|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
1-473 |
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: 942.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 1 MKPILPDYNSAGVLIIGDVMLDRYWYGPTGRISPEAPVPVVKVENNEERPGGAANVAMNIASLGGHAHIVGLTGMDEPAK 80
Cdd:PRK11316 1 MKVTLPDFERAGVLVVGDVMLDRYWYGPTSRISPEAPVPVVKVNQIEERPGGAANVAMNIASLGAQARLVGLTGIDEAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 81 VLTETLNSLKVKCDFVALPDYPTITKLRVMSRGQQLIRLDFEDKFENTDAEPVLSRMETALPSVKAVIMSDYAKGSLEHV 160
Cdd:PRK11316 81 ALSKLLAAVGVKCDFVSVPTHPTITKLRVLSRNQQLIRLDFEEGFEGVDPQPLLERIEQALPSIGALVLSDYAKGALASV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 161 QAYIQKARAANIPVFIDPKGADFERYRGATLLTPNMKEFEDVVGKVKSEQELVEKALALVEEFEFEALLVTRSENGMTLI 240
Cdd:PRK11316 161 QAMIQLARKAGVPVLIDPKGTDFERYRGATLLTPNLSEFEAVVGKCKDEAELVEKGMKLIADYDLSALLVTRSEQGMTLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 241 RRGQEPFHLPTQAKEVYDVTGAGDTVISVLAASVAAGKSFEEACALANAAAGVVVGKLGTSTLSEIELAEAIHGSQDTDY 320
Cdd:PRK11316 241 QPGKAPLHLPTQAREVYDVTGAGDTVISVLAAALAAGNSLEEACALANAAAGVVVGKLGTSTVSPIELENALRGRAETGF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 321 GVISEQALIEAVKKARAKGEKVVMTNGCFDILHAGHVSYLNHAAELGDRLIVAVNTDDSVKRLKGPGRPVNPTDRRMAVL 400
Cdd:PRK11316 321 GVMSEEQLKLAVAQARARGEKIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEGRPVNPLEQRMAVL 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491592829 401 AGLGAVDWVVPFSEDTPQRLISEVLPSLLVKGGDYKPEEIAGGKEVIAAGGEVRVLNFEDGCSTSEIINAIKG 473
Cdd:PRK11316 401 AALEAVDWVVPFEEDTPQRLIAEILPDLLVKGGDYKPEEIAGSKEVWANGGEVKVLNFEDGCSTTNIIKKIRQ 473
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
1-310 |
6.49e-151 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 432.31 E-value: 6.49e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 1 MKPILPDYNSAGVLIIGDVMLDRYWYGPTGRISPEAPVPVVKVENNEERPGGAANVAMNIASLGGHAHIVGLTGMDEPAK 80
Cdd:COG2870 6 LKELLPRFSRARVLVVGDVMLDRYWYGDVERISPEAPVPVVRVEREEERPGGAANVAANLAALGAQVTLVGVVGDDEAGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 81 VLTETLNSLKVKCDFVALPDYP-TITKLRVMSRGQQLIRLDFEDKFENTDA--EPVLSRMETALPSVKAVIMSDYAKGSL 157
Cdd:COG2870 86 ELRRLLEEAGIDTDGLVVDPRRpTTTKTRVIAGGQQLLRLDFEDRFPLSAEleARLLAALEAALPEVDAVILSDYGKGVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 158 --EHVQAYIQKARAANIPVFIDPKGADFERYRGATLLTPNMKEFEDVVG-KVKSEQELVEKALALVEEFEFEALLVTRSE 234
Cdd:COG2870 166 tpELIQALIALARAAGKPVLVDPKGRDFSRYRGATLLTPNLKEAEAAVGiPIADEEELVAAAAELLERLGLEALLVTRGE 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491592829 235 NGMTLIRRGQEPFHLPTQAKEVYDVTGAGDTVISVLAASVAAGKSFEEACALANAAAGVVVGKLGTSTLSEIELAE 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 |
5.76e-149 |
|
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: 427.42 E-value: 5.76e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 4 ILPDYNSAGVLIIGDVMLDRYWYGPTGRISPEAPVPVVKVENNEERPGGAANVAMNIASLGGHAHIVGLTGMDEPAKVLT 83
Cdd:TIGR02198 1 LIASFKGAKVLVVGDVMLDRYWYGKVSRISPEAPVPVVKVEREEDRLGGAANVARNIASLGARVFLVGVVGDDEAGKRLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 84 ETLNSLKVKC-DFVALPDYPTITKLRVMSRGQQLIRLDFEDK--FENTDAEPVLSRMETALPSVKAVIMSDYAKGSLEH- 159
Cdd:TIGR02198 81 ALLAEEGIDTsGLIRDKDRPTTTKTRVLARNQQLLRVDFEERdpINAELEARLLAAIREQLASADAVVLSDYAKGVLTPr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 160 -VQAYIQKARAANIPVFIDPKGADFERYRGATLLTPNMKEFEDVVGKVKSEQELVEKALALVEEFEFEALLVTRSENGMT 238
Cdd:TIGR02198 161 vVQEVIAAARKHGKPVLVDPKGKDFSRYRGATLITPNRKEAEAAVGACDTEAELVQAAEKLLEELDLEALLVTRSEKGMT 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491592829 239 LIRRGQEPFHLPTQAKEVYDVTGAGDTVISVLAASVAAGKSFEEACALANAAAGVVVGKLGTSTLSEIELAEAIH 313
Cdd:TIGR02198 241 LFTREGEPIHIPAQAREVYDVTGAGDTVIATLALALAAGASLEEACRLANAAAGVVVGKLGTATVSPAELANALQ 315
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
13-310 |
1.82e-122 |
|
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: 359.57 E-value: 1.82e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 13 VLIIGDVMLDRYWYGPTGRISPEAPVPVVKVENNEERPGGAANVAMNIASLGGHAHIVGLTGMDEPAKVLTETLNSLKVK 92
Cdd:cd01172 2 VLVVGDVILDEYLYGDVERISPEAPVPVVKVEREEIRLGGAANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 93 CDFVALPDYPTITKLRVMSRGQQLIRLDFEDKFENTDAEP--VLSRMETALPSVKAVIMSDYAKGSL--EHVQAYIQKAR 168
Cdd:cd01172 82 TDGIVDEGRPTTTKTRVIARNQQLLRVDREDDSPLSAEEEqrLIERIAERLPEADVVILSDYGKGVLtpRVIEALIAAAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 169 AANIPVFIDPKGADFERYRGATLLTPNMKEFEDVVG-KVKSEQELVEKALALVEEFEFEALLVTRSENGMTLIRRGQEPF 247
Cdd:cd01172 162 ELGIPVLVDPKGRDYSKYRGATLLTPNEKEAREALGdEINDDDELEAAGEKLLELLNLEALLVTLGEEGMTLFERDGEVQ 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491592829 248 HLPTQAKEVYDVTGAGDTVISVLAASVAAGKSFEEACALANAAAGVVVGKLGTSTLSEIELAE 310
Cdd:cd01172 242 HIPALAKEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGTAPVTPKELLL 304
|
|
| rfaE_dom_II |
TIGR02199 |
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ... |
331-473 |
5.13e-77 |
|
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: 237.20 E-value: 5.13e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 331 AVKKARAKGEKVVMTNGCFDILHAGHVSYLNHAAELGDRLIVAVNTDDSVKRLKGPGRPVNPTDRRMAVLAGLGAVDWVV 410
Cdd:TIGR02199 2 LVARARARGKKIVFTNGCFDILHAGHVSYLQQARALGDRLVVGVNSDASVKRLKGETRPINPEEDRAEVLAALSSVDYVV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491592829 411 PFSEDTPQRLISEVLPSLLVKGGDYKPEEIAGGKEVIAAGGEVRVLNFEDGCSTSEIINAIKG 473
Cdd:TIGR02199 82 IFDEDTPEELIGELKPDILVKGGDYKVETLVGAELVESYGGQVVLLPFVEGRSTTAIIEKILK 144
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
13-302 |
2.59e-34 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 130.16 E-value: 2.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 13 VLIIGDVMLDRYwygptgRISPEAPVPVVKVENNEERPGGA-ANVAMNIASLGGHAHIVGLTGMDEPAKVLTETLNSLKV 91
Cdd:pfam00294 2 VVVIGEANIDLI------GNVEGLPGELVRVSTVEKGPGGKgANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 92 KCDFV-ALPDYPTITKLRVMSR-GQQLIRLDFED--KFENTDAEPVLSRMETALPSVKAVIMSDYAKGSLEHVQAYIQKA 167
Cdd:pfam00294 76 DTDYVvIDEDTRTGTALIEVDGdGERTIVFNRGAaaDLTPEELEENEDLLENADLLYISGSLPLGLPEATLEELIEAAKN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 168 RAANIPVFIDPKGADFERYR----GATLLTPNMKEFEDVVG-KVKSEQELVEKALALVEEFEfEALLVTRSENGMTLIRR 242
Cdd:pfam00294 156 GGTFDPNLLDPLGAAREALLellpLADLLKPNEEELEALTGaKLDDIEEALAALHKLLAKGI-KTVIVTLGADGALVVEG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 243 GQEPFHLPTQAKEVYDVTGAGDTVISVLAASVAAGKSFEEACALANAAAGVVVGKLGTST 302
Cdd:pfam00294 235 DGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| RfaE_N |
cd02172 |
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ... |
337-471 |
6.70e-34 |
|
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: 124.45 E-value: 6.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 337 AKGEKVVMTNGCFDILHAGHVSYLNHAAELGDRLIVAVNTDDSVKrlKGPGRPVNPTDRRMAVLAGLGAVDWVVPFSEDT 416
Cdd:cd02172 1 QRGKTVVLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVN--KGPGRPIFPEDLRAEVLAALGFVDYVVLFDNPT 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491592829 417 PQRLISEVLPSLLVKGGDYK------PEEIAGGKEVIAAGGEVRVLNFEDGCSTSEIINAI 471
Cdd:cd02172 79 ALEIIDALQPNIYVKGGDYEnpendvTGKIAPEAEAVKAYGGKIVFTGEIVFSSSALINRI 139
|
|
| TagD |
COG0615 |
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ... |
341-471 |
3.42e-30 |
|
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: 114.05 E-value: 3.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 341 KVVMTNGCFDILHAGHVSYLNHAAELGDRLIVAVNTDDSVKrLKGPgRPVNPTDRRMAVLAGLGAVDWVVPFSEDTPQRL 420
Cdd:COG0615 1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVA-SKGR-KPIIPEEQRKEIVEALKYVDEVILGEEWDKFED 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 491592829 421 ISEVLPSLLVKGGD--YKPEEIAGGKEVIAAGGEVRVLNFEDGCSTSEIINAI 471
Cdd:COG0615 79 IEEIKPDVIVLGDDwkGDFDFLKEELEKRGIGCEVVYLPRTEGISSTKIKKRI 131
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
13-282 |
4.03e-26 |
|
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: 107.66 E-value: 4.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 13 VLIIGDVMLDRYWYGPtgriSPEAPVPVVKVENNEERPGG-AANVAMNIASLGGHAHIVGLTGMDEPAKVLTETLNSLKV 91
Cdd:COG0524 2 VLVIGEALVDLVARVD----RLPKGGETVLAGSFRRSPGGaAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 92 KCDFVA-LPDYPTitklrvmsrGQQLIRLDFEDkfENT-----------DAEPVlsrMETALPSVKAVIMSDYAKGS--- 156
Cdd:COG0524 78 DTSGVRrDPGAPT---------GLAFILVDPDG--ERTivfyrganaelTPEDL---DEALLAGADILHLGGITLASepp 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 157 LEHVQAYIQKARAANIPVFIDP--KGADFERYR--------GATLLTPNMKEFEDVVGKvkseqELVEKALALVEEFEFE 226
Cdd:COG0524 144 REALLAALEAARAAGVPVSLDPnyRPALWEPARellrellaLVDILFPNEEEAELLTGE-----TDPEEAAAALLARGVK 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 491592829 227 ALLVTRSENGMTLIRRGQEpFHLPTQAKEVYDVTGAGDTVISVLAASVAAGKSFEE 282
Cdd:COG0524 219 LVVVTLGAEGALLYTGGEV-VHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEE 273
|
|
| cytidylyltransferase |
cd02170 |
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ... |
340-472 |
4.31e-25 |
|
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: 100.06 E-value: 4.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 340 EKVVMTNGCFDILHAGHVSYLNHAAELGDRLIVAVNTDDSVKRLKgpGRPVNPTDRRMAVLAGLGAVDWVVPFSEDTPQR 419
Cdd:cd02170 1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIK--RRPILPEEQRAEVVEALKYVDEVILGHPWSYFK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 491592829 420 LISEVLPSLLVKGGDYK-PEEIAGGKEVIAAGGEVRVLNFED--GCSTSEIINAIK 472
Cdd:cd02170 79 PLEELKPDVIVLGDDQKnGVDEEEVYEELKKRGKVIEVPRKKteGISSSDIIKRIL 134
|
|
| CTP_transf_like |
pfam01467 |
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ... |
344-470 |
1.75e-19 |
|
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: 84.29 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 344 MTNGCFDILHAGHVSYLNHAAELGDR-LIVAVNTDDSVKRLKgpgRPVNPTDRRMAVLAGLGAVDWVVPFSEDTPQR-LI 421
Cdd:pfam01467 1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPPHKLK---RPLFSAEERLEMLELAKWVDEVIVVAPWELTReLL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 422 SEVLPSLLVKGGD------YKPEEIAGGKEVIaagGEVR-----VLNFEDGCSTSEIINA 470
Cdd:pfam01467 78 KELNPDVLVIGADslldfwYELDEILGNVKLV---VVVRpvffiPLKPTNGISSTDIRER 134
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
13-277 |
3.29e-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: 85.00 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 13 VLIIGDVMLDRYwygptgrispeaPVPVVKVENNEERPGGA-ANVAMNIASLGGHAHIVGLTGMDEPAKVLTETLNSLKV 91
Cdd:cd01167 2 VVCFGEALIDFI------------PEGSGAPETFTKAPGGApANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 92 KCDFVAL-PDYPT-ITKLRVMSRGQqlirLDFEdkFENTDAEPVLSRMETALPSVKAVIMSDYakGSL--------EHVQ 161
Cdd:cd01167 70 DTRGIQFdPAAPTtLAFVTLDADGE----RSFE--FYRGPAADLLLDTELNPDLLSEADILHF--GSIalasepsrSALL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 162 AYIQKARAANIPVFIDPK-GADFerYRGATLLTPNMKEF---EDVVgKVkSEQELV--------EKALALVEEFEFEALL 229
Cdd:cd01167 142 ELLEAAKKAGVLISFDPNlRPPL--WRDEEEARERIAELlelADIV-KL-SDEELEllfgeedpEEIAALLLLFGLKLVL 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 491592829 230 VTRSENGMTLIRRGQEpFHLPTQAKEVYDVTGAGDTVISVLAASVAAG 277
Cdd:cd01167 218 VTRGADGALLYTKGGV-GEVPGIPVEVVDTTGAGDAFVAGLLAQLLSR 264
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
13-282 |
3.47e-18 |
|
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: 84.67 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 13 VLIIGDVMLDRYWYgPTGRISPEAPVPVVKvennEERPGGAA-NVAMNIASLGGHAHIVGLTGMDEPAKVLTETLNSLKV 91
Cdd:cd01941 2 IVVIGAANIDLRGK-VSGSLVPGTSNPGHV----KQSPGGVGrNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 92 KCDFVALPDYPTITKLRVMSR-GQQLIRLDFEDKFENTDAEpVLSRMETALPSVKAVIM-SDYAKGSLEHVqayIQKARA 169
Cdd:cd01941 77 NVRGIVFEGRSTASYTAILDKdGDLVVALADMDIYELLTPD-FLRKIREALKEAKPIVVdANLPEEALEYL---LALAAK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 170 ANIPVFIDPKGAD-----FERYRGATLLTPNMKEFEDVVGKVKSEQELVEKALALVEEFEFEALLVTRSENGMTLIRR-- 242
Cdd:cd01941 153 HGVPVAFEPTSAPklkklFYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSReg 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 491592829 243 GQEPFHLPT-QAKEVYDVTGAGDTVISVLAASVAAGKSFEE 282
Cdd:cd01941 233 GVETKLFPApQPETVVNVTGAGDAFVAGLVAGLLEGMSLDD 273
|
|
| cyt_tran_rel |
TIGR00125 |
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ... |
342-409 |
7.11e-17 |
|
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: 74.65 E-value: 7.11e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491592829 342 VVMTNGCFDILHAGHVSYLNHAAELGDRLIVAVNTDDSVKRLKgpGRPVNPTDRRMAVLAGLGAVDWV 409
Cdd:TIGR00125 1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLK--GEPVFSLEERLEMLKALKYVDEV 66
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
133-275 |
1.49e-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: 74.82 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 133 VLSRM--ETALPSVKAVIMSDYAKGsLEHVQAYIQKARAANIPVFIDP--------KGADFERYRGATLLTPNMKEFEDV 202
Cdd:cd00287 45 ALARLgvSVTLVGADAVVISGLSPA-PEAVLDALEEARRRGVPVVLDPgpravrldGEELEKLLPGVDILTPNEEEAEAL 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491592829 203 VGKVKSEQELVEKALALVEEFEFEALLVTRSENGMTLIRRGQEPFHLPTQAKEVYDVTGAGDTVISVLAASVA 275
Cdd:cd00287 124 TGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
12-282 |
1.72e-15 |
|
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: 76.82 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 12 GVLIIGDVMLDRYWYgpTGRIspeaPVP--VVKVENNEERPGG-AANVAMNIASLGGHAHIVGLTGMDEPAKVLTETLNS 88
Cdd:cd01174 1 KVVVVGSINVDLVTR--VDRL----PKPgeTVLGSSFETGPGGkGANQAVAAARLGARVAMIGAVGDDAFGDELLENLRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 89 LKVKCDFV-ALPDYPT----ITklrVMSRGQQLI--------------RLDFEDKFENTDAepVLSRMETalpsvkavim 149
Cdd:cd01174 75 EGIDVSYVeVVVGAPTgtavIT---VDESGENRIvvvpgangeltpadVDAALELIAAADV--LLLQLEI---------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 150 sdyakgSLEHVQAYIQKARAANIPVFIDPKGA---DFERYRGATLLTPNMKEFEDVVGKVKSEQELVEKALALVEEFEFE 226
Cdd:cd01174 140 ------PLETVLAALRAARRAGVTVILNPAPArplPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVK 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 491592829 227 ALLVTRSENGmTLIRRGQEPFHLPTQAKEVYDVTGAGDTVISVLAASVAAGKSFEE 282
Cdd:cd01174 214 NVIVTLGAKG-ALLASGGEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEE 268
|
|
| ECT |
cd02173 |
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ... |
339-472 |
5.78e-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: 69.21 E-value: 5.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 339 GEKVVMTNGCFDILHAGHVSYLNHAAELGDRLIVAVNTDDSVKRLKGPGRPV-NPTDRRMAVLAgLGAVDWVV---PFSe 414
Cdd:cd02173 1 GDKVVYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSNYPImNLHERVLSVLA-CRYVDEVVigaPYV- 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491592829 415 dTPQRLISEVLPSLLVKGGDYKPEEIAGGKEVIAAG---GEVRVLNFEDGCSTSEIINAIK 472
Cdd:cd02173 79 -ITKELIEHFKIDVVVHGKTEETPDSLDGEDPYAVPkemGIFKEIDSGSDLTTRDIVNRII 138
|
|
| PLN02406 |
PLN02406 |
ethanolamine-phosphate cytidylyltransferase |
333-431 |
1.80e-12 |
|
ethanolamine-phosphate cytidylyltransferase
Pssm-ID: 215227 [Multi-domain] Cd Length: 418 Bit Score: 68.94 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 333 KKARAKGEKVVMtNGCFDILHAGHVSYLNHAAELGDRLIVAVNTDDSVKRLKGPgrPVNPTDRRMAVLAGLGAVDWVVPf 412
Cdd:PLN02406 47 KKKKKKPVRVYM-DGCFDMMHYGHANALRQARALGDELVVGVVSDEEIIANKGP--PVTPMHERMIMVSGVKWVDEVIP- 122
|
90
....*....|....*....
gi 491592829 413 seDTPQRLISEVLPSLLVK 431
Cdd:PLN02406 123 --DAPYAITEEFMNKLFNE 139
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
40-286 |
5.52e-12 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 66.31 E-value: 5.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 40 VVKVENNEERPGG-AANVAMNIASLGGHAHIVGLTGMDePAKVLTETLNSLKVKCDFVALP-DYPTITKLRVMSRGQQLi 117
Cdd:COG1105 24 VNRASEVRLDPGGkGINVARVLKALGVDVTALGFLGGF-TGEFIEELLDEEGIPTDFVPIEgETRINIKIVDPSDGTET- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 118 rlDFEDK---FENTDAEPVLSRMETALPSVKAVIMSdyakGSL------EHVQAYIQKARAANIPVFIDPKGADFE---R 185
Cdd:COG1105 102 --EINEPgpeISEEELEALLERLEELLKEGDWVVLS----GSLppgvppDFYAELIRLARARGAKVVLDTSGEALKaalE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 186 YrGATLLTPNMKEFEDVVG-KVKSEQELVEKALALVEEfEFEALLVTRSENGMTLIRRGQEpFHLPTQAKEVYDVTGAGD 264
Cdd:COG1105 176 A-GPDLIKPNLEELEELLGrPLETLEDIIAAARELLER-GAENVVVSLGADGALLVTEDGV-YRAKPPKVEVVSTVGAGD 252
|
250 260
....*....|....*....|..
gi 491592829 265 TVISVLAASVAAGKSFEEACAL 286
Cdd:COG1105 253 SMVAGFLAGLARGLDLEEALRL 274
|
|
| G3P_Cytidylyltransferase |
cd02171 |
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ... |
340-411 |
1.76e-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: 61.35 E-value: 1.76e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491592829 340 EKVVMTNGCFDILHAGHVSYLNHAAELGDRLIVAVNTDDsVKRLKGPgRPVNPTDRRMAVLAGLGAVDWVVP 411
Cdd:cd02171 1 MKVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDE-FNAGKGK-KAVIPYEQRAEILESIRYVDLVIP 70
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
336-468 |
1.32e-10 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 62.88 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 336 RAKGEKVVMTNGCFDILHAGHVSYLNHAAELGDRLIVAVNTDDSVKRLKGPgrPVNPTDRRMAVLAGLGAVDWVVpfsED 415
Cdd:PTZ00308 7 KKPGTIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGP--PVMHQEERYEALRACKWVDEVV---EG 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 416 TPQRLISEVLPSL----LVKGGDYKPEeiAGGK---EVIAAGGEVRVLNFEDGCSTSEII 468
Cdd:PTZ00308 82 YPYTTRLEDLERLecdfVVHGDDISVD--LNGRnsyQEIIDAGKFKVVKRTEGISTTDLV 139
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
339-471 |
4.83e-10 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 60.95 E-value: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 339 GEKVVMTNGCFDILHAGHVSYLNHAAELGDRLIVAVNTDDSVKRLKGPGRPV-NPTDRRMAVLAGLGAVDWVVPFSEDTP 417
Cdd:PTZ00308 191 GDRIVYVDGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQVVNEQKGSNYPImNLNERVLGVLSCRYVDEVVIGAPFDVT 270
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 491592829 418 QRLISEVLPSLLVKGGDYKPEEIAGGK---EVIAAGGEVRVLNFEDGCSTSEIINAI 471
Cdd:PTZ00308 271 KEVIDSLHINVVVGGKFSDLVNEEGGSdpyEVPKAMGIFKEVDSGCDLTTDSIVDRV 327
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
13-265 |
8.29e-10 |
|
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: 59.63 E-value: 8.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 13 VLIIGDVMLDRYWYGPTG-RISPEAPVPVVKvennEERPGGAANVAMNIASLGGHAHIVGLTGMDEPAKVLTETLNSLKV 91
Cdd:cd01942 2 VAVVGHLNYDIILKVESFpGPFESVLVKDLR----REFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 92 KCDFValpdyptiTKLRVMSRGQQLIRLDFEDK---FENTDAEPVLSRMETALPSVKAVIMSdyakgsLEHVQAYIQKAR 168
Cdd:cd01942 78 DTSHV--------RVVDEDSTGVAFILTDGDDNqiaYFYPGAMDELEPNDEADPDGLADIVH------LSSGPGLIELAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 169 ---AANIPVFIDPKGADF--------ERYRGATLLTPNMKEFEDVVGKV-KSEQELVEKALALVeefefeallVTRSENG 236
Cdd:cd01942 144 elaAGGITVSFDPGQELPrlsgeeleEILERADILFVNDYEAELLKERTgLSEAELASGVRVVV---------VTLGPKG 214
|
250 260
....*....|....*....|....*....
gi 491592829 237 MTLIRRGQEPFHLPTQAKEVYDVTGAGDT 265
Cdd:cd01942 215 AIVFEDGEEVEVPAVPAVKVVDTTGAGDA 243
|
|
| CCT |
cd02174 |
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ... |
347-471 |
1.69e-09 |
|
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: 56.42 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 347 GCFDILHAGHVSYLNHAAELG--DRLIVAVNTDDSVKRLKGPgrPVNPTDRRMAVLAGLGAVDWVVpfsEDTPQRLISEV 424
Cdd:cd02174 9 GCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKGP--PVMTEEERYEAVRHCKWVDEVV---EGAPYVTTPEF 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491592829 425 L-------------PSLLVKGGD-YkpeeiaggKEVIAAGgevRVLNFE--DGCSTSEIINAI 471
Cdd:cd02174 84 LdkykcdyvahgddIYLDADGEDcY--------QEVKDAG---RFKEVKrtEGVSTTDLIGRI 135
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
13-264 |
1.80e-09 |
|
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: 58.74 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 13 VLIIGDVMLdrywygptgRISPEAPVPVVKVENNEERPGGA-ANVAMNIASLGGHAHIVGLTGMDEPAKVLTETLNSLKV 91
Cdd:cd01166 2 VVTIGEVMV---------DLSPPGGGRLEQADSFRKFFGGAeANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 92 KCDFVAL-PDYPTitklrvmsrGQQLIRLDFEDKFENT-----------DAEPVlsrMETALPSVKAVIMSDYA----KG 155
Cdd:cd01166 73 DTSHVRVdPGRPT---------GLYFLEIGAGGERRVLyyragsaasrlTPEDL---DEAALAGADHLHLSGITlalsES 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 156 SLEHVQAYIQKARAANIPVFID----PKGADFERYR--------GATLLTPNMKEFEDVVGKvKSEQELVEKALALveEF 223
Cdd:cd01166 141 AREALLEALEAAKARGVTVSFDlnyrPKLWSAEEARealeellpYVDIVLPSEEEAEALLGD-EDPTDAAERALAL--AL 217
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 491592829 224 EFEALLVTRSENGMTLIRRGQEpFHLPTQAKEVYDVTGAGD 264
Cdd:cd01166 218 GVKAVVVKLGAEGALVYTGGGR-VFVPAYPVEVVDTTGAGD 257
|
|
| PLN02406 |
PLN02406 |
ethanolamine-phosphate cytidylyltransferase |
334-471 |
4.25e-09 |
|
ethanolamine-phosphate cytidylyltransferase
Pssm-ID: 215227 [Multi-domain] Cd Length: 418 Bit Score: 58.54 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 334 KARAKGEKVVMTNGCFDILHAGHVSYLNHAAELGDRLIVAVNTDDSVKRLKGPGRPV-NPTDRRMAVLAGLGAVDWVVPF 412
Cdd:PLN02406 245 KGPGPDARIVYIDGAFDLFHAGHVEILRLARALGDFLLVGIHTDQTVSAHRGAHRPImNLHERSLSVLACRYVDEVIIGA 324
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491592829 413 SEDTPQRLISEVLPSLLVKGGDYKPEEIAGGK----EVIAAGGEVRVLNFEDGCSTSEIINAI 471
Cdd:PLN02406 325 PWEVSKDMITTFNISLVVHGTVAENNDFLKGEddpyAVPKSMGIFQVLESPLDITTSTIIRRI 387
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
40-282 |
7.00e-09 |
|
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: 56.77 E-value: 7.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 40 VVKVENNEERPGG-AANVAMNIASLGGHAHIVGLTGmDEPAKVLTETLNSLKVKCDFVALPDyPTITKLRVMSRGQQLIR 118
Cdd:cd01164 25 VNRVSSTRKDAGGkGINVARVLKDLGVEVTALGFLG-GFTGDFFEALLKEEGIPDDFVEVAG-ETRINVKIKEEDGTETE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 119 LDF------EDKFENtdaepVLSRMETALPSVKAVIMSdyakGSL-EHV--QAY---IQKARAANIPVFIDPKGADFERY 186
Cdd:cd01164 103 INEpgpeisEEELEA-----LLEKLKALLKKGDIVVLS----GSLpPGVpaDFYaelVRLAREKGARVILDTSGEALLAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 187 --RGATLLTPNMKEFEDVVGK-VKSEQELVEKALALVEEFEfEALLVTRSENGMTLIRRgQEPFHLPTQAKEVYDVTGAG 263
Cdd:cd01164 174 laAKPFLIKPNREELEELFGRpLGDEEDVIAAARKLIERGA-ENVLVSLGADGALLVTK-DGVYRASPPKVKVVSTVGAG 251
|
250
....*....|....*....
gi 491592829 264 DTVISVLAASVAAGKSFEE 282
Cdd:cd01164 252 DSMVAGFVAGLAQGLSLEE 270
|
|
| PRK00777 |
PRK00777 |
pantetheine-phosphate adenylyltransferase; |
343-400 |
2.18e-08 |
|
pantetheine-phosphate adenylyltransferase;
Pssm-ID: 234834 Cd Length: 153 Bit Score: 53.30 E-value: 2.18e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 491592829 343 VMTNGCFDILHAGHVSYLNHAAELGDRLIVAVNTDDSVKRLKgpGRPVNPTDRRMAVL 400
Cdd:PRK00777 4 VAVGGTFDPLHDGHRALLRKAFELGKRVTIGLTSDEFAKSYK--KHKVRPYEVRLKNL 59
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
13-282 |
3.64e-08 |
|
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: 54.35 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 13 VLIIGDVMLDRYWYGPtgriSPEAPVPVVKVENNEERPGGA-ANVAMNIASLGGHAHIVGLTGMDEPAKVLTETLnSLKV 91
Cdd:cd01947 2 IAVVGHVEWDIFLSLD----APPQPGGISHSSDSRESPGGGgANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEEL-ESGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 92 KCDFVALPDYPTITKLRVM-SRGQQLIRLDFEDKFENTDAePVLSRMETAlpsvkavimsdYAKGSLEHVQAyIQKARAA 170
Cdd:cd01947 77 DKHTVAWRDKPTRKTLSFIdPNGERTITVPGERLEDDLKW-PILDEGDGV-----------FITAAAVDKEA-IRKCRET 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 171 NIPVFIDPKGADFERYRGATLLtpnmkeFEDVVGkvkSEQELVEKALALVEEFEFEALLV-TRSENGMTLIRrGQEPFHL 249
Cdd:cd01947 144 KLVILQVTPRVRVDELNQALIP------LDILIG---SRLDPGELVVAEKIAGPFPRYLIvTEGELGAILYP-GGRYNHV 213
|
250 260 270
....*....|....*....|....*....|...
gi 491592829 250 PTQAKEVYDVTGAGDTVISVLAASVAAGKSFEE 282
Cdd:cd01947 214 PAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEE 246
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
50-280 |
1.17e-07 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 53.45 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 50 PGGAA-NVAMNIASLGGHAHIVGLTGMDEPAKVLTETLNSLKVKCD-FVALPDYPTITKLRVMSR-GQQLIRLDFEDKFE 126
Cdd:PRK09850 39 PGGVGrNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDkCLIVPGENTSSYLSLLDNtGEMLVAINDMNISN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 127 NTDAEpVLSRMETALPSVKaVIMSDYAKGslEHVQAYIQKaRAANIPVFIDPKGA-----DFERYRGATLLTPNMKEFED 201
Cdd:PRK09850 119 AITAE-YLAQHREFIQRAK-VIVADCNIS--EEALAWILD-NAANVPVFVDPVSAwkcvkVRDRLNQIHTLKPNRLEAET 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 202 VVGKVKSEQELVEKALALVEEFEFEALLVTRSENGMTLIR-RGQEPFHLPTQAKeVYDVTGAGDTVISVLAASVAAGKSF 280
Cdd:PRK09850 194 LSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYSDiSGESGWSAPIKTN-VINVTGAGDAMMAGLASCWVDGMPF 272
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
178-302 |
1.24e-05 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 47.04 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 178 PKGADFERYrgATLLTPNMKEFEDVVGKVKSEQELVEKALALVEEFEFEALLVTRSENGMTLIRRGQEPFHLPTQAKEVY 257
Cdd:PTZ00292 190 EIIKPFLKY--VSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEKENEPVHVPGKRVKAV 267
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 491592829 258 DVTGAGDTVISVLAASVAAGKSFEEACALANAAAGVVVGKLGTST 302
Cdd:PTZ00292 268 DTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQS 312
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
50-277 |
3.14e-05 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 45.70 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 50 PGGA-ANVAMNIASLGGHAHIVGLTGMDEPAKVLTETLNSLKVKCDFVAL-PDYPTITklrvmsrgqQLIRLDFE----- 122
Cdd:PRK09434 27 PGGApANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLdPAHRTST---------VVVDLDDQgersf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 123 --------DKFENTDAEPVLSRME---------TALPSVKAVImsdyakgslehvQAyIQKARAANIPVFIDPKGADfer 185
Cdd:PRK09434 98 tfmvrpsaDLFLQPQDLPPFRQGEwlhlcsialSAEPSRSTTF------------EA-MRRIKAAGGFVSFDPNLRE--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 186 yrgatLLTPNMKEFEDVVGK-------VK-SEQEL--------VEKAL-ALVEEFEFEALLVTRSENGMTLIRRGQEpFH 248
Cdd:PRK09434 162 -----DLWQDEAELRECLRQalaladvVKlSEEELcflsgtsqLEDAIyALADRYPIALLLVTLGAEGVLVHTRGQV-QH 235
|
250 260
....*....|....*....|....*....
gi 491592829 249 LPTQAKEVYDVTGAGDTVISVLAASVAAG 277
Cdd:PRK09434 236 FPAPSVDPVDTTGAGDAFVAGLLAGLSQA 264
|
|
| PRK01170 |
PRK01170 |
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase; |
341-399 |
7.14e-05 |
|
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
Pssm-ID: 234912 [Multi-domain] Cd Length: 322 Bit Score: 44.81 E-value: 7.14e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 491592829 341 KVVMTNGCFDILHAGHVSYLNHAAELGDRLIVAVNTDDSVKRLKgpGRPVNPTDRRMAV 399
Cdd:PRK01170 1 MITVVGGTFSKLHKGHKALLKKAIETGDEVVIGLTSDEYVRKNK--VYPIPYEDRKRKL 57
|
|
| FAD_syn |
pfam06574 |
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ... |
340-436 |
1.04e-04 |
|
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme riboflavin kinase / FAD synthetase. These enzymes have both ATP:riboflavin 5'-phospho transferase and ATP:FMN-adenylyltransferase activity. They catalyze the 5'-phosphorylation of riboflavin to FMN and the adenylylation of FMN to FAD. This domain is thought to have the flavin mononucleotide (FMN) adenylyltransferase activity.
Pssm-ID: 429011 [Multi-domain] Cd Length: 158 Bit Score: 42.55 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 340 EKVVMTNGCFDILHAGHVSYLNHAAELGDRL---IVAVNTDDSVKRLKGPGRPV---NPTDRRMAVLAGLGaVD--WVVP 411
Cdd:pfam06574 6 EGCVVTIGNFDGVHLGHQALIAKAKEIARELglpSVVVTFEPHPREVFNPDSAPfrlTTLEEKIELLAELG-VDylLVLP 84
|
90 100 110
....*....|....*....|....*....|....
gi 491592829 412 FSED----TPQRLISEVL-----PSLLVKGGDYK 436
Cdd:pfam06574 85 FTKEfaslSAEEFIENVLvdglnVKHVVVGFDFR 118
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
49-282 |
4.98e-04 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 41.62 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 49 RPGGAANVAMNIAS-LGGHAHIVGLTGMDEPAKVLTETLNSLkvkcDFVALPDYPTIT-KLRVMSRGQQLIrldfedKFE 126
Cdd:cd01937 22 KPGGPATYASLTLSrLGLTVKLVTKVGRDYPDKWSDLFDNGI----EVISLLSTETTTfELNYTNEGRTRT------LLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 127 NTDAEPVLSRMETALpSVKAVIMsdyakGSLEHvqAYIQKARAANIPVFIDPKG-----ADFERYRGATLLTPNMKEFED 201
Cdd:cd01937 92 KCAAIPDTESPLSTI-TAEIVIL-----GPVPE--EISPSLFRKFAFISLDAQGflrraNQEKLIKCVILKLHDVLKLSR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 202 VVGKVKSEQElveKALALVEEFEFEALLVTRSENGMTLIRRGQePFHLPTQAKEVYDVTGAGDTVISVLAASVAAGKSFE 281
Cdd:cd01937 164 VEAEVISTPT---ELARLIKETGVKEIIVTDGEEGGYIFDGNG-KYTIPASKKDVVDPTGAGDVFLAAFLYSRLSGKDIK 239
|
.
gi 491592829 282 E 282
Cdd:cd01937 240 E 240
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
13-277 |
8.25e-04 |
|
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.
Pssm-ID: 238915 [Multi-domain] Cd Length: 264 Bit Score: 41.19 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 13 VLIIGDVMLDRYwygPTGRISpeapvpvvkvenneeRPGG-AANVAMNIASLGGHAHIVGLTGMDEPAKVLTETLNSLKV 91
Cdd:cd01940 2 LAAIGDNVVDKY---LHLGKM---------------YPGGnALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 92 KCDFVALPDYPTitklrvmsrGQQLIRLD-------FEDKFENTDAEPVLSRMEtALPSVKAVIMSDYakGSLEHVQAYI 164
Cdd:cd01940 64 DISHCRVKEGEN---------AVADVELVdgdrifgLSNKGGVAREHPFEADLE-YLSQFDLVHTGIY--SHEGHLEKAL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 165 QKARAANIPVfidpkGADFErYRGATlltpnmKEFEDVVGKVK--------SEQELVEKALALVEEFEFEALLVTRSENG 236
Cdd:cd01940 132 QALVGAGALI-----SFDFS-DRWDD------DYLQLVCPYVDfaffsasdLSDEEVKAKLKEAVSRGAKLVIVTRGEDG 199
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 491592829 237 MTLIRrGQEPFHLPTQAKEVYDVTGAGDTVISVLAASVAAG 277
Cdd:cd01940 200 AIAYD-GAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLAG 239
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
51-277 |
1.03e-03 |
|
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: 41.13 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 51 GGAANVAMNIASLGGHAHIVGLTGMDEPAKVLTETLNSLKVKCDFV-----ALPDYPTITKLRVMSRGQQLIRLDFEDKf 125
Cdd:cd01945 37 GNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIvvapgARSPISSITDITGDRATISITAIDTQAA- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 126 enTDAEPvlsrmETALPSVKAVIMSDYAkgsLEHVQAYIQKARAANIPVFIDPKGADFERYRGatlLTPnmkeFEDVVgk 205
Cdd:cd01945 116 --PDSLP-----DAILGGADAVLVDGRQ---PEAALHLAQEARARGIPIPLDLDGGGLRVLEE---LLP----LADHA-- 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491592829 206 VKSEQELVEKA-LALVEEFEFEALL------VTRSENGMTLIRRGQEPFHLPTQAKEVYDVTGAGDTVISVLAASVAAG 277
Cdd:cd01945 177 ICSENFLRPNTgSADDEALELLASLgipfvaVTLGEAGCLWLERDGELFHVPAFPVEVVDTTGAGDVFHGAFAHALAEG 255
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
12-301 |
1.03e-03 |
|
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: 41.06 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 12 GVLIIGDVMLDRY---------WYG--PTGRISPEAPV--PVVKVENNEERPGG-AANVAMNIASLGGHAHIVGLTGMDE 77
Cdd:cd01168 3 DVLGLGNALVDILaqvddafleKLGlkKGDMILADMEEqeELLAKLPVKYIAGGsAANTIRGAAALGGSAAFIGRVGDDK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 78 PAKVLTETLNSLKVKCDFVALPDYPTITKLRVMSRGQQ-------LIRLDFEDKFENTDAepvlsrMETAlpsvKAVIMS 150
Cdd:cd01168 83 LGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDAErtmctylGAANELSPDDLDWSL------LAKA----KYLYLE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 151 DYA-KGSLEHVQAYIQKARAANIPV---FIDPKGADFerYR--------GATLLTPNMKEFEDVVGKvkSEQELVEKALA 218
Cdd:cd01168 153 GYLlTVPPEAILLAAEHAKENGVKIalnLSAPFIVQR--FKeallellpYVDILFGNEEEAEALAEA--ETTDDLEAALK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 219 LVEEFEfEALLVTRSENGmTLIRRGQEPFHLPTQAKE-VYDVTGAGDTVISVLAASVAAGKSFEEACALANAAAGVVVGK 297
Cdd:cd01168 229 LLALRC-RIVVITQGAKG-AVVVEGGEVYPVPAIPVEkIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQ 306
|
....
gi 491592829 298 LGTS 301
Cdd:cd01168 307 LGPR 310
|
|
| PanC |
COG0414 |
Panthothenate synthetase [Coenzyme transport and metabolism]; Panthothenate synthetase is part ... |
326-372 |
1.07e-03 |
|
Panthothenate synthetase [Coenzyme transport and metabolism]; Panthothenate synthetase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 440183 [Multi-domain] Cd Length: 280 Bit Score: 40.79 E-value: 1.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 491592829 326 QALIEAVKKARAKGEKV--VMTNGCfdiLHAGHVSYLNHAAELGDRLIV 372
Cdd:COG0414 8 AELRAALAAWRAAGKRIglVPTMGA---LHEGHLSLVRRARAEADVVVV 53
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
189-299 |
1.12e-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: 40.87 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 189 ATLLTPNMKEFEDVVGKVKSEQELVEKALALveefEFEALLVTRSENGMTLIR-RGQEPFHLPTQAKEVYDVTGAGDTVI 267
Cdd:cd01944 182 RPIWSCNREEAAIFAERGDPAAEASALRIYA----KTAAPVVVRLGSNGAWIRlPDGNTHIIPGFKVKAVDTIGAGDTHA 257
|
90 100 110
....*....|....*....|....*....|..
gi 491592829 268 SVLAASVAAGKSFEEACALANAAAGVVVGKLG 299
Cdd:cd01944 258 GGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
32-310 |
1.19e-03 |
|
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: 40.79 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 32 ISPEAPVPVVKVENNeeRPGGAANVAM---NIASLGGHAHIVGLT---GMDEPaKVLTETLNSLKVKCdfVALPDYPTIT 105
Cdd:cd01943 9 IIDEIEYPDSEPVTN--VLGGAGTYAIlgaRLFLPPPLSRSISWIvdkGSDFP-KSVEDELESWGTGM--VFRRDPGRLT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 106 klrvmSRGqqLIRLDFEDKFENTDAEPVLSRM------ETALPSVKAVIMSDYAKGSLEHVQAYIQKARAANI-----PV 174
Cdd:cd01943 84 -----TRG--LNIYDGNDRRFFKYLTPKKRIDvsddlnSTPLIRSSCIHLICSPERCASIVDDIINLFKLLKGnsptrPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 175 FI---DPKGADFERYRGAT-------LLTPNMKEFEDVVGKVKSEQELVEKALALVEEFEFEALLvtRSENGMTLIRRGQ 244
Cdd:cd01943 157 IVwepLPDSCDPENLEDLLqalprvdVFSPNLEEAARLLGLPTSEPSSDEEKEAVLQALLFSGIL--QDPGGGVVLRCGK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 245 E-----------PFHLP---TQAKEVYDVTGAGDTVISVLAASVAAGKSFEEACALANAAAGVVVGKLGTSTLSEIELAE 310
Cdd:cd01943 235 LgcyvgsadsgpELWLPayhTKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVGLPRLTKVEGEE 314
|
|
| Pantoate_ligase |
pfam02569 |
Pantoate-beta-alanine ligase; Pantoate-beta-alanine ligase, also know as pantothenate synthase, ... |
326-375 |
1.88e-03 |
|
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: 40.10 E-value: 1.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 491592829 326 QALIEAVKKARAKGEKV--VMTNGCfdiLHAGHVSYLNHAAELGDRLIVA--VN 375
Cdd:pfam02569 7 AELRAWLRAWRRAGKTIglVPTMGA---LHEGHLSLVRRARAENDVVVVSifVN 57
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
51-282 |
3.01e-03 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 39.91 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 51 GGAANVAMNIASLGGHAHIVGLTGMDEPAKVLTETLNSLKVK-CDFVALPDYPTITKLRVMSRGQQLIrLDFEDKFENTD 129
Cdd:PRK09954 94 GVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNvSGCIRLHGQSTSTYLAIANRQDETV-LAINDTHILQQ 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 130 AEPVLSRMETALPSVKAVIMSD--YAKGSLEHVQAYiqkarAANIPVFIDP----KGADFER-YRGATLLTPNMKEFEDV 202
Cdd:PRK09954 173 LTPQLLNGSRDLIRHAGVVLADcnLTAEALEWVFTL-----ADEIPVFVDTvsefKAGKIKHwLAHIHTLKPTQPELEIL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 203 VGK-VKSEQELVEKALALVEEfEFEALLVTRSENGMTLIRRGQEPFHLPTQAKEVYDVTGAGDTVISVLAASVAAGKSFE 281
Cdd:PRK09954 248 WGQaITSDADRNAAVNALHQQ-GVQQIFVYLPDESVFCSEKDGEQFLLTAPAHTTVDSFGADDGFMAGLVYSFLEGYSFR 326
|
.
gi 491592829 282 E 282
Cdd:PRK09954 327 D 327
|
|
| FAD_synthetase_N |
cd02064 |
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ... |
342-431 |
3.57e-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: 38.29 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 342 VVMTNGCFDILHAGHVSYLNHAAELGDR--LIVAVNTDD----SVKRLKGPGRPVNPTDRRMAVLAGLGaVDW--VVPFS 413
Cdd:cd02064 1 TVVAIGNFDGVHLGHQALIKTLKKIARErgLPSAVLTFDphprEVFLPDKAPPRLTTLEEKLELLESLG-VDYllVLPFD 79
|
90 100
....*....|....*....|..
gi 491592829 414 ED----TPQRLISEVLPSLLVK 431
Cdd:cd02064 80 KEfaslSAEEFVEDLLVKLNAK 101
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
157-282 |
5.14e-03 |
|
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: 38.72 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 157 LEHVQAYIQKARAAN--IPVFIDP------KGADF-----ERYR-----GATLLTPNMKEFEDVVGKVKSEQELVEKAL- 217
Cdd:cd01173 87 VEAVAEIVKRLKEKNpnLLYVCDPvmgdngKLYVVaeeivPVYRdllvpLADIITPNQFELELLTGKKINDLEDAKAAAr 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 218 ---------------ALVEEFEFEALLVTRSENGMtlirrgqepFHLPTQAKEVYdVTGAGDTVISVLAASVAAGKSFEE 282
Cdd:cd01173 167 alhakgpktvvvtsvELADDDRIEMLGSTATEAWL---------VQRPKIPFPAY-FNGTGDLFAALLLARLLKGKSLAE 236
|
|
| PPAT_CoAS |
cd02164 |
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ... |
342-400 |
6.95e-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: 36.87 E-value: 6.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 342 VVMTNGCFDILHAGHVSYLNHAAELG-DRLIVAVnTDDSVKRLKGPGRPVNPTDRRMAVL 400
Cdd:cd02164 1 KVAVGGTFDRLHDGHKILLSVAFLLAgEKLIIGV-TSDELLKNKSLKELIEPYEERIANL 59
|
|
| PRK05627 |
PRK05627 |
bifunctional riboflavin kinase/FAD synthetase; |
343-425 |
7.51e-03 |
|
bifunctional riboflavin kinase/FAD synthetase;
Pssm-ID: 235536 [Multi-domain] Cd Length: 305 Bit Score: 38.21 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592829 343 VMTNGCFDILHAGHVSYLNHAAELGDRL---IVAVNTDDSVKRLKGPGRPV---NPTDRRMAVLAGLGaVDWV--VPFSE 414
Cdd:PRK05627 16 VLTIGNFDGVHRGHQALLARAREIARERglpSVVMTFEPHPREVFAPDKAParlTPLRDKAELLAELG-VDYVlvLPFDE 94
|
90
....*....|....*
gi 491592829 415 D----TPQRLISEVL 425
Cdd:PRK05627 95 EfaklSAEEFIEDLL 109
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
50-94 |
7.62e-03 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 38.45 E-value: 7.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 491592829 50 PGGA-ANVAMNIASLGGHAHIVGLTGMDEPAKVLTETLNSLKVKCD 94
Cdd:PLN02323 42 PGGApANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNE 87
|
|
| |
