|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09220 |
PRK09220 |
methylthioribulose 1-phosphate dehydratase; |
10-205 |
3.17e-107 |
|
methylthioribulose 1-phosphate dehydratase;
Pssm-ID: 236415 [Multi-domain] Cd Length: 204 Bit Score: 306.09 E-value: 3.17e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 10 WVEACQQIMQAGRRMDARGWVPATAGNLSCRLADGRIAITRSGGHKGFLSENGVIEIDPQGTPLNPGDRASAETLLHTQL 89
Cdd:PRK09220 3 LEELLQQLIAAGRWIGARGWVPATSGNMSVRLDEQHCAITVSGKDKGSLTAEDFLQVDIAGNAVPSGRKPSAETLLHTQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 90 YAHDASIGAVLHGHSVAATVLSMDEVSDAITLADYEILKVFEGQKTHETSLELPLFHNDQDIARLATVVAPVLADMKL-- 167
Cdd:PRK09220 83 YRLFPEIGAVLHTHSVNATVLSRVEKSDALVLEGYELQKAFAGQTTHETAVVVPIFDNDQDIARLAARVAPYLDAQPLry 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 1723950321 168 GYLIRGHGVYVWGPDMPTALARLEGLEFLLACHLARQQ 205
Cdd:PRK09220 163 GYLIRGHGLYCWGRDMAEARRHLEGLEFLFECELERRL 200
|
|
| salvage_mtnB |
TIGR03328 |
methylthioribulose-1-phosphate dehydratase; Members of this family are the ... |
17-205 |
1.02e-87 |
|
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: 256.42 E-value: 1.02e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 17 IMQAGRRMDARGWVPATAGNLSCRLADGRIAITRSGGHKGFLSENGVIEIDPQGTPLNPGDRASAETLLHTQLYAHDaSI 96
Cdd:TIGR03328 1 LIEAGRDLYKRGWVPGTGGNLSARLDEDEILITPSGVDKGRLTPEDFLVVDLQGKPVSGGLKPSAETLLHTQLYRLT-GA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 97 GAVLHGHSVAATVLSMDEVSDA-ITLADYEILKVFEGQKTHETSLELPLFHNDQDIARLATVVAPVL--ADMKLGYLIRG 173
Cdd:TIGR03328 80 GAVLHTHSVEATVLSRLYPSNGgFELEGYEMLKGLPGITTHEDTLVVPIIENTQDIARLADSVAPALnaYPDVPGVLIRG 159
|
170 180 190
....*....|....*....|....*....|..
gi 1723950321 174 HGVYVWGPDMPTALARLEGLEFLLACHLARQQ 205
Cdd:TIGR03328 160 HGLYAWGRDWEEAKRHLEALEFLFECELEMLK 191
|
|
| AraD |
COG0235 |
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ... |
12-205 |
6.71e-48 |
|
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: 155.76 E-value: 6.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 12 EACQQIMQAGRRMDARGWVPATAGNLSCRLADGRIAITRSGGHKGFLSENGVIEIDPQGTPLNPGDRASAETLLHTQLYA 91
Cdd:COG0235 5 ELREELAAAGRRLARRGLVDGTAGNISVRLDDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKPSSETPLHLAIYR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 92 HDASIGAVLHGHSVAATVLSMdeVSDAITLADYEILKVFEGqkthetslELPLF-HNDQDIARLATVVAPVLADMKlGYL 170
Cdd:COG0235 85 ARPDVGAVVHTHSPYATALSA--LGEPLPPLEQTEAAAFLG--------DVPVVpYAGPGTEELAEAIAEALGDRP-AVL 153
|
170 180 190
....*....|....*....|....*....|....*
gi 1723950321 171 IRGHGVYVWGPDMPTALARLEGLEFLLACHLARQQ 205
Cdd:COG0235 154 LRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALA 188
|
|
| Aldolase_II |
pfam00596 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
15-201 |
3.14e-47 |
|
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: 153.09 E-value: 3.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 15 QQIMQAGRRMDARGWVPATAGNLSCRLADGRIAITRSGGHKGFLSENGVIEIDPQGTPLNPGDRASAETLLHTQLYAHDA 94
Cdd:pfam00596 1 EELAAAGRLLARRGLVEGTGGNISVRLPGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGLKPSSETPLHLAIYRARP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 95 SIGAVLHGHSVAATVLSMDEvsDAITLADYEILKVFEGqkthetslELPLFHNDQ-DIARLATVVAPVLADMKLGYLIRG 173
Cdd:pfam00596 81 DAGAVVHTHSPYATALSLAK--EGLPPITQEAADFLGG--------DIPIIPYYTpGTEELGERIAEALGGDRKAVLLRN 150
|
170 180
....*....|....*....|....*...
gi 1723950321 174 HGVYVWGPDMPTALARLEGLEFLLACHL 201
Cdd:pfam00596 151 HGLLVWGKTLEEAFYLAEELERAAEIQL 178
|
|
| Aldolase_II |
smart01007 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
20-201 |
1.77e-44 |
|
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: 146.24 E-value: 1.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 20 AGRRMDARGWVPATAGNLSCRLAD-GRIAITRSGGHKGFLSENGVIEIDPQGTPLNPGD--RASAETLLHTQLYAHDASI 96
Cdd:smart01007 4 ACRLLARRGLVEGTGGNISARVGEeDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGgpKPSSETPLHLAIYRARPDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 97 GAVLHGHSVAATVLSMdeVSDAITLADYEILKVFEGQKTHETSLELPLFHNDQDIARLATVVAPVLADMKlGYLIRGHGV 176
Cdd:smart01007 84 GAVVHTHSPYATALAA--LGKPLPLLPTEQAAAFLGGEIPYAPYAGPGTELAEEGAELAEALAEALPDRP-AVLLRNHGL 160
|
170 180
....*....|....*....|....*
gi 1723950321 177 YVWGPDMPTALARLEGLEFLLACHL 201
Cdd:smart01007 161 LVWGKTLEEAFDLAEELEEAAEIQL 185
|
|
| Aldolase_II |
cd00398 |
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ... |
15-187 |
3.05e-13 |
|
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: 65.46 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 15 QQIMQAGRRMDARGWVPATAGNLSCRL-ADGRIAITRSGGHKGFLSENGVIEIDPQGTPLNpGDRASAETLLHTQLYAHD 93
Cdd:cd00398 5 RKIIAACLLLDLYGWVTGTGGNVSARDrDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVE-GKKPSSETPLHLALYRAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 94 ASIGAVLHGHSVAATVLSMDEVSDAI----TLADYEILKV----FEGQKTHETslelplfhndqdiaRLATVVAPVLADM 165
Cdd:cd00398 84 PDIGCIVHTHSTHATAVSQLKEGLIPaghtACAVYFTGDIpctpYMTPETGED--------------EIGTQRALGFPNS 149
|
170 180
....*....|....*....|..
gi 1723950321 166 KlGYLIRGHGVYVWGPDMPTAL 187
Cdd:cd00398 150 K-AVLLRNHGLFAWGPTLDEAF 170
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09220 |
PRK09220 |
methylthioribulose 1-phosphate dehydratase; |
10-205 |
3.17e-107 |
|
methylthioribulose 1-phosphate dehydratase;
Pssm-ID: 236415 [Multi-domain] Cd Length: 204 Bit Score: 306.09 E-value: 3.17e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 10 WVEACQQIMQAGRRMDARGWVPATAGNLSCRLADGRIAITRSGGHKGFLSENGVIEIDPQGTPLNPGDRASAETLLHTQL 89
Cdd:PRK09220 3 LEELLQQLIAAGRWIGARGWVPATSGNMSVRLDEQHCAITVSGKDKGSLTAEDFLQVDIAGNAVPSGRKPSAETLLHTQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 90 YAHDASIGAVLHGHSVAATVLSMDEVSDAITLADYEILKVFEGQKTHETSLELPLFHNDQDIARLATVVAPVLADMKL-- 167
Cdd:PRK09220 83 YRLFPEIGAVLHTHSVNATVLSRVEKSDALVLEGYELQKAFAGQTTHETAVVVPIFDNDQDIARLAARVAPYLDAQPLry 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 1723950321 168 GYLIRGHGVYVWGPDMPTALARLEGLEFLLACHLARQQ 205
Cdd:PRK09220 163 GYLIRGHGLYCWGRDMAEARRHLEGLEFLFECELERRL 200
|
|
| salvage_mtnB |
TIGR03328 |
methylthioribulose-1-phosphate dehydratase; Members of this family are the ... |
17-205 |
1.02e-87 |
|
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: 256.42 E-value: 1.02e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 17 IMQAGRRMDARGWVPATAGNLSCRLADGRIAITRSGGHKGFLSENGVIEIDPQGTPLNPGDRASAETLLHTQLYAHDaSI 96
Cdd:TIGR03328 1 LIEAGRDLYKRGWVPGTGGNLSARLDEDEILITPSGVDKGRLTPEDFLVVDLQGKPVSGGLKPSAETLLHTQLYRLT-GA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 97 GAVLHGHSVAATVLSMDEVSDA-ITLADYEILKVFEGQKTHETSLELPLFHNDQDIARLATVVAPVL--ADMKLGYLIRG 173
Cdd:TIGR03328 80 GAVLHTHSVEATVLSRLYPSNGgFELEGYEMLKGLPGITTHEDTLVVPIIENTQDIARLADSVAPALnaYPDVPGVLIRG 159
|
170 180 190
....*....|....*....|....*....|..
gi 1723950321 174 HGVYVWGPDMPTALARLEGLEFLLACHLARQQ 205
Cdd:TIGR03328 160 HGLYAWGRDWEEAKRHLEALEFLFECELEMLK 191
|
|
| AraD |
COG0235 |
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ... |
12-205 |
6.71e-48 |
|
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: 155.76 E-value: 6.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 12 EACQQIMQAGRRMDARGWVPATAGNLSCRLADGRIAITRSGGHKGFLSENGVIEIDPQGTPLNPGDRASAETLLHTQLYA 91
Cdd:COG0235 5 ELREELAAAGRRLARRGLVDGTAGNISVRLDDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKPSSETPLHLAIYR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 92 HDASIGAVLHGHSVAATVLSMdeVSDAITLADYEILKVFEGqkthetslELPLF-HNDQDIARLATVVAPVLADMKlGYL 170
Cdd:COG0235 85 ARPDVGAVVHTHSPYATALSA--LGEPLPPLEQTEAAAFLG--------DVPVVpYAGPGTEELAEAIAEALGDRP-AVL 153
|
170 180 190
....*....|....*....|....*....|....*
gi 1723950321 171 IRGHGVYVWGPDMPTALARLEGLEFLLACHLARQQ 205
Cdd:COG0235 154 LRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALA 188
|
|
| Aldolase_II |
pfam00596 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
15-201 |
3.14e-47 |
|
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: 153.09 E-value: 3.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 15 QQIMQAGRRMDARGWVPATAGNLSCRLADGRIAITRSGGHKGFLSENGVIEIDPQGTPLNPGDRASAETLLHTQLYAHDA 94
Cdd:pfam00596 1 EELAAAGRLLARRGLVEGTGGNISVRLPGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGLKPSSETPLHLAIYRARP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 95 SIGAVLHGHSVAATVLSMDEvsDAITLADYEILKVFEGqkthetslELPLFHNDQ-DIARLATVVAPVLADMKLGYLIRG 173
Cdd:pfam00596 81 DAGAVVHTHSPYATALSLAK--EGLPPITQEAADFLGG--------DIPIIPYYTpGTEELGERIAEALGGDRKAVLLRN 150
|
170 180
....*....|....*....|....*...
gi 1723950321 174 HGVYVWGPDMPTALARLEGLEFLLACHL 201
Cdd:pfam00596 151 HGLLVWGKTLEEAFYLAEELERAAEIQL 178
|
|
| Aldolase_II |
smart01007 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
20-201 |
1.77e-44 |
|
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: 146.24 E-value: 1.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 20 AGRRMDARGWVPATAGNLSCRLAD-GRIAITRSGGHKGFLSENGVIEIDPQGTPLNPGD--RASAETLLHTQLYAHDASI 96
Cdd:smart01007 4 ACRLLARRGLVEGTGGNISARVGEeDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGgpKPSSETPLHLAIYRARPDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 97 GAVLHGHSVAATVLSMdeVSDAITLADYEILKVFEGQKTHETSLELPLFHNDQDIARLATVVAPVLADMKlGYLIRGHGV 176
Cdd:smart01007 84 GAVVHTHSPYATALAA--LGKPLPLLPTEQAAAFLGGEIPYAPYAGPGTELAEEGAELAEALAEALPDRP-AVLLRNHGL 160
|
170 180
....*....|....*....|....*
gi 1723950321 177 YVWGPDMPTALARLEGLEFLLACHL 201
Cdd:smart01007 161 LVWGKTLEEAFDLAEELEEAAEIQL 185
|
|
| mtnB |
PRK06754 |
methylthioribulose 1-phosphate dehydratase; |
26-205 |
1.90e-33 |
|
methylthioribulose 1-phosphate dehydratase;
Pssm-ID: 180679 [Multi-domain] Cd Length: 208 Bit Score: 118.61 E-value: 1.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 26 ARGWVPATAGNLSCRLADGRI--AITRSGGHKGFLSENGVIEIDPQGTPLNPGD-RASAETLLHTQLYAH-DAsiGAVLH 101
Cdd:PRK06754 20 ARDWFPATSGNLSIKVSDDPLtfLVTASGKDKRKTTPEDFLLVDHDGKPVEETElKPSAETLLHTHIYNNtNA--GCVLH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 102 GHSVAATVLS-MDEVSDAITLADYEILKVFeGQKTHETSLELPLFHNDQDIARLATVVAPVLADMKLGYLIRGHGVYVWG 180
Cdd:PRK06754 98 VHTVDNNVISeLYGDDGAVTFQGQEIIKAL-GIWEENAEIHIPIIENHADIPTLAEEFAKHIQGDSGAVLIRNHGITVWG 176
|
170 180
....*....|....*....|....*
gi 1723950321 181 PDMPTALARLEGLEFLLACHLARQQ 205
Cdd:PRK06754 177 RDAFEAKKHLEAYEFLFSYHIKLLS 201
|
|
| PRK08130 |
PRK08130 |
putative aldolase; Validated |
15-194 |
1.81e-22 |
|
putative aldolase; Validated
Pssm-ID: 181241 [Multi-domain] Cd Length: 213 Bit Score: 90.32 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 15 QQIMQAGRRMDARGWVPATAGNLSCRLADGRIAITRSGGHKGFLSENGVIEIDPQGTPLNpGDRASAETLLHTQLYAHDA 94
Cdd:PRK08130 8 EEIVRLGRSLFQRGYTVGSAGNISARLDDGGWLVTPTGSCLGRLDPARLSKVDADGNWLS-GDKPSKEVPLHRAIYRNNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 95 SIGAVLHGHSVAATVLSMDEVSD------AITlaDYEILKVfeGQkthetsleLPL--FHNDQDiARLATVVAPvLADMK 166
Cdd:PRK08130 87 ECGAVVHLHSTHLTALSCLGGLDptnvlpPFT--PYYVMRV--GH--------VPLipYYRPGD-PAIAEALAG-LAARY 152
|
170 180
....*....|....*....|....*...
gi 1723950321 167 LGYLIRGHGVYVWGPDMPTALARLEGLE 194
Cdd:PRK08130 153 RAVLLANHGPVVWGSSLEAAVNATEELE 180
|
|
| PRK08660 |
PRK08660 |
aldolase; |
15-187 |
2.13e-14 |
|
aldolase;
Pssm-ID: 181527 [Multi-domain] Cd Length: 181 Bit Score: 68.06 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 15 QQIMQAGRRMDARGWVPATAGNLSCRlADGRIAITRSGGHKGFLSENGVIEIDPQGTPLNPGDrASAETLLHTQLYAHdA 94
Cdd:PRK08660 3 QEFARIGKKLFAHGLVSSHFGNISVR-TGDGLLITRTGSMLDEITEGDVIEVGIDDDGSVDPL-ASSETPVHRAIYRR-T 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 95 SIGAVLHGHSVAATVLSMDEvsDAITLADYEiLKVFEGqkthetslELPLFHNDQDIARLATVVAPVLADMKlGYLIRGH 174
Cdd:PRK08660 80 SAKAIVHAHPPYAVALSLLE--DEIVPLDSE-GLYFLG--------TIPVVGGDIGSGELAENVARALSEHK-GVVVRGH 147
|
170
....*....|...
gi 1723950321 175 GVYVWGPDMPTAL 187
Cdd:PRK08660 148 GTFAIGKTLEEAY 160
|
|
| Aldolase_II |
cd00398 |
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ... |
15-187 |
3.05e-13 |
|
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: 65.46 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 15 QQIMQAGRRMDARGWVPATAGNLSCRL-ADGRIAITRSGGHKGFLSENGVIEIDPQGTPLNpGDRASAETLLHTQLYAHD 93
Cdd:cd00398 5 RKIIAACLLLDLYGWVTGTGGNVSARDrDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVE-GKKPSSETPLHLALYRAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 94 ASIGAVLHGHSVAATVLSMDEVSDAI----TLADYEILKV----FEGQKTHETslelplfhndqdiaRLATVVAPVLADM 165
Cdd:cd00398 84 PDIGCIVHTHSTHATAVSQLKEGLIPaghtACAVYFTGDIpctpYMTPETGED--------------EIGTQRALGFPNS 149
|
170 180
....*....|....*....|..
gi 1723950321 166 KlGYLIRGHGVYVWGPDMPTAL 187
Cdd:cd00398 150 K-AVLLRNHGLFAWGPTLDEAF 170
|
|
| PRK05874 |
PRK05874 |
L-fuculose-phosphate aldolase; Validated |
15-112 |
3.19e-12 |
|
L-fuculose-phosphate aldolase; Validated
Pssm-ID: 102036 [Multi-domain] Cd Length: 217 Bit Score: 63.12 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 15 QQIMQAGRRMDARGWVPATAGNLSCRLADGRIAITRSGGHKGFLSENGVIEIDPQGTPLNP--GDRASAETLLHTQLYAH 92
Cdd:PRK05874 9 SAVLAAAKDMLRRGLVEGTAGNISARRSDGNVVITPSSVDYAEMLLHDLVLVDAGGAVLHAkdGRSPSTELNLHLACYRA 88
|
90 100
....*....|....*....|
gi 1723950321 93 DASIGAVLHGHSVAATVLSM 112
Cdd:PRK05874 89 FDDIGSVIHSHPVWATMFAV 108
|
|
| PRK06833 |
PRK06833 |
L-fuculose-phosphate aldolase; |
15-111 |
7.70e-08 |
|
L-fuculose-phosphate aldolase;
Pssm-ID: 180717 [Multi-domain] Cd Length: 214 Bit Score: 50.90 E-value: 7.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 15 QQIMQAGRRMDARGWVPATAGNLS-CRLADGRIAITRSGGHKGFLSENGVIEIDPQGTPLNPGDRASAETLLHTQLYAHD 93
Cdd:PRK06833 8 EEIVAYGKKLISSGLTKGTGGNISiFNREQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVEGERKPSSELDMHLIFYRNR 87
|
90
....*....|....*...
gi 1723950321 94 ASIGAVLHGHSVAATVLS 111
Cdd:PRK06833 88 EDINAIVHTHSPYATTLA 105
|
|
| PRK08087 |
PRK08087 |
L-fuculose-phosphate aldolase; |
15-112 |
3.22e-06 |
|
L-fuculose-phosphate aldolase;
Pssm-ID: 181226 [Multi-domain] Cd Length: 215 Bit Score: 45.89 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 15 QQIMQAGRRMDARGWVPATAGNLSCRLADGRIaITRSGGHKGFLSENGVIEIDPQGTPlNPGDRASAETLLHTQLYAHDA 94
Cdd:PRK08087 8 RQIIDTCLEMTRLGLNQGTAGNVSVRYQDGML-ITPTGIPYEKLTESHIVFVDGNGKH-EEGKLPSSEWRFHMAAYQTRP 85
|
90
....*....|....*...
gi 1723950321 95 SIGAVLHGHSVAATVLSM 112
Cdd:PRK08087 86 DANAVVHNHAVHCTAVSI 103
|
|
| PRK06755 |
PRK06755 |
hypothetical protein; Validated |
52-201 |
1.52e-05 |
|
hypothetical protein; Validated
Pssm-ID: 102532 Cd Length: 209 Bit Score: 44.25 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 52 GGHKGFLSENGVIEIDPQGTPLNPGD-RASAETLLHTQLYaHDASIGAVLHGHSVAATVLS-MDEVSDAITLADYEILKV 129
Cdd:PRK06755 48 GRDKGLFSEEDFIVVNCMCEPVFENEeKPAAESFMHADIY-KKSSAECILQVQTVDSHLISeLYGEEGEVTFDKRSVERV 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1723950321 130 FEGQKTHEtsLELPLFHNDQDIARLATVVAPVLADMKLGYLIRGHGVYVWGPDMPTALARLEGLEFLLACHL 201
Cdd:PRK06755 127 FGKEGITE--MTIPIVEDEKKFADLLENNVPNFIEGGGVVLVHNYGMIVWGKTPEEAKKWLEGIEYLMNYHV 196
|
|
| araD |
PRK13213 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
15-205 |
3.83e-05 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 106181 Cd Length: 231 Bit Score: 43.18 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 15 QQIMQAGRRMDARGWVPATAGNLS-CRLADGRIAITRSGGHKGFLSENGVIEIDPQGTPLNPGDRA-SAETLLHTQLYAH 92
Cdd:PRK13213 7 QQVFEANLALPKYKLVTFTWGNVSgIDREHGLVVIKPSGVEYDVMSVNDMVVVDLATGKVVEGDKKpSSDTDTHLVLYRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 93 DASIGAVLHGHSVAATVLSMDEVSDA---ITLADY--------EILKVFE--GQKTHETSLELPLFHNDQDIaRLATVVA 159
Cdd:PRK13213 87 FAEIGGIVHTHSRHATIWAQAGKSLSalgTTHADYfygpipctRLMTEAEitGDYEHETGKVIVETFAEQGL-RAADIPA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1723950321 160 pvladmklgYLIRGHGVYVWGPDMPTALARLEGLEFLLACHLARQQ 205
Cdd:PRK13213 166 ---------VLVNGHGPFAWGSNAANAVHNAVVLEEIAYMNLFTHQ 202
|
|
| PRK06557 |
PRK06557 |
L-ribulose-5-phosphate 4-epimerase; Validated |
28-109 |
1.55e-04 |
|
L-ribulose-5-phosphate 4-epimerase; Validated
Pssm-ID: 235829 [Multi-domain] Cd Length: 221 Bit Score: 41.15 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 28 GWVPATAGNLSCRLAD-GRIAITRSGGHKGFLSENGVIEIDPQGTPLnPGDRA-SAETLLHTQLYAHDASIGAVLHGHSV 105
Cdd:PRK06557 26 GLVVWTSGNVSARDPGtDLVVIKPSGVSYDDLTPEDMVVVDLDGNVV-EGDLKpSSDTASHLYVYRHMPDVGGVVHTHST 104
|
....
gi 1723950321 106 AATV 109
Cdd:PRK06557 105 YATA 108
|
|
| araD |
PRK13145 |
L-ribulose-5-phosphate 4-epimerase; Provisional |
12-107 |
2.11e-04 |
|
L-ribulose-5-phosphate 4-epimerase; Provisional
Pssm-ID: 183870 [Multi-domain] Cd Length: 234 Bit Score: 40.97 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 12 EACQQIMQAGRRMDARGWVPATAGNLS--CRLAdGRIAITRSGGHKGFLSENGVIEIDPQGTPLNPGDRASAETLLHTQL 89
Cdd:PRK13145 5 EMRERVCAANKSLPKHGLVKFTWGNVSevCREL-GRIVIKPSGVDYDELTPENMVVTDLDGNVVEGDLNPSSDLPTHVEL 83
|
90
....*....|....*...
gi 1723950321 90 YAHDASIGAVLHGHSVAA 107
Cdd:PRK13145 84 YKAWPEVGGIVHTHSTEA 101
|
|
| sgaE |
PRK12348 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
15-124 |
2.56e-04 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 183460 Cd Length: 228 Bit Score: 40.55 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723950321 15 QQIMQAGRRMDARGWVPATAGNLSC-RLADGRIAITRSGGHKGFLSENGVIEIDPQGTPLNPGDRASAETLLHTQLYAHD 93
Cdd:PRK12348 6 QQVFEANMDLPRYGLVTFTWGNVSAiDRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEGEYRPSSDTATHLELYRRY 85
|
90 100 110
....*....|....*....|....*....|....
gi 1723950321 94 ASIGAVLHGHSVAATVLS---MDEVSDAITLADY 124
Cdd:PRK12348 86 PSLGGIVHTHSTHATAWAqagLAIPALGTTHADY 119
|
|
| |
