|
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: 1015.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 1 MKVTLPEFERAGVMVVGDVMLDRYWYGPTSRISPEAPVPVVKVNTIEERPGGAANVAMNIASLGANARLVGLTGIDDAAR 80
Cdd:PRK11316 1 MKVTLPDFERAGVLVVGDVMLDRYWYGPTSRISPEAPVPVVKVNQIEERPGGAANVAMNIASLGAQARLVGLTGIDEAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 81 ALSKSLADVNVKCDFVSVPTHPTITKLRVLSRNQQLIRLDFEEGFEGVDPQPLHERINQALSSIGALVLSDYAKGALASV 160
Cdd:PRK11316 81 ALSKLLAAVGVKCDFVSVPTHPTITKLRVLSRNQQLIRLDFEEGFEGVDPQPLLERIEQALPSIGALVLSDYAKGALASV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 161 QQMIQLARKAGVPVLIDPKGTDFERYRGATLLTPNLSEFEAVVGKCKTEEEIVERGMKLIADYELSALLVTRSEQGMSLL 240
Cdd:PRK11316 161 QAMIQLARKAGVPVLIDPKGTDFERYRGATLLTPNLSEFEAVVGKCKDEAELVEKGMKLIADYDLSALLVTRSEQGMTLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 241 QPGKAPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACFFANAAAGVVVGKLGTSTVSPIELENAVRGRADTGF 320
Cdd:PRK11316 241 QPGKAPLHLPTQAREVYDVTGAGDTVISVLAAALAAGNSLEEACALANAAAGVVVGKLGTSTVSPIELENALRGRAETGF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 321 GVMTEEELKLAVAAARKRGEKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGDSRPVNPLEQRMIVL 400
Cdd:PRK11316 321 GVMSEEQLKLAVAQARARGEKIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEGRPVNPLEQRMAVL 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929626096 401 GALEAVDWVVSFEEDTPQRLIAGILPDLLVKGGDYKPEEIAGSKEVWANGGEVLVLNFEDGCSTTNIIKKIQQ 473
Cdd:PRK11316 401 AALEAVDWVVPFEEDTPQRLIAEILPDLLVKGGDYKPEEIAGSKEVWANGGEVKVLNFEDGCSTTNIIKKIRQ 473
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
1-310 |
6.87e-171 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 483.16 E-value: 6.87e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 1 MKVTLPEFERAGVMVVGDVMLDRYWYGPTSRISPEAPVPVVKVNTIEERPGGAANVAMNIASLGANARLVGLTGIDDAAR 80
Cdd:COG2870 6 LKELLPRFSRARVLVVGDVMLDRYWYGDVERISPEAPVPVVRVEREEERPGGAANVAANLAALGAQVTLVGVVGDDEAGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 81 ALSKSLADVNVKCDFVSVPTHP-TITKLRVLSRNQQLIRLDFEEGFE--GVDPQPLHERINQALSSIGALVLSDYAKGAL 157
Cdd:COG2870 86 ELRRLLEEAGIDTDGLVVDPRRpTTTKTRVIAGGQQLLRLDFEDRFPlsAELEARLLAALEAALPEVDAVILSDYGKGVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 158 AS--VQQMIQLARKAGVPVLIDPKGTDFERYRGATLLTPNLSEFEAVVG-KCKTEEEIVERGMKLIADYELSALLVTRSE 234
Cdd:COG2870 166 TPelIQALIALARAAGKPVLVDPKGRDFSRYRGATLLTPNLKEAEAAVGiPIADEEELVAAAAELLERLGLEALLVTRGE 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1929626096 235 QGMSLLQPGKAPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACFFANAAAGVVVGKLGTSTVSPIELEN 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 |
1.09e-166 |
|
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: 472.49 E-value: 1.09e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 4 TLPEFERAGVMVVGDVMLDRYWYGPTSRISPEAPVPVVKVNTIEERPGGAANVAMNIASLGANARLVGLTGIDDAARALS 83
Cdd:TIGR02198 1 LIASFKGAKVLVVGDVMLDRYWYGKVSRISPEAPVPVVKVEREEDRLGGAANVARNIASLGARVFLVGVVGDDEAGKRLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 84 KSLADVNVKC-DFVSVPTHPTITKLRVLSRNQQLIRLDFEE--GFEGVDPQPLHERINQALSSIGALVLSDYAKGALA-- 158
Cdd:TIGR02198 81 ALLAEEGIDTsGLIRDKDRPTTTKTRVLARNQQLLRVDFEErdPINAELEARLLAAIREQLASADAVVLSDYAKGVLTpr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 159 SVQQMIQLARKAGVPVLIDPKGTDFERYRGATLLTPNLSEFEAVVGKCKTEEEIVERGMKLIADYELSALLVTRSEQGMS 238
Cdd:TIGR02198 161 VVQEVIAAARKHGKPVLVDPKGKDFSRYRGATLITPNRKEAEAAVGACDTEAELVQAAEKLLEELDLEALLVTRSEKGMT 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1929626096 239 LLQPGKAPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACFFANAAAGVVVGKLGTSTVSPIELENAVR 313
Cdd:TIGR02198 241 LFTREGEPIHIPAQAREVYDVTGAGDTVIATLALALAAGASLEEACRLANAAAGVVVGKLGTATVSPAELANALQ 315
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
13-309 |
3.94e-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: 406.95 E-value: 3.94e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 13 VMVVGDVMLDRYWYGPTSRISPEAPVPVVKVNTIEERPGGAANVAMNIASLGANARLVGLTGIDDAARALSKSLADVNVK 92
Cdd:cd01172 2 VLVVGDVILDEYLYGDVERISPEAPVPVVKVEREEIRLGGAANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 93 CDFVSVPTHPTITKLRVLSRNQQLIRLDFEEGFEGVD--PQPLHERINQALSSIGALVLSDYAKGALA--SVQQMIQLAR 168
Cdd:cd01172 82 TDGIVDEGRPTTTKTRVIARNQQLLRVDREDDSPLSAeeEQRLIERIAERLPEADVVILSDYGKGVLTprVIEALIAAAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 169 KAGVPVLIDPKGTDFERYRGATLLTPNLSEFEAVVGKC-KTEEEIVERGMKLIADYELSALLVTRSEQGMSLLQPGKAPL 247
Cdd:cd01172 162 ELGIPVLVDPKGRDYSKYRGATLLTPNEKEAREALGDEiNDDDELEAAGEKLLELLNLEALLVTLGEEGMTLFERDGEVQ 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1929626096 248 HMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACFFANAAAGVVVGKLGTSTVSPIELE 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 |
7.59e-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: 254.92 E-value: 7.59e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 331 AVAAARKRGEKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGDSRPVNPLEQRMIVLGALEAVDWVV 410
Cdd:TIGR02199 2 LVARARARGKKIVFTNGCFDILHAGHVSYLQQARALGDRLVVGVNSDASVKRLKGETRPINPEEDRAEVLAALSSVDYVV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929626096 411 SFEEDTPQRLIAGILPDLLVKGGDYKPEEIAGSKEVWANGGEVLVLNFEDGCSTTNIIKKIQQ 473
Cdd:TIGR02199 82 IFDEDTPEELIGELKPDILVKGGDYKVETLVGAELVESYGGQVVLLPFVEGRSTTAIIEKILK 144
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
13-302 |
4.26e-52 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 177.92 E-value: 4.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 13 VMVVGDVMLDRYwygptsRISPEAPVPVVKVNTIEERPGGA-ANVAMNIASLGANARLVGLTGIDDAARALSKSLADVNV 91
Cdd:pfam00294 2 VVVIGEANIDLI------GNVEGLPGELVRVSTVEKGPGGKgANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 92 KCDFVSV-PTHPTITKLRVLSRNQQLI-------RLDFEEGFEGVDPQPLHERINQALSSIGALVLSDyakgalASVQQM 163
Cdd:pfam00294 76 DTDYVVIdEDTRTGTALIEVDGDGERTivfnrgaAADLTPEELEENEDLLENADLLYISGSLPLGLPE------ATLEEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 164 IQLARKAG--VPVLIDPKGTDFERYR----GATLLTPNLSEFEAVVGKC-KTEEEIVERGMKLIADYeLSALLVTRSEQG 236
Cdd:pfam00294 150 IEAAKNGGtfDPNLLDPLGAAREALLellpLADLLKPNEEELEALTGAKlDDIEEALAALHKLLAKG-IKTVIVTLGADG 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1929626096 237 MSLLQPGKAPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACFFANAAAGVVVGKLGTST 302
Cdd:pfam00294 229 ALVVEGDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
13-305 |
7.46e-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: 131.93 E-value: 7.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 13 VMVVGDVMLDRYWYGPtsriSPEAPVPVVKVNTIEERPGG-AANVAMNIASLGANARLVGLTGIDDAARALSKSLADVNV 91
Cdd:COG0524 2 VLVIGEALVDLVARVD----RLPKGGETVLAGSFRRSPGGaAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 92 KCDFVSV-PTHPTITKLRVLSRNQQLIRLDFEEGFEGVDPQPLHErinQALSSIGALVLSDYA---KGALASVQQMIQLA 167
Cdd:COG0524 78 DTSGVRRdPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDE---ALLAGADILHLGGITlasEPPREALLAALEAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 168 RKAGVPVLIDP--KGTDFERYR--------GATLLTPNLSEFEAVVGKcKTEEEIVERgmklIADYELSALLVTRSEQGM 237
Cdd:COG0524 155 RAAGVPVSLDPnyRPALWEPARellrellaLVDILFPNEEEAELLTGE-TDPEEAAAA----LLARGVKLVVVTLGAEGA 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1929626096 238 SLLQPGKApLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACFFANAAAGVVVGKLGTSTVSP 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 |
4.82e-33 |
|
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in Escherichia coli, and separate proteins in other organisms. Domain I is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (this family) adds ADP to yield ADP-D-glycero-D-manno-heptose .
Pssm-ID: 173923 [Multi-domain] Cd Length: 144 Bit Score: 122.14 E-value: 4.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 338 RGEKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGdsRPVNPLEQRMIVLGALEAVDWVVSFEEDTP 417
Cdd:cd02172 2 RGKTVVLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVNKGPG--RPIFPEDLRAEVLAALGFVDYVVLFDNPTA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1929626096 418 QRLIAGILPDLLVKGGDYK------PEEIAGSKE-VWANGGEVLVLNfEDGCSTTNIIKKI 471
Cdd:cd02172 80 LEIIDALQPNIYVKGGDYEnpendvTGKIAPEAEaVKAYGGKIVFTG-EIVFSSSALINRI 139
|
|
| TagD |
COG0615 |
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ... |
341-471 |
8.55e-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: 112.89 E-value: 8.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 341 KVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDaSTKRLKGdSRPVNPLEQRMIVLGALEAVDWVVSFEEDTPQRL 420
Cdd:COG0615 1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATD-EFVASKG-RKPIIPEEQRKEIVEALKYVDEVILGEEWDKFED 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1929626096 421 IAGILPDLLVKGGD--YKPEEIAGSKEVWANGGEVLVLNFEDGCSTTNIIKKI 471
Cdd:COG0615 79 IEEIKPDVIVLGDDwkGDFDFLKEELEKRGIGCEVVYLPRTEGISSTKIKKRI 131
|
|
| cytidylyltransferase |
cd02170 |
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ... |
340-472 |
5.19e-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: 5.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 340 EKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGdsRPVNPLEQRMIVLGALEAVDWVVSFEEDTPQR 419
Cdd:cd02170 1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKR--RPILPEEQRAEVVEALKYVDEVILGHPWSYFK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1929626096 420 LIAGILPDLLVKGGDYK-PEEIAGSKEVWANGGEVLVLNFED--GCSTTNIIKKIQ 472
Cdd:cd02170 79 PLEELKPDVIVLGDDQKnGVDEEEVYEELKKRGKVIEVPRKKteGISSSDIIKRIL 134
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
12-300 |
3.69e-24 |
|
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: 101.86 E-value: 3.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 12 GVMVVGDVMLDRYWYgpTSRIspeaPVP--VVKVNTIEERPGG-AANVAMNIASLGANARLVGLTGIDDAARALSKSLAD 88
Cdd:cd01174 1 KVVVVGSINVDLVTR--VDRL----PKPgeTVLGSSFETGPGGkGANQAVAAARLGARVAMIGAVGDDAFGDELLENLRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 89 VNVKCDFVS-VPTHPTITKLRVLS---RNQQLI------RLDFEegfegvDPQPLHERINQAlssiGALVL----Sdyak 154
Cdd:cd01174 75 EGIDVSYVEvVVGAPTGTAVITVDesgENRIVVvpgangELTPA------DVDAALELIAAA----DVLLLqleiP---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 155 gaLASVQQMIQLARKAGVPVLIDP---KGTDFERYRGATLLTPNLSEFEAVVGKCKTEEEIVERGMKLIADYELSALLVT 231
Cdd:cd01174 141 --LETVLAALRAARRAGVTVILNPapaRPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVT 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1929626096 232 RSEQGmSLLQPGKAPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACFFANAAAGVVVGKLGT 300
Cdd:cd01174 219 LGAKG-ALLASGGEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGA 286
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
13-291 |
8.29e-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: 92.38 E-value: 8.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 13 VMVVGDVMLDRYWYgPTSRISPEAPVPVvkvnTIEERPGGAA-NVAMNIASLGANARLVGLTGIDDAARALSKSLADVNV 91
Cdd:cd01941 2 IVVIGAANIDLRGK-VSGSLVPGTSNPG----HVKQSPGGVGrNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 92 KCDFVSVPTHPTITKLRVLSRNQQLIRL--DFEEgFEGVDPQPLhERINQALSSIGALVL-SDYAKGALASVqqmIQLAR 168
Cdd:cd01941 77 NVRGIVFEGRSTASYTAILDKDGDLVVAlaDMDI-YELLTPDFL-RKIREALKEAKPIVVdANLPEEALEYL---LALAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 169 KAGVPVLIDPKGTD-----FERYRGATLLTPNLSEFEAVVGKCKTEEEIVERGMKLIADYELSALLVTRSEQG--MSLLQ 241
Cdd:cd01941 152 KHGVPVAFEPTSAPklkklFYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGvlLSSRE 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1929626096 242 PGKAPLHMPT-QAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACFFANAAA 291
Cdd:cd01941 232 GGVETKLFPApQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAA 282
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
13-299 |
1.33e-20 |
|
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: 91.93 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 13 VMVVGDVMLDRYwygptsrispeaPVPVVKVNTIEERPGGA-ANVAMNIASLGANARLVGLTGIDDAARALSKSLADVNV 91
Cdd:cd01167 2 VVCFGEALIDFI------------PEGSGAPETFTKAPGGApANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 92 KCDFV-SVPTHPTITKLRVLSRNQQLIrldfeegFEGVDPQP----LHERINQALSS------IGALVLSDyAKGAlASV 160
Cdd:cd01167 70 DTRGIqFDPAAPTTLAFVTLDADGERS-------FEFYRGPAadllLDTELNPDLLSeadilhFGSIALAS-EPSR-SAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 161 QQMIQLARKAGVPVLIDP-------KGTDFERYRGATLLTpnlsefEAVVGKCKTEE-------EIVERGMKLIADYELS 226
Cdd:cd01167 141 LELLEAAKKAGVLISFDPnlrpplwRDEEEARERIAELLE------LADIVKLSDEElellfgeEDPEEIAALLLLFGLK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 227 ALLVTRSEQGMSLLQPGKaPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNS-------LEEACFFANAAAGVVVGKLG 299
Cdd:cd01167 215 LVLVTRGADGALLYTKGG-VGEVPGIPVEVVDTTGAGDAFVAGLLAQLLSRGLlaldedeLAEALRFANAVGALTCTKAG 293
|
|
| CTP_transf_like |
pfam01467 |
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ... |
344-470 |
4.31e-20 |
|
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: 86.22 E-value: 4.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 344 MTNGVFDILHAGHVSYLANARKLGDR-LIVAVNSDASTKRLKgdsRPVNPLEQRMIVLGALEAVDWVVSFEEDTPQRLIA 422
Cdd:pfam01467 1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPPHKLK---RPLFSAEERLEMLELAKWVDEVIVVAPWELTRELL 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1929626096 423 GIL-PDLLVKGGD------YKPEEIAGSKEVWANGGEVLVLNFED--GCSTTNIIKK 470
Cdd:pfam01467 78 KELnPDVLVIGADslldfwYELDEILGNVKLVVVVRPVFFIPLKPtnGISSTDIRER 134
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
40-305 |
1.05e-19 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 89.42 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 40 VVKVNTIEERPGG-AANVAMNIASLGANARLVGLTGiDDAARALSKSLADVNVKCDFVSVPTH-PTITKLRVLSRNQQLi 117
Cdd:COG1105 24 VNRASEVRLDPGGkGINVARVLKALGVDVTALGFLG-GFTGEFIEELLDEEGIPTDFVPIEGEtRINIKIVDPSDGTET- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 118 rlDF-EEGFEgVDP---QPLHERINQALSSIGALVLSdyakGALAS------VQQMIQLARKAGVPVLIDPKGTDFE--- 184
Cdd:COG1105 102 --EInEPGPE-ISEeelEALLERLEELLKEGDWVVLS----GSLPPgvppdfYAELIRLARARGAKVVLDTSGEALKaal 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 185 RYrGATLLTPNLSEFEAVVG-KCKTEEEIVERGMKLIADYeLSALLVTRSEQGMSLLQPGKApLHMPTQAQEVYDVTGAG 263
Cdd:COG1105 175 EA-GPDLIKPNLEELEELLGrPLETLEDIIAAARELLERG-AENVVVSLGADGALLVTEDGV-YRAKPPKVEVVSTVGAG 251
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1929626096 264 DTVIGVLAATLAAGNSLEEACFFANAAAGVVVGKLGTSTVSP 305
Cdd:COG1105 252 DSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTGLPDR 293
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
13-299 |
2.70e-18 |
|
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: 84.94 E-value: 2.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 13 VMVVGDVMLdrywygptsRISPEAPVPVVKVNTIEERPGGA-ANVAMNIASLGANARLVGLTGIDDAARALSKSLADVNV 91
Cdd:cd01166 2 VVTIGEVMV---------DLSPPGGGRLEQADSFRKFFGGAeANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 92 KCDFVSV-PTHPT----ITKL-----RVLS-RNQ----QLIRLDF-EEGFEGVDPqpLHerinqaLSSIGALVLSDYAKG 155
Cdd:cd01166 73 DTSHVRVdPGRPTglyfLEIGaggerRVLYyRAGsaasRLTPEDLdEAALAGADH--LH------LSGITLALSESAREA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 156 ALASVQQmiqlARKAGVPVLID----PKGTDFERYR--------GATLLTPNLSEFEAVVGkCKTEEEIVERGmkLIADY 223
Cdd:cd01166 145 LLEALEA----AKARGVTVSFDlnyrPKLWSAEEARealeellpYVDIVLPSEEEAEALLG-DEDPTDAAERA--LALAL 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1929626096 224 ELSALLVTRSEQGmSLLQPGKAPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACFFANAAAGVVVGKLG 299
Cdd:cd01166 218 GVKAVVVKLGAEG-ALVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPG 292
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
13-275 |
3.85e-18 |
|
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: 82.53 E-value: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 13 VMVVGDVMLDRYWYGPTSrisPEAPVPVVKVNTIEERPGGAANVAMNIASLGANARLVGltgiddaaralsksladvnvk 92
Cdd:cd00287 2 VLVVGSLLVDVILRVDAL---PLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG--------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 93 cdfvsvpthptitklrvlsrnqqlirldfeegfegvdpqplherinqalssIGALVLSDYAKgALASVQQMIQLARKAGV 172
Cdd:cd00287 58 ---------------------------------------------------ADAVVISGLSP-APEAVLDALEEARRRGV 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 173 PVLIDP--------KGTDFERYRGATLLTPNLSEFEAVVGKCKTEEEIVERGMKLIADYELSALLVTRSEQGMSLLQPGK 244
Cdd:cd00287 86 PVVLDPgpravrldGEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGG 165
|
250 260 270
....*....|....*....|....*....|.
gi 1929626096 245 APLHMPTQAQEVYDVTGAGDTVIGVLAATLA 275
Cdd:cd00287 166 TEVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| cyt_tran_rel |
TIGR00125 |
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ... |
342-409 |
6.99e-18 |
|
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: 77.73 E-value: 6.99e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1929626096 342 VVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGdsRPVNPLEQRMIVLGALEAVDWV 409
Cdd:TIGR00125 1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKG--EPVFSLEERLEMLKALKYVDEV 66
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
40-300 |
2.18e-16 |
|
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: 79.50 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 40 VVKVNTIEERPGG-AANVAMNIASLGANARLVGLTGiDDAARALSKSLADVNVKCDFVSVPThPTITKLRVLSRNQQLIR 118
Cdd:cd01164 25 VNRVSSTRKDAGGkGINVARVLKDLGVEVTALGFLG-GFTGDFFEALLKEEGIPDDFVEVAG-ETRINVKIKEEDGTETE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 119 LDfEEGFEgVDP---QPLHERINQALSSIGALVLSdyakGALAS------VQQMIQLARKAGVPVLIDpkgTDFERYR-- 187
Cdd:cd01164 103 IN-EPGPE-ISEeelEALLEKLKALLKKGDIVVLS----GSLPPgvpadfYAELVRLAREKGARVILD---TSGEALLaa 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 188 ---GATLLTPNLSEFEAVVGK-CKTEEEIVERGMKLIADyELSALLVTRSEQGMSLLQPGKApLHMPTQAQEVYDVTGAG 263
Cdd:cd01164 174 laaKPFLIKPNREELEELFGRpLGDEEDVIAAARKLIER-GAENVLVSLGADGALLVTKDGV-YRASPPKVKVVSTVGAG 251
|
250 260 270
....*....|....*....|....*....|....*..
gi 1929626096 264 DTVIGVLAATLAAGNSLEEACFFANAAAGVVVGKLGT 300
Cdd:cd01164 252 DSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGT 288
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
13-301 |
3.36e-16 |
|
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: 78.51 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 13 VMVVGDVMLDRYWYGPTS-RISPEAPVPVVKvntiEERPGGAANVAMNIASLGANARLVGLTGIDDAARALSKSLADVNV 91
Cdd:cd01942 2 VAVVGHLNYDIILKVESFpGPFESVLVKDLR----REFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 92 KCDFV--SVPTHPTITKLRVLSRNQQLIrldfeegfeGVDPQPLheriNQALSSIGALVLSDYAKGALASVQQMIQLAR- 168
Cdd:cd01942 78 DTSHVrvVDEDSTGVAFILTDGDDNQIA---------YFYPGAM----DELEPNDEADPDGLADIVHLSSGPGLIELARe 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 169 --KAGVPVLIDPkGTDFERYRGATL---------LTPNLSEFEAVVGKCKTEEEIVERGMKLIadyelsalLVTRSEQGM 237
Cdd:cd01942 145 laAGGITVSFDP-GQELPRLSGEELeeileradiLFVNDYEAELLKERTGLSEAELASGVRVV--------VVTLGPKGA 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1929626096 238 SLLQPGKAPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACFFANAAAGVVVGKLGTS 301
Cdd:cd01942 216 IVFEDGEEVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
51-305 |
8.39e-13 |
|
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: 68.47 E-value: 8.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 51 GGAANVAMNIASLGANARLVGLTGIDDAARALSKSLADVNVKCDFV-----SVPTHPTITKLRVLSRNQQLIRLDFEEgf 125
Cdd:cd01945 37 GNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIvvapgARSPISSITDITGDRATISITAIDTQA-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 126 egvDPQPLHERInqaLSSIGALVLSDYAKGALASVqqmIQLARKAGVPVLIDPKGTDFERYRGATLLTPNL--SEfEAVV 203
Cdd:cd01945 115 ---APDSLPDAI---LGGADAVLVDGRQPEAALHL---AQEARARGIPIPLDLDGGGLRVLEELLPLADHAicSE-NFLR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 204 GKCKTEEEIVergMKLIADYELSALLVTRSEQGMSLLQPGKAPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEA 283
Cdd:cd01945 185 PNTGSADDEA---LELLASLGIPFVAVTLGEAGCLWLERDGELFHVPAFPVEVVDTTGAGDVFHGAFAHALAEGMPLREA 261
|
250 260
....*....|....*....|..
gi 1929626096 284 CFFANAAAGVVVGKLGTSTVSP 305
Cdd:cd01945 262 LRFASAAAALKCRGLGGRAGLP 283
|
|
| ECT |
cd02173 |
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ... |
339-410 |
1.08e-12 |
|
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: 65.74 E-value: 1.08e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929626096 339 GEKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGDSRPV-NPLEQRMIVLgALEAVDWVV 410
Cdd:cd02173 1 GDKVVYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSNYPImNLHERVLSVL-ACRYVDEVV 72
|
|
| G3P_Cytidylyltransferase |
cd02171 |
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ... |
340-471 |
1.44e-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: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 340 EKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDaSTKRLKGdSRPVNPLEQRMIVLGALEAVDWVVSfEEDTPQR 419
Cdd:cd02171 1 MKVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTD-EFNAGKG-KKAVIPYEQRAEILESIRYVDLVIP-ETNWEQK 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1929626096 420 L--IAGILPDLLVKGGDYKpeeiaGSKEVWANGGEVLVLNFEDGCSTTnIIKKI 471
Cdd:cd02171 78 IedIKKYNVDVFVMGDDWE-----GKFDFLKEYCEVVYLPRTKGISST-QLKEM 125
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
51-305 |
2.24e-12 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 67.84 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 51 GGAANVAMNIASLGANARLVGLTGIDDAARALSKSLADVNVKCDFVSVpthptitkLRVLSRNQQLIRLDFEEG------ 124
Cdd:PTZ00292 53 GKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSR--------TENSSTGLAMIFVDTKTGnneivi 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 125 ----FEGVDPQPLHERINQALSSIGALVLSDyaKGALASVQQMIQLARKAGVPVLIDP----------KGTDFERYrgAT 190
Cdd:PTZ00292 125 ipgaNNALTPQMVDAQTDNIQNICKYLICQN--EIPLETTLDALKEAKERGCYTVFNPapapklaeveIIKPFLKY--VS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 191 LLTPNLSEFEAVVGKCKTEEEIVERGMKLIADYELSALLVTRSEQGMSLLQPGKAPLHMPTQAQEVYDVTGAGDTVIGVL 270
Cdd:PTZ00292 201 LFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEKENEPVHVPGKRVKAVDTTGAGDCFVGSM 280
|
250 260 270
....*....|....*....|....*....|....*
gi 1929626096 271 AATLAAGNSLEEACFFANAAAGVVVGKLGTSTVSP 305
Cdd:PTZ00292 281 AYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYP 315
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
15-301 |
1.44e-11 |
|
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: 65.33 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 15 VVGDVMLDRYWYGPTSRISPEAPV--PVVKVNTIEERPGG-AANVAMNIASLGANARLVGLTGIDDAARALSKSLADVNV 91
Cdd:cd01168 17 QVDDAFLEKLGLKKGDMILADMEEqeELLAKLPVKYIAGGsAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 92 KCDFVSVPTHPTitklrvlSRNQQLIRLDFEEG---FEGVDPQPLHERINQALSSiGALVLsdYAKGAL-----ASVQQM 163
Cdd:cd01168 97 DTRYQVQPDGPT-------GTCAVLVTPDAERTmctYLGAANELSPDDLDWSLLA-KAKYL--YLEGYLltvppEAILLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 164 IQLARKAGVPV---LIDPKGTDFerYR--------GATLLTPNLSEFEAVVGKCKTEEEIVERGMkLIADYELSAllVTR 232
Cdd:cd01168 167 AEHAKENGVKIalnLSAPFIVQR--FKeallellpYVDILFGNEEEAEALAEAETTDDLEAALKL-LALRCRIVV--ITQ 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1929626096 233 SEQGMSLLQPGKApLHMPTQAQE-VYDVTGAGDT-VIGVLAAtLAAGNSLEEACFFANAAAGVVVGKLGTS 301
Cdd:cd01168 242 GAKGAVVVEGGEV-YPVPAIPVEkIVDTNGAGDAfAGGFLYG-LVQGEPLEECIRLGSYAAAEVIQQLGPR 310
|
|
| CCT |
cd02174 |
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ... |
347-417 |
6.01e-11 |
|
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: 60.66 E-value: 6.01e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929626096 347 GVFDILHAGHVSYLANARKLG--DRLIVAVNSDASTKRLKGdsRPVNPLEQRMIVLGALEAVDWVVsfeEDTP 417
Cdd:cd02174 9 GCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKG--PPVMTEEERYEAVRHCKWVDEVV---EGAP 76
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
337-471 |
6.71e-11 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 63.65 E-value: 6.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 337 KRGEKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGDSRPVNPLEQRmiVLGALEA--VDWVV-SFE 413
Cdd:PTZ00308 189 KPGDRIVYVDGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQVVNEQKGSNYPIMNLNER--VLGVLSCryVDEVViGAP 266
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1929626096 414 EDTPQRLIAGILPDLLVKGGDYKPEEIAGSKEVWANGGEV-LVLNFEDGC--STTNIIKKI 471
Cdd:PTZ00308 267 FDVTKEVIDSLHINVVVGGKFSDLVNEEGGSDPYEVPKAMgIFKEVDSGCdlTTDSIVDRV 327
|
|
| PLN02406 |
PLN02406 |
ethanolamine-phosphate cytidylyltransferase |
336-436 |
8.07e-11 |
|
ethanolamine-phosphate cytidylyltransferase
Pssm-ID: 215227 [Multi-domain] Cd Length: 418 Bit Score: 63.93 E-value: 8.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 336 RKRGEKVVMtNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGDsrPVNPLEQRMIVLGALEAVDWVVS---- 411
Cdd:PLN02406 50 KKKPVRVYM-DGCFDMMHYGHANALRQARALGDELVVGVVSDEEIIANKGP--PVTPMHERMIMVSGVKWVDEVIPdapy 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1929626096 412 ----------FEEDTPQRLIAG----ILPD------LLVKGGDYK 436
Cdd:PLN02406 127 aiteefmnklFNEYNIDYIIHGddpcLLPDgtdayaLAKKAGRYK 171
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
150-299 |
4.26e-10 |
|
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: 60.51 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 150 SDYAKGALASVQQMIQlarkAGVPVLIDPKGTDFERYR--------GATLLTPNLSEFEAVVGKCKTEEEIVERGMKLia 221
Cdd:cd01944 139 ENASKVILLEWLEALP----AGTTLVFDPGPRISDIPDtilqalmaKRPIWSCNREEAAIFAERGDPAAEASALRIYA-- 212
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1929626096 222 dyELSALLVTRS-EQGMSLLQPGKAPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACFFANAAAGVVVGKLG 299
Cdd:cd01944 213 --KTAAPVVVRLgSNGAWIRLPDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
13-299 |
1.31e-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: 58.97 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 13 VMVVGDVMLDRYWYGPtsriSPEAPVPVVKVNTIEERPGGA-ANVAMNIASLGANARLVGLTGIDDAARALSKSLADVNV 91
Cdd:cd01947 2 IAVVGHVEWDIFLSLD----APPQPGGISHSSDSRESPGGGgANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 92 kCDFVSVPTHPTITKLRVLSRNQQliRLDFEEGFEGVDPQPLHErinqaLSSIGALVLSdyakgALASVQQMIQLARKAG 171
Cdd:cd01947 78 -KHTVAWRDKPTRKTLSFIDPNGE--RTITVPGERLEDDLKWPI-----LDEGDGVFIT-----AAAVDKEAIRKCRETK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 172 VPVLIDPKGTDFERY----RGATLLTPNLSEFEAVVgkckTEEEIVERGMKLiadyelsaLLVTRSEQGmSLLQPGKAPL 247
Cdd:cd01947 145 LVILQVTPRVRVDELnqalIPLDILIGSRLDPGELV----VAEKIAGPFPRY--------LIVTEGELG-AILYPGGRYN 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1929626096 248 HMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACFFANAAAGVVVGKLG 299
Cdd:cd01947 212 HVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFG 263
|
|
| PLN02406 |
PLN02406 |
ethanolamine-phosphate cytidylyltransferase |
341-410 |
1.08e-08 |
|
ethanolamine-phosphate cytidylyltransferase
Pssm-ID: 215227 [Multi-domain] Cd Length: 418 Bit Score: 57.00 E-value: 1.08e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 341 KVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGDSRPVNPLEQRMIVLGALEAVDWVV 410
Cdd:PLN02406 252 RIVYIDGAFDLFHAGHVEILRLARALGDFLLVGIHTDQTVSAHRGAHRPIMNLHERSLSVLACRYVDEVI 321
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
333-417 |
1.20e-08 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 56.72 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 333 AAARKRGEKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGDsrPVNPLEQRMIVLGALEAVDWVVsf 412
Cdd:PTZ00308 4 IPPKKPGTIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGP--PVMHQEERYEALRACKWVDEVV-- 79
|
....*
gi 1929626096 413 eEDTP 417
Cdd:PTZ00308 80 -EGYP 83
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
16-299 |
9.71e-08 |
|
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: 53.13 E-value: 9.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 16 VGDVMLDRYwygPTSRISpeapvpvvkvntieeRPGG-AANVAMNIASLGANARLVGLTGIDDAARALSKSLADVNVKCD 94
Cdd:cd01940 5 IGDNVVDKY---LHLGKM---------------YPGGnALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDIS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 95 FVSVPTHPTiTKLRVLSRNQQLIRLDFEEGfeGV-DPQPLHERINqALSSIGALVLSDYakGALASVQQMIQLARKAGVP 173
Cdd:cd01940 67 HCRVKEGEN-AVADVELVDGDRIFGLSNKG--GVaREHPFEADLE-YLSQFDLVHTGIY--SHEGHLEKALQALVGAGAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 174 VLID--PKGTDFEryrgATLLTPNLsEFEAVVGKCKTEEEiVERGMKLIADYELSALLVTRSEQGmSLLQPGKAPLHMPT 251
Cdd:cd01940 141 ISFDfsDRWDDDY----LQLVCPYV-DFAFFSASDLSDEE-VKAKLKEAVSRGAKLVIVTRGEDG-AIAYDGAVFYSVAP 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1929626096 252 QAQEVYDVTGAGDTVI-GVLAATLAAGNSLEEACFFANAAAGVVVGKLG 299
Cdd:cd01940 214 RPVEVVDTLGAGDSFIaGFLLSLLAGGTAIAEAMRQGAQFAAKTCGHEG 262
|
|
| PRK00777 |
PRK00777 |
pantetheine-phosphate adenylyltransferase; |
343-397 |
1.14e-07 |
|
pantetheine-phosphate adenylyltransferase;
Pssm-ID: 234834 Cd Length: 153 Bit Score: 50.99 E-value: 1.14e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1929626096 343 VMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGdsRPVNPLEQRM 397
Cdd:PRK00777 4 VAVGGTFDPLHDGHRALLRKAFELGKRVTIGLTSDEFAKSYKK--HKVRPYEVRL 56
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
157-299 |
2.48e-07 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 52.18 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 157 LASVQQMIQLARKAGVPVLIDP----KGTDfERYRGATLLTPNLSEFEAVVGKCKTEEEIVERGMKLIADYELSALLVTR 232
Cdd:PRK11142 144 LETVLAAAKIAKQHGTKVILNPaparELPD-ELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITL 222
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1929626096 233 SEQGMSLLQPGKAPLhMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACFFANAAAGVVVGKLG 299
Cdd:PRK11142 223 GSRGVWLSENGEGQR-VPGFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKG 288
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
191-299 |
1.33e-06 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 50.03 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 191 LLTPNLSEFEAVVGkCKTEEEIVERGMKLIADYELSALLVTRSEQGMSL----------LQPGKAPLHMP---TQAQEVY 257
Cdd:cd01943 183 VFSPNLEEAARLLG-LPTSEPSSDEEKEAVLQALLFSGILQDPGGGVVLrcgklgcyvgSADSGPELWLPayhTKSTKVV 261
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1929626096 258 DVTGAGDTVIGVLAATLAAGNSLEEACFFANAAAGVVVGKLG 299
Cdd:cd01943 262 DPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG 303
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
124-283 |
1.72e-06 |
|
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: 49.02 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 124 GFEGVDPQPLHERINQALSSIGAlvlsDYAK-GALASVQQMIQLA---RKAGVPVLIDP----KGTD-------FERYRG 188
Cdd:pfam08543 39 GVHPLPPEFVAAQLDAVLEDIPV----DAVKtGMLGSAEIIEAVAeklDKYGVPVVLDPvmvaKSGDsllddeaIEALKE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 189 -----ATLLTPNLSEFEAVVG-KCKTEEEIVERGMKLiADYELSALLVT------RSEQGMSLLQPGKAPLHMPTQAQEV 256
Cdd:pfam08543 115 ellplATLITPNLPEAEALTGrKIKTLEDMKEAAKKL-LALGAKAVLIKgghlegEEAVVTDVLYDGGGFYTLEAPRIPT 193
|
170 180
....*....|....*....|....*..
gi 1929626096 257 YDVTGAGDTVIGVLAATLAAGNSLEEA 283
Cdd:pfam08543 194 KNTHGTGCTLSAAIAANLAKGLSLPEA 220
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
40-295 |
6.52e-06 |
|
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: 47.40 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 40 VVKVNTIEERPGGAANVAMNIAS-LGANARLVGLTGIDDAARalsKSLADVNVKcDFVSVPTHPTIT-KLRVLSRNQQLI 117
Cdd:cd01937 13 IVTNGSGVVKPGGPATYASLTLSrLGLTVKLVTKVGRDYPDK---WSDLFDNGI-EVISLLSTETTTfELNYTNEGRTRT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 118 -------------RLDFEEGfEGVDPQPLHERINQALSSIGALVLSDyAKGALasvqqmiqlaRKAGVPVLIdpkgtdfe 184
Cdd:cd01937 89 llakcaaipdtesPLSTITA-EIVILGPVPEEISPSLFRKFAFISLD-AQGFL----------RRANQEKLI-------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 185 RYRGATLLTP-NLSEFEAVVgkCKTEEEIVERGMKLIADyelsALLVTRSEQGMSLLQpGKAPLHMPTQAQEVYDVTGAG 263
Cdd:cd01937 149 KCVILKLHDVlKLSRVEAEV--ISTPTELARLIKETGVK----EIIVTDGEEGGYIFD-GNGKYTIPASKKDVVDPTGAG 221
|
250 260 270
....*....|....*....|....*....|..
gi 1929626096 264 DTVIGVLAATLAAGNSLEEACFFANAAAGVVV 295
Cdd:cd01937 222 DVFLAAFLYSRLSGKDIKEAAEFAAAAAAKFI 253
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
226-300 |
3.23e-05 |
|
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: 45.48 E-value: 3.23e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1929626096 226 SALLVTRSEQGMSLLQPGKAPLHMPTQAQE-VYDVTGAGDT-VIGVLAATLAAGNSLEEACFFANAAAGVVVGKLGT 300
Cdd:cd01939 213 ALLVCTWGDQGAGALGPDGEYVHSPAHKPIrVVDTLGAGDTfNAAVIYALNKGPDDLSEALDFGNRVASQKCTGVGF 289
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
46-287 |
4.00e-05 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 45.36 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 46 IEERPGGAA-NVAMNIASLGANARLVGLTGIDDAARAL--SKSLADVNV-KCdfVSVPTHPTITKLRVLSRNQQLIrldf 121
Cdd:PRK09850 35 IKFTPGGVGrNIAQNLALLGNKAWLLSAVGSDFYGQSLltQTNQSGVYVdKC--LIVPGENTSSYLSLLDNTGEML---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 122 eegfEGVDPQPLHERINQALSSIGAlvlsDYAKGALASV-------QQMIQLARKAG-VPVLIDPK-----GTDFERYRG 188
Cdd:PRK09850 109 ----VAINDMNISNAITAEYLAQHR----EFIQRAKVIVadcniseEALAWILDNAAnVPVFVDPVsawkcVKVRDRLNQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 189 ATLLTPNLSEFEAVVGKCKTEEEIVERGMKLIADYELSALLVTRSEQGM--SLLQpGKAPLHMPTQAQeVYDVTGAGDTV 266
Cdd:PRK09850 181 IHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVyySDIS-GESGWSAPIKTN-VINVTGAGDAM 258
|
250 260
....*....|....*....|.
gi 1929626096 267 IGVLAATLAAGNSLEEACFFA 287
Cdd:PRK09850 259 MAGLASCWVDGMPFAESVRFA 279
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
51-300 |
4.18e-04 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 42.46 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 51 GGAANVAMNIASLGANARLV----GLTGiddaaRALSKSLADVNVKCDFVSVPTHpTITKLRVLSRNQQlirldfeEGFE 126
Cdd:PRK10294 39 GGGINVARAIAHLGGSATAIfpagGATG-----EHLVSLLADENVPVATVEAKDW-TRQNLHVHVEASG-------EQYR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 127 GVDP---------QPLHERINQaLSSIGALVLSdyakGAL------ASVQQMIQLARKAGVPVLIDPKGTDFE---RYRG 188
Cdd:PRK10294 106 FVMPgaalnedefRQLEEQVLE-IESGAILVIS----GSLppgvklEKLTQLISAAQKQGIRCIIDSSGDALSaalAIGN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 189 ATLLTPNLSEFEAVVGKCKTE-EEIVERGMKLIADYELSALLVTRSEQGmSLLQPGKAPLHM---PTQAQEVydvTGAGD 264
Cdd:PRK10294 181 IELVKPNQKELSALVNRDLTQpDDVRKAAQELVNSGKAKRVVVSLGPQG-ALGVDSENCIQVvppPVKSQST---VGAGD 256
|
250 260 270
....*....|....*....|....*....|....*.
gi 1929626096 265 TVIGVLAATLAAGNSLEEACFFANAAAGVVVGKLGT 300
Cdd:PRK10294 257 SMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQGT 292
|
|
| PanC |
COG0414 |
Panthothenate synthetase [Coenzyme transport and metabolism]; Panthothenate synthetase is part ... |
326-372 |
1.85e-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: 1.85e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1929626096 326 EELKLAVAAARKRGEKV--VMTNGVfdiLHAGHVSYLANARKLGDRLIV 372
Cdd:COG0414 8 AELRAALAAWRAAGKRIglVPTMGA---LHEGHLSLVRRARAEADVVVV 53
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
124-287 |
2.23e-03 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 39.72 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 124 GFEGVDPQPLHERINQALSSIGAlvlsDYAK-GALASVQqMI-----QLARKAGVPVLIDP----KGTDferyRG----- 188
Cdd:PRK06427 52 RVHPIPPEFVAAQLDAVFSDIRI----DAVKiGMLASAE-IIetvaeALKRYPIPPVVLDPvmiaKSGD----PLladda 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626096 189 -----------ATLLTPNLSEFEAVVG-KCKTEEEIVERGMKLIADYELSALLVTrseqGMSLLQPGKAP--LHMPTQAQ 254
Cdd:PRK06427 123 vaalrerllplATLITPNLPEAEALTGlPIADTEDEMKAAARALHALGCKAVLIK----GGHLLDGEESVdwLFDGEGEE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1929626096 255 EV-------YDVTGAGDTVIGVLAATLAAGNSLEEACFFA 287
Cdd:PRK06427 199 RFsapriptKNTHGTGCTLSAAIAAELAKGASLLDAVQTA 238
|
|
| Pantoate_ligase |
pfam02569 |
Pantoate-beta-alanine ligase; Pantoate-beta-alanine ligase, also know as pantothenate synthase, ... |
326-375 |
4.05e-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: 4.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1929626096 326 EELKLAVAAARKRGEKV--VMTNGVfdiLHAGHVSYLANARKLGDRLIVA--VN 375
Cdd:pfam02569 7 AELRAWLRAWRRAGKTIglVPTMGA---LHEGHLSLVRRARAENDVVVVSifVN 57
|
|
| |
