|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
1-472 |
0e+00 |
|
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: 992.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 1 MAQYSAEFKQAKVLVLGDVMLDRYWFGATNRISPEAPVPVVRVQENEERAGGAANVAMNIASLNVPVQLMGLIGQDETGS 80
Cdd:PRK11316 1 MKVTLPDFERAGVLVVGDVMLDRYWYGPTSRISPEAPVPVVKVNQIEERPGGAANVAMNIASLGAQARLVGLTGIDEAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 81 ALSHLLEKQKIDCNFVALETHPTITKLRILSRHQQLLRLDFEEDFNNVDCKDLLAKLESAVKNYGALILSDYGKGTLKDV 160
Cdd:PRK11316 81 ALSKLLAAVGVKCDFVSVPTHPTITKLRVLSRNQQLIRLDFEEGFEGVDPQPLLERIEQALPSIGALVLSDYAKGALASV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 161 QKMIQIARKANVPVLIDPKGTDFERYRGATLLTPNMSEFEAVVGKCNTEEEIIKKGLKLISDIELTALLVTRSEKGMTLL 240
Cdd:PRK11316 161 QAMIQLARKAGVPVLIDPKGTDFERYRGATLLTPNLSEFEAVVGKCKDEAELVEKGMKLIADYDLSALLVTRSEQGMTLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 241 RPNQEPYHLPTVAKEVFDVTGAGDTVISVLATALADGRSFEESCYLANVAAGIVVGKLGTSTVSTVELENAIHARPETGF 320
Cdd:PRK11316 241 QPGKAPLHLPTQAREVYDVTGAGDTVISVLAAALAAGNSLEEACALANAAAGVVVGKLGTSTVSPIELENALRGRAETGF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 321 GIMSEAELKDAVAQAKARGEKIVMTNGCFDILHPGHISYLENARKLGDRLIVAVNSDDSVKRLKGESRPINNLENRMAVL 400
Cdd:PRK11316 321 GVMSEEQLKLAVAQARARGEKIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEGRPVNPLEQRMAVL 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1356821756 401 AGLASVDWLVPFTEDTPQRLIGEILPDLLVKGGDYKPEEIAGSKEVWANGGDVKVLNFENGCSTTNVIEKIK 472
Cdd:PRK11316 401 AALEAVDWVVPFEEDTPQRLIAEILPDLLVKGGDYKPEEIAGSKEVWANGGEVKVLNFEDGCSTTNIIKKIR 472
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
1-310 |
2.25e-171 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 484.31 E-value: 2.25e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 1 MAQYSAEFKQAKVLVLGDVMLDRYWFGATNRISPEAPVPVVRVQENEERAGGAANVAMNIASLNVPVQLMGLIGQDETGS 80
Cdd:COG2870 6 LKELLPRFSRARVLVVGDVMLDRYWYGDVERISPEAPVPVVRVEREEERPGGAANVAANLAALGAQVTLVGVVGDDEAGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 81 ALSHLLEKQKIDCNFVALETHP-TITKLRILSRHQQLLRLDFEEDF--NNVDCKDLLAKLESAVKNYGALILSDYGKGTL 157
Cdd:COG2870 86 ELRRLLEEAGIDTDGLVVDPRRpTTTKTRVIAGGQQLLRLDFEDRFplSAELEARLLAALEAALPEVDAVILSDYGKGVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 158 --KDVQKMIQIARKANVPVLIDPKGTDFERYRGATLLTPNMSEFEAVVG-KCNTEEEIIKKGLKLISDIELTALLVTRSE 234
Cdd:COG2870 166 tpELIQALIALARAAGKPVLVDPKGRDFSRYRGATLLTPNLKEAEAAVGiPIADEEELVAAAAELLERLGLEALLVTRGE 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1356821756 235 KGMTLLRPNQEPYHLPTVAKEVFDVTGAGDTVISVLATALADGRSFEESCYLANVAAGIVVGKLGTSTVSTVELEN 310
Cdd:COG2870 246 EGMTLFDADGPPHHLPAQAREVFDVTGAGDTVIATLALALAAGASLEEAAELANLAAGIVVGKLGTATVSPEELLA 321
|
|
| rfaE_dom_I |
TIGR02198 |
rfaE bifunctional protein, domain I; RfaE is a protein involved in the biosynthesis of ... |
4-313 |
4.35e-169 |
|
rfaE bifunctional protein, domain I; 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. The longer, N-terminal domain I (this family) is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (TIGR02199) adds ADP to yield ADP-D-glycero-D-manno-heptose. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 274029 [Multi-domain] Cd Length: 315 Bit Score: 478.27 E-value: 4.35e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 4 YSAEFKQAKVLVLGDVMLDRYWFGATNRISPEAPVPVVRVQENEERAGGAANVAMNIASLNVPVQLMGLIGQDETGSALS 83
Cdd:TIGR02198 1 LIASFKGAKVLVVGDVMLDRYWYGKVSRISPEAPVPVVKVEREEDRLGGAANVARNIASLGARVFLVGVVGDDEAGKRLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 84 HLLEKQKIDCN-FVALETHPTITKLRILSRHQQLLRLDFEED--FNNVDCKDLLAKLESAVKNYGALILSDYGKGTLKD- 159
Cdd:TIGR02198 81 ALLAEEGIDTSgLIRDKDRPTTTKTRVLARNQQLLRVDFEERdpINAELEARLLAAIREQLASADAVVLSDYAKGVLTPr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 160 -VQKMIQIARKANVPVLIDPKGTDFERYRGATLLTPNMSEFEAVVGKCNTEEEIIKKGLKLISDIELTALLVTRSEKGMT 238
Cdd:TIGR02198 161 vVQEVIAAARKHGKPVLVDPKGKDFSRYRGATLITPNRKEAEAAVGACDTEAELVQAAEKLLEELDLEALLVTRSEKGMT 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1356821756 239 LLRPNQEPYHLPTVAKEVFDVTGAGDTVISVLATALADGRSFEESCYLANVAAGIVVGKLGTSTVSTVELENAIH 313
Cdd:TIGR02198 241 LFTREGEPIHIPAQAREVYDVTGAGDTVIATLALALAAGASLEEACRLANAAAGVVVGKLGTATVSPAELANALQ 315
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
12-309 |
3.19e-137 |
|
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: 396.93 E-value: 3.19e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 12 KVLVLGDVMLDRYWFGATNRISPEAPVPVVRVQENEERAGGAANVAMNIASLNVPVQLMGLIGQDETGSALSHLLEKQKI 91
Cdd:cd01172 1 KVLVVGDVILDEYLYGDVERISPEAPVPVVKVEREEIRLGGAANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 92 DCNFVALETHPTITKLRILSRHQQLLRLDFEEDFN-NVDCKD-LLAKLESAVKNYGALILSDYGKGTLKD--VQKMIQIA 167
Cdd:cd01172 81 DTDGIVDEGRPTTTKTRVIARNQQLLRVDREDDSPlSAEEEQrLIERIAERLPEADVVILSDYGKGVLTPrvIEALIAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 168 RKANVPVLIDPKGTDFERYRGATLLTPNMSEFEAVVGKC-NTEEEIIKKGLKLISDIELTALLVTRSEKGMTLLRPNQEP 246
Cdd:cd01172 161 RELGIPVLVDPKGRDYSKYRGATLLTPNEKEAREALGDEiNDDDELEAAGEKLLELLNLEALLVTLGEEGMTLFERDGEV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1356821756 247 YHLPTVAKEVFDVTGAGDTVISVLATALADGRSFEESCYLANVAAGIVVGKLGTSTVSTVELE 309
Cdd:cd01172 241 QHIPALAKEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGTAPVTPKELL 303
|
|
| rfaE_dom_II |
TIGR02199 |
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ... |
331-472 |
1.02e-85 |
|
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: 259.54 E-value: 1.02e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 331 AVAQAKARGEKIVMTNGCFDILHPGHISYLENARKLGDRLIVAVNSDDSVKRLKGESRPINNLENRMAVLAGLASVDWLV 410
Cdd:TIGR02199 2 LVARARARGKKIVFTNGCFDILHAGHVSYLQQARALGDRLVVGVNSDASVKRLKGETRPINPEEDRAEVLAALSSVDYVV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1356821756 411 PFTEDTPQRLIGEILPDLLVKGGDYKPEEIAGSKEVWANGGDVKVLNFENGCSTTNVIEKIK 472
Cdd:TIGR02199 82 IFDEDTPEELIGELKPDILVKGGDYKVETLVGAELVESYGGQVVLLPFVEGRSTTAIIEKIL 143
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
12-302 |
9.88e-45 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 158.28 E-value: 9.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 12 KVLVLGDVMLDRYwfgatnRISPEAPVPVVRVQENEERAGGA-ANVAMNIASLNVPVQLMGLIGQDETGSALSHLLEKQK 90
Cdd:pfam00294 1 KVVVIGEANIDLI------GNVEGLPGELVRVSTVEKGPGGKgANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 91 IDCNFV-ALETHPTITKLRILSRHQQLLRLDFEEDFNNVDcKDLLAKLESAVKNYGALILSDYGKGTLKD--VQKMIQIA 167
Cdd:pfam00294 75 VDTDYVvIDEDTRTGTALIEVDGDGERTIVFNRGAAADLT-PEELEENEDLLENADLLYISGSLPLGLPEatLEELIEAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 168 RKAN--VPVLIDPKGTDFERYR----GATLLTPNMSEFEAVVGKC-NTEEEIIKKGLKLISDIeLTALLVTRSEKGmTLL 240
Cdd:pfam00294 154 KNGGtfDPNLLDPLGAAREALLellpLADLLKPNEEELEALTGAKlDDIEEALAALHKLLAKG-IKTVIVTLGADG-ALV 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1356821756 241 RPNQEPYHLPTVAK-EVFDVTGAGDTVISVLATALADGRSFEESCYLANVAAGIVVGKLGTST 302
Cdd:pfam00294 232 VEGDGEVHVPAVPKvKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
12-302 |
1.64e-34 |
|
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: 131.16 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 12 KVLVLGDVMLDRYwfgATNRISPEaPVPVVRVQENEERAGG-AANVAMNIASLNVPVQLMGLIGQDETGSALSHLLEKQK 90
Cdd:COG0524 1 DVLVIGEALVDLV---ARVDRLPK-GGETVLAGSFRRSPGGaAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 91 IDCNFVA-LETHPTITKLRILSRHQQLLRLDFEEDFNNVDCKDLLaklESAVKNYGALILSDY---GKGTLKDVQKMIQI 166
Cdd:COG0524 77 VDTSGVRrDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLD---EALLAGADILHLGGItlaSEPPREALLAALEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 167 ARKANVPVLIDP--KGTDFERYR--------GATLLTPNMSEFEAVVGKCNTEE---EIIKKGLKLIsdieltalLVTRS 233
Cdd:COG0524 154 ARAAGVPVSLDPnyRPALWEPARellrellaLVDILFPNEEEAELLTGETDPEEaaaALLARGVKLV--------VVTLG 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1356821756 234 EKGMTLLRPNQEpYHLPTVAKEVFDVTGAGDTVISVLATALADGRSFEESCYLANVAAGIVVGKLGTST 302
Cdd:COG0524 226 AEGALLYTGGEV-VHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQP 293
|
|
| RfaE_N |
cd02172 |
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ... |
337-471 |
4.81e-33 |
|
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: 122.14 E-value: 4.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 337 ARGEKIVMTNGCFDILHPGHISYLENARKLGDRLIVAVNSDDSVKRLKGesRPINNLENRMAVLAGLASVDWLVPFTEDT 416
Cdd:cd02172 1 QRGKTVVLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVNKGPG--RPIFPEDLRAEVLAALGFVDYVVLFDNPT 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1356821756 417 PQRLIGEILPDLLVKGGDYK------PEEIAGSKE-VWANGGDVkVLNFENGCSTTNVIEKI 471
Cdd:cd02172 79 ALEIIDALQPNIYVKGGDYEnpendvTGKIAPEAEaVKAYGGKI-VFTGEIVFSSSALINRI 139
|
|
| TagD |
COG0615 |
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ... |
341-471 |
4.04e-29 |
|
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: 110.96 E-value: 4.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 341 KIVMTNGCFDILHPGHISYLENARKLGDRLIVAVNSDDSVKrLKGEsRPINNLENRMAVLAGLASVDWLVPFTEDTPQRL 420
Cdd:COG0615 1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVA-SKGR-KPIIPEEQRKEIVEALKYVDEVILGEEWDKFED 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1356821756 421 IGEILPDLLVKGGDYKPEEIAGSKEVWANGGDVKVLNFEN--GCSTTNVIEKI 471
Cdd:COG0615 79 IEEIKPDVIVLGDDWKGDFDFLKEELEKRGIGCEVVYLPRteGISSTKIKKRI 131
|
|
| cytidylyltransferase |
cd02170 |
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ... |
340-474 |
8.09e-26 |
|
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: 101.98 E-value: 8.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 340 EKIVMTNGCFDILHPGHISYLENARKLGDRLIVAVNSDDSVKRLKGesRPINNLENRMAVLAGLASVDWLVPFTEDTPQR 419
Cdd:cd02170 1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKR--RPILPEEQRAEVVEALKYVDEVILGHPWSYFK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1356821756 420 LIGEILPDLLVKGGDYKPEEI--AGSKEVWANGGDVKV-LNFENGCSTTNVIEKIKLL 474
Cdd:cd02170 79 PLEELKPDVIVLGDDQKNGVDeeEVYEELKKRGKVIEVpRKKTEGISSSDIIKRILEL 136
|
|
| CTP_transf_like |
pfam01467 |
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ... |
344-470 |
8.53e-24 |
|
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: 96.62 E-value: 8.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 344 MTNGCFDILHPGHISYLENARKLGDR-LIVAVNSDDSVKRLKgesRPINNLENRMAVLAGLASVDWLVPFTEDTPQR-LI 421
Cdd:pfam01467 1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPPHKLK---RPLFSAEERLEMLELAKWVDEVIVVAPWELTReLL 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1356821756 422 GEILPDLLVKGGD------YKPEEIAGSKEVWANGGDV--KVLNFENGCSTTNVIEK 470
Cdd:pfam01467 78 KELNPDVLVIGADslldfwYELDEILGNVKLVVVVRPVffIPLKPTNGISSTDIRER 134
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
12-293 |
8.79e-24 |
|
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: 100.85 E-value: 8.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 12 KVLVLGDVMLDRYwFGATNRISPEAPVPVVRVQEneerAGGAA-NVAMNIASLNVPVQLMGLIGQDETGSALSHLLEKQK 90
Cdd:cd01941 1 EIVVIGAANIDLR-GKVSGSLVPGTSNPGHVKQS----PGGVGrNIAENLARLGVSVALLSAVGDDSEGESILEESEKAG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 91 IDCNFVALETHPTITKLRILSRHQQLLRLDFEEDFNNVDCKDLLAKLESAVKNYGALIL-SDYGKGTLKDVqkmIQIARK 169
Cdd:cd01941 76 LNVRGIVFEGRSTASYTAILDKDGDLVVALADMDIYELLTPDFLRKIREALKEAKPIVVdANLPEEALEYL---LALAAK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 170 ANVPVLIDPKGTD-----FERYRGATLLTPNMSEFEAVVGKCNTEEEIIKKGLKLISDIELTALLVTRSEKG--MTLLRP 242
Cdd:cd01941 153 HGVPVAFEPTSAPklkklFYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGvlLSSREG 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1356821756 243 NQEPYHLPTVA-KEVFDVTGAGDTVISVLATALADGRSFEESCYLANVAAGI 293
Cdd:cd01941 233 GVETKLFPAPQpETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAAL 284
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
40-292 |
8.36e-22 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 95.59 E-value: 8.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 40 VVRVQENEERAGG-AANVAMNIASLNVPVQLMGLIGqDETGSALSHLLEKQKIDCNFVAL--EThPTITKLRILSRHQQL 116
Cdd:COG1105 24 VNRASEVRLDPGGkGINVARVLKALGVDVTALGFLG-GFTGEFIEELLDEEGIPTDFVPIegET-RINIKIVDPSDGTET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 117 lrldfeeDFNN-------VDCKDLLAKLESAVKNYGALILSdygkGTL------KDVQKMIQIARKANVPVLIDPKGTDF 183
Cdd:COG1105 102 -------EINEpgpeiseEELEALLERLEELLKEGDWVVLS----GSLppgvppDFYAELIRLARARGAKVVLDTSGEAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 184 E---RYrGATLLTPNMSEFEAVVG-KCNTEEEIIKKGLKLI-SDIEltALLVTRSEKGMtLLRPNQEPYHLPTVAKEVFD 258
Cdd:COG1105 171 KaalEA-GPDLIKPNLEELEELLGrPLETLEDIIAAARELLeRGAE--NVVVSLGADGA-LLVTEDGVYRAKPPKVEVVS 246
|
250 260 270
....*....|....*....|....*....|....
gi 1356821756 259 VTGAGDTVISVLATALADGRSFEESCYLAnVAAG 292
Cdd:COG1105 247 TVGAGDSMVAGFLAGLARGLDLEEALRLA-VAAG 279
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
12-300 |
1.63e-19 |
|
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: 88.76 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 12 KVLVLGDVMLDRYWFgaTNRIspeaPVP--VVRVQENEERAGG-AANVAMNIASLNVPVQLMGLIGQDETGSALSHLLEK 88
Cdd:cd01174 1 KVVVVGSINVDLVTR--VDRL----PKPgeTVLGSSFETGPGGkGANQAVAAARLGARVAMIGAVGDDAFGDELLENLRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 89 QKIDCNFV-ALETHPTITKL---------RIL------SRHQQLLRLDFEEDFnnVDCKDLLAKLESavknygalilsdy 152
Cdd:cd01174 75 EGIDVSYVeVVVGAPTGTAVitvdesgenRIVvvpganGELTPADVDAALELI--AAADVLLLQLEI------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 153 gkgTLKDVQKMIQIARKANVPVLIDP---KGTDFERYRGATLLTPNMSEFEAVVGKCNTEEEIIKKGLKLISDIELTALL 229
Cdd:cd01174 140 ---PLETVLAALRAARRAGVTVILNPapaRPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVI 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1356821756 230 VTRSEKGmTLLRPNQEPYHLPTVAKEVFDVTGAGDTVISVLATALADGRSFEESCYLANVAAGIVVGKLGT 300
Cdd:cd01174 217 VTLGAKG-ALLASGGEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGA 286
|
|
| cyt_tran_rel |
TIGR00125 |
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ... |
342-408 |
7.81e-19 |
|
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: 80.43 E-value: 7.81e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1356821756 342 IVMTNGCFDILHPGHISYLENARKLGDRLIVAVNSDDSVKRLKGEsrPINNLENRMAVLAGLASVDW 408
Cdd:TIGR00125 1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGE--PVFSLEERLEMLKALKYVDE 65
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
40-300 |
9.34e-19 |
|
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: 86.43 E-value: 9.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 40 VVRVQENEERAGG-AANVAMNIASLNVPVQLMGLIGQDeTGSALSHLLEKQKIDCNFVALEThPTITKLRILSRHQQLLR 118
Cdd:cd01164 25 VNRVSSTRKDAGGkGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVEVAG-ETRINVKIKEEDGTETE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 119 LDF------EEDFNNvdckdLLAKLESAVKNYGALILSdyG---KGTLKDV-QKMIQIARKANVPVLIDpkgTDFERYR- 187
Cdd:cd01164 103 INEpgpeisEEELEA-----LLEKLKALLKKGDIVVLS--GslpPGVPADFyAELVRLAREKGARVILD---TSGEALLa 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 188 ----GATLLTPNMSEFEAVVGK-CNTEEEIIKKGLKLISD-IELtaLLVTRSEKGMTLLRPNqEPYHLPTVAKEVFDVTG 261
Cdd:cd01164 173 alaaKPFLIKPNREELEELFGRpLGDEEDVIAAARKLIERgAEN--VLVSLGADGALLVTKD-GVYRASPPKVKVVSTVG 249
|
250 260 270
....*....|....*....|....*....|....*....
gi 1356821756 262 AGDTVISVLATALADGRSFEESCYLANVAAGIVVGKLGT 300
Cdd:cd01164 250 AGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGT 288
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
12-299 |
1.06e-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: 86.15 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 12 KVLVLGDVMLDRYwfgatnrispeaPVPVVRVQENEERAGGA-ANVAMNIASLNVPVQLMGLIGQDETGSALSHLLEKQK 90
Cdd:cd01167 1 KVVCFGEALIDFI------------PEGSGAPETFTKAPGGApANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 91 IDCNFVALETH--PTITKLRILSRHQqllrLDFEedFNNVDCKDLLAKLESAVK--------NYGALILSDygkGTLKD- 159
Cdd:cd01167 69 VDTRGIQFDPAapTTLAFVTLDADGE----RSFE--FYRGPAADLLLDTELNPDllseadilHFGSIALAS---EPSRSa 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 160 VQKMIQIARKANVPVLIDPKgtdferYRGAtLLTPNMSEFEAV--------VGKCNTEE-------EIIKKGLKLISDIE 224
Cdd:cd01167 140 LLELLEAAKKAGVLISFDPN------LRPP-LWRDEEEARERIaelleladIVKLSDEElellfgeEDPEEIAALLLLFG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 225 LTALLVTRSEKGMTLLRPNQEpYHLPTVAKEVFDVTGAGDTVISVLATALA-------DGRSFEESCYLANVAAGIVVGK 297
Cdd:cd01167 213 LKLVLVTRGADGALLYTKGGV-GEVPGIPVEVVDTTGAGDAFVAGLLAQLLsrgllalDEDELAEALRFANAVGALTCTK 291
|
..
gi 1356821756 298 LG 299
Cdd:cd01167 292 AG 293
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
13-301 |
1.92e-17 |
|
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: 82.36 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 13 VLVLGDVMLDRYWFG-ATNRISPEAPVPVVRvqenEERAGGAANVAMNIASLNVPVQLMGLIGQDETGSALSHLLEKQKI 91
Cdd:cd01942 2 VAVVGHLNYDIILKVeSFPGPFESVLVKDLR----REFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 92 DCNFVALE---------THPTITKLRILSRHQ---QLLRLDFEEDFnnvdckDLLAKLESAVKNYGALILSdygkgtlkd 159
Cdd:cd01942 78 DTSHVRVVdedstgvafILTDGDDNQIAYFYPgamDELEPNDEADP------DGLADIVHLSSGPGLIELA--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 160 vqkmiQIARKANVPVLIDPkGTDFERYRGATL---------LTPNMSEFEAVVGKCNTEEEIIKKGLKLIsdieltalLV 230
Cdd:cd01942 143 -----RELAAGGITVSFDP-GQELPRLSGEELeeileradiLFVNDYEAELLKERTGLSEAELASGVRVV--------VV 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1356821756 231 TRSEKGMTLLRPNQEPYHLPTVAKEVFDVTGAGDTVISVLATALADGRSFEESCYLANVAAGIVVGKLGTS 301
Cdd:cd01942 209 TLGPKGAIVFEDGEEVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| ECT |
cd02173 |
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ... |
339-401 |
7.42e-16 |
|
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: 74.60 E-value: 7.42e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1356821756 339 GEKIVMTNGCFDILHPGHISYLENARKLGDRLIVAVNSDDSVKRLKGESRPINNLENR-MAVLA 401
Cdd:cd02173 1 GDKVVYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSNYPIMNLHERvLSVLA 64
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
133-275 |
2.03e-15 |
|
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: 74.44 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 133 LLAKL--ESAVKNYGALILSDYGKGtLKDVQKMIQIARKANVPVLIDP--------KGTDFERYRGATLLTPNMSEFEAV 202
Cdd:cd00287 45 ALARLgvSVTLVGADAVVISGLSPA-PEAVLDALEEARRRGVPVVLDPgpravrldGEELEKLLPGVDILTPNEEEAEAL 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1356821756 203 VGKCNTEEEIIKKGLKLISDIELTALLVTRSEKGMTLLRPNQEPYHLPTVAKEVFDVTGAGDTVISVLATALA 275
Cdd:cd00287 124 TGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
12-299 |
1.39e-13 |
|
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: 70.52 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 12 KVLVLGDVMLDRYWFGAtnriSPEAPVPVVRVQENEER-AGGAANVAMNIASLNVPVQLMGLIGQDETGSALSHLLEkQK 90
Cdd:cd01947 1 KIAVVGHVEWDIFLSLD----APPQPGGISHSSDSRESpGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELE-SG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 91 IDCNFVALETHPTITKLRILSRHQQLL------RLDFEEDFNNVDCKDLLaklesavknygalilsdYGKGTLKDVqKMI 164
Cdd:cd01947 76 GDKHTVAWRDKPTRKTLSFIDPNGERTitvpgeRLEDDLKWPILDEGDGV-----------------FITAAAVDK-EAI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 165 QIARKANVPVLIDPKGTDFERY----RGATLLTPNMSEFEAVVgkcnTEEEIIKKGLKLisdieltaLLVTRSEKGMTLL 240
Cdd:cd01947 138 RKCRETKLVILQVTPRVRVDELnqalIPLDILIGSRLDPGELV----VAEKIAGPFPRY--------LIVTEGELGAILY 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1356821756 241 rPNQEPYHLPTVAKEVFDVTGAGDTVISVLATALADGRSFEESCYLANVAAGIVVGKLG 299
Cdd:cd01947 206 -PGGRYNHVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFG 263
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
13-301 |
2.12e-13 |
|
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: 70.72 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 13 VLVLGDVMLDRYWFGATNRISPEAPV--PVVRVQENEERAGG-AANVAMNIASLNVPVQLMGLIGQDETGSALSHLLEKQ 89
Cdd:cd01168 15 LAQVDDAFLEKLGLKKGDMILADMEEqeELLAKLPVKYIAGGsAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 90 KIDCNFVALETHPTITKLRILSR-HQQLLR--LDFEEDFNNVDCKdlLAKLESAVKNY--GALILSDygkgtLKDVQKMI 164
Cdd:cd01168 95 GVDTRYQVQPDGPTGTCAVLVTPdAERTMCtyLGAANELSPDDLD--WSLLAKAKYLYleGYLLTVP-----PEAILLAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 165 QIARKANVPV---LIDPKGTDFerYR--------GATLLTPNMSEFEAVVGKCNTE-EEIIKKGLKLISDIeltaLLVTR 232
Cdd:cd01168 168 EHAKENGVKIalnLSAPFIVQR--FKeallellpYVDILFGNEEEAEALAEAETTDdLEAALKLLALRCRI----VVITQ 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1356821756 233 SEKGmTLLRPNQEPYHLPTVAKE-VFDVTGAGDT-VISVLAtALADGRSFEESCYLANVAAGIVVGKLGTS 301
Cdd:cd01168 242 GAKG-AVVVEGGEVYPVPAIPVEkIVDTNGAGDAfAGGFLY-GLVQGEPLEECIRLGSYAAAEVIQQLGPR 310
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
339-471 |
1.03e-12 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 69.04 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 339 GEKIVMTNGCFDILHPGHISYLENARKLGDRLIVAVNSDDSVKRLKGESRPINNLENRmaVLAGLAS--VDWLV---PFt 413
Cdd:PTZ00308 191 GDRIVYVDGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQVVNEQKGSNYPIMNLNER--VLGVLSCryVDEVVigaPF- 267
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1356821756 414 eDTPQRLIGEILPDLLVKGGDYKPEEIAGSKEVWA---NGGDVKVLNFENGCSTTNVIEKI 471
Cdd:PTZ00308 268 -DVTKEVIDSLHINVVVGGKFSDLVNEEGGSDPYEvpkAMGIFKEVDSGCDLTTDSIVDRV 327
|
|
| PLN02406 |
PLN02406 |
ethanolamine-phosphate cytidylyltransferase |
343-434 |
6.78e-12 |
|
ethanolamine-phosphate cytidylyltransferase
Pssm-ID: 215227 [Multi-domain] Cd Length: 418 Bit Score: 67.01 E-value: 6.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 343 VMTNGCFDILHPGHISYLENARKLGDRLIVAVNSDDSVKRLKGEsrPINNLENRMAVLAGLASVDWLVP-----FTEDTP 417
Cdd:PLN02406 56 VYMDGCFDMMHYGHANALRQARALGDELVVGVVSDEEIIANKGP--PVTPMHERMIMVSGVKWVDEVIPdapyaITEEFM 133
|
90
....*....|....*..
gi 1356821756 418 QRLIGEILPDLLVKGGD 434
Cdd:PLN02406 134 NKLFNEYNIDYIIHGDD 150
|
|
| G3P_Cytidylyltransferase |
cd02171 |
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ... |
340-474 |
1.07e-11 |
|
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: 62.12 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 340 EKIVMTNGCFDILHPGHISYLENARKLGDRLIVAVnSDDSVKRLKGEsRPINNLENRMAVLAGLASVDWLVPFT--EDTP 417
Cdd:cd02171 1 MKVVITYGTFDLLHIGHLNLLERAKALGDKLIVAV-STDEFNAGKGK-KAVIPYEQRAEILESIRYVDLVIPETnwEQKI 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1356821756 418 QRLIGEILpDLLVKGGDYKpeeiaGSKEVWANGGDVKVLNFENGCSTTNVIEKIKLL 474
Cdd:cd02171 79 EDIKKYNV-DVFVMGDDWE-----GKFDFLKEYCEVVYLPRTKGISSTQLKEMLKKL 129
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
51-302 |
2.06e-11 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 65.14 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 51 GGAANVAMNIASLNVPVQLMGLIGQDETGSALSHLLEKQKIDCNFVA-LETHPT----ITKLRILSRHQ----------- 114
Cdd:PTZ00292 53 GKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSrTENSSTglamIFVDTKTGNNEiviipgannal 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 115 --QLLRlDFEEDFNNVdCKDLLAKLESAVK-NYGALilsdyGKGTLKDVQKMIQIARKANVPVLidPKGTDFERYrgATL 191
Cdd:PTZ00292 133 tpQMVD-AQTDNIQNI-CKYLICQNEIPLEtTLDAL-----KEAKERGCYTVFNPAPAPKLAEV--EIIKPFLKY--VSL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 192 LTPNMSEFEAVVGKCNTEEEIIKKGLKLISDIELTALLVTRSEKGMTLLRPNQEPYHLPTVAKEVFDVTGAGDTVISVLA 271
Cdd:PTZ00292 202 FCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEKENEPVHVPGKRVKAVDTTGAGDCFVGSMA 281
|
250 260 270
....*....|....*....|....*....|.
gi 1356821756 272 TALADGRSFEESCYLANVAAGIVVGKLGTST 302
Cdd:PTZ00292 282 YFMSRGKDLKESCKRANRIAAISVTRHGTQS 312
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
132-299 |
3.11e-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: 63.98 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 132 DLLAKLESAVKNY-----GALILSDYGKGTLKDVQKMIQiarkANVPVLIDPKGTDFERYRG--------ATLLTPNMSE 198
Cdd:cd01944 116 EWFATLTVAPYDYvylsgYTLASENASKVILLEWLEALP----AGTTLVFDPGPRISDIPDTilqalmakRPIWSCNREE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 199 FEAVVGKCNTEEEIIKKGLKLisdiELTALLVTRS-EKGMTLLRPNQEPYHLPTVAKEVFDVTGAGDTVISVLATALADG 277
Cdd:cd01944 192 AAIFAERGDPAAEASALRIYA----KTAAPVVVRLgSNGAWIRLPDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKG 267
|
170 180
....*....|....*....|..
gi 1356821756 278 RSFEESCYLANVAAGIVVGKLG 299
Cdd:cd01944 268 MSLADAVLLANAAAAIVVTRSG 289
|
|
| CCT |
cd02174 |
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ... |
347-411 |
3.95e-10 |
|
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: 57.96 E-value: 3.95e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1356821756 347 GCFDILHPGHISYLENARKLG--DRLIVAVNSDDSVKRLKGesRPINNLENRMAVLAGLASVDWLVP 411
Cdd:cd02174 9 GCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKG--PPVMTEEERYEAVRHCKWVDEVVE 73
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
336-473 |
1.34e-09 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 59.80 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 336 KARGEKIVMTNGCFDILHPGHISYLENARKLGDRLIVAVNSDDSVKRLKGEsrPINNLENRMAVLAGLASVDWLV---PF 412
Cdd:PTZ00308 7 KKPGTIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGP--PVMHQEERYEALRACKWVDEVVegyPY 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1356821756 413 T--EDTPQRLigEIlpDLLVKGGDYkpeeiagskEVWANGGDV----------KVLNFENGCSTTNVIEKIKL 473
Cdd:PTZ00308 85 TtrLEDLERL--EC--DFVVHGDDI---------SVDLNGRNSyqeiidagkfKVVKRTEGISTTDLVGRMLL 144
|
|
| PLN02406 |
PLN02406 |
ethanolamine-phosphate cytidylyltransferase |
341-401 |
5.69e-09 |
|
ethanolamine-phosphate cytidylyltransferase
Pssm-ID: 215227 [Multi-domain] Cd Length: 418 Bit Score: 58.16 E-value: 5.69e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1356821756 341 KIVMTNGCFDILHPGHISYLENARKLGDRLIVAVNSDDSVKRLKGESRPINNLENR-MAVLA 401
Cdd:PLN02406 252 RIVYIDGAFDLFHAGHVEILRLARALGDFLLVGIHTDQTVSAHRGAHRPIMNLHERsLSVLA 313
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
48-291 |
3.40e-08 |
|
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: 54.61 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 48 ERAGG-AANVAMNIASLNVPVQLMGLIGQDETGSALSHLLEKQKIDCNF------------VALETHPTITKLRILSRHQ 114
Cdd:cd01945 33 VIGGGnAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFivvapgarspisSITDITGDRATISITAIDT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 115 QLLRLDFEEDfnnvdckdllaklesAVKNYGALILSDYGKGTLKDVqkmIQIARKANVPVLIDPKG---TDFER-YRGAT 190
Cdd:cd01945 113 QAAPDSLPDA---------------ILGGADAVLVDGRQPEAALHL---AQEARARGIPIPLDLDGgglRVLEElLPLAD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 191 LLTPnmSE-FEAVVGKCNTEEEiikkgLKLISDIELTALLVTRSEKGMTLLRPNQEPYHLPTVAKEVFDVTGAGDTVISV 269
Cdd:cd01945 175 HAIC--SEnFLRPNTGSADDEA-----LELLASLGIPFVAVTLGEAGCLWLERDGELFHVPAFPVEVVDTTGAGDVFHGA 247
|
250 260
....*....|....*....|..
gi 1356821756 270 LATALADGRSFEESCYLANVAA 291
Cdd:cd01945 248 FAHALAEGMPLREALRFASAAA 269
|
|
| PRK00777 |
PRK00777 |
pantetheine-phosphate adenylyltransferase; |
343-400 |
1.02e-07 |
|
pantetheine-phosphate adenylyltransferase;
Pssm-ID: 234834 Cd Length: 153 Bit Score: 51.37 E-value: 1.02e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1356821756 343 VMTNGCFDILHPGHISYLENARKLGDRLIVAVNSDDSVKRLKGesRPINNLENRMAVL 400
Cdd:PRK00777 4 VAVGGTFDPLHDGHRALLRKAFELGKRVTIGLTSDEFAKSYKK--HKVRPYEVRLKNL 59
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
191-307 |
1.08e-06 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 50.42 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 191 LLTPNMSEFEAVVG-KCNTEEEIIKKGLKLISDIELTALLvtrSEKGMTLLR-----------PNQEPYHLP---TVAKE 255
Cdd:cd01943 183 VFSPNLEEAARLLGlPTSEPSSDEEKEAVLQALLFSGILQ---DPGGGVVLRcgklgcyvgsaDSGPELWLPayhTKSTK 259
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1356821756 256 VFDVTGAGDTVISVLATALADGRSFEESCYLANVAAGIVVGKLGTSTVSTVE 307
Cdd:cd01943 260 VVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVGLPRLTKVE 311
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
51-299 |
1.48e-06 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 49.87 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 51 GGAANVAMNIASLNVPVQLMGLIGQDETGSALSHLLEKQKIDCNFV-ALETHPTITKL---------------------- 107
Cdd:PRK11142 40 GKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVsVIKGESTGVALifvndegensigihaganaalt 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 108 -RILSRHQQLLRldfeedfnNVDCkdLLAKLESAvknygalilsdygkgtLKDVQKMIQIARKANVPVLIDP----KGTD 182
Cdd:PRK11142 120 pALVEAHRELIA--------NADA--LLMQLETP----------------LETVLAAAKIAKQHGTKVILNPaparELPD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 183 fERYRGATLLTPNMSEFEAVVGKCNTEEEIIKKGLKLISDIELTALLVTRSEKGMTLLRPNQEPYhLPTVAKEVFDVTGA 262
Cdd:PRK11142 174 -ELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGEGQR-VPGFRVQAVDTIAA 251
|
250 260 270
....*....|....*....|....*....|....*..
gi 1356821756 263 GDTVISVLATALADGRSFEESCYLANVAAGIVVGKLG 299
Cdd:PRK11142 252 GDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKG 288
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
168-287 |
5.72e-05 |
|
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.
Pssm-ID: 430062 [Multi-domain] Cd Length: 246 Bit Score: 44.39 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 168 RKANVPVLIDP----KGTD-------FERYRG-----ATLLTPNMSEFEAVVG-KCNTEEEiIKKGLKLISDIELTALLV 230
Cdd:pfam08543 83 DKYGVPVVLDPvmvaKSGDsllddeaIEALKEellplATLITPNLPEAEALTGrKIKTLED-MKEAAKKLLALGAKAVLI 161
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1356821756 231 T------RSEKGMTLLRPNQEPYHLPTvakEVFDVT---GAGDTVISVLATALADGRSFEESCYLA 287
Cdd:pfam08543 162 KgghlegEEAVVTDVLYDGGGFYTLEA---PRIPTKnthGTGCTLSAAIAANLAKGLSLPEAVREA 224
|
|
| Pantoate_ligase |
pfam02569 |
Pantoate-beta-alanine ligase; Pantoate-beta-alanine ligase, also know as pantothenate synthase, ... |
326-375 |
6.30e-05 |
|
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: 44.72 E-value: 6.30e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1356821756 326 AELKDAVAQAKARGEKI--VMTNGCfdiLHPGHISYLENARKLGDRLIVA--VN 375
Cdd:pfam02569 7 AELRAWLRAWRRAGKTIglVPTMGA---LHEGHLSLVRRARAENDVVVVSifVN 57
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
132-288 |
2.64e-04 |
|
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.
Pssm-ID: 238578 [Multi-domain] Cd Length: 254 Bit Score: 42.57 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 132 DLLAKLES--AVKNYGAlILSDY--GKGTLKDVQKMIQIARKAN--VPVLIDP------KGTDF-----ERYR-----GA 189
Cdd:cd01173 59 DLLEGLEAlgLLLEYDA-VLTGYlgSAEQVEAVAEIVKRLKEKNpnLLYVCDPvmgdngKLYVVaeeivPVYRdllvpLA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 190 TLLTPNMSEFEAVVG-KCNTEEEIIKKGLKLISD----IELTALLVTRSEKGMTLLRPNQEPYHL--PTVAKEvFDVTGA 262
Cdd:cd01173 138 DIITPNQFELELLTGkKINDLEDAKAAARALHAKgpktVVVTSVELADDDRIEMLGSTATEAWLVqrPKIPFP-AYFNGT 216
|
170 180
....*....|....*....|....*.
gi 1356821756 263 GDTVISVLATALADGRSFEESCYLAN 288
Cdd:cd01173 217 GDLFAALLLARLLKGKSLAEALEKAL 242
|
|
| PRK01170 |
PRK01170 |
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase; |
341-397 |
3.33e-04 |
|
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
Pssm-ID: 234912 [Multi-domain] Cd Length: 322 Bit Score: 42.50 E-value: 3.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1356821756 341 KIVMTNGCFDILHPGHISYLENARKLGDRLIVAVNSDDSVKRLKgeSRPIN------NLENRM 397
Cdd:PRK01170 1 MITVVGGTFSKLHKGHKALLKKAIETGDEVVIGLTSDEYVRKNK--VYPIPyedrkrKLENFI 61
|
|
| PanC |
cd00560 |
Pantoate-beta-alanine ligase; PanC Pantoate-beta-alanine ligase, also known as pantothenate ... |
326-374 |
4.00e-04 |
|
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: 42.14 E-value: 4.00e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1356821756 326 AELKDAVAQAKARGEKI--VMTNGCfdiLHPGHISYLENARKLGDRLIVAV 374
Cdd:cd00560 8 AELRAWLRNWRAQGKTIgfVPTMGA---LHEGHLSLVRRARAENDVVVVSI 55
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
222-309 |
1.16e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 40.95 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 222 DIE----LTALLVTRSEKGMTLLRPNQEPYHLPTVAKEVfDVTGAGDTVISVLATALADGRSFEESCYLANVAAGIVVGK 297
Cdd:PLN02630 196 DVEevrqKCCVIVTNGKKGCRIYWKDGEMRVPPFPAIQV-DPTGAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLAVEQ 274
|
90
....*....|..
gi 1356821756 298 LGTSTVSTVELE 309
Cdd:PLN02630 275 VGIPKFDLRQLQ 286
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
170-287 |
1.46e-03 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 40.74 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 170 ANVPVLIDPK-----GTDFERYRGATLLTPNMSEFEAVVGKCNTEEEIIKKGLKLISDIELTALLVTRSEKGMTLLRPNQ 244
Cdd:PRK09850 157 ANVPVFVDPVsawkcVKVRDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYSDISG 236
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1356821756 245 EPYHLPTVAKEVFDVTGAGDTVISVLATALADGRSFEESCYLA 287
Cdd:PRK09850 237 ESGWSAPIKTNVINVTGAGDAMMAGLASCWVDGMPFAESVRFA 279
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
168-291 |
2.20e-03 |
|
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: 39.69 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 168 RKANVPVLIDPKG-----TDFERYRGATLLTP---NMSEFEAVVgkCNTEEEIIKKGLKLISDIeltaLLVTRSEKGMTL 239
Cdd:cd01937 125 FRKFAFISLDAQGflrraNQEKLIKCVILKLHdvlKLSRVEAEV--ISTPTELARLIKETGVKE----IIVTDGEEGGYI 198
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1356821756 240 LRPNQePYHLPTVAKEVFDVTGAGDT-VISVLATALADGRSFEESCYLANVAA 291
Cdd:cd01937 199 FDGNG-KYTIPASKKDVVDPTGAGDVfLAAFLYSRLSGKDIKEAAEFAAAAAA 250
|
|
| PPAT_CoAS |
cd02164 |
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ... |
342-400 |
3.07e-03 |
|
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; The PPAT domain of the bifunctional enzyme with PPAT and DPCK functions. The final two steps of the CoA biosynthesis pathway are catalyzed by phosphopantetheine adenylyltransferase (PPAT) and dephospho-CoA (dPCoA) kinase (DPCK). The PPAT reaction involves the reversible adenylation of 4'-phosphopantetheine to form 3'-dPCoA and PPi, and DPCK catalyses phosphorylation of the 3'-hydroxy group of the ribose moiety of dPCoA. In eukaryotes the two enzymes are part of a large multienzyme complex . Studies in Corynebacterium ammoniagenes suggested that separate enzymes were present, and this was confirmed through identification of the bacterial PPAT/CoAD.
Pssm-ID: 173915 Cd Length: 143 Bit Score: 38.03 E-value: 3.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 342 IVMTNGCFDILHPGHISYLENARKLG-DRLIVAVNSDDSVKRlKGESRPINNLENRMAVL 400
Cdd:cd02164 1 KVAVGGTFDRLHDGHKILLSVAFLLAgEKLIIGVTSDELLKN-KSLKELIEPYEERIANL 59
|
|
| FAD_synthetase_N |
cd02064 |
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ... |
343-431 |
9.12e-03 |
|
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal domain of the bifunctional riboflavin biosynthesis protein riboflavin kinase/FAD synthetase. These enzymes have both ATP:riboflavin 5'-phosphotransferase and ATP:FMN-adenylyltransferase activities. The N-terminal domain is believed to play a role in the adenylylation reaction of FAD synthetases. The C-terminal domain is thought to have kinase activity. FAD synthetase is present among all kingdoms of life. However, the bifunctional enzyme is not found in mammals, which use separate enzymes for FMN and FAD formation.
Pssm-ID: 185679 [Multi-domain] Cd Length: 180 Bit Score: 37.13 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356821756 343 VMTNGCFDILHPGHISYLENARKLGDR--LIVAV----NSDDSVKRLKGESRPINNLENRMAVLAGLAsVDWL--VPFTE 414
Cdd:cd02064 2 VVAIGNFDGVHLGHQALIKTLKKIARErgLPSAVltfdPHPREVFLPDKAPPRLTTLEEKLELLESLG-VDYLlvLPFDK 80
|
90 100
....*....|....*....|.
gi 1356821756 415 D----TPQRLIGEILPDLLVK 431
Cdd:cd02064 81 EfaslSAEEFVEDLLVKLNAK 101
|
|
| |
