|
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: 1012.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 1 MKVTLPEFERAGVLVVGDVMLDRYWYGPTSRISPEAPVPVVKVENIEERPGGAANVAMNIASLGATSRLVGLTGIDDAAR 80
Cdd:PRK11316 1 MKVTLPDFERAGVLVVGDVMLDRYWYGPTSRISPEAPVPVVKVNQIEERPGGAANVAMNIASLGAQARLVGLTGIDEAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 81 ALSKALADVNVKCDFVSVPTHPTITKLRVLSRNQQLIRLDFEEGFSGVDPQPMHERIQQALSSIGALVLSDYAKGALTSV 160
Cdd:PRK11316 81 ALSKLLAAVGVKCDFVSVPTHPTITKLRVLSRNQQLIRLDFEEGFEGVDPQPLLERIEQALPSIGALVLSDYAKGALASV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 161 QTMIKLARDAGVPVLIDPKGTDFERYRGATLLTPNLSEFEAVAGKCKDEEEIVERGMKIIADFDLSALLVTRSEQGMTLL 240
Cdd:PRK11316 161 QAMIQLARKAGVPVLIDPKGTDFERYRGATLLTPNLSEFEAVVGKCKDEAELVEKGMKLIADYDLSALLVTRSEQGMTLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 241 QPGRPPLHMPTQAQEVYDVTGAGDTVIGVLAATLASGNTLEEACYFANAAAGVVVGKLGTSTVSPIELENAVRGRSETGF 320
Cdd:PRK11316 241 QPGKAPLHLPTQAREVYDVTGAGDTVISVLAAALAAGNSLEEACALANAAAGVVVGKLGTSTVSPIELENALRGRAETGF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 321 GVMSEEELKLAVAAARKRGEKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTRRLKGDSRPVNPLDQRMIVL 400
Cdd:PRK11316 321 GVMSEEQLKLAVAQARARGEKIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEGRPVNPLEQRMAVL 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503992890 401 GALEAVDWVVSFEEDTPQRLIAGILPDLLVKGGDYKPEQIAGSEEVWANGGEVLVLNFEDGCSTTNIIKKIQK 473
Cdd:PRK11316 401 AALEAVDWVVPFEEDTPQRLIAEILPDLLVKGGDYKPEEIAGSKEVWANGGEVKVLNFEDGCSTTNIIKKIRQ 473
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
1-310 |
9.10e-172 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 485.47 E-value: 9.10e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 1 MKVTLPEFERAGVLVVGDVMLDRYWYGPTSRISPEAPVPVVKVENIEERPGGAANVAMNIASLGATSRLVGLTGIDDAAR 80
Cdd:COG2870 6 LKELLPRFSRARVLVVGDVMLDRYWYGDVERISPEAPVPVVRVEREEERPGGAANVAANLAALGAQVTLVGVVGDDEAGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 81 ALSKALADVNVKCDFVSVPTHP-TITKLRVLSRNQQLIRLDFEEGF--SGVDPQPMHERIQQALSSIGALVLSDYAKGAL 157
Cdd:COG2870 86 ELRRLLEEAGIDTDGLVVDPRRpTTTKTRVIAGGQQLLRLDFEDRFplSAELEARLLAALEAALPEVDAVILSDYGKGVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 158 TS--VQTMIKLARDAGVPVLIDPKGTDFERYRGATLLTPNLSEFEAVAG-KCKDEEEIVERGMKIIADFDLSALLVTRSE 234
Cdd:COG2870 166 TPelIQALIALARAAGKPVLVDPKGRDFSRYRGATLLTPNLKEAEAAVGiPIADEEELVAAAAELLERLGLEALLVTRGE 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503992890 235 QGMTLLQPGRPPLHMPTQAQEVYDVTGAGDTVIGVLAATLASGNTLEEACYFANAAAGVVVGKLGTSTVSPIELEN 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 |
3.07e-165 |
|
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: 468.64 E-value: 3.07e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 4 TLPEFERAGVLVVGDVMLDRYWYGPTSRISPEAPVPVVKVENIEERPGGAANVAMNIASLGATSRLVGLTGIDDAARALS 83
Cdd:TIGR02198 1 LIASFKGAKVLVVGDVMLDRYWYGKVSRISPEAPVPVVKVEREEDRLGGAANVARNIASLGARVFLVGVVGDDEAGKRLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 84 KALADVNVKC-DFVSVPTHPTITKLRVLSRNQQLIRLDFEE--GFSGVDPQPMHERIQQALSSIGALVLSDYAKGALT-- 158
Cdd:TIGR02198 81 ALLAEEGIDTsGLIRDKDRPTTTKTRVLARNQQLLRVDFEErdPINAELEARLLAAIREQLASADAVVLSDYAKGVLTpr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 159 SVQTMIKLARDAGVPVLIDPKGTDFERYRGATLLTPNLSEFEAVAGKCKDEEEIVERGMKIIADFDLSALLVTRSEQGMT 238
Cdd:TIGR02198 161 VVQEVIAAARKHGKPVLVDPKGKDFSRYRGATLITPNRKEAEAAVGACDTEAELVQAAEKLLEELDLEALLVTRSEKGMT 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503992890 239 LLQPGRPPLHMPTQAQEVYDVTGAGDTVIGVLAATLASGNTLEEACYFANAAAGVVVGKLGTSTVSPIELENAVR 313
Cdd:TIGR02198 241 LFTREGEPIHIPAQAREVYDVTGAGDTVIATLALALAAGASLEEACRLANAAAGVVVGKLGTATVSPAELANALQ 315
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
13-309 |
6.43e-141 |
|
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: 406.56 E-value: 6.43e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 13 VLVVGDVMLDRYWYGPTSRISPEAPVPVVKVENIEERPGGAANVAMNIASLGATSRLVGLTGIDDAARALSKALADVNVK 92
Cdd:cd01172 2 VLVVGDVILDEYLYGDVERISPEAPVPVVKVEREEIRLGGAANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 93 CDFVSVPTHPTITKLRVLSRNQQLIRLDFEEGFSGVD--PQPMHERIQQALSSIGALVLSDYAKGALT--SVQTMIKLAR 168
Cdd:cd01172 82 TDGIVDEGRPTTTKTRVIARNQQLLRVDREDDSPLSAeeEQRLIERIAERLPEADVVILSDYGKGVLTprVIEALIAAAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 169 DAGVPVLIDPKGTDFERYRGATLLTPNLSEFEAVAGKC-KDEEEIVERGMKIIADFDLSALLVTRSEQGMTLLQPGRPPL 247
Cdd:cd01172 162 ELGIPVLVDPKGRDYSKYRGATLLTPNEKEAREALGDEiNDDDELEAAGEKLLELLNLEALLVTLGEEGMTLFERDGEVQ 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503992890 248 HMPTQAQEVYDVTGAGDTVIGVLAATLASGNTLEEACYFANAAAGVVVGKLGTSTVSPIELE 309
Cdd:cd01172 242 HIPALAKEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGTAPVTPKELL 303
|
|
| rfaE_dom_II |
TIGR02199 |
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ... |
331-473 |
5.31e-84 |
|
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: 255.31 E-value: 5.31e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 331 AVAAARKRGEKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTRRLKGDSRPVNPLDQRMIVLGALEAVDWVV 410
Cdd:TIGR02199 2 LVARARARGKKIVFTNGCFDILHAGHVSYLQQARALGDRLVVGVNSDASVKRLKGETRPINPEEDRAEVLAALSSVDYVV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503992890 411 SFEEDTPQRLIAGILPDLLVKGGDYKPEQIAGSEEVWANGGEVLVLNFEDGCSTTNIIKKIQK 473
Cdd:TIGR02199 82 IFDEDTPEELIGELKPDILVKGGDYKVETLVGAELVESYGGQVVLLPFVEGRSTTAIIEKILK 144
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
13-302 |
3.36e-48 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 167.52 E-value: 3.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 13 VLVVGDVMLDRYwygptsRISPEAPVPVVKVENIEERPGGA-ANVAMNIASLGATSRLVGLTGIDDAARALSKALADVNV 91
Cdd:pfam00294 2 VVVIGEANIDLI------GNVEGLPGELVRVSTVEKGPGGKgANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 92 KCDFVSV-PTHPTITKLRVLSRNQQLIRLDFEEGFSGVDPQPMhERIQQALSSIGALVLSDYAKGAL--TSVQTMIKLAR 168
Cdd:pfam00294 76 DTDYVVIdEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEEL-EENEDLLENADLLYISGSLPLGLpeATLEELIEAAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 169 DAG--VPVLIDPKGTDFERYR----GATLLTPNLSEFEAVAGKC-KDEEEIVERGMKIIADFdLSALLVTRSEQGMTLLQ 241
Cdd:pfam00294 155 NGGtfDPNLLDPLGAAREALLellpLADLLKPNEEELEALTGAKlDDIEEALAALHKLLAKG-IKTVIVTLGADGALVVE 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503992890 242 PGRPPLHMPTQAQEVYDVTGAGDTVIGVLAATLASGNTLEEACYFANAAAGVVVGKLGTST 302
Cdd:pfam00294 234 GDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
13-305 |
4.97e-35 |
|
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: 132.32 E-value: 4.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 13 VLVVGDVMLDRYWYGPtsriSPEAPVPVVKVENIEERPGG-AANVAMNIASLGATSRLVGLTGIDDAARALSKALADVNV 91
Cdd:COG0524 2 VLVIGEALVDLVARVD----RLPKGGETVLAGSFRRSPGGaAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 92 KCDFVSV-PTHPTITKLRVLSRNQQLIRLDFEEGFSGVDPQPMHEriqQALSSIGALVLSDYAKGALTSVQTM---IKLA 167
Cdd:COG0524 78 DTSGVRRdPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDE---ALLAGADILHLGGITLASEPPREALlaaLEAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 168 RDAGVPVLIDP--KGTDFERYR--------GATLLTPNLSEFEAVAGKcKDEEEIVERgmkiIADFDLSALLVTRSEQGM 237
Cdd:COG0524 155 RAAGVPVSLDPnyRPALWEPARellrellaLVDILFPNEEEAELLTGE-TDPEEAAAA----LLARGVKLVVVTLGAEGA 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503992890 238 TLLQPGRPpLHMPTQAQEVYDVTGAGDTVIGVLAATLASGNTLEEACYFANAAAGVVVGKLGTSTVSP 305
Cdd:COG0524 230 LLYTGGEV-VHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALP 296
|
|
| RfaE_N |
cd02172 |
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ... |
338-471 |
7.37e-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: 7.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 338 RGEKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTRRLKGdsRPVNPLDQRMIVLGALEAVDWVVSFEEDTP 417
Cdd:cd02172 2 RGKTVVLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVNKGPG--RPIFPEDLRAEVLAALGFVDYVVLFDNPTA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503992890 418 QRLIAGILPDLLVKGGDYK-------PEQIAGSEEVWANGGEVLVLNfEDGCSTTNIIKKI 471
Cdd:cd02172 80 LEIIDALQPNIYVKGGDYEnpendvtGKIAPEAEAVKAYGGKIVFTG-EIVFSSSALINRI 139
|
|
| TagD |
COG0615 |
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ... |
341-471 |
6.12e-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: 110.58 E-value: 6.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 341 KVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDaSTRRLKGdSRPVNPLDQRMIVLGALEAVDWVVSFEEDTPQRL 420
Cdd:COG0615 1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATD-EFVASKG-RKPIIPEEQRKEIVEALKYVDEVILGEEWDKFED 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 503992890 421 IAGILPDLLVKGGD--YKPEQIAGSEEVWANGGEVLVLNFEDGCSTTNIIKKI 471
Cdd:COG0615 79 IEEIKPDVIVLGDDwkGDFDFLKEELEKRGIGCEVVYLPRTEGISSTKIKKRI 131
|
|
| cytidylyltransferase |
cd02170 |
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ... |
340-473 |
1.38e-24 |
|
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: 98.90 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 340 EKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTRRLKGdsRPVNPLDQRMIVLGALEAVDWVVSFEEDTPQR 419
Cdd:cd02170 1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKR--RPILPEEQRAEVVEALKYVDEVILGHPWSYFK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 503992890 420 LIAGILPDLLVKGGDYK-PEQIAGSEEVWANGGEVLVLNFED--GCSTTNIIKKIQK 473
Cdd:cd02170 79 PLEELKPDVIVLGDDQKnGVDEEEVYEELKKRGKVIEVPRKKteGISSSDIIKRILE 135
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
13-299 |
1.69e-21 |
|
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: 94.24 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 13 VLVVGDVMLDRYwygptsrispeaPVPVVKVENIEERPGGA-ANVAMNIASLGATSRLVGLTGIDDAARALSKALADVNV 91
Cdd:cd01167 2 VVCFGEALIDFI------------PEGSGAPETFTKAPGGApANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 92 KCDFV-SVPTHPTITKLRVLSRNQQLIrldfeegFSGVDPQP----MHERIQQALSS------IGALVLSDyAKGALTSV 160
Cdd:cd01167 70 DTRGIqFDPAAPTTLAFVTLDADGERS-------FEFYRGPAadllLDTELNPDLLSeadilhFGSIALAS-EPSRSALL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 161 QTMiKLARDAGVPVLIDPKgtdferYRGAtLLTPNLSEFEAVAG--------KCKDEE-------EIVERGMKIIADFDL 225
Cdd:cd01167 142 ELL-EAAKKAGVLISFDPN------LRPP-LWRDEEEARERIAElleladivKLSDEElellfgeEDPEEIAALLLLFGL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 226 SALLVTRSEQGMTLLQPGRPpLHMPTQAQEVYDVTGAGDTVIGVLAATLASG-------NTLEEACYFANAAAGVVVGKL 298
Cdd:cd01167 214 KLVLVTRGADGALLYTKGGV-GEVPGIPVEVVDTTGAGDAFVAGLLAQLLSRgllaldeDELAEALRFANAVGALTCTKA 292
|
.
gi 503992890 299 G 299
Cdd:cd01167 293 G 293
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
12-300 |
2.13e-21 |
|
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: 94.15 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 12 GVLVVGDVMLDRYWYgpTSRIspeaPVP--VVKVENIEERPGG-AANVAMNIASLGATSRLVGLTGIDDAARALSKALAD 88
Cdd:cd01174 1 KVVVVGSINVDLVTR--VDRL----PKPgeTVLGSSFETGPGGkGANQAVAAARLGARVAMIGAVGDDAFGDELLENLRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 89 VNVKCDFVS-VPTHPTITKLRVLS---RNQQLI------RLDFEegfsgvDPQPMHERIQQAlssiGALVL----Sdyak 154
Cdd:cd01174 75 EGIDVSYVEvVVGAPTGTAVITVDesgENRIVVvpgangELTPA------DVDAALELIAAA----DVLLLqleiP---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 155 gaLTSVQTMIKLARDAGVPVLIDP---KGTDFERYRGATLLTPNLSEFEAVAGKCKDEEEIVERGMKIIADFDLSALLVT 231
Cdd:cd01174 141 --LETVLAALRAARRAGVTVILNPapaRPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVT 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503992890 232 RSEQGMTLLQPGRPpLHMPTQAQEVYDVTGAGDTVIGVLAATLASGNTLEEACYFANAAAGVVVGKLGT 300
Cdd:cd01174 219 LGAKGALLASGGEV-EHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGA 286
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
13-291 |
4.03e-21 |
|
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: 93.15 E-value: 4.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 13 VLVVGDVMLDRYWYgPTSRISPEAPVPVVkvenIEERPGGAA-NVAMNIASLGATSRLVGLTGIDDAARALSKALADVNV 91
Cdd:cd01941 2 IVVIGAANIDLRGK-VSGSLVPGTSNPGH----VKQSPGGVGrNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 92 KCDFVSVPTHPTITKLRVLSRNQQLIrldfeEGFSGVD-----PQPMHERIQQALSSIGALVL-SDYAKGALtsvQTMIK 165
Cdd:cd01941 77 NVRGIVFEGRSTASYTAILDKDGDLV-----VALADMDiyellTPDFLRKIREALKEAKPIVVdANLPEEAL---EYLLA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 166 LARDAGVPVLIDPKGTD-----FERYRGATLLTPNLSEFEAVAGKCKDEEEIVERGMKIIADFDLSALLVTRSEQGMTLL 240
Cdd:cd01941 149 LAAKHGVPVAFEPTSAPklkklFYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLS 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 503992890 241 QPGRP--PLHMPT-QAQEVYDVTGAGDTVIGVLAATLASGNTLEEACYFANAAA 291
Cdd:cd01941 229 SREGGveTKLFPApQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAA 282
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
40-305 |
2.48e-18 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 85.19 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 40 VVKVENIEERPGG-AANVAMNIASLGATSRLVGLTGiDDAARALSKALADVNVKCDFVSVPTH-PTITKLRVLSRNQQLi 117
Cdd:COG1105 24 VNRASEVRLDPGGkGINVARVLKALGVDVTALGFLG-GFTGEFIEELLDEEGIPTDFVPIEGEtRINIKIVDPSDGTET- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 118 rlDF-EEGFSgVDP---QPMHERIQQALSSIGALVLSdyakGAL------TSVQTMIKLARDAGVPVLIDPKGTDFE--- 184
Cdd:COG1105 102 --EInEPGPE-ISEeelEALLERLEELLKEGDWVVLS----GSLppgvppDFYAELIRLARARGAKVVLDTSGEALKaal 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 185 RYrGATLLTPNLSEFEAVAG-KCKDEEEIVERGMKIIADfDLSALLVTRSEQGMTLLQPGRPpLHMPTQAQEVYDVTGAG 263
Cdd:COG1105 175 EA-GPDLIKPNLEELEELLGrPLETLEDIIAAARELLER-GAENVVVSLGADGALLVTEDGV-YRAKPPKVEVVSTVGAG 251
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 503992890 264 DTVIGVLAATLASGNTLEEACYFANAAAGVVVGKLGTSTVSP 305
Cdd:COG1105 252 DSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTGLPDR 293
|
|
| CTP_transf_like |
pfam01467 |
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ... |
344-470 |
8.36e-18 |
|
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: 79.67 E-value: 8.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 344 MTNGVFDILHAGHVSYLANARKLGDR-LIVAVNSDASTRRLKgdsRPVNPLDQRMIVLGALEAVDWVVSFEEDTPQRLIA 422
Cdd:pfam01467 1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPPHKLK---RPLFSAEERLEMLELAKWVDEVIVVAPWELTRELL 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 503992890 423 GIL-PDLLVKGGDYKPEQIAGSEEVWANGGEV--------LVLNFEDGCSTTNIIKK 470
Cdd:pfam01467 78 KELnPDVLVIGADSLLDFWYELDEILGNVKLVvvvrpvffIPLKPTNGISSTDIRER 134
|
|
| cyt_tran_rel |
TIGR00125 |
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ... |
342-409 |
2.34e-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: 76.19 E-value: 2.34e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503992890 342 VVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTRRLKGdsRPVNPLDQRMIVLGALEAVDWV 409
Cdd:TIGR00125 1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKG--EPVFSLEERLEMLKALKYVDEV 66
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
13-275 |
2.98e-17 |
|
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: 79.83 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 13 VLVVGDVMLDRYWYGPTSrisPEAPVPVVKVENIEERPGGAANVAMNIASLGATSRLVGltgiddaaralskaladvnvk 92
Cdd:cd00287 2 VLVVGSLLVDVILRVDAL---PLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG--------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 93 cdfvsvpthptitklrvlsrnqqlirldfeegfsgvdpqpmheriqqalssIGALVLSDYAKgALTSVQTMIKLARDAGV 172
Cdd:cd00287 58 ---------------------------------------------------ADAVVISGLSP-APEAVLDALEEARRRGV 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 173 PVLIDP--------KGTDFERYRGATLLTPNLSEFEAVAGKCKDEEEIVERGMKIIADFDLSALLVTRSEQGMTLLQPGR 244
Cdd:cd00287 86 PVVLDPgpravrldGEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGG 165
|
250 260 270
....*....|....*....|....*....|.
gi 503992890 245 PPLHMPTQAQEVYDVTGAGDTVIGVLAATLA 275
Cdd:cd00287 166 TEVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
13-299 |
7.26e-17 |
|
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: 80.70 E-value: 7.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 13 VLVVGDVMLdrywygptsRISPEAPVPVVKVENIEERPGGA-ANVAMNIASLGATSRLVGLTGIDDAARALSKALADVNV 91
Cdd:cd01166 2 VVTIGEVMV---------DLSPPGGGRLEQADSFRKFFGGAeANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 92 KCDFVSV-PTHPTITklrvlsrnqQLIRLDFEEGFSGV-----------DPQPMHER-IQQA----LSSIGALVLSDYAK 154
Cdd:cd01166 73 DTSHVRVdPGRPTGL---------YFLEIGAGGERRVLyyragsaasrlTPEDLDEAaLAGAdhlhLSGITLALSESARE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 155 GALTSVqtmiKLARDAGVPVLID----PKGTDFERYR--------GATLLTPNLSEFEAVAGkCKDEEEIVERGMKIiaD 222
Cdd:cd01166 144 ALLEAL----EAAKARGVTVSFDlnyrPKLWSAEEARealeellpYVDIVLPSEEEAEALLG-DEDPTDAAERALAL--A 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503992890 223 FDLSALLVTRSEQGMTLLQPGRPpLHMPTQAQEVYDVTGAGDTVIGVLAATLASGNTLEEACYFANAAAGVVVGKLG 299
Cdd:cd01166 217 LGVKAVVVKLGAEGALVYTGGGR-VFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPG 292
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
13-301 |
2.81e-15 |
|
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: 75.81 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 13 VLVVGDVMLDRYWYGPTSrisPEAPVPVVkVENIEERPGG-AANVAMNIASLGATSRLVGLTGIDDAARALSKALADVNV 91
Cdd:cd01942 2 VAVVGHLNYDIILKVESF---PGPFESVL-VKDLRREFGGsAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 92 KCDFV--SVPTH-PTITKLRVLSRNQqlirldfeegFSGVDPQPMheriQQALSSIGALVLSDYAKGALTSVQTMIKLAR 168
Cdd:cd01942 78 DTSHVrvVDEDStGVAFILTDGDDNQ----------IAYFYPGAM----DELEPNDEADPDGLADIVHLSSGPGLIELAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 169 DA---GVPVLIDPkGTDFERYRGATL---------LTPNLSEFEAVAGKCKDEEEIVERGMKIIadfdlsalLVTRSEQG 236
Cdd:cd01942 144 ELaagGITVSFDP-GQELPRLSGEELeeileradiLFVNDYEAELLKERTGLSEAELASGVRVV--------VVTLGPKG 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503992890 237 MTLLQPGRPPLHMPTQAQEVYDVTGAGDTVIGVLAATLASGNTLEEACYFANAAAGVVVGKLGTS 301
Cdd:cd01942 215 AIVFEDGEEVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
40-300 |
1.37e-14 |
|
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: 74.11 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 40 VVKVENIEERPGG-AANVAMNIASLGATSRLVGLTGiDDAARALSKALADVNVKCDFVSVPThPTITKLRVLSRNQQLIR 118
Cdd:cd01164 25 VNRVSSTRKDAGGkGINVARVLKDLGVEVTALGFLG-GFTGDFFEALLKEEGIPDDFVEVAG-ETRINVKIKEEDGTETE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 119 LDfEEGFSgVDP---QPMHERIQQALSSIGALVLSdyakGALTS------VQTMIKLARDAGVPVLIDpkgTDFERYR-- 187
Cdd:cd01164 103 IN-EPGPE-ISEeelEALLEKLKALLKKGDIVVLS----GSLPPgvpadfYAELVRLAREKGARVILD---TSGEALLaa 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 188 ---GATLLTPNLSEFEAVAGK-CKDEEEIVERGMKIIADfDLSALLVTRSEQGMTLLQPGRPpLHMPTQAQEVYDVTGAG 263
Cdd:cd01164 174 laaKPFLIKPNREELEELFGRpLGDEEDVIAAARKLIER-GAENVLVSLGADGALLVTKDGV-YRASPPKVKVVSTVGAG 251
|
250 260 270
....*....|....*....|....*....|....*..
gi 503992890 264 DTVIGVLAATLASGNTLEEACYFANAAAGVVVGKLGT 300
Cdd:cd01164 252 DSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGT 288
|
|
| ECT |
cd02173 |
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ... |
339-477 |
3.46e-13 |
|
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: 66.90 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 339 GEKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTRRLKGDSRPVNPLDQRMIVLGALEAVDWVV-----SFE 413
Cdd:cd02173 1 GDKVVYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVigapyVIT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503992890 414 EDtpqrLIAGILPDLLVKGGDYKPEQIAGSEEVWA---NGGEVLVLNFEDGCSTTNIIKKIqKDNKQ 477
Cdd:cd02173 81 KE----LIEHFKIDVVVHGKTEETPDSLDGEDPYAvpkEMGIFKEIDSGSDLTTRDIVNRI-IKNRL 142
|
|
| G3P_Cytidylyltransferase |
cd02171 |
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ... |
340-473 |
1.83e-12 |
|
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: 64.43 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 340 EKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDaSTRRLKGdSRPVNPLDQRMIVLGALEAVDWVVSfEEDTPQR 419
Cdd:cd02171 1 MKVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTD-EFNAGKG-KKAVIPYEQRAEILESIRYVDLVIP-ETNWEQK 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 503992890 420 L--IAGILPDLLVKGGDYKpeqiaGSEEVWANGGEVLVLNFEDGCSTTNIIKKIQK 473
Cdd:cd02171 78 IedIKKYNVDVFVMGDDWE-----GKFDFLKEYCEVVYLPRTKGISSTQLKEMLKK 128
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
51-305 |
3.59e-12 |
|
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: 66.93 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 51 GGAANVAMNIASLGATSRLVGLTGIDDAARALSKALADVNVKCDFVSV---PTHPTITKLRVLSRNQQlirldfeEGFSG 127
Cdd:cd01945 37 GNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVapgARSPISSITDITGDRAT-------ISITA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 128 VDPQPMHERIQQA-LSSIGALVLSDYAKGALTSVqtmIKLARDAGVPVLIDPKGTDFERYRGATLLTPNL--SE-FEAVA 203
Cdd:cd01945 110 IDTQAAPDSLPDAiLGGADAVLVDGRQPEAALHL---AQEARARGIPIPLDLDGGGLRVLEELLPLADHAicSEnFLRPN 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 204 GKCKDEEEivergMKIIADFDLSALLVTRSEQGMTLLQPGRPPLHMPTQAQEVYDVTGAGDTVIGVLAATLASGNTLEEA 283
Cdd:cd01945 187 TGSADDEA-----LELLASLGIPFVAVTLGEAGCLWLERDGELFHVPAFPVEVVDTTGAGDVFHGAFAHALAEGMPLREA 261
|
250 260
....*....|....*....|..
gi 503992890 284 CYFANAAAGVVVGKLGTSTVSP 305
Cdd:cd01945 262 LRFASAAAALKCRGLGGRAGLP 283
|
|
| PLN02406 |
PLN02406 |
ethanolamine-phosphate cytidylyltransferase |
298-471 |
8.14e-12 |
|
ethanolamine-phosphate cytidylyltransferase
Pssm-ID: 215227 [Multi-domain] Cd Length: 418 Bit Score: 67.01 E-value: 8.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 298 LGTSTVSPIELENAVRGRSETGFGVMSEEELKLAVAAARKRGEKV--VMTNGVFDILHAGHVSYLANARKLGDRLIVAVN 375
Cdd:PLN02406 9 VASCLIGGLMLGASVLGLSLAGFGSSLPYAWPDLGIFKKKKKKKPvrVYMDGCFDMMHYGHANALRQARALGDELVVGVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 376 SDASTRRLKGDsrPVNPLDQRMIVLGALEAVDWVVS--------------FEEDTPQRLIAG----ILPD------LLVK 431
Cdd:PLN02406 89 SDEEIIANKGP--PVTPMHERMIMVSGVKWVDEVIPdapyaiteefmnklFNEYNIDYIIHGddpcLLPDgtdayaLAKK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503992890 432 GGDYKpeQIAGSEevwanggevlvlnfedGCSTTNIIKKI 471
Cdd:PLN02406 167 AGRYK--QIKRTE----------------GVSSTDIVGRM 188
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
301-474 |
1.12e-11 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 65.96 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 301 STVSPIELENAVRGRSETG-FGVMSEEELKLAVAAARKRGEKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDAS 379
Cdd:PTZ00308 152 KSVDEVQLESSLFPYTPTShCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQV 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 380 TRRLKGDSRPVNPLDQRmiVLGALEA--VDWVV-SFEEDTPQRLIAGILPDLLVKGGDYKPEQIAGSEEVWANGGEV-LV 455
Cdd:PTZ00308 232 VNEQKGSNYPIMNLNER--VLGVLSCryVDEVViGAPFDVTKEVIDSLHINVVVGGKFSDLVNEEGGSDPYEVPKAMgIF 309
|
170 180
....*....|....*....|.
gi 503992890 456 LNFEDGC--STTNIIKKIQKD 474
Cdd:PTZ00308 310 KEVDSGCdlTTDSIVDRVVKN 330
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
13-301 |
1.05e-10 |
|
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: 62.63 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 13 VLVVGDVMLDRYWYGPTSRISPEAPV--PVVKVENIEERPGG-AANVAMNIASLGATSRLVGLTGIDDAARALSKALADV 89
Cdd:cd01168 15 LAQVDDAFLEKLGLKKGDMILADMEEqeELLAKLPVKYIAGGsAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 90 NVKCDFVSVPTHPTITKLRVLSRNQQliR-LDFEEGFSgVDPQPMH---ERIQQALSSI--GALVLSDyakgaLTSVQTM 163
Cdd:cd01168 95 GVDTRYQVQPDGPTGTCAVLVTPDAE--RtMCTYLGAA-NELSPDDldwSLLAKAKYLYleGYLLTVP-----PEAILLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 164 IKLARDAGVPV---LIDPKGTDFerYR--------GATLLTPNLSEFEAVAGKckDEEEIVERGMKIIADFDlSALLVTR 232
Cdd:cd01168 167 AEHAKENGVKIalnLSAPFIVQR--FKeallellpYVDILFGNEEEAEALAEA--ETTDDLEAALKLLALRC-RIVVITQ 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503992890 233 SEQGMTLLQPGRPpLHMPTQAQE-VYDVTGAGDT-VIGVLAAtLASGNTLEEACYFANAAAGVVVGKLGTS 301
Cdd:cd01168 242 GAKGAVVVEGGEV-YPVPAIPVEkIVDTNGAGDAfAGGFLYG-LVQGEPLEECIRLGSYAAAEVIQQLGPR 310
|
|
| CCT |
cd02174 |
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ... |
347-417 |
1.29e-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: 59.50 E-value: 1.29e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503992890 347 GVFDILHAGHVSYLANARKLG--DRLIVAVNSDASTRRLKGdsRPVNPLDQRMIVLGALEAVDWVVsfeEDTP 417
Cdd:cd02174 9 GCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKG--PPVMTEEERYEAVRHCKWVDEVV---EGAP 76
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
51-305 |
1.65e-10 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 62.06 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 51 GGAANVAMNIASLGATSRLVGLTGIDDAARALSKALADVNVKCDFVSVpthptitkLRVLSRNQQLIRLDFEEGFSG--V 128
Cdd:PTZ00292 53 GKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSR--------TENSSTGLAMIFVDTKTGNNEivI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 129 DPQPMHERIQQALSSIGalvlSDYAKGA----------LTSVQTMIKLARDAGVPVLIDP----------KGTDFERYrg 188
Cdd:PTZ00292 125 IPGANNALTPQMVDAQT----DNIQNICkylicqneipLETTLDALKEAKERGCYTVFNPapapklaeveIIKPFLKY-- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 189 ATLLTPNLSEFEAVAGKCKDEEEIVERGMKIIADFDLSALLVTRSEQGMTLLQPGRPPLHMPTQAQEVYDVTGAGDTVIG 268
Cdd:PTZ00292 199 VSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEKENEPVHVPGKRVKAVDTTGAGDCFVG 278
|
250 260 270
....*....|....*....|....*....|....*..
gi 503992890 269 VLAATLASGNTLEEACYFANAAAGVVVGKLGTSTVSP 305
Cdd:PTZ00292 279 SMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYP 315
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
13-299 |
1.81e-09 |
|
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: 58.58 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 13 VLVVGDVMLDRYWYGPtsriSPEAPVPVVKVENIEERPGGA-ANVAMNIASLGATSRLVGLTGIDDAARALSKALADVNV 91
Cdd:cd01947 2 IAVVGHVEWDIFLSLD----APPQPGGISHSSDSRESPGGGgANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 92 kCDFVSVPTHPTITKLRVLSRNQQliRLDFEEGFSGVDPQPmheriQQALSSIGALVLSDYAKGAltsvqTMIKLARDAG 171
Cdd:cd01947 78 -KHTVAWRDKPTRKTLSFIDPNGE--RTITVPGERLEDDLK-----WPILDEGDGVFITAAAVDK-----EAIRKCRETK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 172 VPVLIDPKGTDFERY----RGATLLTPNLSEFEAVAgkckDEEEIVERGMKIiadfdlsaLLVTRSEQGMTLLqPGRPPL 247
Cdd:cd01947 145 LVILQVTPRVRVDELnqalIPLDILIGSRLDPGELV----VAEKIAGPFPRY--------LIVTEGELGAILY-PGGRYN 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 503992890 248 HMPTQAQEVYDVTGAGDTVIGVLAATLASGNTLEEACYFANAAAGVVVGKLG 299
Cdd:cd01947 212 HVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFG 263
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
170-299 |
3.18e-09 |
|
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: 57.82 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 170 AGVPVLIDPKGTDFERYR--------GATLLTPNLSEFEAVAGKCKDEEEIVERGmkIIADFDlSALLVTRSEQGMTLLQ 241
Cdd:cd01944 155 AGTTLVFDPGPRISDIPDtilqalmaKRPIWSCNREEAAIFAERGDPAAEASALR--IYAKTA-APVVVRLGSNGAWIRL 231
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 503992890 242 PGRPPLHMPTQAQEVYDVTGAGDTVIGVLAATLASGNTLEEACYFANAAAGVVVGKLG 299
Cdd:cd01944 232 PDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| PLN02406 |
PLN02406 |
ethanolamine-phosphate cytidylyltransferase |
341-410 |
7.51e-09 |
|
ethanolamine-phosphate cytidylyltransferase
Pssm-ID: 215227 [Multi-domain] Cd Length: 418 Bit Score: 57.77 E-value: 7.51e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 341 KVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTRRLKGDSRPVNPLDQRMIVLGALEAVDWVV 410
Cdd:PLN02406 252 RIVYIDGAFDLFHAGHVEILRLARALGDFLLVGIHTDQTVSAHRGAHRPIMNLHERSLSVLACRYVDEVI 321
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
333-417 |
6.79e-08 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 54.41 E-value: 6.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 333 AAARKRGEKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTRRLKGDsrPVNPLDQRMIVLGALEAVDWVVsf 412
Cdd:PTZ00308 4 IPPKKPGTIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGP--PVMHQEERYEALRACKWVDEVV-- 79
|
....*
gi 503992890 413 eEDTP 417
Cdd:PTZ00308 80 -EGYP 83
|
|
| PRK00777 |
PRK00777 |
pantetheine-phosphate adenylyltransferase; |
343-397 |
2.40e-07 |
|
pantetheine-phosphate adenylyltransferase;
Pssm-ID: 234834 Cd Length: 153 Bit Score: 50.22 E-value: 2.40e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 503992890 343 VMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSD--ASTRRlkgdSRPVNPLDQRM 397
Cdd:PRK00777 4 VAVGGTFDPLHDGHRALLRKAFELGKRVTIGLTSDefAKSYK----KHKVRPYEVRL 56
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
13-299 |
5.55e-07 |
|
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: 50.82 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 13 VLVVGDVMLDRYwygPTSRISpeapvpvvkvenieeRPGG-AANVAMNIASLGATSRLVGLTGIDDAARALSKALADVNV 91
Cdd:cd01940 2 LAAIGDNVVDKY---LHLGKM---------------YPGGnALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 92 KCDFVSVPTHPTiTKLRVLSRNQQLIRLDFEEGfSGVDPQPMHERI----QQALSSIGALVLSDYAKGALTSVQ-TMIKL 166
Cdd:cd01940 64 DISHCRVKEGEN-AVADVELVDGDRIFGLSNKG-GVAREHPFEADLeylsQFDLVHTGIYSHEGHLEKALQALVgAGALI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 167 ARDAGVpvlidpKGTDFEryrgATLLTPNLsefEAVAGKCKDE-EEIVERGMKIIADFDLSALLVTRSEQGMTLLQpGRP 245
Cdd:cd01940 142 SFDFSD------RWDDDY----LQLVCPYV---DFAFFSASDLsDEEVKAKLKEAVSRGAKLVIVTRGEDGAIAYD-GAV 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 503992890 246 PLHMPTQAQEVYDVTGAGDTVI-GVLAATLASGNTLEEACYFANAAAGVVVGKLG 299
Cdd:cd01940 208 FYSVAPRPVEVVDTLGAGDSFIaGFLLSLLAGGTAIAEAMRQGAQFAAKTCGHEG 262
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
242-299 |
8.90e-07 |
|
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: 50.80 E-value: 8.90e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503992890 242 PGRPPLHMP---TQAQEVYDVTGAGDTVIGVLAATLASGNTLEEACYFANAAAGVVVGKLG 299
Cdd:cd01943 243 DSGPELWLPayhTKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG 303
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
157-299 |
6.04e-06 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 47.94 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 157 LTSVQTMIKLARDAGVPVLIDP----KGTDfERYRGATLLTPNLSEFEAVAGKCKDEEEIVERGMKIIADFDLSALLVTR 232
Cdd:PRK11142 144 LETVLAAAKIAKQHGTKVILNPaparELPD-ELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITL 222
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503992890 233 SEQGMTLLQPGRPPLhMPTQAQEVYDVTGAGDTVIGVLAATLASGNTLEEACYFANAAAGVVVGKLG 299
Cdd:PRK11142 223 GSRGVWLSENGEGQR-VPGFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKG 288
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
151-287 |
1.17e-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: 46.71 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 151 DYAK-GALTSVQTMIKLA---RDAGVPVLIDP----KGTD-------FERYRG-----ATLLTPNLSEFEAVAG-KCKDE 209
Cdd:pfam08543 62 DAVKtGMLGSAEIIEAVAeklDKYGVPVVLDPvmvaKSGDsllddeaIEALKEellplATLITPNLPEAEALTGrKIKTL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 210 EEIVERGMKIIADFDLSAL-----LVTRSEQGMTLLQPGRPPLHMPTQAQEVYDVTGAGDTVIGVLAATLASGNTLEEAC 284
Cdd:pfam08543 142 EDMKEAAKKLLALGAKAVLikgghLEGEEAVVTDVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAV 221
|
...
gi 503992890 285 YFA 287
Cdd:pfam08543 222 REA 224
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
168-295 |
1.52e-05 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 46.24 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 168 RDAGVPVLIDPKG-----TDFERYRGATLLTP---NLSEFEAVagKCKDEEEIVergmKIIADFDLSALLVTRSEQGMTL 239
Cdd:cd01937 125 FRKFAFISLDAQGflrraNQEKLIKCVILKLHdvlKLSRVEAE--VISTPTELA----RLIKETGVKEIIVTDGEEGGYI 198
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 503992890 240 LQPGRPpLHMPTQAQEVYDVTGAGDTVIGVLAATLASGNTLEEACYFANAAAGVVV 295
Cdd:cd01937 199 FDGNGK-YTIPASKKDVVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAKFI 253
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
226-300 |
2.29e-04 |
|
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.
Pssm-ID: 238914 [Multi-domain] Cd Length: 290 Bit Score: 43.16 E-value: 2.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503992890 226 SALLVTRSEQGMTLLQPGRPPLHMPTQAQE-VYDVTGAGDT-VIGVLAATLASGNTLEEACYFANAAAGVVVGKLGT 300
Cdd:cd01939 213 ALLVCTWGDQGAGALGPDGEYVHSPAHKPIrVVDTLGAGDTfNAAVIYALNKGPDDLSEALDFGNRVASQKCTGVGF 289
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
46-287 |
3.98e-04 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 42.28 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 46 IEERPGGAA-NVAMNIASLGATSRLVGLTGIDDAARAL--SKALADVNV-KCdfVSVPTHPTITKLRVLSRNQQLIrldf 121
Cdd:PRK09850 35 IKFTPGGVGrNIAQNLALLGNKAWLLSAVGSDFYGQSLltQTNQSGVYVdKC--LIVPGENTSSYLSLLDNTGEML---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 122 eegfsgVDPQPMHerIQQALSSIGALVLSDYAKGALTSV-------QTMIKLARDAG-VPVLIDPK-----GTDFERYRG 188
Cdd:PRK09850 109 ------VAINDMN--ISNAITAEYLAQHREFIQRAKVIVadcniseEALAWILDNAAnVPVFVDPVsawkcVKVRDRLNQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 189 ATLLTPNLSEFEAVAGKCKDEEEIVERGMKIIADFDLSALLVTRSEQGMTLLQ-PGRPPLHMPTQAQeVYDVTGAGDTVI 267
Cdd:PRK09850 181 IHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYSDiSGESGWSAPIKTN-VINVTGAGDAMM 259
|
250 260
....*....|....*....|
gi 503992890 268 GVLAATLASGNTLEEACYFA 287
Cdd:PRK09850 260 AGLASCWVDGMPFAESVRFA 279
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
189-287 |
5.92e-04 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 41.65 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 189 ATLLTPNLSEFEAVAG-KCKDEEEIVERGMKIIADFDLSALLVTrseqGMTLLQPGRPP--LHMPTQAQEV-------YD 258
Cdd:PRK06427 134 ATLITPNLPEAEALTGlPIADTEDEMKAAARALHALGCKAVLIK----GGHLLDGEESVdwLFDGEGEERFsapriptKN 209
|
90 100
....*....|....*....|....*....
gi 503992890 259 VTGAGDTVIGVLAATLASGNTLEEACYFA 287
Cdd:PRK06427 210 THGTGCTLSAAIAAELAKGASLLDAVQTA 238
|
|
| PanC |
COG0414 |
Panthothenate synthetase [Coenzyme transport and metabolism]; Panthothenate synthetase is part ... |
326-372 |
1.83e-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: 40.02 E-value: 1.83e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 503992890 326 EELKLAVAAARKRGEKV--VMTNGVfdiLHAGHVSYLANARKLGDRLIV 372
Cdd:COG0414 8 AELRAALAAWRAAGKRIglVPTMGA---LHEGHLSLVRRARAEADVVVV 53
|
|
| Pantoate_ligase |
pfam02569 |
Pantoate-beta-alanine ligase; Pantoate-beta-alanine ligase, also know as pantothenate synthase, ... |
326-375 |
4.02e-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: 38.94 E-value: 4.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 503992890 326 EELKLAVAAARKRGEKV--VMTNGVfdiLHAGHVSYLANARKLGDRLIVA--VN 375
Cdd:pfam02569 7 AELRAWLRAWRRAGKTIglVPTMGA---LHEGHLSLVRRARAENDVVVVSifVN 57
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
155-292 |
7.50e-03 |
|
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of the ATP binding site, the substrate binding site and the Mg2+binding site and structural homology this group is a member of the ribokinase-like superfamily.
Pssm-ID: 238576 Cd Length: 254 Bit Score: 37.98 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 155 GALTSVQTMIKLARDAGVPVLID-------PKGTDFERYRGATLLTPNLSEFEAVAGKCKDEEE---------------- 211
Cdd:cd01171 88 GRDEEAAEILEKALAKDKPLVLDadalnllADEPSLIKRYGPVVLTPHPGEFARLLGALVEEIQadrlaaareaaaklga 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992890 212 -IVERGMK-IIADFDLSALLVTRSEQGMTllqpgrpplhmptqaqevydVTGAGDTVIGVLAATLASGNTLEEACY---F 286
Cdd:cd01171 168 tVVLKGAVtVIADPDGRVYVNPTGNPGLA--------------------TGGSGDVLAGIIAALLAQGLSPLEAAAlavY 227
|
....*.
gi 503992890 287 ANAAAG 292
Cdd:cd01171 228 LHGLAG 233
|
|
| |
