGAGDLFASGFLYGLIKGLSLEECCKVGA 329
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
202-286 |
9.14e-06 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 46.34 E-value: 9.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 202 QSAEEALRGLYGRVRKGAVLVCAwAEEGADALGPDGKLLHSDAFPPPrVVDTLGAGDTFNASVIFSLSQGRSVQEALRFG 281
Cdd:COG2870 221 EELVAAAAELLERLGLEALLVTR-GEEGMTLFDADGPPHHLPAQARE-VFDVTGAGDTVIATLALALAAGASLEEAAELA 298
|
....*
gi 816380035 282 CQVAG 286
Cdd:COG2870 299 NLAAG 303
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
5-288 |
1.17e-05 |
|
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: 45.86 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 5 QILCVGLVVLDVIslvdkypkedseIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFlvADFRRrgvdvS 84
Cdd:cd01937 1 KIVIIGHVTIDEI------------VTNGSGVVKPGGPATYASLTLSRLGLTVKLVTKVGRDYPDKW--SDLFD-----N 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 85 QVAWQSKGDTPSSCCIINNSNGNRTIVLHDTSLPDvSATDFEKVDLTQFKwIHIeGRNASEQVKMLQRIDAhntrqppeq 164
Cdd:cd01937 62 GIEVISLLSTETTTFELNYTNEGRTRTLLAKCAAI-PDTESPLSTITAEI-VIL-GPVPEEISPSLFRKFA--------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 165 KIRVSV-----EVEKPREELFQLFGYGDVVFVSKDVAKHLgfQSAEEALRGLygRVRKGAVLVCAWAEEGADALgpDGKL 239
Cdd:cd01937 130 FISLDAqgflrRANQEKLIKCVILKLHDVLKLSRVEAEVI--STPTELARLI--KETGVKEIIVTDGEEGGYIF--DGNG 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 816380035 240 LHSDAFPPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKK 288
Cdd:cd01937 204 KYTIPASKKDVVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAKF 252
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
233-281 |
1.72e-05 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 45.63 E-value: 1.72e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 816380035 233 LGPDGKLLHSDAF----PPPRV--VDTLGAGDTFNASVIFSLSQGRSVQEALRFG 281
Cdd:PRK11142 222 LGSRGVWLSENGEgqrvPGFRVqaVDTIAAGDTFNGALVTALLEGKPLPEAIRFA 276
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
202-290 |
6.86e-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: 40.62 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 202 QSAEEALRGLYGRVRKGAVLVcAWAEEGADALGPDGKLLHSDAFPPPrVVDTLGAGDTFNASVIFSLSQGRSVQEALRFG 281
Cdd:cd01172 204 DELEAAGEKLLELLNLEALLV-TLGEEGMTLFERDGEVQHIPALAKE-VYDVTGAGDTVIATLALALAAGADLEEAAFLA 281
|
....*....
gi 816380035 282 CQVAGKKCG 290
Cdd:cd01172 282 NAAAGVVVG 290
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
172-277 |
2.61e-03 |
|
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238921 [Multi-domain] Cd Length: 277 Bit Score: 38.60 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 172 VEKPREELFQLFGYGDVVFVSKDVAKHLgfqsaeealRGLYGRVrKGAVLVCAWaeeGADAL----GPDGKLLHSD---- 243
Cdd:cd01946 150 ISIKPEKLKKVLAKVDVVIINDGEARQL---------TGAANLV-KAARLILAM---GPKALiikrGEYGALLFTDdgyf 216
|
90 100 110
....*....|....*....|....*....|....*..
gi 816380035 244 ---AFPPPRVVDTLGAGDTFNASVIFSLSQGRSVQEA 277
Cdd:cd01946 217 aapAYPLESVFDPTGAGDTFAGGFIGYLASQKDTSEA 253
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
227-285 |
3.50e-03 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 38.52 E-value: 3.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 227 EEGADALGPDGKLLhsdAFPPP-RVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVA 285
Cdd:PRK09513 226 AEGALWVNASGEWI---AKPPAcDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVS 282
|
|
| RRM3_NGR1_NAM8_like |
cd12346 |
RNA recognition motif 3 (RRM3) found in yeast negative growth regulatory protein NGR1 (RBP1), ... |
177-225 |
3.58e-03 |
|
RNA recognition motif 3 (RRM3) found in yeast negative growth regulatory protein NGR1 (RBP1), yeast protein NAM8 and similar proteins; This subfamily corresponds to the RRM3 of NGR1 and NAM8. NGR1, also termed RNA-binding protein RBP1, is a putative glucose-repressible protein that binds both RNA and single-stranded DNA (ssDNA) in yeast. It may function in regulating cell growth in early log phase, possibly through its participation in RNA metabolism. NGR1 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a glutamine-rich stretch that may be involved in transcriptional activity. In addition, NGR1 has an asparagine-rich region near the carboxyl terminus which also harbors a methionine-rich region. The family also includes protein NAM8, which is a putative RNA-binding protein that acts as a suppressor of mitochondrial splicing deficiencies when overexpressed in yeast. It may be a non-essential component of the mitochondrial splicing machinery. Like NGR1, NAM8 contains two RRMs.
Pssm-ID: 409782 [Multi-domain] Cd Length: 72 Bit Score: 35.38 E-value: 3.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 816380035 177 EELFQLFG-YGDVVFVSKDVAKHLGF------QSAEEALRGLYGRVRKGAVLVCAW 225
Cdd:cd12346 16 EDLRVLFGpFGEIVYVKIPPGKGCGFvqfvnrASAEAAIQKLQGTPIGGSRIRLSW 71
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
176-271 |
7.58e-03 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 37.22 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816380035 176 REELFQLFGYGDVvfvskdvakhlgfQSAEEALRGLYGR----VRKGAVLVCAWAEegadalgpdGKLLHsdaFPPPRV- 250
Cdd:PRK09434 188 EEELCFLSGTSQL-------------EDAIYALADRYPIalllVTLGAEGVLVHTR---------GQVQH---FPAPSVd 242
|
90 100
....*....|....*....|..
gi 816380035 251 -VDTLGAGDTFNASVIFSLSQG 271
Cdd:PRK09434 243 pVDTTGAGDAFVAGLLAGLSQA 264
|
|
| |
