|
Name |
Accession |
Description |
Interval |
E-value |
| salvage_mtnB |
TIGR03328 |
methylthioribulose-1-phosphate dehydratase; Members of this family are the ... |
45-244 |
6.28e-101 |
|
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: 291.86 E-value: 6.28e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 45 IPELCKQFYHLGWVTGTGGGISLK-HGDEIYIAPSGVQKERIQPEDMFVCDINEKDISGpspskKLKKSQCTPLFMNAYT 123
Cdd:TIGR03328 1 LIEAGRDLYKRGWVPGTGGNLSARlDEDEILITPSGVDKGRLTPEDFLVVDLQGKPVSG-----GLKPSAETLLHTQLYR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 124 MRGAGAVIHTHSKAAVMATLLFPGRE-FKITHQEMIKGIKkctsgGYYRYDDMLVVPIIENTPEEKDLKDRMAHAMNEYP 202
Cdd:TIGR03328 76 LTGAGAVLHTHSVEATVLSRLYPSNGgFELEGYEMLKGLP-----GITTHEDTLVVPIIENTQDIARLADSVAPALNAYP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767966013 203 DSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKV 244
Cdd:TIGR03328 151 DVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLKL 192
|
|
| Aldolase_II |
pfam00596 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
45-239 |
2.24e-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: 459862 [Multi-domain] Cd Length: 178 Bit Score: 163.10 E-value: 2.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 45 IPELCKQFYHLGWVTGTGGGISLK-HGDEIYIAPSGVQKERIQPEDMFVCDINEKDISGPspskkLKKSQCTPLFMNAYT 123
Cdd:pfam00596 3 LAAAGRLLARRGLVEGTGGNISVRlPGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGG-----LKPSSETPLHLAIYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 124 MR-GAGAVIHTHSKAAVMATLLfpGREFKITHQEMIKgikkctsggyYRYDDmlvVPIIEN-TPEEKDLKDRMAHAMNEy 201
Cdd:pfam00596 78 ARpDAGAVVHTHSPYATALSLA--KEGLPPITQEAAD----------FLGGD---IPIIPYyTPGTEELGERIAEALGG- 141
|
170 180 190
....*....|....*....|....*....|....*...
gi 767966013 202 pDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAV 239
Cdd:pfam00596 142 -DRKAVLLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
|
|
| Aldolase_II |
smart01007 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
45-239 |
2.52e-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: 214970 [Multi-domain] Cd Length: 185 Bit Score: 158.18 E-value: 2.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 45 IPELCKQFYHLGWVTGTGGGISLKHGDE--IYIAPSGVQKERIQPEDMFVCDINEKDISGPSPskkLKKSQCTPLFMNAY 122
Cdd:smart01007 1 LAAACRLLARRGLVEGTGGNISARVGEEdlFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG---PKPSSETPLHLAIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 123 TMR-GAGAVIHTHSKAAVMATLLfpGREFKITHQEMIKGIkkctSGGYYRYDDmLVVPIIENTPEEKDLKDRMAHAMNEY 201
Cdd:smart01007 78 RARpDVGAVVHTHSPYATALAAL--GKPLPLLPTEQAAAF----LGGEIPYAP-YAGPGTELAEEGAELAEALAEALPDR 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 767966013 202 PdscAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAV 239
Cdd:smart01007 151 P---AVLLRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
|
|
| AraD |
COG0235 |
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ... |
47-252 |
3.13e-33 |
|
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: 119.93 E-value: 3.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 47 ELCKQFYHLGWVTGTGGGISLKHGDE-IYIAPSGVQKERIQPEDMFVCDINEKDISGPS-PSKklkksqCTPLFMNAYTM 124
Cdd:COG0235 12 AAGRRLARRGLVDGTAGNISVRLDDDrFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLkPSS------ETPLHLAIYRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 125 R-GAGAVIHTHSKAAVMATLLfpGREFKITHQEMikgikkctsgGYYRYDDmlvVPIIE-NTPEEKDLKDRMAHAMNEYP 202
Cdd:COG0235 86 RpDVGAVVHTHSPYATALSAL--GEPLPPLEQTE----------AAAFLGD---VPVVPyAGPGTEELAEAIAEALGDRP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767966013 203 dscAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKVGlDPSQLP 252
Cdd:COG0235 151 ---AVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALG-GPLVLS 196
|
|
| Aldolase_II |
cd00398 |
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ... |
39-246 |
5.41e-32 |
|
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: 116.70 E-value: 5.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 39 EHPRYLIPELCKQFYHLGWVTGTGGGISLKHGDEIY--IAPSGVQKERIQPEDMFVCDINEKDISGPSPSkklkksQCTP 116
Cdd:cd00398 1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYflITPSGVDYEEMTASDLVVVDAQGKVVEGKKPS------SETP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 117 LFMNAYTMR-GAGAVIHTHSKAAVMATLLFpGREFKITHQEMikgikkctsgGYYRYDDmlvVPIIENTPEEKDLKDRMA 195
Cdd:cd00398 75 LHLALYRARpDIGCIVHTHSTHATAVSQLK-EGLIPAGHTAC----------AVYFTGD---IPCTPYMTPETGEDEIGT 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767966013 196 HAMNEYPDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKVGL 246
Cdd:cd00398 141 QRALGFPNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGG 191
|
|
| mtnB |
PRK06754 |
methylthioribulose 1-phosphate dehydratase; |
47-235 |
1.49e-27 |
|
methylthioribulose 1-phosphate dehydratase;
Pssm-ID: 180679 [Multi-domain] Cd Length: 208 Bit Score: 105.13 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 47 ELCKQFYHLGWVTGTGGGISLKHGDE---IYIAPSGVQKERIQPEDMFVCDINEKdisgPSPSKKLKKSQCTPLFMNAYT 123
Cdd:PRK06754 13 EIKKELAARDWFPATSGNLSIKVSDDpltFLVTASGKDKRKTTPEDFLLVDHDGK----PVEETELKPSAETLLHTHIYN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 124 MRGAGAVIHTHSKAA-VMATLLFPGREFKITHQEMIKGIkkctsgGYYRYDDMLVVPIIENTPEEKDLKDRMAHAMNeyP 202
Cdd:PRK06754 89 NTNAGCVLHVHTVDNnVISELYGDDGAVTFQGQEIIKAL------GIWEENAEIHIPIIENHADIPTLAEEFAKHIQ--G 160
|
170 180 190
....*....|....*....|....*....|...
gi 767966013 203 DSCAVLVRRHGVYVWGETWEKAKTMCECYDYLF 235
Cdd:PRK06754 161 DSGAVLIRNHGITVWGRDAFEAKKHLEAYEFLF 193
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| salvage_mtnB |
TIGR03328 |
methylthioribulose-1-phosphate dehydratase; Members of this family are the ... |
45-244 |
6.28e-101 |
|
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: 291.86 E-value: 6.28e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 45 IPELCKQFYHLGWVTGTGGGISLK-HGDEIYIAPSGVQKERIQPEDMFVCDINEKDISGpspskKLKKSQCTPLFMNAYT 123
Cdd:TIGR03328 1 LIEAGRDLYKRGWVPGTGGNLSARlDEDEILITPSGVDKGRLTPEDFLVVDLQGKPVSG-----GLKPSAETLLHTQLYR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 124 MRGAGAVIHTHSKAAVMATLLFPGRE-FKITHQEMIKGIKkctsgGYYRYDDMLVVPIIENTPEEKDLKDRMAHAMNEYP 202
Cdd:TIGR03328 76 LTGAGAVLHTHSVEATVLSRLYPSNGgFELEGYEMLKGLP-----GITTHEDTLVVPIIENTQDIARLADSVAPALNAYP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767966013 203 DSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKV 244
Cdd:TIGR03328 151 DVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLKL 192
|
|
| Aldolase_II |
pfam00596 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
45-239 |
2.24e-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: 459862 [Multi-domain] Cd Length: 178 Bit Score: 163.10 E-value: 2.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 45 IPELCKQFYHLGWVTGTGGGISLK-HGDEIYIAPSGVQKERIQPEDMFVCDINEKDISGPspskkLKKSQCTPLFMNAYT 123
Cdd:pfam00596 3 LAAAGRLLARRGLVEGTGGNISVRlPGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGG-----LKPSSETPLHLAIYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 124 MR-GAGAVIHTHSKAAVMATLLfpGREFKITHQEMIKgikkctsggyYRYDDmlvVPIIEN-TPEEKDLKDRMAHAMNEy 201
Cdd:pfam00596 78 ARpDAGAVVHTHSPYATALSLA--KEGLPPITQEAAD----------FLGGD---IPIIPYyTPGTEELGERIAEALGG- 141
|
170 180 190
....*....|....*....|....*....|....*...
gi 767966013 202 pDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAV 239
Cdd:pfam00596 142 -DRKAVLLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
|
|
| Aldolase_II |
smart01007 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
45-239 |
2.52e-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: 214970 [Multi-domain] Cd Length: 185 Bit Score: 158.18 E-value: 2.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 45 IPELCKQFYHLGWVTGTGGGISLKHGDE--IYIAPSGVQKERIQPEDMFVCDINEKDISGPSPskkLKKSQCTPLFMNAY 122
Cdd:smart01007 1 LAAACRLLARRGLVEGTGGNISARVGEEdlFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG---PKPSSETPLHLAIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 123 TMR-GAGAVIHTHSKAAVMATLLfpGREFKITHQEMIKGIkkctSGGYYRYDDmLVVPIIENTPEEKDLKDRMAHAMNEY 201
Cdd:smart01007 78 RARpDVGAVVHTHSPYATALAAL--GKPLPLLPTEQAAAF----LGGEIPYAP-YAGPGTELAEEGAELAEALAEALPDR 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 767966013 202 PdscAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAV 239
Cdd:smart01007 151 P---AVLLRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
|
|
| AraD |
COG0235 |
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ... |
47-252 |
3.13e-33 |
|
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: 119.93 E-value: 3.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 47 ELCKQFYHLGWVTGTGGGISLKHGDE-IYIAPSGVQKERIQPEDMFVCDINEKDISGPS-PSKklkksqCTPLFMNAYTM 124
Cdd:COG0235 12 AAGRRLARRGLVDGTAGNISVRLDDDrFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLkPSS------ETPLHLAIYRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 125 R-GAGAVIHTHSKAAVMATLLfpGREFKITHQEMikgikkctsgGYYRYDDmlvVPIIE-NTPEEKDLKDRMAHAMNEYP 202
Cdd:COG0235 86 RpDVGAVVHTHSPYATALSAL--GEPLPPLEQTE----------AAAFLGD---VPVVPyAGPGTEELAEAIAEALGDRP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767966013 203 dscAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKVGlDPSQLP 252
Cdd:COG0235 151 ---AVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALG-GPLVLS 196
|
|
| Aldolase_II |
cd00398 |
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ... |
39-246 |
5.41e-32 |
|
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: 116.70 E-value: 5.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 39 EHPRYLIPELCKQFYHLGWVTGTGGGISLKHGDEIY--IAPSGVQKERIQPEDMFVCDINEKDISGPSPSkklkksQCTP 116
Cdd:cd00398 1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYflITPSGVDYEEMTASDLVVVDAQGKVVEGKKPS------SETP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 117 LFMNAYTMR-GAGAVIHTHSKAAVMATLLFpGREFKITHQEMikgikkctsgGYYRYDDmlvVPIIENTPEEKDLKDRMA 195
Cdd:cd00398 75 LHLALYRARpDIGCIVHTHSTHATAVSQLK-EGLIPAGHTAC----------AVYFTGD---IPCTPYMTPETGEDEIGT 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767966013 196 HAMNEYPDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKVGL 246
Cdd:cd00398 141 QRALGFPNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGG 191
|
|
| mtnB |
PRK06754 |
methylthioribulose 1-phosphate dehydratase; |
47-235 |
1.49e-27 |
|
methylthioribulose 1-phosphate dehydratase;
Pssm-ID: 180679 [Multi-domain] Cd Length: 208 Bit Score: 105.13 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 47 ELCKQFYHLGWVTGTGGGISLKHGDE---IYIAPSGVQKERIQPEDMFVCDINEKdisgPSPSKKLKKSQCTPLFMNAYT 123
Cdd:PRK06754 13 EIKKELAARDWFPATSGNLSIKVSDDpltFLVTASGKDKRKTTPEDFLLVDHDGK----PVEETELKPSAETLLHTHIYN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 124 MRGAGAVIHTHSKAA-VMATLLFPGREFKITHQEMIKGIkkctsgGYYRYDDMLVVPIIENTPEEKDLKDRMAHAMNeyP 202
Cdd:PRK06754 89 NTNAGCVLHVHTVDNnVISELYGDDGAVTFQGQEIIKAL------GIWEENAEIHIPIIENHADIPTLAEEFAKHIQ--G 160
|
170 180 190
....*....|....*....|....*....|...
gi 767966013 203 DSCAVLVRRHGVYVWGETWEKAKTMCECYDYLF 235
Cdd:PRK06754 161 DSGAVLIRNHGITVWGRDAFEAKKHLEAYEFLF 193
|
|
| PRK09220 |
PRK09220 |
methylthioribulose 1-phosphate dehydratase; |
44-244 |
1.02e-19 |
|
methylthioribulose 1-phosphate dehydratase;
Pssm-ID: 236415 [Multi-domain] Cd Length: 204 Bit Score: 84.22 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 44 LIPELCKQFYHLGWVTGTGGGISLKHGD-EIYIAPSGVQKERIQPEDMFVCDINekdiSGPSPSKKlKKSQCTPLFMNAY 122
Cdd:PRK09220 9 QLIAAGRWIGARGWVPATSGNMSVRLDEqHCAITVSGKDKGSLTAEDFLQVDIA----GNAVPSGR-KPSAETLLHTQLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 123 TMR-GAGAVIHTHSKAAVMATLLFPGREFKITHQEMIKgikkcTSGGYYRYDDMLVVPIIENTPEEKDLKDRMAHAMNEY 201
Cdd:PRK09220 84 RLFpEIGAVLHTHSVNATVLSRVEKSDALVLEGYELQK-----AFAGQTTHETAVVVPIFDNDQDIARLAARVAPYLDAQ 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767966013 202 PDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKV 244
Cdd:PRK09220 159 PLRYGYLIRGHGLYCWGRDMAEARRHLEGLEFLFECELERRLL 201
|
|
| PRK08130 |
PRK08130 |
putative aldolase; Validated |
42-224 |
1.30e-10 |
|
putative aldolase; Validated
Pssm-ID: 181241 [Multi-domain] Cd Length: 213 Bit Score: 59.50 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 42 RYLIPELCKQFYHLGWVTGTGGGISLKHGDE-IYIAPSGVQKERIQPEDMFVCDINEKDISGPSPSKKLkksqctPLFMN 120
Cdd:PRK08130 7 REEIVRLGRSLFQRGYTVGSAGNISARLDDGgWLVTPTGSCLGRLDPARLSKVDADGNWLSGDKPSKEV------PLHRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 121 AYTMRG-AGAVIHTHSKAAVMATLLfPGrefkITHQEMIKGIKKctsggYY--RYDDMLVVPIIEntPEEKDLKDRMAHA 197
Cdd:PRK08130 81 IYRNNPeCGAVVHLHSTHLTALSCL-GG----LDPTNVLPPFTP-----YYvmRVGHVPLIPYYR--PGDPAIAEALAGL 148
|
170 180
....*....|....*....|....*..
gi 767966013 198 MNEYPdscAVLVRRHGVYVWGETWEKA 224
Cdd:PRK08130 149 AARYR---AVLLANHGPVVWGSSLEAA 172
|
|
| PRK06557 |
PRK06557 |
L-ribulose-5-phosphate 4-epimerase; Validated |
56-229 |
5.41e-09 |
|
L-ribulose-5-phosphate 4-epimerase; Validated
Pssm-ID: 235829 [Multi-domain] Cd Length: 221 Bit Score: 55.01 E-value: 5.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 56 GWVTGTGGGIS--LKHGDEIYIAPSGVQKERIQPEDMFVCDINEKDISGpspskKLKKSQCTPLFMNAYT-MRGAGAVIH 132
Cdd:PRK06557 26 GLVVWTSGNVSarDPGTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVEG-----DLKPSSDTASHLYVYRhMPDVGGVVH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 133 THSKAAVMatllFPGREfkithqEMIKGIkkCTS-----GGyyryddmlVVPIienTPEEKDLKDRMAHAMNEY---PDS 204
Cdd:PRK06557 101 THSTYATA----WAARG------EPIPCV--LTAmadefGG--------PIPV---GPFALIGDEAIGKGIVETlkgGRS 157
|
170 180
....*....|....*....|....*...
gi 767966013 205 CAVLVRRHGVYVWGETWE---KAKTMCE 229
Cdd:PRK06557 158 PAVLMQNHGVFTIGKDAEdavKAAVMVE 185
|
|
| araD |
PRK13145 |
L-ribulose-5-phosphate 4-epimerase; Provisional |
44-224 |
5.85e-08 |
|
L-ribulose-5-phosphate 4-epimerase; Provisional
Pssm-ID: 183870 [Multi-domain] Cd Length: 234 Bit Score: 52.14 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 44 LIPELCKQFYHL-------GWVTGTGGGISL--KHGDEIYIAPSGVQKERIQPEDMFVCDINEKDISGpspskKLKKSQC 114
Cdd:PRK13145 2 NLQEMRERVCAAnkslpkhGLVKFTWGNVSEvcRELGRIVIKPSGVDYDELTPENMVVTDLDGNVVEG-----DLNPSSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 115 TPLFMNAYTMRG-AGAVIHTHSKAAVmaTLLFPGRE---FKITHQEMIKGIKKCTSG-------GYYRYDDMLVvpIIEN 183
Cdd:PRK13145 77 LPTHVELYKAWPeVGGIVHTHSTEAV--GWAQAGRDipfYGTTHADYFYGPIPCARSltkdevnGAYEKETGSV--IIEE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767966013 184 TpEEKDLkDRMAHAmneypdscAVLVRRHGVYVWGETWEKA 224
Cdd:PRK13145 153 F-EKRGL-DPMAVP--------GIVVRNHGPFTWGKNPEQA 183
|
|
| PRK08660 |
PRK08660 |
aldolase; |
56-224 |
7.48e-08 |
|
aldolase;
Pssm-ID: 181527 [Multi-domain] Cd Length: 181 Bit Score: 51.11 E-value: 7.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 56 GWVTGTGGGISLKHGDEIYIAPSGVQKERIQPEDmfvcdINEKDISGPSPSKKLKKSQcTPLFMNAYTMRGAGAVIHTHS 135
Cdd:PRK08660 16 GLVSSHFGNISVRTGDGLLITRTGSMLDEITEGD-----VIEVGIDDDGSVDPLASSE-TPVHRAIYRRTSAKAIVHAHP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 136 KAAVMATLLfpgrefkithQEMIKGIkkCTSGGYYryddMLVVPIIENTPEEKDLKDRMAHAMNEYPdscAVLVRRHGVY 215
Cdd:PRK08660 90 PYAVALSLL----------EDEIVPL--DSEGLYF----LGTIPVVGGDIGSGELAENVARALSEHK---GVVVRGHGTF 150
|
....*....
gi 767966013 216 VWGETWEKA 224
Cdd:PRK08660 151 AIGKTLEEA 159
|
|
| sgaE |
PRK12348 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
56-219 |
5.25e-07 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 183460 Cd Length: 228 Bit Score: 49.03 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 56 GWVTGTGGGISL--KHGDEIYIAPSGVQKERIQPEDMFVCDINEKDISGpspskKLKKSQCTPLFMNAY-TMRGAGAVIH 132
Cdd:PRK12348 19 GLVTFTWGNVSAidRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEG-----EYRPSSDTATHLELYrRYPSLGGIVH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 133 THSKAAV---MATLLFPGreFKITHQEMIKGIKKCTSG-------GYYRYDDMLVvpIIENTPEEKDLkdrmahamnEYP 202
Cdd:PRK12348 94 THSTHATawaQAGLAIPA--LGTTHADYFFGDIPCTRGlseeevqGEYELNTGKV--IIETLGNAEPL---------HTP 160
|
170
....*....|....*..
gi 767966013 203 dscAVLVRRHGVYVWGE 219
Cdd:PRK12348 161 ---GIVVYQHGPFAWGK 174
|
|
| araD |
PRK08193 |
L-ribulose-5-phosphate 4-epimerase AraD; |
51-224 |
1.40e-06 |
|
L-ribulose-5-phosphate 4-epimerase AraD;
Pssm-ID: 236181 Cd Length: 231 Bit Score: 47.91 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 51 QFYHLGWVTGTGG---GISLKHGdEIYIAPSGVQKERIQPEDMFVCDINEKDISGpspskKLKKSQCTPLFMNAY-TMRG 126
Cdd:PRK08193 15 ALPKHGLVTFTWGnvsAIDRERG-LFVIKPSGVDYDKMTAEDMVVVDLEGNVVEG-----KLKPSSDTPTHLVLYkAFPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 127 AGAVIHTHSKAAVM---AtllfpGRE---FKITHQEMIKGIKKCTS-------GGYYRYDDMLVvpIIEnTPEEKDLkdr 193
Cdd:PRK08193 89 IGGIVHTHSRHATAwaqA-----GRDipaLGTTHADYFYGDIPCTRkmtdeeiNGEYEWETGKV--IVE-TFEKRGI--- 157
|
170 180 190
....*....|....*....|....*....|.
gi 767966013 194 mahamnEYPDSCAVLVRRHGVYVWGETWEKA 224
Cdd:PRK08193 158 ------DPAAVPGVLVHSHGPFTWGKDAEDA 182
|
|
| PRK08087 |
PRK08087 |
L-fuculose-phosphate aldolase; |
31-224 |
2.06e-06 |
|
L-fuculose-phosphate aldolase;
Pssm-ID: 181226 [Multi-domain] Cd Length: 215 Bit Score: 47.43 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 31 RSLLSQDkehprylIPELCKQFYHLGWVTGTGGGISLKHGDEIYIAPSGVQKERIQPEDMFVCDINEKDISGPSPSKKLK 110
Cdd:PRK08087 3 RNKLARQ-------IIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKLTESHIVFVDGNGKHEEGKLPSSEWR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 111 ksqctpLFMNAYTMR-GAGAVIHTHSKAAVMATLLfpGREFKITHQeMIkgikkCTSGGyyryDDMLVVPIIenTPEEKD 189
Cdd:PRK08087 76 ------FHMAAYQTRpDANAVVHNHAVHCTAVSIL--NRPIPAIHY-MI-----AAAGG----NSIPCAPYA--TFGTRE 135
|
170 180 190
....*....|....*....|....*....|....*
gi 767966013 190 LKDRMAHAMNEypdSCAVLVRRHGVYVWGETWEKA 224
Cdd:PRK08087 136 LSEHVALALKN---RKATLLQHHGLIACEVNLEKA 167
|
|
| sgbE |
PRK12347 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
53-218 |
2.47e-06 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 183459 Cd Length: 231 Bit Score: 47.12 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 53 YHLgwVTGTGGGISLKHGDE--IYIAPSGVQKERIQPEDMFVCDInekdISGPSPSKKLKKSQCTPLFMNAY-TMRGAGA 129
Cdd:PRK12347 19 HHL--VTFTWGNVSAVDETRqlMVIKPSGVEYDVMTADDMVVVEI----ASGKVVEGSKKPSSDTPTHLALYrRYPEIGG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 130 VIHTHSKAAVM---ATLLFPgrEFKITHQEMIKGIKKCTS-------GGYYRYDDMLVvpIIEnTPEEKDLKDRmahamn 199
Cdd:PRK12347 93 IVHTHSRHATIwsqAGLDLP--AWGTTHADYFYGAIPCTRlmtaeeiNGEYEYQTGEV--IIE-TFEERGISPA------ 161
|
170
....*....|....*....
gi 767966013 200 eypDSCAVLVRRHGVYVWG 218
Cdd:PRK12347 162 ---QIPAVLVHSHGPFAWG 177
|
|
| PRK06833 |
PRK06833 |
L-fuculose-phosphate aldolase; |
39-143 |
9.70e-06 |
|
L-fuculose-phosphate aldolase;
Pssm-ID: 180717 [Multi-domain] Cd Length: 214 Bit Score: 45.12 E-value: 9.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 39 EHPRYLIPELCKQFYHLGWVTGTGGGISLKHGDEIYIA--PSGVQKERIQPEDMFVCDINEKDISG---PSPSKKLKKSQ 113
Cdd:PRK06833 4 QKEREEIVAYGKKLISSGLTKGTGGNISIFNREQGLMAitPSGIDYFEIKPEDIVIMDLDGKVVEGerkPSSELDMHLIF 83
|
90 100 110
....*....|....*....|....*....|..
gi 767966013 114 ctplfmnaYTMR-GAGAVIHTHSK-AAVMATL 143
Cdd:PRK06833 84 --------YRNReDINAIVHTHSPyATTLACL 107
|
|
| PRK06755 |
PRK06755 |
hypothetical protein; Validated |
176-241 |
1.77e-04 |
|
hypothetical protein; Validated
Pssm-ID: 102532 Cd Length: 209 Bit Score: 41.56 E-value: 1.77e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767966013 176 LVVPIIENTPEEKDLKDRMAHAMNEypDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSM 241
Cdd:PRK06755 135 MTIPIVEDEKKFADLLENNVPNFIE--GGGVVLVHNYGMIVWGKTPEEAKKWLEGIEYLMNYHVKL 198
|
|
| araD |
PRK13213 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
60-224 |
3.47e-03 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 106181 Cd Length: 231 Bit Score: 37.78 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 60 GTGGGISLKHGdEIYIAPSGVQKERIQPEDMFVCDInekdISGPSPSKKLKKSQCTPLFMNAY-TMRGAGAVIHTHSK-A 137
Cdd:PRK13213 27 GNVSGIDREHG-LVVIKPSGVEYDVMSVNDMVVVDL----ATGKVVEGDKKPSSDTDTHLVLYrAFAEIGGIVHTHSRhA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966013 138 AVMATLLFPGREFKITHQEMIKGIKKCTS-------GGYYRYDdmlVVPIIENTPEEKDLKDrmahamneyPDSCAVLVR 210
Cdd:PRK13213 102 TIWAQAGKSLSALGTTHADYFYGPIPCTRlmteaeiTGDYEHE---TGKVIVETFAEQGLRA---------ADIPAVLVN 169
|
170
....*....|....
gi 767966013 211 RHGVYVWGETWEKA 224
Cdd:PRK13213 170 GHGPFAWGSNAANA 183
|
|
|