|
Name |
Accession |
Description |
Interval |
E-value |
| araD |
PRK08193 |
L-ribulose-5-phosphate 4-epimerase AraD; |
1-231 |
1.44e-175 |
|
L-ribulose-5-phosphate 4-epimerase AraD;
Pssm-ID: 236181 Cd Length: 231 Bit Score: 481.26 E-value: 1.44e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 1 MLEELKNEVYQANMSLPKLGLVTFTWGNVSGIDREKGLFVIKPSGVAYEDLKPDDMVVVDLDGNVVEGDLNPSSDTPTHA 80
Cdd:PRK08193 1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLEGNVVEGKLKPSSDTPTHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 81 YLYRHFKNIGGITHTHSPWGVSFAAAQMDIPAVSTTHADTFYGDIPCTPALSQEEIQSAYELNTGKVIVSEFEQRQIDPD 160
Cdd:PRK08193 81 VLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKRGIDPA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497978338 161 ATPAVLVSQHGPFTWGVDASKSVYNAKVLEVSAEISYHALQSTRSDIHVPQYLLDKHYYRKHGVNAYYGQK 231
Cdd:PRK08193 161 AVPGVLVHSHGPFTWGKDAEDAVHNAVVLEEVAKMAYFTRQLNPQLPDMQQTLLDKHYLRKHGKNAYYGQK 231
|
|
| araD |
TIGR00760 |
L-ribulose-5-phosphate 4-epimerase; E. coli has two genes, sgaE and sgbE (YiaS), that are very ... |
1-230 |
5.63e-118 |
|
L-ribulose-5-phosphate 4-epimerase; E. coli has two genes, sgaE and sgbE (YiaS), that are very close homologs of araD, the established L-ribulose-5-phosphate 4-epimerase of E. coli. SgbE, part of an operon for L-xylulose metabolism, also has L-ribulose-5-phosphate 4-epimerase activity; L-xylulose-5-phosphate may be converted into L-ribulose-5-phosphate by another product of that operon. The homolog to this family from Mycobacterium smegmatis is flanked by putative araB and araA genes, consistent with it also being araD. [Energy metabolism, Sugars]
Pssm-ID: 129843 Cd Length: 231 Bit Score: 336.03 E-value: 5.63e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 1 MLEELKNEVYQANMSLPKLGLVTFTWGNVSGIDREKGLFVIKPSGVAYEDLKPDDMVVVDLD-GNVVEGDLNPSSDTPTH 79
Cdd:TIGR00760 1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLEtGNVVEGSKKPSSDTPTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 80 AYLYRHFKNIGGITHTHSPWGVSFAAAQMDIPAVSTTHADTFYGDIPCTPALSQEEIQSAYELNTGKVIVSEFEQRQIDP 159
Cdd:TIGR00760 81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEKRGIDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497978338 160 DATPAVLVSQHGPFTWGVDASKSVYNAKVLEVSAEISYHALQSTRSDIHVPQYLLDKHYYRKHGVNAYYGQ 230
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
|
|
| Aldolase_II |
cd00398 |
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ... |
3-222 |
5.58e-71 |
|
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). Class II enzymes are further divided into two sub-classes A and B. This family includes class II A aldolases and adducins which has not been ascribed any enzymatic function. Members of this class are primarily bacterial and eukaryotic in origin and include L-fuculose-1-phosphate, L-rhamnulose-1-phosphate aldolases and L-ribulose-5-phosphate 4-epimerases. They all share the ability to promote carbon-carbon bond cleavage and stabilize enolate intermediates using divalent cations.
Pssm-ID: 238232 [Multi-domain] Cd Length: 209 Bit Score: 216.08 E-value: 5.58e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 3 EELKNEVYQANMSLPKLGLVTFTWGNVSGIDREKGLFVIKPSGVAYEDLKPDDMVVVDLDGNVVEGDLnPSSDTPTHAYL 82
Cdd:cd00398 1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVEGKK-PSSETPLHLAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 83 YRHFKNIGGITHTHSPWGVSFAAAQ-MDIPAVSTTHADTFYGDIPCTPALSQEeiqsayelnTGKVIVSEFEQRQIdpDA 161
Cdd:cd00398 80 YRARPDIGCIVHTHSTHATAVSQLKeGLIPAGHTACAVYFTGDIPCTPYMTPE---------TGEDEIGTQRALGF--PN 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497978338 162 TPAVLVSQHGPFTWGVDASKSVYNAKVLEVSAEISYHALQSTRSDIHVPQYLLDKHYYRKH 222
Cdd:cd00398 149 SKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
|
|
| AraD |
COG0235 |
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ... |
1-223 |
1.86e-69 |
|
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440005 [Multi-domain] Cd Length: 208 Bit Score: 212.00 E-value: 1.86e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 1 MLEELKNEVYQANMSLPKLGLVTFTWGNVSGIDREkGLFVIKPSGVAYEDLKPDDMVVVDLDGNVVEGDLNPSSDTPTHA 80
Cdd:COG0235 2 EEEELREELAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKPSSETPLHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 81 YLYRHFKNIGGITHTHSPWGVSFAAAQMDIPAVSTTHADTFYGDIPCTPalsqeeiqsaYElntgkVIVSEFEQRQIDPD 160
Cdd:COG0235 81 AIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVP----------YA-----GPGTEELAEAIAEA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497978338 161 A--TPAVLVSQHGPFTWGVDASKSVYNAKVLEVSAEISYHALQsTRSDIHVPQYLLDKHyYRKHG 223
Cdd:COG0235 146 LgdRPAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALA-LGGPLVLSDEEIDKL-ARKFG 208
|
|
| Aldolase_II |
pfam00596 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
7-197 |
7.22e-61 |
|
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.
Pssm-ID: 459862 [Multi-domain] Cd Length: 178 Bit Score: 188.91 E-value: 7.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 7 NEVYQANMSLPKLGLVTFTWGNVSGIDrEKGLFVIKPSGVAYEDLKPDDMVVVDLDGNVVEGDLNPSSDTPTHAYLYRHF 86
Cdd:pfam00596 1 EELAAAGRLLARRGLVEGTGGNISVRL-PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGLKPSSETPLHLAIYRAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 87 KNIGGITHTHSPWGVSFAAAQMDIPAVSTTHADTFYGDIPCTPALSQEEIQsayelnTGKVIVSEFEqrqidpDATPAVL 166
Cdd:pfam00596 80 PDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTEE------LGERIAEALG------GDRKAVL 147
|
170 180 190
....*....|....*....|....*....|.
gi 497978338 167 VSQHGPFTWGVDASKSVYNAKVLEVSAEISY 197
Cdd:pfam00596 148 LRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
|
|
| Aldolase_II |
smart01007 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
9-197 |
1.01e-57 |
|
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.
Pssm-ID: 214970 [Multi-domain] Cd Length: 185 Bit Score: 181.30 E-value: 1.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 9 VYQANMSLPKLGLVTFTWGNVSGIDREKGLFVIKPSGVAYEDLKPDDMVVVDLDGNVVEGDL--NPSSDTPTHAYLYRHF 86
Cdd:smart01007 1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGgpKPSSETPLHLAIYRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 87 KNIGGITHTHSPWGVSFAAAQMDIPAVSTTHADTFYG-DIPCTPALSQEEIQSAYELNTGKVIVSEFEQRqidpdatPAV 165
Cdd:smart01007 81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGAELAEALAEALPDR-------PAV 153
|
170 180 190
....*....|....*....|....*....|..
gi 497978338 166 LVSQHGPFTWGVDASKSVYNAKVLEVSAEISY 197
Cdd:smart01007 154 LLRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| araD |
PRK08193 |
L-ribulose-5-phosphate 4-epimerase AraD; |
1-231 |
1.44e-175 |
|
L-ribulose-5-phosphate 4-epimerase AraD;
Pssm-ID: 236181 Cd Length: 231 Bit Score: 481.26 E-value: 1.44e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 1 MLEELKNEVYQANMSLPKLGLVTFTWGNVSGIDREKGLFVIKPSGVAYEDLKPDDMVVVDLDGNVVEGDLNPSSDTPTHA 80
Cdd:PRK08193 1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLEGNVVEGKLKPSSDTPTHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 81 YLYRHFKNIGGITHTHSPWGVSFAAAQMDIPAVSTTHADTFYGDIPCTPALSQEEIQSAYELNTGKVIVSEFEQRQIDPD 160
Cdd:PRK08193 81 VLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKRGIDPA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497978338 161 ATPAVLVSQHGPFTWGVDASKSVYNAKVLEVSAEISYHALQSTRSDIHVPQYLLDKHYYRKHGVNAYYGQK 231
Cdd:PRK08193 161 AVPGVLVHSHGPFTWGKDAEDAVHNAVVLEEVAKMAYFTRQLNPQLPDMQQTLLDKHYLRKHGKNAYYGQK 231
|
|
| sgaE |
PRK12348 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
2-231 |
1.80e-123 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 183460 Cd Length: 228 Bit Score: 349.87 E-value: 1.80e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 2 LEELKNEVYQANMSLPKLGLVTFTWGNVSGIDREKGLFVIKPSGVAYEDLKPDDMVVVDLDGNVVEGDLNPSSDTPTHAY 81
Cdd:PRK12348 1 MQKLKQQVFEANMDLPRYGLVTFTWGNVSAIDRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEGEYRPSSDTATHLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 82 LYRHFKNIGGITHTHSPWGVSFAAAQMDIPAVSTTHADTFYGDIPCTPALSQEEIQSAYELNTGKVIVSEFeqRQIDPDA 161
Cdd:PRK12348 81 LYRRYPSLGGIVHTHSTHATAWAQAGLAIPALGTTHADYFFGDIPCTRGLSEEEVQGEYELNTGKVIIETL--GNAEPLH 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 162 TPAVLVSQHGPFTWGVDASKSVYNAKVLEVSAEISYHALQSTRSDIHVPQYLLDKHYYRKHGVNAYYGQK 231
Cdd:PRK12348 159 TPGIVVYQHGPFAWGKDAHDAVHNAVVMEEVAKMAWIARGINPQLNHIDSYLMNKHFMRKHGPNAYYGQK 228
|
|
| araD |
TIGR00760 |
L-ribulose-5-phosphate 4-epimerase; E. coli has two genes, sgaE and sgbE (YiaS), that are very ... |
1-230 |
5.63e-118 |
|
L-ribulose-5-phosphate 4-epimerase; E. coli has two genes, sgaE and sgbE (YiaS), that are very close homologs of araD, the established L-ribulose-5-phosphate 4-epimerase of E. coli. SgbE, part of an operon for L-xylulose metabolism, also has L-ribulose-5-phosphate 4-epimerase activity; L-xylulose-5-phosphate may be converted into L-ribulose-5-phosphate by another product of that operon. The homolog to this family from Mycobacterium smegmatis is flanked by putative araB and araA genes, consistent with it also being araD. [Energy metabolism, Sugars]
Pssm-ID: 129843 Cd Length: 231 Bit Score: 336.03 E-value: 5.63e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 1 MLEELKNEVYQANMSLPKLGLVTFTWGNVSGIDREKGLFVIKPSGVAYEDLKPDDMVVVDLD-GNVVEGDLNPSSDTPTH 79
Cdd:TIGR00760 1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLEtGNVVEGSKKPSSDTPTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 80 AYLYRHFKNIGGITHTHSPWGVSFAAAQMDIPAVSTTHADTFYGDIPCTPALSQEEIQSAYELNTGKVIVSEFEQRQIDP 159
Cdd:TIGR00760 81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEKRGIDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497978338 160 DATPAVLVSQHGPFTWGVDASKSVYNAKVLEVSAEISYHALQSTRSDIHVPQYLLDKHYYRKHGVNAYYGQ 230
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
|
|
| araD |
PRK13145 |
L-ribulose-5-phosphate 4-epimerase; Provisional |
1-231 |
1.70e-116 |
|
L-ribulose-5-phosphate 4-epimerase; Provisional
Pssm-ID: 183870 [Multi-domain] Cd Length: 234 Bit Score: 332.18 E-value: 1.70e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 1 MLEELKNEVYQANMSLPKLGLVTFTWGNVSGIDREKGLFVIKPSGVAYEDLKPDDMVVVDLDGNVVEGDLNPSSDTPTHA 80
Cdd:PRK13145 2 NLQEMRERVCAANKSLPKHGLVKFTWGNVSEVCRELGRIVIKPSGVDYDELTPENMVVTDLDGNVVEGDLNPSSDLPTHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 81 YLYRHFKNIGGITHTHSPWGVSFAAAQMDIPAVSTTHADTFYGDIPCTPALSQEEIQSAYELNTGKVIVSEFEQRQIDPD 160
Cdd:PRK13145 82 ELYKAWPEVGGIVHTHSTEAVGWAQAGRDIPFYGTTHADYFYGPIPCARSLTKDEVNGAYEKETGSVIIEEFEKRGLDPM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497978338 161 ATPAVLVSQHGPFTWGVDASKSVYNAKVLEVSAEISYHALQSTRSDIHVPQYLLDKHYYRKHGVNAYYGQK 231
Cdd:PRK13145 162 AVPGIVVRNHGPFTWGKNPEQAVYHSVVLEEVAKMNRLTEQINPRVEPAPQYIMDKHYLRKHGPNAYYGQK 232
|
|
| sgbE |
PRK12347 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
1-230 |
5.55e-109 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 183459 Cd Length: 231 Bit Score: 313.29 E-value: 5.55e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 1 MLEELKNEVYQANMSLPKLGLVTFTWGNVSGIDREKGLFVIKPSGVAYEDLKPDDMVVVDL-DGNVVEGDLNPSSDTPTH 79
Cdd:PRK12347 1 MLEQLKADVLAANLALPAHHLVTFTWGNVSAVDETRQLMVIKPSGVEYDVMTADDMVVVEIaSGKVVEGSKKPSSDTPTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 80 AYLYRHFKNIGGITHTHSPWGVSFAAAQMDIPAVSTTHADTFYGDIPCTPALSQEEIQSAYELNTGKVIVSEFEQRQIDP 159
Cdd:PRK12347 81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTAEEINGEYEYQTGEVIIETFEERGISP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497978338 160 DATPAVLVSQHGPFTWGVDASKSVYNAKVLEvsaEISYHALQSTRSDIHVP---QYLLDKHYYRKHGVNAYYGQ 230
Cdd:PRK12347 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLE---ECAYMGLFSRQLAPQLPamqNELLDKHYLRKHGANAYYGQ 231
|
|
| araD |
PRK13213 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
1-230 |
2.70e-87 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 106181 Cd Length: 231 Bit Score: 258.12 E-value: 2.70e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 1 MLEELKNEVYQANMSLPKLGLVTFTWGNVSGIDREKGLFVIKPSGVAYEDLKPDDMVVVDL-DGNVVEGDLNPSSDTPTH 79
Cdd:PRK13213 1 MLEQLKQQVFEANLALPKYKLVTFTWGNVSGIDREHGLVVIKPSGVEYDVMSVNDMVVVDLaTGKVVEGDKKPSSDTDTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 80 AYLYRHFKNIGGITHTHSPWGVSFAAAQMDIPAVSTTHADTFYGDIPCTPALSQEEIQSAYELNTGKVIVSEFEQRQIDP 159
Cdd:PRK13213 81 LVLYRAFAEIGGIVHTHSRHATIWAQAGKSLSALGTTHADYFYGPIPCTRLMTEAEITGDYEHETGKVIVETFAEQGLRA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497978338 160 DATPAVLVSQHGPFTWGVDASKSVYNAKVLEVSAEISYHALQSTRSDIHVPQYLLDKHYYRKHGVNAYYGQ 230
Cdd:PRK13213 161 ADIPAVLVNGHGPFAWGSNAANAVHNAVVLEEIAYMNLFTHQLTPGVGDMQQTLLDKHYLRKHGAAAYYGQ 231
|
|
| PRK06557 |
PRK06557 |
L-ribulose-5-phosphate 4-epimerase; Validated |
1-230 |
2.03e-75 |
|
L-ribulose-5-phosphate 4-epimerase; Validated
Pssm-ID: 235829 [Multi-domain] Cd Length: 221 Bit Score: 227.58 E-value: 2.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 1 MLEELKNEVYQANMSLPKLGLVTFTWGNVSGIDREKGLFVIKPSGVAYEDLKPDDMVVVDLDGNVVEGDLNPSSDTPTHA 80
Cdd:PRK06557 7 MVEKLREEVCKLHLELPKYGLVVWTSGNVSARDPGTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVEGDLKPSSDTASHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 81 YLYRHFKNIGGITHTHSPWGVSFAAAQMDIPAVSTTHADTFYGDIPCTP-AL-SQEEIqsayelntGKVIVsefeqRQID 158
Cdd:PRK06557 87 YVYRHMPDVGGVVHTHSTYATAWAARGEPIPCVLTAMADEFGGPIPVGPfALiGDEAI--------GKGIV-----ETLK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497978338 159 PDATPAVLVSQHGPFTWGVDASKSVYNAKVLEVSAEISYHALQSTRSdIHVPQYLLDKHYYRKHGVnayYGQ 230
Cdd:PRK06557 154 GGRSPAVLMQNHGVFTIGKDAEDAVKAAVMVEEVARTVHIARQLGEP-IPIPQEEIDRLYDRYQNV---YGQ 221
|
|
| Aldolase_II |
cd00398 |
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ... |
3-222 |
5.58e-71 |
|
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). Class II enzymes are further divided into two sub-classes A and B. This family includes class II A aldolases and adducins which has not been ascribed any enzymatic function. Members of this class are primarily bacterial and eukaryotic in origin and include L-fuculose-1-phosphate, L-rhamnulose-1-phosphate aldolases and L-ribulose-5-phosphate 4-epimerases. They all share the ability to promote carbon-carbon bond cleavage and stabilize enolate intermediates using divalent cations.
Pssm-ID: 238232 [Multi-domain] Cd Length: 209 Bit Score: 216.08 E-value: 5.58e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 3 EELKNEVYQANMSLPKLGLVTFTWGNVSGIDREKGLFVIKPSGVAYEDLKPDDMVVVDLDGNVVEGDLnPSSDTPTHAYL 82
Cdd:cd00398 1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVEGKK-PSSETPLHLAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 83 YRHFKNIGGITHTHSPWGVSFAAAQ-MDIPAVSTTHADTFYGDIPCTPALSQEeiqsayelnTGKVIVSEFEQRQIdpDA 161
Cdd:cd00398 80 YRARPDIGCIVHTHSTHATAVSQLKeGLIPAGHTACAVYFTGDIPCTPYMTPE---------TGEDEIGTQRALGF--PN 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497978338 162 TPAVLVSQHGPFTWGVDASKSVYNAKVLEVSAEISYHALQSTRSDIHVPQYLLDKHYYRKH 222
Cdd:cd00398 149 SKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
|
|
| AraD |
COG0235 |
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ... |
1-223 |
1.86e-69 |
|
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440005 [Multi-domain] Cd Length: 208 Bit Score: 212.00 E-value: 1.86e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 1 MLEELKNEVYQANMSLPKLGLVTFTWGNVSGIDREkGLFVIKPSGVAYEDLKPDDMVVVDLDGNVVEGDLNPSSDTPTHA 80
Cdd:COG0235 2 EEEELREELAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKPSSETPLHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 81 YLYRHFKNIGGITHTHSPWGVSFAAAQMDIPAVSTTHADTFYGDIPCTPalsqeeiqsaYElntgkVIVSEFEQRQIDPD 160
Cdd:COG0235 81 AIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVP----------YA-----GPGTEELAEAIAEA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497978338 161 A--TPAVLVSQHGPFTWGVDASKSVYNAKVLEVSAEISYHALQsTRSDIHVPQYLLDKHyYRKHG 223
Cdd:COG0235 146 LgdRPAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALA-LGGPLVLSDEEIDKL-ARKFG 208
|
|
| Aldolase_II |
pfam00596 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
7-197 |
7.22e-61 |
|
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.
Pssm-ID: 459862 [Multi-domain] Cd Length: 178 Bit Score: 188.91 E-value: 7.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 7 NEVYQANMSLPKLGLVTFTWGNVSGIDrEKGLFVIKPSGVAYEDLKPDDMVVVDLDGNVVEGDLNPSSDTPTHAYLYRHF 86
Cdd:pfam00596 1 EELAAAGRLLARRGLVEGTGGNISVRL-PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGLKPSSETPLHLAIYRAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 87 KNIGGITHTHSPWGVSFAAAQMDIPAVSTTHADTFYGDIPCTPALSQEEIQsayelnTGKVIVSEFEqrqidpDATPAVL 166
Cdd:pfam00596 80 PDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTEE------LGERIAEALG------GDRKAVL 147
|
170 180 190
....*....|....*....|....*....|.
gi 497978338 167 VSQHGPFTWGVDASKSVYNAKVLEVSAEISY 197
Cdd:pfam00596 148 LRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
|
|
| Aldolase_II |
smart01007 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
9-197 |
1.01e-57 |
|
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.
Pssm-ID: 214970 [Multi-domain] Cd Length: 185 Bit Score: 181.30 E-value: 1.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 9 VYQANMSLPKLGLVTFTWGNVSGIDREKGLFVIKPSGVAYEDLKPDDMVVVDLDGNVVEGDL--NPSSDTPTHAYLYRHF 86
Cdd:smart01007 1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGgpKPSSETPLHLAIYRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 87 KNIGGITHTHSPWGVSFAAAQMDIPAVSTTHADTFYG-DIPCTPALSQEEIQSAYELNTGKVIVSEFEQRqidpdatPAV 165
Cdd:smart01007 81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGAELAEALAEALPDR-------PAV 153
|
170 180 190
....*....|....*....|....*....|..
gi 497978338 166 LVSQHGPFTWGVDASKSVYNAKVLEVSAEISY 197
Cdd:smart01007 154 LLRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
|
|
| PRK06833 |
PRK06833 |
L-fuculose-phosphate aldolase; |
1-199 |
2.36e-27 |
|
L-fuculose-phosphate aldolase;
Pssm-ID: 180717 [Multi-domain] Cd Length: 214 Bit Score: 104.06 E-value: 2.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 1 MLEELKNEVYQANMSLPKLGLVTFTWGNVSGIDREKGLFVIKPSGVAYEDLKPDDMVVVDLDGNVVEGDLNPSSDTPTHA 80
Cdd:PRK06833 2 LLQKEREEIVAYGKKLISSGLTKGTGGNISIFNREQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVEGERKPSSELDMHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 81 YLYRHFKNIGGITHTHSPWGVSFAAAQMDIPAVSTTHAdtFYG-DIPCTPAL---SQEEIQSAYElntgkvivsEFEQRQ 156
Cdd:PRK06833 82 IFYRNREDINAIVHTHSPYATTLACLGWELPAVHYLIA--VAGpNVRCAEYAtfgTKELAENAFE---------AMEDRR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 497978338 157 idpdatpAVLVSQHGPFTWGVDASKSVYNAKVLEVSAEISYHA 199
Cdd:PRK06833 151 -------AVLLANHGLLAGANNLKNAFNIAEEIEFCAEIYYQT 186
|
|
| PRK05874 |
PRK05874 |
L-fuculose-phosphate aldolase; Validated |
9-199 |
9.02e-21 |
|
L-fuculose-phosphate aldolase; Validated
Pssm-ID: 102036 [Multi-domain] Cd Length: 217 Bit Score: 87.01 E-value: 9.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 9 VYQANMSLPKLGLVTFTWGNVSGiDREKGLFVIKPSGVAYEDLKPDDMVVVDLDGNVVEGD--LNPSSDTPTHAYLYRHF 86
Cdd:PRK05874 11 VLAAAKDMLRRGLVEGTAGNISA-RRSDGNVVITPSSVDYAEMLLHDLVLVDAGGAVLHAKdgRSPSTELNLHLACYRAF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 87 KNIGGITHTHSPWGVSFAAAQMDIPAVSTTHADTFYGDIPCTpalsqeEIQSAYELNTGKVIVSEFEQRQidpdatpAVL 166
Cdd:PRK05874 90 DDIGSVIHSHPVWATMFAVAHEPIPACIDEFAIYCGGDVRCT------EYAASGTPEVGRNAVRALEGRA-------AAL 156
|
170 180 190
....*....|....*....|....*....|...
gi 497978338 167 VSQHGPFTWGVDASKSVYNAKVLEVSAEISYHA 199
Cdd:PRK05874 157 IANHGLVAVGPRPDQVLRVTALVERTAQIVWGA 189
|
|
| PRK08087 |
PRK08087 |
L-fuculose-phosphate aldolase; |
3-209 |
5.93e-14 |
|
L-fuculose-phosphate aldolase;
Pssm-ID: 181226 [Multi-domain] Cd Length: 215 Bit Score: 68.23 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 3 EELKNEVYQANMSLPKLGLVTFTWGNVSGidREKGLFVIKPSGVAYEDLKPDDMVVVDLDGNVVEGDLnPSSDTPTHAYL 82
Cdd:PRK08087 4 NKLARQIIDTCLEMTRLGLNQGTAGNVSV--RYQDGMLITPTGIPYEKLTESHIVFVDGNGKHEEGKL-PSSEWRFHMAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 83 YRHFKNIGGITHTHSPWGVSFAAAQMDIPAVSTTHADTFYGDIPCTPALSQEEIQSAYELNTGkvivseFEQRQidpdat 162
Cdd:PRK08087 81 YQTRPDANAVVHNHAVHCTAVSILNRPIPAIHYMIAAAGGNSIPCAPYATFGTRELSEHVALA------LKNRK------ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497978338 163 pAVLVSQHGPFTWGVDASKSVYNAKVLEVSAEIsYHALQSTRSDIHV 209
Cdd:PRK08087 149 -ATLLQHHGLIACEVNLEKALWLAHEVEVLAQL-YLKTLAITDPVPV 193
|
|
| PRK08130 |
PRK08130 |
putative aldolase; Validated |
4-193 |
1.21e-12 |
|
putative aldolase; Validated
Pssm-ID: 181241 [Multi-domain] Cd Length: 213 Bit Score: 64.90 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 4 ELKNEVYQANMSLPKLGLVTFTWGNVSgIDREKGLFVIKPSGVAYEDLKPDDMVVVDLDGNVVEGDlNPSSDTPTHAYLY 83
Cdd:PRK08130 5 ALREEIVRLGRSLFQRGYTVGSAGNIS-ARLDDGGWLVTPTGSCLGRLDPARLSKVDADGNWLSGD-KPSKEVPLHRAIY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 84 RHFKNIGGITHTHSPWGVSFAAA-----QMDIPAVstthadTFY-----GDIPCTPALSQEEIQSAYELntgkvivsefe 153
Cdd:PRK08130 83 RNNPECGAVVHLHSTHLTALSCLggldpTNVLPPF------TPYyvmrvGHVPLIPYYRPGDPAIAEAL----------- 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 497978338 154 qRQIDPDATpAVLVSQHGPFTWGVDASKSVYNAKVLEVSA 193
Cdd:PRK08130 146 -AGLAARYR-AVLLANHGPVVWGSSLEAAVNATEELEETA 183
|
|
| PRK08333 |
PRK08333 |
aldolase; |
20-197 |
1.73e-11 |
|
aldolase;
Pssm-ID: 181393 [Multi-domain] Cd Length: 184 Bit Score: 60.99 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 20 GLVTFTWGNVSgiDREKGLFVIKPSGVAYEDLKPDDMVVVDLDGNVVEgDLNPSSDTPTHAYLYRHFKNIGGITHTHSPW 99
Cdd:PRK08333 19 GLTAAFGGNLS--IRVGNLVFIKATGSVMDELTREQVAVIDLNGNQLS-SVRPSSEYRLHLAVYRNRPDVRAIAHLHPPY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 100 GVSFAAA-QMDIPAVsTTHADTFYGDIPCTPALSQEEIQSAYElntgkviVSEFeQRQIDpdatpAVLVSQHGPFTWGVD 178
Cdd:PRK08333 96 SIVASTLlEEELPII-TPEAELYLKKIPILPFRPAGSVELAEQ-------VAEA-MKEYD-----AVIMERHGIVTVGRS 161
|
170
....*....|....*....
gi 497978338 179 ASKSVYNAKVLEVSAEISY 197
Cdd:PRK08333 162 LREAFYKAELVEESAKLWY 180
|
|
| PRK09220 |
PRK09220 |
methylthioribulose 1-phosphate dehydratase; |
51-98 |
3.40e-10 |
|
methylthioribulose 1-phosphate dehydratase;
Pssm-ID: 236415 [Multi-domain] Cd Length: 204 Bit Score: 57.64 E-value: 3.40e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 497978338 51 LKPDDMVVVDLDGNVVEGDLNPSSDTPTHAYLYRHFKNIGGITHTHSP 98
Cdd:PRK09220 51 LTAEDFLQVDIAGNAVPSGRKPSAETLLHTQLYRLFPEIGAVLHTHSV 98
|
|
| mtnB |
PRK06754 |
methylthioribulose 1-phosphate dehydratase; |
25-190 |
2.84e-09 |
|
methylthioribulose 1-phosphate dehydratase;
Pssm-ID: 180679 [Multi-domain] Cd Length: 208 Bit Score: 55.06 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 25 TWGNVS-GIDREKGLFVIKPSGVAYEDLKPDDMVVVDLDGNVVEG-DLNPSSDTPTHAYLYRHfKNIGGITHTHSPWG-- 100
Cdd:PRK06754 27 TSGNLSiKVSDDPLTFLVTASGKDKRKTTPEDFLLVDHDGKPVEEtELKPSAETLLHTHIYNN-TNAGCVLHVHTVDNnv 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 101 ----------VSFAAAQMdIPAVSTTHADTF--------YGDIpctPALSQEeiqsayelnTGKVIVSEfeqrqidpdaT 162
Cdd:PRK06754 106 iselygddgaVTFQGQEI-IKALGIWEENAEihipiienHADI---PTLAEE---------FAKHIQGD----------S 162
|
170 180
....*....|....*....|....*...
gi 497978338 163 PAVLVSQHGPFTWGVDASKSvynAKVLE 190
Cdd:PRK06754 163 GAVLIRNHGITVWGRDAFEA---KKHLE 187
|
|
| PRK07090 |
PRK07090 |
class II aldolase/adducin domain protein; Provisional |
2-194 |
2.28e-08 |
|
class II aldolase/adducin domain protein; Provisional
Pssm-ID: 180832 Cd Length: 260 Bit Score: 53.10 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 2 LEELKNEVYQANMSL-PKLGL---VTFTWGNVSGI-------DREKGLFVIKPSGVAYEDLKPDDMVVVDLDGNVVEGDL 70
Cdd:PRK07090 17 QRQMDNELKDSGWTLrQKLALtcrILFDAGHDSGLagqitarAEAPGTYYTQRLGLGFDEITASNLLLVDEDLNVLDGEG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 71 NPSSDTPTHAYLYRHFKNIGGITHTHSPWgVSfAAAQMDIPAVsTTHADT--------FYGDIPCTPALSQEeiqsayel 142
Cdd:PRK07090 97 MPNPANRFHSWIYRARPDVNCIIHTHPPH-VA-ALSMLEVPLV-VSHMDTcplyddcaFLKDWPGVPVGNEE-------- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497978338 143 ntGKVIVSEFEQRQidpdatpAVLVSQHGPFTwgvdASKSVYNAKVLEVSAE 194
Cdd:PRK07090 166 --GEIISAALGDKR-------AILLSHHGQLV----AGKSIEEACVLALLIE 204
|
|
| PRK06357 |
PRK06357 |
hypothetical protein; Provisional |
27-200 |
3.24e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 180541 [Multi-domain] Cd Length: 216 Bit Score: 52.47 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 27 GNVS---GIDREKGLFVIKPSGVA---YEDLKPDDMVVVDLD-GNVVEGDLNPSSDTPTHAYLYRHFKNIGGITHTHSPW 99
Cdd:PRK06357 28 GNISvrmTAEKNKEYIIMTPTLMSeakLCDLSPYQILVVDLNtGEVIEGVGRVTREINMHEAAYVANPKIKCVYHSHAKE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 100 GVSFAAAQMDIPAVstTHADTFYGDIPC---TPALSQE--EIQSAYELNTGKvivsefeqrqidpDATP-AVLVSQHGPF 173
Cdd:PRK06357 108 SMFWATLGLEMPNL--TEATQKLGKIPTlpfAPATSPElaEIVRKHLIELGD-------------KAVPsAFLLNSHGIV 172
|
170 180
....*....|....*....|....*..
gi 497978338 174 TWGVDASKSVYNAKVLEVSAEISYHAL 200
Cdd:PRK06357 173 ITDTSLHKAYDILETIEWNAYIAYQAT 199
|
|
| PRK06486 |
PRK06486 |
aldolase; |
37-99 |
7.58e-08 |
|
aldolase;
Pssm-ID: 235814 Cd Length: 262 Bit Score: 51.64 E-value: 7.58e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497978338 37 GLFVIKPSGVAYEDLKPDDMVVVDLDGNVVEGDLNPSsdtPT----HAYLYRHFKNIGGITHTHSPW 99
Cdd:PRK06486 60 DLFLVNPYGYAFSEITASDLLICDFDGNVLAGRGEPE---ATaffiHARIHRAIPRAKAAFHTHMPY 123
|
|
| PRK07044 |
PRK07044 |
aldolase II superfamily protein; Provisional |
35-217 |
7.22e-07 |
|
aldolase II superfamily protein; Provisional
Pssm-ID: 235916 Cd Length: 252 Bit Score: 48.69 E-value: 7.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 35 EKGLFVIKPSGVAYEDLKPDDMVVVDLDGNVVEG---DLNPSSDTpTHAYLYRHFKNIGGITHTHSPWGVSFAAAQMDIP 111
Cdd:PRK07044 48 EEHHFLINPYGLLFDEITASNLVKIDLDGNVVDDspyPVNPAGFT-IHSAIHAARPDAHCVMHTHTTAGVAVSAQRDGLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 112 AVStTHADTFYGDIpctpalsqeeiqsAYELNTGkVIVSEFEQRQIDPDA--TPAVLVSQHGPFTWGVDASKSVYNAKVL 189
Cdd:PRK07044 127 PLS-QHALQFYGRL-------------AYHDYEG-IALDLDEGERLVADLgdKPAMLLRNHGLLTVGRTVAEAFLLMYTL 191
|
170 180
....*....|....*....|....*...
gi 497978338 190 EVSAEISYHALQSTRSDIHVPQYLLDKH 217
Cdd:PRK07044 192 ERACEIQVAAQAGGGELVLPPPEVAERT 219
|
|
| PRK06208 |
PRK06208 |
class II aldolase/adducin family protein; |
38-105 |
7.82e-06 |
|
class II aldolase/adducin family protein;
Pssm-ID: 235743 Cd Length: 274 Bit Score: 45.75 E-value: 7.82e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 38 LFVIKPSGVAYEDLKPDDMVVVDLDGNVVEGD--LNPSSDTpTHAYLYRHFKNIGGITHTHSPWGVSFAA 105
Cdd:PRK06208 77 HFWVNPLGVHFSQIKVSDLLLVDHDGEVVEGDrpLNRAAFA-IHSAIHEARPDVVAAAHTHSTYGKAWST 145
|
|
| RhaD |
COG3347 |
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ... |
30-185 |
9.56e-06 |
|
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase [Carbohydrate transport and metabolism];
Pssm-ID: 442576 [Multi-domain] Cd Length: 674 Bit Score: 46.06 E-value: 9.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 30 SGIDrekgLFVIKPSGVA---YEDLKP---------DDMVVVdLDGNVVE-GDLNPSSDTPTHAYL-YRHfkniggITHT 95
Cdd:COG3347 64 SGGD----LATIEPAGFAalrLDPLRAlrelgvlsdDEMVNL-LRHCLFDlNAPAPSIETLLHAFLpHKH------VDHT 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 96 HSPWGVSFAAAQmDIPAVstthADTFYGD----IPctpalsqeEIQSAYELntGKVIVSEFEQrqiDPDATPAVLVSqHG 171
Cdd:COG3347 133 HPDAVIAIANAP-DGEEL----TREIFGDrvgwVP--------YVRPGFDL--ALALAEAFRA---NPGAEGVVLGK-HG 193
|
170
....*....|....
gi 497978338 172 PFTWGvDASKSVYN 185
Cdd:COG3347 194 LFTWG-DTAKESYE 206
|
|
| PRK06661 |
PRK06661 |
hypothetical protein; Provisional |
4-210 |
2.19e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 168637 Cd Length: 231 Bit Score: 44.05 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 4 ELKNEVYQANMSLPKLGLVTFTWGNVSGIDREKGLFVIKPSGVAYEDLKPDDMVVVDLDGNVVEGDLNPSSDTP--THAY 81
Cdd:PRK06661 2 DIKYNLAAAYRIMAYLSLDDHTYTHLSARPKNADFYYIYPFGLRFEEVTTENLLKVSLDGQILEGEEYQYNKTGyfIHGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 82 LYRHFKNIGGITHTHSPWGVSFAAAQMDIPAVStTHADTFYGDIpctpalsqeeiqSAYELNT--------GKVIVSEFE 153
Cdd:PRK06661 82 IYKTRPDISAIFHYHTPASIAVSALKCGLLPIS-QWALHFYDRI------------SYHNYNSlaldadkqSSRLVNDLK 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497978338 154 QRQidpdatpAVLVSQHGPFTWGVDASKSVYNAKVLEVSAEISYHALQSTRSDIHVP 210
Cdd:PRK06661 149 QNY-------VMLLRNHGAITCGKTIHEAMFYTYHLEQACKTQCLLNSTKKQELIIP 198
|
|
| PRK08660 |
PRK08660 |
aldolase; |
20-101 |
4.71e-05 |
|
aldolase;
Pssm-ID: 181527 [Multi-domain] Cd Length: 181 Bit Score: 42.64 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 20 GLVTFTWGNVSgiDREKGLFVIKPSGVAYEDLKPDDMVVVDLDGNvveGDLNP--SSDTPTHAYLYRHfKNIGGITHTHS 97
Cdd:PRK08660 16 GLVSSHFGNIS--VRTGDGLLITRTGSMLDEITEGDVIEVGIDDD---GSVDPlaSSETPVHRAIYRR-TSAKAIVHAHP 89
|
....
gi 497978338 98 PWGV 101
Cdd:PRK08660 90 PYAV 93
|
|
| PRK08324 |
PRK08324 |
bifunctional aldolase/short-chain dehydrogenase; |
38-185 |
9.05e-04 |
|
bifunctional aldolase/short-chain dehydrogenase;
Pssm-ID: 236241 [Multi-domain] Cd Length: 681 Bit Score: 40.21 E-value: 9.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 38 LFViKPSGVAYEDLKPDDMVVVDLD------GNVVEGD----------------LNPSSDTPTHAYL-YRHfkniggITH 94
Cdd:PRK08324 57 LWV-KGSGGDLATITAAGFAALRLDplralkELGVLSDdemvaylrhclfdpnaPAPSIETLLHAFLpFKH------VDH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497978338 95 THSPWGVSFAAAQmDIPAVSTThadtFYGD----IPctpalsqeEIQSAYELntGKVIVSEFEQrqiDPDATPAVLVSqH 170
Cdd:PRK08324 130 THPDAIIAIANAP-DGEELTRE----IFGDrvgwVP--------YVRPGFDL--ALAIAEAVRA---NPGAEGVVLGK-H 190
|
170
....*....|....*
gi 497978338 171 GPFTWGvDASKSVYN 185
Cdd:PRK08324 191 GLFTWG-DTAKEAYE 204
|
|
| |
