|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09220 |
PRK09220 |
methylthioribulose 1-phosphate dehydratase; |
1-204 |
3.24e-143 |
|
methylthioribulose 1-phosphate dehydratase;
Pssm-ID: 236415 [Multi-domain] Cd Length: 204 Bit Score: 397.00 E-value: 3.24e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 1 MTENPQLTALLAACHWIGDKGWCPATGGNMSLRLDERQCLVTESGKDKGSLSAADFLQVDIADNHVPSGRTPSAETGLHT 80
Cdd:PRK09220 1 MTLEELLQQLIAAGRWIGARGWVPATSGNMSVRLDEQHCAITVSGKDKGSLTAEDFLQVDIAGNAVPSGRKPSAETLLHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 81 LLYRLYPHLGAVLHTHSVNATVLSRVERGDALVLQGYEMQKSLAGQRSHLDSVAIPIFDNDQDIPRLASRVAAYAEVTPL 160
Cdd:PRK09220 81 QLYRLFPEIGAVLHTHSVNATVLSRVEKSDALVLEGYELQKAFAGQTTHETAVVVPIFDNDQDIARLAARVAPYLDAQPL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515495745 161 QYGFLVRGHGLYCWGSQVAEARRHLEGLEFLFQCELQRRLLEAK 204
Cdd:PRK09220 161 RYGYLIRGHGLYCWGRDMAEARRHLEGLEFLFECELERRLLEAK 204
|
|
| salvage_mtnB |
TIGR03328 |
methylthioribulose-1-phosphate dehydratase; Members of this family are the ... |
10-201 |
1.87e-98 |
|
methylthioribulose-1-phosphate dehydratase; Members of this family are the methylthioribulose-1-phosphate dehydratase of the methionine salvage pathway. This pathway allows methylthioadenosine, left over from polyamine biosynthesis, to be recycled to methionine. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 274521 [Multi-domain] Cd Length: 192 Bit Score: 283.39 E-value: 1.87e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 10 LLAACHWIGDKGWCPATGGNMSLRLDERQCLVTESGKDKGSLSAADFLQVDIADNHVPSGRTPSAETGLHTLLYRLYpHL 89
Cdd:TIGR03328 1 LIEAGRDLYKRGWVPGTGGNLSARLDEDEILITPSGVDKGRLTPEDFLVVDLQGKPVSGGLKPSAETLLHTQLYRLT-GA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 90 GAVLHTHSVNATVLSRVERGDA-LVLQGYEMQKSLAGQRSHLDSVAIPIFDNDQDIPRLASRVAAYAEVTPLQYGFLVRG 168
Cdd:TIGR03328 80 GAVLHTHSVEATVLSRLYPSNGgFELEGYEMLKGLPGITTHEDTLVVPIIENTQDIARLADSVAPALNAYPDVPGVLIRG 159
|
170 180 190
....*....|....*....|....*....|...
gi 515495745 169 HGLYCWGSQVAEARRHLEGLEFLFQCELQRRLL 201
Cdd:TIGR03328 160 HGLYAWGRDWEEAKRHLEALEFLFECELEMLKL 192
|
|
| AraD |
COG0235 |
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ... |
1-201 |
1.61e-54 |
|
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: 172.71 E-value: 1.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 1 MTENPQLTALLAACHWIGDKGWCPATGGNMSLRLDERQCLVTESGKDKGSLSAADFLQVDIADNHVPSGRTPSAETGLHT 80
Cdd:COG0235 1 MEEEELREELAAAGRRLARRGLVDGTAGNISVRLDDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKPSSETPLHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 81 LLYRLYPHLGAVLHTHSVNATVLSRVERGdalvLQGYEMQKSLAGQRShldsvaIPIFD-NDQDIPRLASRVAAYAEVTP 159
Cdd:COG0235 81 AIYRARPDVGAVVHTHSPYATALSALGEP----LPPLEQTEAAAFLGD------VPVVPyAGPGTEELAEAIAEALGDRP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515495745 160 lqyGFLVRGHGLYCWGSQVAEARRHLEGLEFLFQCELQRRLL 201
Cdd:COG0235 151 ---AVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALAL 189
|
|
| Aldolase_II |
smart01007 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
10-196 |
1.35e-50 |
|
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: 161.65 E-value: 1.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 10 LLAACHWIGDKGWCPATGGNMSLRLDER-QCLVTESGKDKGSLSAADFLQVDIADNHVPSGRT--PSAETGLHTLLYRLY 86
Cdd:smart01007 1 LAAACRLLARRGLVEGTGGNISARVGEEdLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGGpkPSSETPLHLAIYRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 87 PHLGAVLHTHSVNATVLSRVerGDALVLQGYEMQKSLAGQRSHLDSVAIPIFDNDQDIPRLASRVAAYAEVTPlqyGFLV 166
Cdd:smart01007 81 PDVGAVVHTHSPYATALAAL--GKPLPLLPTEQAAAFLGGEIPYAPYAGPGTELAEEGAELAEALAEALPDRP---AVLL 155
|
170 180 190
....*....|....*....|....*....|
gi 515495745 167 RGHGLYCWGSQVAEARRHLEGLEFLFQCEL 196
Cdd:smart01007 156 RNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
|
|
| Aldolase_II |
pfam00596 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
9-196 |
3.01e-48 |
|
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: 155.40 E-value: 3.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 9 ALLAACHWIGDKGWCPATGGNMSLRLDERQCLVTESGKDKGSLSAADFLQVDIADNHVPSGRTPSAETGLHTLLYRLYPH 88
Cdd:pfam00596 2 ELAAAGRLLARRGLVEGTGGNISVRLPGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGLKPSSETPLHLAIYRARPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 89 LGAVLHTHSVNATVLSRVERGdaLVLQGYEMQKSLAGQrshldsvaIPIFDNDQ-DIPRLASRVAAYAEVTPlqYGFLVR 167
Cdd:pfam00596 82 AGAVVHTHSPYATALSLAKEG--LPPITQEAADFLGGD--------IPIIPYYTpGTEELGERIAEALGGDR--KAVLLR 149
|
170 180
....*....|....*....|....*....
gi 515495745 168 GHGLYCWGSQVAEARRHLEGLEFLFQCEL 196
Cdd:pfam00596 150 NHGLLVWGKTLEEAFYLAEELERAAEIQL 178
|
|
| Aldolase_II |
cd00398 |
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ... |
9-201 |
5.82e-25 |
|
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: 96.67 E-value: 5.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 9 ALLAACHWIGDKGWCPATGGNMSLRLDERQC-LVTESGKDKGSLSAADFLQVDIADNHVPSGRtPSAETGLHTLLYRLYP 87
Cdd:cd00398 6 KIIAACLLLDLYGWVTGTGGNVSARDRDRGYfLITPSGVDYEEMTASDLVVVDAQGKVVEGKK-PSSETPLHLALYRARP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 88 HLGAVLHTHSVNATVLSRVERGdALVLQGYEmqkslagqrsHLDSV--AIPIFDNDQDIPRLASRVAAYAEVTPLQYGFL 165
Cdd:cd00398 85 DIGCIVHTHSTHATAVSQLKEG-LIPAGHTA----------CAVYFtgDIPCTPYMTPETGEDEIGTQRALGFPNSKAVL 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 515495745 166 VRGHGLYCWGSQVAEARRHLEGLEFLfqCELQRRLL 201
Cdd:cd00398 154 LRNHGLFAWGPTLDEAFHLAVVLEVA--AEIQLKAL 187
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09220 |
PRK09220 |
methylthioribulose 1-phosphate dehydratase; |
1-204 |
3.24e-143 |
|
methylthioribulose 1-phosphate dehydratase;
Pssm-ID: 236415 [Multi-domain] Cd Length: 204 Bit Score: 397.00 E-value: 3.24e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 1 MTENPQLTALLAACHWIGDKGWCPATGGNMSLRLDERQCLVTESGKDKGSLSAADFLQVDIADNHVPSGRTPSAETGLHT 80
Cdd:PRK09220 1 MTLEELLQQLIAAGRWIGARGWVPATSGNMSVRLDEQHCAITVSGKDKGSLTAEDFLQVDIAGNAVPSGRKPSAETLLHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 81 LLYRLYPHLGAVLHTHSVNATVLSRVERGDALVLQGYEMQKSLAGQRSHLDSVAIPIFDNDQDIPRLASRVAAYAEVTPL 160
Cdd:PRK09220 81 QLYRLFPEIGAVLHTHSVNATVLSRVEKSDALVLEGYELQKAFAGQTTHETAVVVPIFDNDQDIARLAARVAPYLDAQPL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515495745 161 QYGFLVRGHGLYCWGSQVAEARRHLEGLEFLFQCELQRRLLEAK 204
Cdd:PRK09220 161 RYGYLIRGHGLYCWGRDMAEARRHLEGLEFLFECELERRLLEAK 204
|
|
| salvage_mtnB |
TIGR03328 |
methylthioribulose-1-phosphate dehydratase; Members of this family are the ... |
10-201 |
1.87e-98 |
|
methylthioribulose-1-phosphate dehydratase; Members of this family are the methylthioribulose-1-phosphate dehydratase of the methionine salvage pathway. This pathway allows methylthioadenosine, left over from polyamine biosynthesis, to be recycled to methionine. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 274521 [Multi-domain] Cd Length: 192 Bit Score: 283.39 E-value: 1.87e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 10 LLAACHWIGDKGWCPATGGNMSLRLDERQCLVTESGKDKGSLSAADFLQVDIADNHVPSGRTPSAETGLHTLLYRLYpHL 89
Cdd:TIGR03328 1 LIEAGRDLYKRGWVPGTGGNLSARLDEDEILITPSGVDKGRLTPEDFLVVDLQGKPVSGGLKPSAETLLHTQLYRLT-GA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 90 GAVLHTHSVNATVLSRVERGDA-LVLQGYEMQKSLAGQRSHLDSVAIPIFDNDQDIPRLASRVAAYAEVTPLQYGFLVRG 168
Cdd:TIGR03328 80 GAVLHTHSVEATVLSRLYPSNGgFELEGYEMLKGLPGITTHEDTLVVPIIENTQDIARLADSVAPALNAYPDVPGVLIRG 159
|
170 180 190
....*....|....*....|....*....|...
gi 515495745 169 HGLYCWGSQVAEARRHLEGLEFLFQCELQRRLL 201
Cdd:TIGR03328 160 HGLYAWGRDWEEAKRHLEALEFLFECELEMLKL 192
|
|
| AraD |
COG0235 |
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ... |
1-201 |
1.61e-54 |
|
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: 172.71 E-value: 1.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 1 MTENPQLTALLAACHWIGDKGWCPATGGNMSLRLDERQCLVTESGKDKGSLSAADFLQVDIADNHVPSGRTPSAETGLHT 80
Cdd:COG0235 1 MEEEELREELAAAGRRLARRGLVDGTAGNISVRLDDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKPSSETPLHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 81 LLYRLYPHLGAVLHTHSVNATVLSRVERGdalvLQGYEMQKSLAGQRShldsvaIPIFD-NDQDIPRLASRVAAYAEVTP 159
Cdd:COG0235 81 AIYRARPDVGAVVHTHSPYATALSALGEP----LPPLEQTEAAAFLGD------VPVVPyAGPGTEELAEAIAEALGDRP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515495745 160 lqyGFLVRGHGLYCWGSQVAEARRHLEGLEFLFQCELQRRLL 201
Cdd:COG0235 151 ---AVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALAL 189
|
|
| Aldolase_II |
smart01007 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
10-196 |
1.35e-50 |
|
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: 161.65 E-value: 1.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 10 LLAACHWIGDKGWCPATGGNMSLRLDER-QCLVTESGKDKGSLSAADFLQVDIADNHVPSGRT--PSAETGLHTLLYRLY 86
Cdd:smart01007 1 LAAACRLLARRGLVEGTGGNISARVGEEdLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGGpkPSSETPLHLAIYRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 87 PHLGAVLHTHSVNATVLSRVerGDALVLQGYEMQKSLAGQRSHLDSVAIPIFDNDQDIPRLASRVAAYAEVTPlqyGFLV 166
Cdd:smart01007 81 PDVGAVVHTHSPYATALAAL--GKPLPLLPTEQAAAFLGGEIPYAPYAGPGTELAEEGAELAEALAEALPDRP---AVLL 155
|
170 180 190
....*....|....*....|....*....|
gi 515495745 167 RGHGLYCWGSQVAEARRHLEGLEFLFQCEL 196
Cdd:smart01007 156 RNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
|
|
| Aldolase_II |
pfam00596 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
9-196 |
3.01e-48 |
|
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: 155.40 E-value: 3.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 9 ALLAACHWIGDKGWCPATGGNMSLRLDERQCLVTESGKDKGSLSAADFLQVDIADNHVPSGRTPSAETGLHTLLYRLYPH 88
Cdd:pfam00596 2 ELAAAGRLLARRGLVEGTGGNISVRLPGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGLKPSSETPLHLAIYRARPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 89 LGAVLHTHSVNATVLSRVERGdaLVLQGYEMQKSLAGQrshldsvaIPIFDNDQ-DIPRLASRVAAYAEVTPlqYGFLVR 167
Cdd:pfam00596 82 AGAVVHTHSPYATALSLAKEG--LPPITQEAADFLGGD--------IPIIPYYTpGTEELGERIAEALGGDR--KAVLLR 149
|
170 180
....*....|....*....|....*....
gi 515495745 168 GHGLYCWGSQVAEARRHLEGLEFLFQCEL 196
Cdd:pfam00596 150 NHGLLVWGKTLEEAFYLAEELERAAEIQL 178
|
|
| mtnB |
PRK06754 |
methylthioribulose 1-phosphate dehydratase; |
20-201 |
1.88e-44 |
|
methylthioribulose 1-phosphate dehydratase;
Pssm-ID: 180679 [Multi-domain] Cd Length: 208 Bit Score: 146.73 E-value: 1.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 20 KGWCPATGGNMSLRL--DERQCLVTESGKDKGSLSAADFLQVDiADNHvPSGRT---PSAETGLHTLLYRLyPHLGAVLH 94
Cdd:PRK06754 21 RDWFPATSGNLSIKVsdDPLTFLVTASGKDKRKTTPEDFLLVD-HDGK-PVEETelkPSAETLLHTHIYNN-TNAGCVLH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 95 THSVNATVLSRVERGD-ALVLQGYEMQKSLaGQRSHLDSVAIPIFDNDQDIPRLASRVAAYaeVTPLQYGFLVRGHGLYC 173
Cdd:PRK06754 98 VHTVDNNVISELYGDDgAVTFQGQEIIKAL-GIWEENAEIHIPIIENHADIPTLAEEFAKH--IQGDSGAVLIRNHGITV 174
|
170 180
....*....|....*....|....*...
gi 515495745 174 WGSQVAEARRHLEGLEFLFQCELQRRLL 201
Cdd:PRK06754 175 WGRDAFEAKKHLEAYEFLFSYHIKLLSI 202
|
|
| Aldolase_II |
cd00398 |
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ... |
9-201 |
5.82e-25 |
|
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: 96.67 E-value: 5.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 9 ALLAACHWIGDKGWCPATGGNMSLRLDERQC-LVTESGKDKGSLSAADFLQVDIADNHVPSGRtPSAETGLHTLLYRLYP 87
Cdd:cd00398 6 KIIAACLLLDLYGWVTGTGGNVSARDRDRGYfLITPSGVDYEEMTASDLVVVDAQGKVVEGKK-PSSETPLHLALYRARP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 88 HLGAVLHTHSVNATVLSRVERGdALVLQGYEmqkslagqrsHLDSV--AIPIFDNDQDIPRLASRVAAYAEVTPLQYGFL 165
Cdd:cd00398 85 DIGCIVHTHSTHATAVSQLKEG-LIPAGHTA----------CAVYFtgDIPCTPYMTPETGEDEIGTQRALGFPNSKAVL 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 515495745 166 VRGHGLYCWGSQVAEARRHLEGLEFLfqCELQRRLL 201
Cdd:cd00398 154 LRNHGLFAWGPTLDEAFHLAVVLEVA--AEIQLKAL 187
|
|
| PRK08130 |
PRK08130 |
putative aldolase; Validated |
19-189 |
2.56e-14 |
|
putative aldolase; Validated
Pssm-ID: 181241 [Multi-domain] Cd Length: 213 Bit Score: 68.36 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 19 DKGWCPATGGNMSLRLDERQCLVTESGKDKGSLSAADFLQVDIADNHVpSGRTPSAETGLHTLLYRLYPHLGAVLHTHSV 98
Cdd:PRK08130 19 QRGYTVGSAGNISARLDDGGWLVTPTGSCLGRLDPARLSKVDADGNWL-SGDKPSKEVPLHRAIYRNNPECGAVVHLHST 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 99 NATVLSRVE--RGDALV--LQGYEMQKslAGQrshldsVA-IPIF---DndqdiPRLASRVAAYAevtpLQY-GFLVRGH 169
Cdd:PRK08130 98 HLTALSCLGglDPTNVLppFTPYYVMR--VGH------VPlIPYYrpgD-----PAIAEALAGLA----ARYrAVLLANH 160
|
170 180
....*....|....*....|
gi 515495745 170 GLYCWGSQVAEARRHLEGLE 189
Cdd:PRK08130 161 GPVVWGSSLEAAVNATEELE 180
|
|
| PRK05874 |
PRK05874 |
L-fuculose-phosphate aldolase; Validated |
3-104 |
1.25e-12 |
|
L-fuculose-phosphate aldolase; Validated
Pssm-ID: 102036 [Multi-domain] Cd Length: 217 Bit Score: 63.89 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 3 ENPQlTALLAACHWIGDKGWCPATGGNMSLRLDERQCLVTESGKDKGSLSAADFLQVDIADN--HVPSGRTPSAETGLHT 80
Cdd:PRK05874 5 DDPE-SAVLAAAKDMLRRGLVEGTAGNISARRSDGNVVITPSSVDYAEMLLHDLVLVDAGGAvlHAKDGRSPSTELNLHL 83
|
90 100
....*....|....*....|....
gi 515495745 81 LLYRLYPHLGAVLHTHSVNATVLS 104
Cdd:PRK05874 84 ACYRAFDDIGSVIHSHPVWATMFA 107
|
|
| PRK06557 |
PRK06557 |
L-ribulose-5-phosphate 4-epimerase; Validated |
26-102 |
2.02e-11 |
|
L-ribulose-5-phosphate 4-epimerase; Validated
Pssm-ID: 235829 [Multi-domain] Cd Length: 221 Bit Score: 60.79 E-value: 2.02e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515495745 26 TGGNMSLRLDERQCLVTE-SGKDKGSLSAADFLQVDIADNHVPSGRTPSAETGLHTLLYRLYPHLGAVLHTHSVNATV 102
Cdd:PRK06557 31 TSGNVSARDPGTDLVVIKpSGVSYDDLTPEDMVVVDLDGNVVEGDLKPSSDTASHLYVYRHMPDVGGVVHTHSTYATA 108
|
|
| sgaE |
PRK12348 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
26-181 |
2.25e-11 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 183460 Cd Length: 228 Bit Score: 60.58 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 26 TGGNMSlRLDERQCLVT--ESGKDKGSLSAADFLQVDIADNHVPSGRTPSAETGLHTLLYRLYPHLGAVLHTHSVNATvl 103
Cdd:PRK12348 24 TWGNVS-AIDRERGLVVikPSGVAYETMKADDMVVVDMSGKVVEGEYRPSSDTATHLELYRRYPSLGGIVHTHSTHAT-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 104 SRVERGDALVLQGyemqkslagqRSHLDsvaipIFDNDQDIPRLASR---------------VAAYAEVTPLQY-GFLVR 167
Cdd:PRK12348 101 AWAQAGLAIPALG----------TTHAD-----YFFGDIPCTRGLSEeevqgeyelntgkviIETLGNAEPLHTpGIVVY 165
|
170
....*....|....
gi 515495745 168 GHGLYCWGSQVAEA 181
Cdd:PRK12348 166 QHGPFAWGKDAHDA 179
|
|
| sgbE |
PRK12347 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
26-105 |
2.92e-11 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 183459 Cd Length: 231 Bit Score: 60.60 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 26 TGGNMSLRLDERQCLVTE-SGKDKGSLSAADFLQVDIAD-NHVPSGRTPSAETGLHTLLYRLYPHLGAVLHTHSVNATVL 103
Cdd:PRK12347 25 TWGNVSAVDETRQLMVIKpSGVEYDVMTADDMVVVEIASgKVVEGSKKPSSDTPTHLALYRRYPEIGGIVHTHSRHATIW 104
|
..
gi 515495745 104 SR 105
Cdd:PRK12347 105 SQ 106
|
|
| PRK06833 |
PRK06833 |
L-fuculose-phosphate aldolase; |
26-104 |
2.63e-10 |
|
L-fuculose-phosphate aldolase;
Pssm-ID: 180717 [Multi-domain] Cd Length: 214 Bit Score: 57.45 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 26 TGGNMSLRLDERQCL-VTESGKDKGSLSAADFLQVDIADNHVPSGRTPSAETGLHTLLYRLYPHLGAVLHTHSVNATVLS 104
Cdd:PRK06833 26 TGGNISIFNREQGLMaITPSGIDYFEIKPEDIVIMDLDGKVVEGERKPSSELDMHLIFYRNREDINAIVHTHSPYATTLA 105
|
|
| araD |
PRK08193 |
L-ribulose-5-phosphate 4-epimerase AraD; |
26-181 |
7.46e-10 |
|
L-ribulose-5-phosphate 4-epimerase AraD;
Pssm-ID: 236181 Cd Length: 231 Bit Score: 56.38 E-value: 7.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 26 TGGNMSLRLDERQCLVTE-SGKDKGSLSAADFLQVDIADNHVPSGRTPSAETGLHTLLYRLYPHLGAVLHTHSVNATVLS 104
Cdd:PRK08193 25 TWGNVSAIDRERGLFVIKpSGVDYDKMTAEDMVVVDLEGNVVEGKLKPSSDTPTHLVLYKAFPEIGGIVHTHSRHATAWA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 105 RvergdalvlqgyemqkslAGQrshldsvAIPIF-----DN-DQDIP--RLASR---VAAYAEVT--------------P 159
Cdd:PRK08193 105 Q------------------AGR-------DIPALgtthaDYfYGDIPctRKMTDeeiNGEYEWETgkvivetfekrgidP 159
|
170 180
....*....|....*....|...
gi 515495745 160 LQY-GFLVRGHGLYCWGSQVAEA 181
Cdd:PRK08193 160 AAVpGVLVHSHGPFTWGKDAEDA 182
|
|
| araD |
PRK13213 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
26-181 |
2.41e-09 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 106181 Cd Length: 231 Bit Score: 55.12 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 26 TGGNMSlRLDERQCLVT--ESGKDKGSLSAADFLQVDIADNHVPSG-RTPSAETGLHTLLYRLYPHLGAVLHTHSVNATV 102
Cdd:PRK13213 25 TWGNVS-GIDREHGLVVikPSGVEYDVMSVNDMVVVDLATGKVVEGdKKPSSDTDTHLVLYRAFAEIGGIVHTHSRHATI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 103 LSRVerGDALVLQGYEMQKSLAGQR--SHLDSVAIPIFDNDQDIPRLASRVAAYAEVTPLQY-GFLVRGHGLYCWGSQVA 179
Cdd:PRK13213 104 WAQA--GKSLSALGTTHADYFYGPIpcTRLMTEAEITGDYEHETGKVIVETFAEQGLRAADIpAVLVNGHGPFAWGSNAA 181
|
..
gi 515495745 180 EA 181
Cdd:PRK13213 182 NA 183
|
|
| PRK06755 |
PRK06755 |
hypothetical protein; Validated |
40-191 |
2.46e-07 |
|
hypothetical protein; Validated
Pssm-ID: 102532 Cd Length: 209 Bit Score: 49.26 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 40 LVTESGKDKGSLSAADFLQVD-IADNHVPSGRTPSAETGLHTLLYRlYPHLGAVLHTHSVNATVLSRV--ERGDALVLQG 116
Cdd:PRK06755 43 LVNVEGRDKGLFSEEDFIVVNcMCEPVFENEEKPAAESFMHADIYK-KSSAECILQVQTVDSHLISELygEEGEVTFDKR 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515495745 117 yeMQKSLAGQRShLDSVAIPIFDNDQDIPRL-ASRVAAYAEVTPLqygFLVRGHGLYCWGSQVAEARRHLEGLEFL 191
Cdd:PRK06755 122 --SVERVFGKEG-ITEMTIPIVEDEKKFADLlENNVPNFIEGGGV---VLVHNYGMIVWGKTPEEAKKWLEGIEYL 191
|
|
| PRK08660 |
PRK08660 |
aldolase; |
28-181 |
9.85e-07 |
|
aldolase;
Pssm-ID: 181527 [Multi-domain] Cd Length: 181 Bit Score: 47.26 E-value: 9.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 28 GNMSLRLDERqCLVTESGKDKGSLSAADFLQVDIadnHVPSGRTP--SAETGLHTLLYRLYPHLgAVLHTHSVNATVLSR 105
Cdd:PRK08660 23 GNISVRTGDG-LLITRTGSMLDEITEGDVIEVGI---DDDGSVDPlaSSETPVHRAIYRRTSAK-AIVHAHPPYAVALSL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515495745 106 VErgDALVLQGYEMQKSLAgqrshldsvAIPIFDNDQDIPRLASRVAAYAEvtpLQYGFLVRGHGLYCWGSQVAEA 181
Cdd:PRK08660 98 LE--DEIVPLDSEGLYFLG---------TIPVVGGDIGSGELAENVARALS---EHKGVVVRGHGTFAIGKTLEEA 159
|
|
| PRK08087 |
PRK08087 |
L-fuculose-phosphate aldolase; |
26-108 |
9.91e-07 |
|
L-fuculose-phosphate aldolase;
Pssm-ID: 181226 [Multi-domain] Cd Length: 215 Bit Score: 47.43 E-value: 9.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 26 TGGNMSLRLDERQcLVTESGKDKGSLSAADFLQVDIADNHvPSGRTPSAETGLHTLLYRLYPHLGAVLHTHSVNATVLSR 105
Cdd:PRK08087 26 TAGNVSVRYQDGM-LITPTGIPYEKLTESHIVFVDGNGKH-EEGKLPSSEWRFHMAAYQTRPDANAVVHNHAVHCTAVSI 103
|
...
gi 515495745 106 VER 108
Cdd:PRK08087 104 LNR 106
|
|
| PRK07490 |
PRK07490 |
hypothetical protein; Provisional |
10-104 |
2.91e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 236031 [Multi-domain] Cd Length: 245 Bit Score: 46.25 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 10 LLAACHWIGDKGWCPATGGNMSLRL--DERQCLVTESGKDKGSLSAADFLQVDIADNHVPSGRTPSAET--GLHTLLYRL 85
Cdd:PRK07490 15 LAAAFRWIARLGMHEAVANHFSAAVsaDGKQFLLNPKWKHFSRIRASDLLLLDADDPSTAERPDVPDATawAIHGQIHRR 94
|
90
....*....|....*....
gi 515495745 86 YPHLGAVLHTHSVNATVLS 104
Cdd:PRK07490 95 LPHARCVMHVHSVYATALA 113
|
|
| araD |
PRK13145 |
L-ribulose-5-phosphate 4-epimerase; Provisional |
26-100 |
5.44e-06 |
|
L-ribulose-5-phosphate 4-epimerase; Provisional
Pssm-ID: 183870 [Multi-domain] Cd Length: 234 Bit Score: 45.59 E-value: 5.44e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515495745 26 TGGNMSLRLDERQCLVTE-SGKDKGSLSAADFLQVDIADNHVPSGRTPSAETGLHTLLYRLYPHLGAVLHTHSVNA 100
Cdd:PRK13145 26 TWGNVSEVCRELGRIVIKpSGVDYDELTPENMVVTDLDGNVVEGDLNPSSDLPTHVELYKAWPEVGGIVHTHSTEA 101
|
|
| PRK08333 |
PRK08333 |
aldolase; |
19-114 |
5.91e-05 |
|
aldolase;
Pssm-ID: 181393 [Multi-domain] Cd Length: 184 Bit Score: 42.12 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 19 DKGWCPATGGNMSLRLDERqCLVTESGKDKGSLSAADFLQVDIADNHVPSGRtPSAETGLHTLLYRLYPHLGAVLHTHSV 98
Cdd:PRK08333 17 ERGLTAAFGGNLSIRVGNL-VFIKATGSVMDELTREQVAVIDLNGNQLSSVR-PSSEYRLHLAVYRNRPDVRAIAHLHPP 94
|
90
....*....|....*.
gi 515495745 99 NATVLSRVERGDALVL 114
Cdd:PRK08333 95 YSIVASTLLEEELPII 110
|
|
| PRK08324 |
PRK08324 |
bifunctional aldolase/short-chain dehydrogenase; |
27-186 |
3.80e-04 |
|
bifunctional aldolase/short-chain dehydrogenase;
Pssm-ID: 236241 [Multi-domain] Cd Length: 681 Bit Score: 40.60 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 27 GGNMSLRLDERQCL--------VTESGKDKGSLSAADFLQVDIAD----------------------NHVPSGRTPSAET 76
Cdd:PRK08324 37 GGNTSVKTTETDLTgepvevlwVKGSGGDLATITAAGFAALRLDPlralkelgvlsddemvaylrhcLFDPNAPAPSIET 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495745 77 GLHTLLYrlYPHlgaVLHTHSVNATVLSRVERGDALVLQGYEmqkslagqrshlDSVAI-----PIFDndqdiprLASRV 151
Cdd:PRK08324 117 LLHAFLP--FKH---VDHTHPDAIIAIANAPDGEELTREIFG------------DRVGWvpyvrPGFD-------LALAI 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 515495745 152 AAYAEVTPLQYGFLVRGHGLYCWGSQVAEA-RRHLE 186
Cdd:PRK08324 173 AEAVRANPGAEGVVLGKHGLFTWGDTAKEAyERTIE 208
|
|
| PRK06486 |
PRK06486 |
aldolase; |
51-116 |
6.15e-03 |
|
aldolase;
Pssm-ID: 235814 Cd Length: 262 Bit Score: 36.61 E-value: 6.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515495745 51 LSAADFLQVDiADNHVPSGRTPSAETGL--HTLLYRLYPHLGAVLHTHSVNATVLSRVErGDALVLQG 116
Cdd:PRK06486 74 ITASDLLICD-FDGNVLAGRGEPEATAFfiHARIHRAIPRAKAAFHTHMPYATALSLTE-GRPLTTLG 139
|
|
| |
