|
Name |
Accession |
Description |
Interval |
E-value |
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
202-497 |
7.15e-69 |
|
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: 223.21 E-value: 7.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 202 RILVVGEAILDEYVFCEGLGKSSKDPILAFHDRGLERYAGGSTAVANHLSTFCKEITFVSVVGDLSEDQDFIRGALGDNV 281
Cdd:cd01172 1 KVLVVGDVILDEYLYGDVERISPEAPVPVVKVEREEIRLGGAANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 282 TPIFIERASAPTITKRRFVDTHtkAKLIEIYEMADDVIPRETEAELLSVLRDEITDHDLVVVVDYGHGMMTDSVIKKVCE 361
Cdd:cd01172 81 DTDGIVDEGRPTTTKTRVIARN--QQLLRVDREDDSPLSAEEEQRLIERIAERLPEADVVILSDYGKGVLTPRVIEALIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 362 KAPFLAVNTQHNAGNRGFntiARYPKADYACMNgyesAIESRL---RNVPTQDQIAQ----LKGSVNCSKITVTLGSEGS 434
Cdd:cd01172 159 AARELGIPVLVDPKGRDY---SKYRGATLLTPN----EKEAREalgDEINDDDELEAagekLLELLNLEALLVTLGEEGM 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1200290598 435 MHFYNEGESITAPALAFRVVDRVGAGDAVLALTAPLVYAGVHWEIVAFVTNVVGAEVVGNLGT 497
Cdd:cd01172 232 TLFERDGEVQHIPALAKEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGT 294
|
|
| RfaE_N |
cd02172 |
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ... |
29-172 |
1.89e-64 |
|
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in Escherichia coli, and separate proteins in other organisms. Domain I is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (this family) adds ADP to yield ADP-D-glycero-D-manno-heptose .
Pssm-ID: 173923 [Multi-domain] Cd Length: 144 Bit Score: 205.73 E-value: 1.89e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 29 TSGQTVVHCHGVFDLLHPGHIAHFEAARRQGDRLIVTLTPDRFVNKGPNRPVFDEDLRAHTLASMEVIDAVAINEWPTAV 108
Cdd:cd02172 1 QRGKTVVLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVNKGPGRPIFPEDLRAEVLAALGFVDYVVLFDNPTAL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1200290598 109 ETIKKLRPDVYVKGKDYEDVSDDVTGKIAGEREAVEQNGGRLHITREITFSSSNLINSRLSSYP 172
Cdd:cd02172 81 EIIDALQPNIYVKGGDYENPENDVTGKIAPEAEAVKAYGGKIVFTGEIVFSSSALINRIFDELD 144
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
191-497 |
7.94e-40 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 146.88 E-value: 7.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 191 ILDSFTKIEGLRILVVGEAILDEYVFCEGLGKSSKDPILAFHDRGLERYAGGSTAVANHLSTFCKEITFVSVVGDlseDQ 270
Cdd:COG2870 6 LKELLPRFSRARVLVVGDVMLDRYWYGDVERISPEAPVPVVRVEREEERPGGAANVAANLAALGAQVTLVGVVGD---DE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 271 --DFIRGALGD-NVTPIFIERASA-PTITKRRFVDTHtkAKLIEIYEMADDVIPRETEAELLSVLRDEITDHDLVVVVDY 346
Cdd:COG2870 83 agRELRRLLEEaGIDTDGLVVDPRrPTTTKTRVIAGG--QQLLRLDFEDRFPLSAELEARLLAALEAALPEVDAVILSDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 347 GHGMMTDSVIKKVCEKA-----PFLAVNTQHNagnrgfntIARYPKADYACMNGYESAIESRLRNVPTQD---QIAQLKG 418
Cdd:COG2870 161 GKGVLTPELIQALIALAraagkPVLVDPKGRD--------FSRYRGATLLTPNLKEAEAAVGIPIADEEElvaAAAELLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 419 SVNCSKITVTLGSEGSMHFYNEGESITAPALAFRVVDRVGAGDAVLA-LTAPLVyAGVHWEIVAFVTNVVGAEVVGNLGT 497
Cdd:COG2870 233 RLGLEALLVTRGEEGMTLFDADGPPHHLPAQAREVFDVTGAGDTVIAtLALALA-AGASLEEAAELANLAAGIVVGKLGT 311
|
|
| rfaE_dom_II |
TIGR02199 |
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ... |
22-164 |
1.92e-35 |
|
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in E. coli, and separate proteins in some other genome. Domain I (TIGR02198) is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (this family) adds ADP to yield ADP-D-glycero-D-manno-heptose. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 131254 [Multi-domain] Cd Length: 144 Bit Score: 129.35 E-value: 1.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 22 TTVAGWKTSGQTVVHCHGVFDLLHPGHIAHFEAARRQGDRLIVTLTPDRFVN--KGPNRPVFDEDLRAHTLASMEVIDAV 99
Cdd:TIGR02199 1 ALVARARARGKKIVFTNGCFDILHAGHVSYLQQARALGDRLVVGVNSDASVKrlKGETRPINPEEDRAEVLAALSSVDYV 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1200290598 100 AINEWPTAVETIKKLRPDVYVKGKDYEdvSDDVTGkiageREAVEQNGGRLHITR-EITFSSSNLI 164
Cdd:TIGR02199 81 VIFDEDTPEELIGELKPDILVKGGDYK--VETLVG-----AELVESYGGQVVLLPfVEGRSTTAII 139
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
10-165 |
7.74e-21 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 95.28 E-value: 7.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 10 IHRKIKSLAALETTVAGWKTSGQTVVHCHGVFDLLHPGHIAHFEAARRQGDRLIVTLTPDRFVN--KGPNRPVFDEDLRA 87
Cdd:PRK11316 318 TGFGVMSEEQLKLAVAQARARGEKIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKrlKGEGRPVNPLEQRM 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 88 HTLASMEVIDAVAINEWPTAVETIKKLRPDVYVKGKDY--EDvsddvtgkIAGEREaVEQNGGRLHI-TREITFSSSNLI 164
Cdd:PRK11316 398 AVLAALEAVDWVVPFEEDTPQRLIAEILPDLLVKGGDYkpEE--------IAGSKE-VWANGGEVKVlNFEDGCSTTNII 468
|
.
gi 1200290598 165 N 165
Cdd:PRK11316 469 K 469
|
|
| TagD |
COG0615 |
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ... |
33-165 |
1.18e-20 |
|
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]; Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
Pssm-ID: 440380 [Multi-domain] Cd Length: 131 Bit Score: 87.85 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 33 TVVHCHGVFDLLHPGHIAHFEAARRQGDRLIVTLTPDRFV-NKGPnRPVFDEDLRAHTLASMEVIDAVAINEWPTAVETI 111
Cdd:COG0615 1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVaSKGR-KPIIPEEQRKEIVEALKYVDEVILGEEWDKFEDI 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1200290598 112 KKLRPDVYVKGkdyedvsDDVTGKIAGEREAVEQNGGRLHI-----TREItfSSSNLIN 165
Cdd:COG0615 80 EEIKPDVIVLG-------DDWKGDFDFLKEELEKRGIGCEVvylprTEGI--SSTKIKK 129
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
202-499 |
2.89e-11 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 64.29 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 202 RILVVGEAILDEYVFCEGLgksSKDPILAFHdrgLERYAGGSTA-VANHLSTFCKEITFVSVVGDlSEDQDFIRGALGD- 279
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGL---PGELVRVST---VEKGPGGKGAnVAVALARLGGDVAFIGAVGD-DNFGEFLLQELKKe 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 280 NVTPIFIER-ASAPTITKRRFVDTHtKAKLIEIYEMADDVIpretEAELLSVLRDEITDHDLVVVvdyghgmmTDSVIKK 358
Cdd:pfam00294 74 GVDTDYVVIdEDTRTGTALIEVDGD-GERTIVFNRGAAADL----TPEELEENEDLLENADLLYI--------SGSLPLG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 359 VCEKAPFLAVNTQHNAGNRGFN----------TIARY-PKADYACMNGYESAIESRLRNVPTQDQIAQLKGSVNC--SKI 425
Cdd:pfam00294 141 LPEATLEELIEAAKNGGTFDPNlldplgaareALLELlPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKgiKTV 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1200290598 426 TVTLGSEGSMHFYNEGESITAPALAFRVVDRVGAGDAVLA-LTAPLVyAGVHWEIVAFVTNVVGAEVVGNLGTGD 499
Cdd:pfam00294 221 IVTLGADGALVVEGDGEVHVPAVPKVKVVDTTGAGDSFVGgFLAGLL-AGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| CTP_transf_like |
pfam01467 |
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ... |
39-144 |
4.07e-11 |
|
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.
Pssm-ID: 396172 [Multi-domain] Cd Length: 134 Bit Score: 60.80 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 39 GVFDLLHPGHIAHFEAARRQGDR-LIVTLTPDRFVNKgPNRPVFDEDLRAHTL-ASMEVIDAVAINEWPTAVETIKKLRP 116
Cdd:pfam01467 4 GTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPPHK-LKRPLFSAEERLEMLeLAKWVDEVIVVAPWELTRELLKELNP 82
|
90 100
....*....|....*....|....*....
gi 1200290598 117 DVYVKGKD-YEDVSDDVTGKIAGEREAVE 144
Cdd:pfam01467 83 DVLVIGADsLLDFWYELDEILGNVKLVVV 111
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
202-462 |
1.85e-04 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 43.57 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 202 RILVVGEAILDEYVFCEGLGKsskdPILAFHDRGLERYAGGSTA-VANHLSTFCKEITFVSVVGDLSEDQDFIRGALGDN 280
Cdd:PTZ00292 17 DVVVVGSSNTDLIGYVDRMPQ----VGETLHGTSFHKGFGGKGAnQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 281 VTPIFIERAS-APTITKRRFVDTHTKAKLIEIyemaddvIPRETEA---ELLSVLRDEITDHDLVVVVD----------- 345
Cdd:PTZ00292 93 VNTSFVSRTEnSSTGLAMIFVDTKTGNNEIVI-------IPGANNAltpQMVDAQTDNIQNICKYLICQneiplettlda 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 346 ----YGHGMMTdsvikkVCEKAPflAVNTQHNAGNRGFntiarYPKADYACMNGYESAIESRLRNVPTQ--DQIAQLKGS 419
Cdd:PTZ00292 166 lkeaKERGCYT------VFNPAP--APKLAEVEIIKPF-----LKYVSLFCVNEVEAALITGMEVTDTEsaFKASKELQQ 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1200290598 420 VNCSKITVTLGSEGSMHFYNEGESITAPALAFRVVDRVGAGDA 462
Cdd:PTZ00292 233 LGVENVIITLGANGCLIVEKENEPVHVPGKRVKAVDTTGAGDC 275
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
202-497 |
7.15e-69 |
|
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: 223.21 E-value: 7.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 202 RILVVGEAILDEYVFCEGLGKSSKDPILAFHDRGLERYAGGSTAVANHLSTFCKEITFVSVVGDLSEDQDFIRGALGDNV 281
Cdd:cd01172 1 KVLVVGDVILDEYLYGDVERISPEAPVPVVKVEREEIRLGGAANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 282 TPIFIERASAPTITKRRFVDTHtkAKLIEIYEMADDVIPRETEAELLSVLRDEITDHDLVVVVDYGHGMMTDSVIKKVCE 361
Cdd:cd01172 81 DTDGIVDEGRPTTTKTRVIARN--QQLLRVDREDDSPLSAEEEQRLIERIAERLPEADVVILSDYGKGVLTPRVIEALIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 362 KAPFLAVNTQHNAGNRGFntiARYPKADYACMNgyesAIESRL---RNVPTQDQIAQ----LKGSVNCSKITVTLGSEGS 434
Cdd:cd01172 159 AARELGIPVLVDPKGRDY---SKYRGATLLTPN----EKEAREalgDEINDDDELEAagekLLELLNLEALLVTLGEEGM 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1200290598 435 MHFYNEGESITAPALAFRVVDRVGAGDAVLALTAPLVYAGVHWEIVAFVTNVVGAEVVGNLGT 497
Cdd:cd01172 232 TLFERDGEVQHIPALAKEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGT 294
|
|
| RfaE_N |
cd02172 |
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ... |
29-172 |
1.89e-64 |
|
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in Escherichia coli, and separate proteins in other organisms. Domain I is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (this family) adds ADP to yield ADP-D-glycero-D-manno-heptose .
Pssm-ID: 173923 [Multi-domain] Cd Length: 144 Bit Score: 205.73 E-value: 1.89e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 29 TSGQTVVHCHGVFDLLHPGHIAHFEAARRQGDRLIVTLTPDRFVNKGPNRPVFDEDLRAHTLASMEVIDAVAINEWPTAV 108
Cdd:cd02172 1 QRGKTVVLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVNKGPGRPIFPEDLRAEVLAALGFVDYVVLFDNPTAL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1200290598 109 ETIKKLRPDVYVKGKDYEDVSDDVTGKIAGEREAVEQNGGRLHITREITFSSSNLINSRLSSYP 172
Cdd:cd02172 81 EIIDALQPNIYVKGGDYENPENDVTGKIAPEAEAVKAYGGKIVFTGEIVFSSSALINRIFDELD 144
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
191-497 |
7.94e-40 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 146.88 E-value: 7.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 191 ILDSFTKIEGLRILVVGEAILDEYVFCEGLGKSSKDPILAFHDRGLERYAGGSTAVANHLSTFCKEITFVSVVGDlseDQ 270
Cdd:COG2870 6 LKELLPRFSRARVLVVGDVMLDRYWYGDVERISPEAPVPVVRVEREEERPGGAANVAANLAALGAQVTLVGVVGD---DE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 271 --DFIRGALGD-NVTPIFIERASA-PTITKRRFVDTHtkAKLIEIYEMADDVIPRETEAELLSVLRDEITDHDLVVVVDY 346
Cdd:COG2870 83 agRELRRLLEEaGIDTDGLVVDPRrPTTTKTRVIAGG--QQLLRLDFEDRFPLSAELEARLLAALEAALPEVDAVILSDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 347 GHGMMTDSVIKKVCEKA-----PFLAVNTQHNagnrgfntIARYPKADYACMNGYESAIESRLRNVPTQD---QIAQLKG 418
Cdd:COG2870 161 GKGVLTPELIQALIALAraagkPVLVDPKGRD--------FSRYRGATLLTPNLKEAEAAVGIPIADEEElvaAAAELLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 419 SVNCSKITVTLGSEGSMHFYNEGESITAPALAFRVVDRVGAGDAVLA-LTAPLVyAGVHWEIVAFVTNVVGAEVVGNLGT 497
Cdd:COG2870 233 RLGLEALLVTRGEEGMTLFDADGPPHHLPAQAREVFDVTGAGDTVIAtLALALA-AGASLEEAAELANLAAGIVVGKLGT 311
|
|
| rfaE_dom_II |
TIGR02199 |
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ... |
22-164 |
1.92e-35 |
|
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in E. coli, and separate proteins in some other genome. Domain I (TIGR02198) is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (this family) adds ADP to yield ADP-D-glycero-D-manno-heptose. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 131254 [Multi-domain] Cd Length: 144 Bit Score: 129.35 E-value: 1.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 22 TTVAGWKTSGQTVVHCHGVFDLLHPGHIAHFEAARRQGDRLIVTLTPDRFVN--KGPNRPVFDEDLRAHTLASMEVIDAV 99
Cdd:TIGR02199 1 ALVARARARGKKIVFTNGCFDILHAGHVSYLQQARALGDRLVVGVNSDASVKrlKGETRPINPEEDRAEVLAALSSVDYV 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1200290598 100 AINEWPTAVETIKKLRPDVYVKGKDYEdvSDDVTGkiageREAVEQNGGRLHITR-EITFSSSNLI 164
Cdd:TIGR02199 81 VIFDEDTPEELIGELKPDILVKGGDYK--VETLVG-----AELVESYGGQVVLLPfVEGRSTTAII 139
|
|
| cytidylyltransferase |
cd02170 |
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ... |
33-169 |
1.78e-31 |
|
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate cytidylyltransferase (CCT), glycerol-3-phosphate cytidylyltransferase, RafE and phosphoethanolamine cytidylyltransferase (ECT). All enzymes catalyze the transfer of a cytidylyl group from CTP to various substrates.
Pssm-ID: 173921 [Multi-domain] Cd Length: 136 Bit Score: 118.16 E-value: 1.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 33 TVVHCHGVFDLLHPGHIAHFEAARRQGDRLIVTLTPDRFVNKGPNRPVFDEDLRAHTLASMEVIDAVAINEWPTAVETIK 112
Cdd:cd02170 2 KRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKRRPILPEEQRAEVVEALKYVDEVILGHPWSYFKPLE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1200290598 113 KLRPDVYVKGKDYEdvsddVTGKIAGEREAVEQNGGRLHITR--EITFSSSNLINSRLS 169
Cdd:cd02170 82 ELKPDVIVLGDDQK-----NGVDEEEVYEELKKRGKVIEVPRkkTEGISSSDIIKRILE 135
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
10-165 |
7.74e-21 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 95.28 E-value: 7.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 10 IHRKIKSLAALETTVAGWKTSGQTVVHCHGVFDLLHPGHIAHFEAARRQGDRLIVTLTPDRFVN--KGPNRPVFDEDLRA 87
Cdd:PRK11316 318 TGFGVMSEEQLKLAVAQARARGEKIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKrlKGEGRPVNPLEQRM 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 88 HTLASMEVIDAVAINEWPTAVETIKKLRPDVYVKGKDY--EDvsddvtgkIAGEREaVEQNGGRLHI-TREITFSSSNLI 164
Cdd:PRK11316 398 AVLAALEAVDWVVPFEEDTPQRLIAEILPDLLVKGGDYkpEE--------IAGSKE-VWANGGEVKVlNFEDGCSTTNII 468
|
.
gi 1200290598 165 N 165
Cdd:PRK11316 469 K 469
|
|
| TagD |
COG0615 |
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ... |
33-165 |
1.18e-20 |
|
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]; Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
Pssm-ID: 440380 [Multi-domain] Cd Length: 131 Bit Score: 87.85 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 33 TVVHCHGVFDLLHPGHIAHFEAARRQGDRLIVTLTPDRFV-NKGPnRPVFDEDLRAHTLASMEVIDAVAINEWPTAVETI 111
Cdd:COG0615 1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVaSKGR-KPIIPEEQRKEIVEALKYVDEVILGEEWDKFEDI 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1200290598 112 KKLRPDVYVKGkdyedvsDDVTGKIAGEREAVEQNGGRLHI-----TREItfSSSNLIN 165
Cdd:COG0615 80 EEIKPDVIVLG-------DDWKGDFDFLKEELEKRGIGCEVvylprTEGI--SSTKIKK 129
|
|
| ECT |
cd02173 |
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ... |
31-124 |
2.95e-14 |
|
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine cytidylyltransferase (ECT) catalyzes the conversion of phosphoethanolamine to CDP-ethanolamine as part of the CDP-ethanolamine biosynthesis pathway. ECT expression in hepatocytes is localized predominantly to areas of the cytoplasm that are rich in rough endoplasmic reticulum. Several ECTs, including yeast and human ECT, have large repetitive sequences located within their N- and C-termini.
Pssm-ID: 173924 Cd Length: 152 Bit Score: 69.98 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 31 GQTVVHCHGVFDLLHPGHIAHFEAARRQGDRLIVTLTPDRFVN--KGPNRPVFDEDLRAHTLASMEVIDAVAINEwPTAV 108
Cdd:cd02173 1 GDKVVYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNeyKGSNYPIMNLHERVLSVLACRYVDEVVIGA-PYVI 79
|
90
....*....|....*...
gi 1200290598 109 --ETIKKLRPDVYVKGKD 124
Cdd:cd02173 80 tkELIEHFKIDVVVHGKT 97
|
|
| G3P_Cytidylyltransferase |
cd02171 |
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ... |
34-126 |
6.45e-13 |
|
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase,(CDP-glycerol pyrophosphorylase). Glycerol-3-phosphate cytidyltransferase acts in pathways of teichoic acid biosynthesis. Teichoic acids are substituted polymers, linked by phosphodiester bonds, of glycerol, ribitol, etc. An example is poly(glycerol phosphate), the major teichoic acid of the Bacillus subtilis cell wall. Most, but not all, species encoding proteins in this family are Gram-positive bacteria. A closely related protein assigned a different function experimentally is a human ethanolamine-phosphate cytidylyltransferase.
Pssm-ID: 173922 [Multi-domain] Cd Length: 129 Bit Score: 65.58 E-value: 6.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 34 VVHCHGVFDLLHPGHIAHFEAARRQGDRLIVTLTPDRFVNKGPNRPVFDEDLRAHTLASMEVIDAVaINE--WPTAVETI 111
Cdd:cd02171 3 VVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLV-IPEtnWEQKIEDI 81
|
90
....*....|....*
gi 1200290598 112 KKLRPDVYVKGKDYE 126
Cdd:cd02171 82 KKYNVDVFVMGDDWE 96
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
202-499 |
2.89e-11 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 64.29 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 202 RILVVGEAILDEYVFCEGLgksSKDPILAFHdrgLERYAGGSTA-VANHLSTFCKEITFVSVVGDlSEDQDFIRGALGD- 279
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGL---PGELVRVST---VEKGPGGKGAnVAVALARLGGDVAFIGAVGD-DNFGEFLLQELKKe 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 280 NVTPIFIER-ASAPTITKRRFVDTHtKAKLIEIYEMADDVIpretEAELLSVLRDEITDHDLVVVvdyghgmmTDSVIKK 358
Cdd:pfam00294 74 GVDTDYVVIdEDTRTGTALIEVDGD-GERTIVFNRGAAADL----TPEELEENEDLLENADLLYI--------SGSLPLG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 359 VCEKAPFLAVNTQHNAGNRGFN----------TIARY-PKADYACMNGYESAIESRLRNVPTQDQIAQLKGSVNC--SKI 425
Cdd:pfam00294 141 LPEATLEELIEAAKNGGTFDPNlldplgaareALLELlPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKgiKTV 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1200290598 426 TVTLGSEGSMHFYNEGESITAPALAFRVVDRVGAGDAVLA-LTAPLVyAGVHWEIVAFVTNVVGAEVVGNLGTGD 499
Cdd:pfam00294 221 IVTLGADGALVVEGDGEVHVPAVPKVKVVDTTGAGDSFVGgFLAGLL-AGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| cyt_tran_rel |
TIGR00125 |
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ... |
39-92 |
3.41e-11 |
|
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.
Pssm-ID: 272920 [Multi-domain] Cd Length: 66 Bit Score: 58.86 E-value: 3.41e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1200290598 39 GVFDLLHPGHIAHFEAARRQGDRLIVTLTPDRFVNKGPNRPVFDEDLRAHTLAS 92
Cdd:TIGR00125 6 GTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPVFSLEERLEMLKA 59
|
|
| CTP_transf_like |
pfam01467 |
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ... |
39-144 |
4.07e-11 |
|
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.
Pssm-ID: 396172 [Multi-domain] Cd Length: 134 Bit Score: 60.80 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 39 GVFDLLHPGHIAHFEAARRQGDR-LIVTLTPDRFVNKgPNRPVFDEDLRAHTL-ASMEVIDAVAINEWPTAVETIKKLRP 116
Cdd:pfam01467 4 GTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPPHK-LKRPLFSAEERLEMLeLAKWVDEVIVVAPWELTRELLKELNP 82
|
90 100
....*....|....*....|....*....
gi 1200290598 117 DVYVKGKD-YEDVSDDVTGKIAGEREAVE 144
Cdd:pfam01467 83 DVLVIGADsLLDFWYELDEILGNVKLVVV 111
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
30-124 |
5.60e-11 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 64.04 E-value: 5.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 30 SGQTVVHCHGVFDLLHPGHIAHFEAARRQGDRLIVTLTPDRFVN--KGPNRPVFDEDLRAHTLASMEVIDAVAINEwPTA 107
Cdd:PTZ00308 190 PGDRIVYVDGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQVVNeqKGSNYPIMNLNERVLGVLSCRYVDEVVIGA-PFD 268
|
90
....*....|....*....
gi 1200290598 108 V--ETIKKLRPDVYVKGKD 124
Cdd:PTZ00308 269 VtkEVIDSLHINVVVGGKF 287
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
202-462 |
7.23e-11 |
|
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: 63.36 E-value: 7.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 202 RILVVGEAILDEYVFCEGLGKsskdPILAFHDRGLERYAGGSTA-VANHLSTFCKEITFVSVVGDlseDQ--DFIRGAL- 277
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPK----GGETVLAGSFRRSPGGAAAnVAVALARLGARVALVGAVGD---DPfgDFLLAELr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 278 GDNVTPIFIER-ASAPTITKRRFVDTHTKAKLIeIYEMADDVIPREteaellSVLRDEITDHDLVVV-VDYGHGMMTDSV 355
Cdd:COG0524 74 AEGVDTSGVRRdPGAPTGLAFILVDPDGERTIV-FYRGANAELTPE------DLDEALLAGADILHLgGITLASEPPREA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 356 IKKVCEKAP------FLAVNTQHNAGNRGFNTIAR-YPKADYACMNGYESAIesrLRNVPTQDQIAQLKGSVNCSKITVT 428
Cdd:COG0524 147 LLAALEAARaagvpvSLDPNYRPALWEPARELLRElLALVDILFPNEEEAEL---LTGETDPEEAAAALLARGVKLVVVT 223
|
250 260 270
....*....|....*....|....*....|....
gi 1200290598 429 LGSEGSMhFYNEGESITAPALAFRVVDRVGAGDA 462
Cdd:COG0524 224 LGAEGAL-LYTGGEVVHVPAFPVEVVDTTGAGDA 256
|
|
| CCT |
cd02174 |
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ... |
35-135 |
6.02e-08 |
|
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) catalyzes the condensation of CTP and phosphocholine to form CDP-choline as the rate-limiting and regulatory step in the CDP-choline pathway. CCT is unique in that its enzymatic activity is regulated by the extent of its association with membrane structures. A current model posts that the elastic stress of the bilayer curvature is sensed by CCT and this governs the degree of membrane association, thus providing a mechanism for both positive and negative regulation of activity.
Pssm-ID: 173925 Cd Length: 150 Bit Score: 51.80 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 35 VHCHGVFDLLHPGHIAHFEAARRQG--DRLIVTLTPDR--FVNKGPnrPVFDEDLRAHTLASMEVIDAVAIN-EWPTAVE 109
Cdd:cd02174 5 VYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEeiHKHKGP--PVMTEEERYEAVRHCKWVDEVVEGaPYVTTPE 82
|
90 100
....*....|....*....|....*.
gi 1200290598 110 TIKKLRPDVYVKGkdyEDVSDDVTGK 135
Cdd:cd02174 83 FLDKYKCDYVAHG---DDIYLDADGE 105
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
202-497 |
1.20e-07 |
|
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: 53.08 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 202 RILVVGEAILDEYVFCEGL-GKSSKDPIlafhdRGLERYAGGS---TAVAnhLSTFCKEITFVSVVGDlsedqDFIRGAL 277
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFpGPFESVLV-----KDLRREFGGSagnTAVA--LAKLGLSPGLVAAVGE-----DFHGRLY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 278 GDnvtpiFIERASAPTITKRRFVDTHTKakliEIYEMADDVIpRETEAELLSVLR--DEITDHDLVVVVDYGHGMMTDSV 355
Cdd:cd01942 69 LE-----ELREEGVDTSHVRVVDEDSTG----VAFILTDGDD-NQIAYFYPGAMDelEPNDEADPDGLADIVHLSSGPGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 356 IKKVCEKAP---FLAVNTQHNAGNRGFNTIARY-PKADYACMNGYESAIESRLRNVPTQDQIAQLKGSVncskitVTLGS 431
Cdd:cd01942 139 IELARELAAggiTVSFDPGQELPRLSGEELEEIlERADILFVNDYEAELLKERTGLSEAELASGVRVVV------VTLGP 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1200290598 432 EGSMHFYNEGESITAPALAFRVVDRVGAGDAVLA--LTAplVYAGVHWEIVAFVTNVVGAEVVGNLGT 497
Cdd:cd01942 213 KGAIVFEDGEEVEVPAVPAVKVVDTTGAGDAFRAgfLYG--LLRGYDLEESLRLGNLAASLKVERRGA 278
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
411-496 |
2.62e-07 |
|
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: 52.25 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 411 DQIAQLKGSVNCSKITVTLGSEGsMHFYNEGESITAPALAFRVVDRVGAGDAVLA------LTAPLVYAGVHW--EIVAF 482
Cdd:cd01167 202 EEIAALLLLFGLKLVLVTRGADG-ALLYTKGGVGEVPGIPVEVVDTTGAGDAFVAgllaqlLSRGLLALDEDElaEALRF 280
|
90
....*....|....
gi 1200290598 483 vTNVVGAEVVGNLG 496
Cdd:cd01167 281 -ANAVGALTCTKAG 293
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
28-135 |
5.81e-07 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 51.71 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 28 KTSGQTVVHCHGVFDLLHPGHIAHFEAARRQGDRLIVTLTPDRFV--NKGPnrPVFDEDLRAHTLASMEVIDAVAIN-EW 104
Cdd:PTZ00308 7 KKPGTIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEImrNKGP--PVMHQEERYEALRACKWVDEVVEGyPY 84
|
90 100 110
....*....|....*....|....*....|.
gi 1200290598 105 PTAVETIKKLRPDVYVKGkdyEDVSDDVTGK 135
Cdd:PTZ00308 85 TTRLEDLERLECDFVVHG---DDISVDLNGR 112
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
385-462 |
3.86e-05 |
|
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: 45.62 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 385 YPKADYACMNGYESAI--ESRLRNVPTQDQIAQLKGSVNCSKITVTLGSEGSMhFYNEGESITAPALAFRVVDRVGAGDA 462
Cdd:cd01174 173 LALVDILVPNETEAALltGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGAL-LASGGEVEHVPAFKVKAVDTTGAGDT 251
|
|
| PLN02406 |
PLN02406 |
ethanolamine-phosphate cytidylyltransferase |
34-101 |
4.47e-05 |
|
ethanolamine-phosphate cytidylyltransferase
Pssm-ID: 215227 [Multi-domain] Cd Length: 418 Bit Score: 45.83 E-value: 4.47e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 34 VVHCHGVFDLLHPGHIAHFEAARRQGDRLIVTLTPDRFV--NKGPNRPVFDEDLRAHTLASMEVIDAVAI 101
Cdd:PLN02406 253 IVYIDGAFDLFHAGHVEILRLARALGDFLLVGIHTDQTVsaHRGAHRPIMNLHERSLSVLACRYVDEVII 322
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
425-462 |
6.30e-05 |
|
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: 44.87 E-value: 6.30e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1200290598 425 ITVTLGSEGSMhFYNEGESITAPALAFRVVDRVGAGDA 462
Cdd:cd01166 222 VVVKLGAEGAL-VYTGGGRVFVPAYPVEVVDTTGAGDA 258
|
|
| Pantoate_ligase |
pfam02569 |
Pantoate-beta-alanine ligase; Pantoate-beta-alanine ligase, also know as pantothenate synthase, ... |
12-87 |
1.80e-04 |
|
Pantoate-beta-alanine ligase; Pantoate-beta-alanine ligase, also know as pantothenate synthase, (EC:6.3.2.1) catalyzes the formation of pantothenate from pantoate and alanine.
Pssm-ID: 460595 [Multi-domain] Cd Length: 277 Bit Score: 43.56 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 12 RKIKSLAALETTVAGWKTSGQTVVhchgvfdL------LHPGHIAHFEAARRQGDRLIVTLtpdrFVN---KGPNrpvfd 82
Cdd:pfam02569 1 KIIRTIAELRAWLRAWRRAGKTIG-------LvptmgaLHEGHLSLVRRARAENDVVVVSI----FVNptqFGPN----- 64
|
....*
gi 1200290598 83 EDLRA 87
Cdd:pfam02569 65 EDLDA 69
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
202-462 |
1.85e-04 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 43.57 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 202 RILVVGEAILDEYVFCEGLGKsskdPILAFHDRGLERYAGGSTA-VANHLSTFCKEITFVSVVGDLSEDQDFIRGALGDN 280
Cdd:PTZ00292 17 DVVVVGSSNTDLIGYVDRMPQ----VGETLHGTSFHKGFGGKGAnQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 281 VTPIFIERAS-APTITKRRFVDTHTKAKLIEIyemaddvIPRETEA---ELLSVLRDEITDHDLVVVVD----------- 345
Cdd:PTZ00292 93 VNTSFVSRTEnSSTGLAMIFVDTKTGNNEIVI-------IPGANNAltpQMVDAQTDNIQNICKYLICQneiplettlda 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 346 ----YGHGMMTdsvikkVCEKAPflAVNTQHNAGNRGFntiarYPKADYACMNGYESAIESRLRNVPTQ--DQIAQLKGS 419
Cdd:PTZ00292 166 lkeaKERGCYT------VFNPAP--APKLAEVEIIKPF-----LKYVSLFCVNEVEAALITGMEVTDTEsaFKASKELQQ 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1200290598 420 VNCSKITVTLGSEGSMHFYNEGESITAPALAFRVVDRVGAGDA 462
Cdd:PTZ00292 233 LGVENVIITLGANGCLIVEKENEPVHVPGKRVKAVDTTGAGDC 275
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
386-497 |
6.04e-04 |
|
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: 41.83 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 386 PKADYACMNgyESAIESRLRNVPTQDQIAQLKGSVNCSKITV-TLGSEGSmHFYNEGESITAPALAF-RVVDRVGAGDA- 462
Cdd:cd01168 199 PYVDILFGN--EEEAEALAEAETTDDLEAALKLLALRCRIVViTQGAKGA-VVVEGGEVYPVPAIPVeKIVDTNGAGDAf 275
|
90 100 110
....*....|....*....|....*....|....*....
gi 1200290598 463 ----VLALTaplvyAGVHWEIVAFVTNVVGAEVVGNLGT 497
Cdd:cd01168 276 aggfLYGLV-----QGEPLEECIRLGSYAAAEVIQQLGP 309
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
258-471 |
6.79e-04 |
|
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: 41.53 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 258 TFVSVVGDLSEDQDFIRGA--LGDNVTPIFIERASAPTitkrrFVDTHTKAKLIeIYEMADDVIPRETEAELLSVLRDEI 335
Cdd:cd01941 53 ALLSAVGDDSEGESILEESekAGLNVRGIVFEGRSTAS-----YTAILDKDGDL-VVALADMDIYELLTPDFLRKIREAL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 336 TDHDLVVVvDyghGMMTDSVIKKVCEKA----------PFLAVNTQHNAGNRGfntiarypKADYACMNGYES------A 399
Cdd:cd01941 127 KEAKPIVV-D---ANLPEEALEYLLALAakhgvpvafePTSAPKLKKLFYLLH--------AIDLLTPNRAELealagaL 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1200290598 400 IESRLRNVPtqDQIAQLKGSVNCskITVTLGSEGSMHFYNEGESIT---APALAFRVVDRVGAGDAVLA-LTAPLV 471
Cdd:cd01941 195 IENNEDENK--AAKILLLPGIKN--VIVTLGAKGVLLSSREGGVETklfPAPQPETVVNVTGAGDAFVAgLVAGLL 266
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
427-465 |
1.09e-03 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 41.27 E-value: 1.09e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1200290598 427 VTLGSEGSMhFYNEGESITAPALAFRVVDRVGAGDAVLA 465
Cdd:COG1105 219 VSLGADGAL-LVTEDGVYRAKPPKVEVVSTVGAGDSMVA 256
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
410-465 |
1.18e-03 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 41.07 E-value: 1.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1200290598 410 QDQIAQLKGSVNCSKITVTLGSEGSMhFYNEGESITAPALAFRVVDRVGAGDAVLA 465
Cdd:PRK09434 201 EDAIYALADRYPIALLLVTLGAEGVL-VHTRGQVQHFPAPSVDPVDTTGAGDAFVA 255
|
|
| PanC |
cd00560 |
Pantoate-beta-alanine ligase; PanC Pantoate-beta-alanine ligase, also known as pantothenate ... |
14-87 |
5.22e-03 |
|
Pantoate-beta-alanine ligase; PanC Pantoate-beta-alanine ligase, also known as pantothenate synthase, catalyzes the formation of pantothenate from pantoate and alanine. PanC belongs to a large superfamily of nucleotidyltransferases that includes , ATP sulfurylase (ATPS), phosphopantetheine adenylyltransferase (PPAT), and the amino-acyl tRNA synthetases. The enzymes of this family are structurally similar and share a dinucleotide-binding domain.
Pssm-ID: 185673 [Multi-domain] Cd Length: 277 Bit Score: 38.67 E-value: 5.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1200290598 14 IKSLAALETTVAGWKTSGQTV--VHCHGVfdlLHPGHIAHFEAARRQGDRLIVTLtpdrFVNK---GPNrpvfdEDLRA 87
Cdd:cd00560 4 ITTIAELRAWLRNWRAQGKTIgfVPTMGA---LHEGHLSLVRRARAENDVVVVSI----FVNPlqfGPN-----EDLDR 70
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
202-497 |
5.28e-03 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 39.43 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 202 RILVVGEAILDEYVFceglGKSSK----DPILAFHDRGLERYAGGSTAVANHLSTFCKEITFVSVVGDlSEDQDFIRGAL 277
Cdd:PRK11316 12 GVLVVGDVMLDRYWY----GPTSRispeAPVPVVKVNQIEERPGGAANVAMNIASLGAQARLVGLTGI-DEAARALSKLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 278 -GDNVTPIFIERASAPTITKRRFVDTHTkaKLIEIyEMADDVIPRETEAeLLSVLRDEITDHDLVVVVDYGHGMMTD--S 354
Cdd:PRK11316 87 aAVGVKCDFVSVPTHPTITKLRVLSRNQ--QLIRL-DFEEGFEGVDPQP-LLERIEQALPSIGALVLSDYAKGALASvqA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 355 VIKKVCEKA-PFLavntqhnAGNRGfNTIARYPKADYACMNgyESAIESRLRNVPTQDQIA----QLKGSVNCSKITVTL 429
Cdd:PRK11316 163 MIQLARKAGvPVL-------IDPKG-TDFERYRGATLLTPN--LSEFEAVVGKCKDEAELVekgmKLIADYDLSALLVTR 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1200290598 430 GSEGSMHFYNEGESITAPALAFRVVDRVGAGDAVLALTAPLVYAGVHWEIVAFVTNVVGAEVVGNLGT 497
Cdd:PRK11316 233 SEQGMTLLQPGKAPLHLPTQAREVYDVTGAGDTVISVLAAALAAGNSLEEACALANAAAGVVVGKLGT 300
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
425-465 |
8.67e-03 |
|
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: 37.46 E-value: 8.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1200290598 425 ITVTLGSEGSMHFYNEGESITAPALAFRVVDRVGAGDAVLA 465
Cdd:cd00287 149 VIVTLGEKGAIVATRGGTEVHVPAFPVKVVDTTGAGDAFLA 189
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
308-462 |
9.56e-03 |
|
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: 38.17 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200290598 308 LIEIYEMADDVIPRETEAELLSVLRDEITdhdlvVVVDYGH--GMMTDSVIKKVCEKAPFLAVNTQhnagnrgfntiary 385
Cdd:cd01944 130 YLSGYTLASENASKVILLEWLEALPAGTT-----LVFDPGPriSDIPDTILQALMAKRPIWSCNRE-------------- 190
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1200290598 386 pKADYACMNGYESAIESRLRNVPTQDqiaqlkgsvncSKITVTLGSEGSMHFYNEGESITAPALAFRVVDRVGAGDA 462
Cdd:cd01944 191 -EAAIFAERGDPAAEASALRIYAKTA-----------APVVVRLGSNGAWIRLPDGNTHIIPGFKVKAVDTIGAGDT 255
|
|
| |
