|
Name |
Accession |
Description |
Interval |
E-value |
| AraD |
COG0235 |
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ... |
10-210 |
2.59e-80 |
|
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: 239.35 E-value: 2.59e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 10 ALRREMVDICRRMNLSGINQGTAGNLSVRTDDG-FLITPSSMPYDTMQPDDLVEMGFDGTYV--GHRPSSEWRFHRDILR 86
Cdd:COG0235 5 ELREELAAAGRRLARRGLVDGTAGNISVRLDDDrFLITPSGVDFGELTPEDLVVVDLDGNVVegDLKPSSETPLHLAIYR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 87 ARTDIDVVLHCHSIYATTLACHHKTIPSFHYMTGIAGGTTIRCAEYATFGTQALSDNALLALKDRLACLLGQHGQISLGK 166
Cdd:COG0235 85 ARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGPGTEELAEAIAEALGDRPAVLLRNHGVVVWGK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1550132976 167 TLEQALWLAIEVETLSRIYVQALTLGEPPILPDDEMERVIAQMR 210
Cdd:COG0235 165 DLAEAFDRAEVLEEAARIQLLALALGGPLVLSDEEIDKLARKFG 208
|
|
| PRK08087 |
PRK08087 |
L-fuculose-phosphate aldolase; |
7-215 |
1.91e-76 |
|
L-fuculose-phosphate aldolase;
Pssm-ID: 181226 [Multi-domain] Cd Length: 215 Bit Score: 229.63 E-value: 1.91e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 7 DKLALRREMVDICRRMNLSGINQGTAGNLSVRTDDGFLITPSSMPYDTMQPDDLVEMGFDGTY-VGHRPSSEWRFHRDIL 85
Cdd:PRK08087 2 ERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKLTESHIVFVDGNGKHeEGKLPSSEWRFHMAAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 86 RARTDIDVVLHCHSIYATTLACHHKTIPSFHYMTGIAGGTTIRCAEYATFGTQALSDNALLALKDRLACLLGQHGQISLG 165
Cdd:PRK08087 82 QTRPDANAVVHNHAVHCTAVSILNRPIPAIHYMIAAAGGNSIPCAPYATFGTRELSEHVALALKNRKATLLQHHGLIACE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1550132976 166 KTLEQALWLAIEVETLSRIYVQALTLGEP-PILPDDEMERVIAQMRrmSYG 215
Cdd:PRK08087 162 VNLEKALWLAHEVEVLAQLYLKTLAITDPvPVLSDEEIAVVLEKFK--TYG 210
|
|
| Aldolase_II |
pfam00596 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
13-186 |
1.74e-65 |
|
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: 200.46 E-value: 1.74e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 13 REMVDICRRMNLSGINQGTAGNLSVR-TDDGFLITPSSMPYDTMQPDDLVEMGFDGTYV--GHRPSSEWRFHRDILRART 89
Cdd:pfam00596 1 EELAAAGRLLARRGLVEGTGGNISVRlPGDGFLITPSGVDFGELTPEDLVVVDLDGNVVegGLKPSSETPLHLAIYRARP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 90 DIDVVLHCHSIYATTLACHHKTIPSFHYMTGIAGGTTIRCAEYATFGTQALSDNALLALK-DRLACLLGQHGQISLGKTL 168
Cdd:pfam00596 81 DAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTEELGERIAEALGgDRKAVLLRNHGLLVWGKTL 160
|
170
....*....|....*...
gi 1550132976 169 EQALWLAIEVETLSRIYV 186
Cdd:pfam00596 161 EEAFYLAEELERAAEIQL 178
|
|
| Aldolase_II |
smart01007 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
15-186 |
2.72e-54 |
|
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: 172.44 E-value: 2.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 15 MVDICRRMNLSGINQGTAGNLSVR--TDDGFLITPSSMPYDTMQPDDLVEMGFDGTYV----GHRPSSEWRFHRDILRAR 88
Cdd:smart01007 1 LAAACRLLARRGLVEGTGGNISARvgEEDLFLITPSGVDFGELTASDLVVVDLDGNVVegggGPKPSSETPLHLAIYRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 89 TDIDVVLHCHSIYATTLACHHKTIPSFHY-MTGIAGGTTIRCAEYATFGT------QALSDNALLALKDRLACLLGQHGQ 161
Cdd:smart01007 81 PDVGAVVHTHSPYATALAALGKPLPLLPTeQAAAFLGGEIPYAPYAGPGTelaeegAELAEALAEALPDRPAVLLRNHGL 160
|
170 180
....*....|....*....|....*
gi 1550132976 162 ISLGKTLEQALWLAIEVETLSRIYV 186
Cdd:smart01007 161 LVWGKTLEEAFDLAEELEEAAEIQL 185
|
|
| Aldolase_II |
cd00398 |
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ... |
11-203 |
3.97e-48 |
|
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: 157.53 E-value: 3.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 11 LRREMVDICRRMNLSGINQGTAGNLSVRTDD--GFLITPSSMPYDTMQPDDLVEMGFDGTYV-GHRPSSEWRFHRDILRA 87
Cdd:cd00398 3 LKRKIIAACLLLDLYGWVTGTGGNVSARDRDrgYFLITPSGVDYEEMTASDLVVVDAQGKVVeGKKPSSETPLHLALYRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 88 RTDIDVVLHCHSIYATTLA-CHHKTIPSFHYMTGIAGGTTIRCAEYATFGTQALSDNALLAL--KDRLACLLGQHGQISL 164
Cdd:cd00398 83 RPDIGCIVHTHSTHATAVSqLKEGLIPAGHTACAVYFTGDIPCTPYMTPETGEDEIGTQRALgfPNSKAVLLRNHGLFAW 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1550132976 165 GKTLEQALWLAIEVETLSRIYVQALTLGEP-PILPDDEME 203
Cdd:cd00398 163 GPTLDEAFHLAVVLEVAAEIQLKALSMGGQlPPISLELLN 202
|
|
| salvage_mtnB |
TIGR03328 |
methylthioribulose-1-phosphate dehydratase; Members of this family are the ... |
15-191 |
6.47e-21 |
|
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: 86.55 E-value: 6.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 15 MVDICRRMNLSGINQGTAGNLSVRTD-DGFLITPSSMPYDTMQPDDLVEMGFDGTYV--GHRPSSEWRFHRDILRaRTDI 91
Cdd:TIGR03328 1 LIEAGRDLYKRGWVPGTGGNLSARLDeDEILITPSGVDKGRLTPEDFLVVDLQGKPVsgGLKPSAETLLHTQLYR-LTGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 92 DVVLHCHSIYATTLACHHK-----TIPSFHYMTGIAGGTTIRCAEYA-----TFGTQALSD---NALLALKDRLACLLGQ 158
Cdd:TIGR03328 80 GAVLHTHSVEATVLSRLYPsnggfELEGYEMLKGLPGITTHEDTLVVpiienTQDIARLADsvaPALNAYPDVPGVLIRG 159
|
170 180 190
....*....|....*....|....*....|...
gi 1550132976 159 HGQISLGKTLEQALWLAIEVETLSRIYVQALTL 191
Cdd:TIGR03328 160 HGLYAWGRDWEEAKRHLEALEFLFECELEMLKL 192
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| AraD |
COG0235 |
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ... |
10-210 |
2.59e-80 |
|
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: 239.35 E-value: 2.59e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 10 ALRREMVDICRRMNLSGINQGTAGNLSVRTDDG-FLITPSSMPYDTMQPDDLVEMGFDGTYV--GHRPSSEWRFHRDILR 86
Cdd:COG0235 5 ELREELAAAGRRLARRGLVDGTAGNISVRLDDDrFLITPSGVDFGELTPEDLVVVDLDGNVVegDLKPSSETPLHLAIYR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 87 ARTDIDVVLHCHSIYATTLACHHKTIPSFHYMTGIAGGTTIRCAEYATFGTQALSDNALLALKDRLACLLGQHGQISLGK 166
Cdd:COG0235 85 ARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGPGTEELAEAIAEALGDRPAVLLRNHGVVVWGK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1550132976 167 TLEQALWLAIEVETLSRIYVQALTLGEPPILPDDEMERVIAQMR 210
Cdd:COG0235 165 DLAEAFDRAEVLEEAARIQLLALALGGPLVLSDEEIDKLARKFG 208
|
|
| PRK08087 |
PRK08087 |
L-fuculose-phosphate aldolase; |
7-215 |
1.91e-76 |
|
L-fuculose-phosphate aldolase;
Pssm-ID: 181226 [Multi-domain] Cd Length: 215 Bit Score: 229.63 E-value: 1.91e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 7 DKLALRREMVDICRRMNLSGINQGTAGNLSVRTDDGFLITPSSMPYDTMQPDDLVEMGFDGTY-VGHRPSSEWRFHRDIL 85
Cdd:PRK08087 2 ERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKLTESHIVFVDGNGKHeEGKLPSSEWRFHMAAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 86 RARTDIDVVLHCHSIYATTLACHHKTIPSFHYMTGIAGGTTIRCAEYATFGTQALSDNALLALKDRLACLLGQHGQISLG 165
Cdd:PRK08087 82 QTRPDANAVVHNHAVHCTAVSILNRPIPAIHYMIAAAGGNSIPCAPYATFGTRELSEHVALALKNRKATLLQHHGLIACE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1550132976 166 KTLEQALWLAIEVETLSRIYVQALTLGEP-PILPDDEMERVIAQMRrmSYG 215
Cdd:PRK08087 162 VNLEKALWLAHEVEVLAQLYLKTLAITDPvPVLSDEEIAVVLEKFK--TYG 210
|
|
| Aldolase_II |
pfam00596 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
13-186 |
1.74e-65 |
|
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: 200.46 E-value: 1.74e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 13 REMVDICRRMNLSGINQGTAGNLSVR-TDDGFLITPSSMPYDTMQPDDLVEMGFDGTYV--GHRPSSEWRFHRDILRART 89
Cdd:pfam00596 1 EELAAAGRLLARRGLVEGTGGNISVRlPGDGFLITPSGVDFGELTPEDLVVVDLDGNVVegGLKPSSETPLHLAIYRARP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 90 DIDVVLHCHSIYATTLACHHKTIPSFHYMTGIAGGTTIRCAEYATFGTQALSDNALLALK-DRLACLLGQHGQISLGKTL 168
Cdd:pfam00596 81 DAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTEELGERIAEALGgDRKAVLLRNHGLLVWGKTL 160
|
170
....*....|....*...
gi 1550132976 169 EQALWLAIEVETLSRIYV 186
Cdd:pfam00596 161 EEAFYLAEELERAAEIQL 178
|
|
| PRK06833 |
PRK06833 |
L-fuculose-phosphate aldolase; |
12-216 |
1.19e-63 |
|
L-fuculose-phosphate aldolase;
Pssm-ID: 180717 [Multi-domain] Cd Length: 214 Bit Score: 197.28 E-value: 1.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 12 RREMVDICRRMNLSGINQGTAGNLSV-RTDDGFL-ITPSSMPYDTMQPDDLVEMGFDGTYV-GHR-PSSEWRFHRDILRA 87
Cdd:PRK06833 7 REEIVAYGKKLISSGLTKGTGGNISIfNREQGLMaITPSGIDYFEIKPEDIVIMDLDGKVVeGERkPSSELDMHLIFYRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 88 RTDIDVVLHCHSIYATTLACHHKTIPSFHYMTGIAGgTTIRCAEYATFGTQALSDNALLALKDRLACLLGQHGQISLGKT 167
Cdd:PRK06833 87 REDINAIVHTHSPYATTLACLGWELPAVHYLIAVAG-PNVRCAEYATFGTKELAENAFEAMEDRRAVLLANHGLLAGANN 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1550132976 168 LEQALWLAIEVETLSRIYVQALTLGEPPILPDDEMERVIAQMRrmSYGQ 216
Cdd:PRK06833 166 LKNAFNIAEEIEFCAEIYYQTKSIGEPKLLPEDEMENMAEKFK--TYGQ 212
|
|
| Aldolase_II |
smart01007 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
15-186 |
2.72e-54 |
|
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: 172.44 E-value: 2.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 15 MVDICRRMNLSGINQGTAGNLSVR--TDDGFLITPSSMPYDTMQPDDLVEMGFDGTYV----GHRPSSEWRFHRDILRAR 88
Cdd:smart01007 1 LAAACRLLARRGLVEGTGGNISARvgEEDLFLITPSGVDFGELTASDLVVVDLDGNVVegggGPKPSSETPLHLAIYRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 89 TDIDVVLHCHSIYATTLACHHKTIPSFHY-MTGIAGGTTIRCAEYATFGT------QALSDNALLALKDRLACLLGQHGQ 161
Cdd:smart01007 81 PDVGAVVHTHSPYATALAALGKPLPLLPTeQAAAFLGGEIPYAPYAGPGTelaeegAELAEALAEALPDRPAVLLRNHGL 160
|
170 180
....*....|....*....|....*
gi 1550132976 162 ISLGKTLEQALWLAIEVETLSRIYV 186
Cdd:smart01007 161 LVWGKTLEEAFDLAEELEEAAEIQL 185
|
|
| Aldolase_II |
cd00398 |
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ... |
11-203 |
3.97e-48 |
|
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: 157.53 E-value: 3.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 11 LRREMVDICRRMNLSGINQGTAGNLSVRTDD--GFLITPSSMPYDTMQPDDLVEMGFDGTYV-GHRPSSEWRFHRDILRA 87
Cdd:cd00398 3 LKRKIIAACLLLDLYGWVTGTGGNVSARDRDrgYFLITPSGVDYEEMTASDLVVVDAQGKVVeGKKPSSETPLHLALYRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 88 RTDIDVVLHCHSIYATTLA-CHHKTIPSFHYMTGIAGGTTIRCAEYATFGTQALSDNALLAL--KDRLACLLGQHGQISL 164
Cdd:cd00398 83 RPDIGCIVHTHSTHATAVSqLKEGLIPAGHTACAVYFTGDIPCTPYMTPETGEDEIGTQRALgfPNSKAVLLRNHGLFAW 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1550132976 165 GKTLEQALWLAIEVETLSRIYVQALTLGEP-PILPDDEME 203
Cdd:cd00398 163 GPTLDEAFHLAVVLEVAAEIQLKALSMGGQlPPISLELLN 202
|
|
| PRK05874 |
PRK05874 |
L-fuculose-phosphate aldolase; Validated |
17-200 |
1.39e-37 |
|
L-fuculose-phosphate aldolase; Validated
Pssm-ID: 102036 [Multi-domain] Cd Length: 217 Bit Score: 130.53 E-value: 1.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 17 DICRRmnlsGINQGTAGNLSVRTDDG-FLITPSSMPYDTMQPDDLVEMGFDGTYV----GHRPSSEWRFHRDILRARTDI 91
Cdd:PRK05874 17 DMLRR----GLVEGTAGNISARRSDGnVVITPSSVDYAEMLLHDLVLVDAGGAVLhakdGRSPSTELNLHLACYRAFDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 92 DVVLHCHSIYATTLACHHKTIPSFHYMTGIAGGTTIRCAEYATFGTQALSDNALLALKDRLACLLGQHGQISLGKTLEQA 171
Cdd:PRK05874 93 GSVIHSHPVWATMFAVAHEPIPACIDEFAIYCGGDVRCTEYAASGTPEVGRNAVRALEGRAAALIANHGLVAVGPRPDQV 172
|
170 180
....*....|....*....|....*....
gi 1550132976 172 LWLAIEVETLSRIYVQALTLGEPPILPDD 200
Cdd:PRK05874 173 LRVTALVERTAQIVWGARALGGPVPIPED 201
|
|
| PRK06557 |
PRK06557 |
L-ribulose-5-phosphate 4-epimerase; Validated |
1-216 |
5.31e-28 |
|
L-ribulose-5-phosphate 4-epimerase; Validated
Pssm-ID: 235829 [Multi-domain] Cd Length: 221 Bit Score: 105.86 E-value: 5.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 1 MAETETDKLALRREMVDICRRMNLSGINQGTAGNLSVR--TDDGFLITPSSMPYDTMQPDDLVEMGFDGTYV-GHR-PSS 76
Cdd:PRK06557 1 GPEVRAMVEKLREEVCKLHLELPKYGLVVWTSGNVSARdpGTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVeGDLkPSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 77 EWRFHRDILRARTDIDVVLHCHSIYATTLACHHKTIPSfhYMTGIAG--GTTIRCAEYATFGTQALSDNALLALKD--RL 152
Cdd:PRK06557 81 DTASHLYVYRHMPDVGGVVHTHSTYATAWAARGEPIPC--VLTAMADefGGPIPVGPFALIGDEAIGKGIVETLKGgrSP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550132976 153 ACLLGQHGQISLGKTLEQALWLAIEVETLSRIYVQALTLGEPPILPDDEMERVIAQMRRMsYGQ 216
Cdd:PRK06557 159 AVLMQNHGVFTIGKDAEDAVKAAVMVEEVARTVHIARQLGEPIPIPQEEIDRLYDRYQNV-YGQ 221
|
|
| PRK08660 |
PRK08660 |
aldolase; |
13-184 |
1.05e-22 |
|
aldolase;
Pssm-ID: 181527 [Multi-domain] Cd Length: 181 Bit Score: 90.79 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 13 REMVDICRRMNLSGINQGTAGNLSVRTDDGFLITPSSMPYDTMQPDDLVEMGFDGTYVGHR-PSSEWRFHRDILRaRTDI 91
Cdd:PRK08660 3 QEFARIGKKLFAHGLVSSHFGNISVRTGDGLLITRTGSMLDEITEGDVIEVGIDDDGSVDPlASSETPVHRAIYR-RTSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 92 DVVLHCHSIYATTLACHHKTIPSF----HYMTGiaggtTIRCAEyATFGTQALSDNALLALKDRLACLLGQHGQISLGKT 167
Cdd:PRK08660 82 KAIVHAHPPYAVALSLLEDEIVPLdsegLYFLG-----TIPVVG-GDIGSGELAENVARALSEHKGVVVRGHGTFAIGKT 155
|
170
....*....|....*..
gi 1550132976 168 LEQALWLAIEVETLSRI 184
Cdd:PRK08660 156 LEEAYIYTSQLEHSCKV 172
|
|
| PRK08130 |
PRK08130 |
putative aldolase; Validated |
6-203 |
6.04e-21 |
|
putative aldolase; Validated
Pssm-ID: 181241 [Multi-domain] Cd Length: 213 Bit Score: 86.85 E-value: 6.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 6 TDKLALRREMVDICRRMNLSGINQGTAGNLSVRTDD-GFLITPSSMPYDTMQPDDLVEMGFDGTYV-GHRPSSEWRFHRD 83
Cdd:PRK08130 1 MTEQALREEIVRLGRSLFQRGYTVGSAGNISARLDDgGWLVTPTGSCLGRLDPARLSKVDADGNWLsGDKPSKEVPLHRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 84 ILRARTDIDVVLHCHSIYATTLAC-----HHKTIPSF--HYMTGIAGGTTIRcaeYATFGTQALSDN-ALLALKDRlACL 155
Cdd:PRK08130 81 IYRNNPECGAVVHLHSTHLTALSClggldPTNVLPPFtpYYVMRVGHVPLIP---YYRPGDPAIAEAlAGLAARYR-AVL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1550132976 156 LGQHGQISLGKTLEQALWLAIEVETLSRIYvqaLTLGEPPI--LPDDEME 203
Cdd:PRK08130 157 LANHGPVVWGSSLEAAVNATEELEETAKLI---LLLGGRPPryLTDEEIA 203
|
|
| salvage_mtnB |
TIGR03328 |
methylthioribulose-1-phosphate dehydratase; Members of this family are the ... |
15-191 |
6.47e-21 |
|
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: 86.55 E-value: 6.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 15 MVDICRRMNLSGINQGTAGNLSVRTD-DGFLITPSSMPYDTMQPDDLVEMGFDGTYV--GHRPSSEWRFHRDILRaRTDI 91
Cdd:TIGR03328 1 LIEAGRDLYKRGWVPGTGGNLSARLDeDEILITPSGVDKGRLTPEDFLVVDLQGKPVsgGLKPSAETLLHTQLYR-LTGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 92 DVVLHCHSIYATTLACHHK-----TIPSFHYMTGIAGGTTIRCAEYA-----TFGTQALSD---NALLALKDRLACLLGQ 158
Cdd:TIGR03328 80 GAVLHTHSVEATVLSRLYPsnggfELEGYEMLKGLPGITTHEDTLVVpiienTQDIARLADsvaPALNAYPDVPGVLIRG 159
|
170 180 190
....*....|....*....|....*....|...
gi 1550132976 159 HGQISLGKTLEQALWLAIEVETLSRIYVQALTL 191
Cdd:TIGR03328 160 HGLYAWGRDWEEAKRHLEALEFLFECELEMLKL 192
|
|
| PRK07490 |
PRK07490 |
hypothetical protein; Provisional |
26-210 |
4.26e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 236031 [Multi-domain] Cd Length: 245 Bit Score: 74.76 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 26 GINQGTAGNLSVRT-DDG--FLITPSSMPYDTMQPDDLVEMGFDGTYVGHRP----SSEWRFHRDILRARTDIDVVLHCH 98
Cdd:PRK07490 26 GMHEAVANHFSAAVsADGkqFLLNPKWKHFSRIRASDLLLLDADDPSTAERPdvpdATAWAIHGQIHRRLPHARCVMHVH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 99 SIYATTLAC-HHKTIPSFHYMTGIAGGttiRCAEYATFGTQALSDNA-----LLALKDRLacLLGQHGQISLGKTLEQAL 172
Cdd:PRK07490 106 SVYATALAClADPTLPPIDQNTARFFN---RVAVDTLYGGMALEEEGerlagLLGDKRRL--LMGNHGVLVTGDTVAEAF 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 1550132976 173 WLAIEVETLSRIYVQALTLGEP-PILPDDEMERVIAQMR 210
Cdd:PRK07490 181 DDLYYFERACQTYITALSTGQPlRVLSDAVAEKTARDWE 219
|
|
| PRK08333 |
PRK08333 |
aldolase; |
12-187 |
3.72e-15 |
|
aldolase;
Pssm-ID: 181393 [Multi-domain] Cd Length: 184 Bit Score: 71.01 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 12 RREMVDICRRMNLSGINQGTAGNLSVRTDDGFLITPSSMPYDTMQPDDLVEMGFDGTYV-GHRPSSEWRFHRDILRARTD 90
Cdd:PRK08333 5 KAQLVKYSKLAHERGLTAAFGGNLSIRVGNLVFIKATGSVMDELTREQVAVIDLNGNQLsSVRPSSEYRLHLAVYRNRPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 91 IDVVLHCHSIYATTLACHHK------TIPSFHYMTGIAggttirCAEYATFGTQALSDNALLALKDRLACLLGQHGQISL 164
Cdd:PRK08333 85 VRAIAHLHPPYSIVASTLLEeelpiiTPEAELYLKKIP------ILPFRPAGSVELAEQVAEAMKEYDAVIMERHGIVTV 158
|
170 180
....*....|....*....|...
gi 1550132976 165 GKTLEQALWLAIEVETLSRIYVQ 187
Cdd:PRK08333 159 GRSLREAFYKAELVEESAKLWYL 181
|
|
| PRK09220 |
PRK09220 |
methylthioribulose 1-phosphate dehydratase; |
13-105 |
4.94e-13 |
|
methylthioribulose 1-phosphate dehydratase;
Pssm-ID: 236415 [Multi-domain] Cd Length: 204 Bit Score: 65.34 E-value: 4.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 13 REMVDICRRMNLSGINQGTAGNLSVRTDDGF-LITPSSMPYDTMQPDDLVEMGFDGTYV--GHRPSSEWRFHRDILRART 89
Cdd:PRK09220 8 QQLIAAGRWIGARGWVPATSGNMSVRLDEQHcAITVSGKDKGSLTAEDFLQVDIAGNAVpsGRKPSAETLLHTQLYRLFP 87
|
90
....*....|....*.
gi 1550132976 90 DIDVVLHCHSIYATTL 105
Cdd:PRK09220 88 EIGAVLHTHSVNATVL 103
|
|
| araD |
PRK08193 |
L-ribulose-5-phosphate 4-epimerase AraD; |
31-191 |
1.48e-12 |
|
L-ribulose-5-phosphate 4-epimerase AraD;
Pssm-ID: 236181 Cd Length: 231 Bit Score: 64.47 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 31 TAGNLS-VRTDDG-FLITPSSMPYDTMQPDDLVEMGFDGTYV-GH-RPSSEWRFHRDILRARTDIDVVLHCHSIYATTLA 106
Cdd:PRK08193 25 TWGNVSaIDRERGlFVIKPSGVDYDKMTAEDMVVVDLEGNVVeGKlKPSSDTPTHLVLYKAFPEIGGIVHTHSRHATAWA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 107 CHHKTIPSFhymtgiagGTT--------IRCA----------EYA---------TFGTQALSDNALlalkdrLACLLGQH 159
Cdd:PRK08193 105 QAGRDIPAL--------GTThadyfygdIPCTrkmtdeeingEYEwetgkviveTFEKRGIDPAAV------PGVLVHSH 170
|
170 180 190
....*....|....*....|....*....|..
gi 1550132976 160 GQISLGKTLEQALWLAIEVETLSRIYVQALTL 191
Cdd:PRK08193 171 GPFTWGKDAEDAVHNAVVLEEVAKMAYFTRQL 202
|
|
| sgaE |
PRK12348 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
31-191 |
1.18e-11 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 183460 Cd Length: 228 Bit Score: 62.13 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 31 TAGNLSV--RTDDGFLITPSSMPYDTMQPDDLVEMGFDGTYV--GHRPSSEWRFHRDILRARTDIDVVLHCHSIYATTLA 106
Cdd:PRK12348 24 TWGNVSAidRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVegEYRPSSDTATHLELYRRYPSLGGIVHTHSTHATAWA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 107 CHHKTIPSFhymtgiagGTTirCAEYaTFG----TQALSDNAL---------------LALKDRL---ACLLGQHGQISL 164
Cdd:PRK12348 104 QAGLAIPAL--------GTT--HADY-FFGdipcTRGLSEEEVqgeyelntgkviietLGNAEPLhtpGIVVYQHGPFAW 172
|
170 180
....*....|....*....|....*..
gi 1550132976 165 GKTLEQALWLAIEVETLSRIYVQALTL 191
Cdd:PRK12348 173 GKDAHDAVHNAVVMEEVAKMAWIARGI 199
|
|
| PRK06208 |
PRK06208 |
class II aldolase/adducin family protein; |
19-215 |
6.67e-09 |
|
class II aldolase/adducin family protein;
Pssm-ID: 235743 Cd Length: 274 Bit Score: 54.61 E-value: 6.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 19 CRRMNLSGINQGTAGNLSVRtD----DGFLITPSSMPYDTMQPDDLVEMGFDGTYV-GHRPSSEWRF--HRDILRARTDI 91
Cdd:PRK06208 51 FRLFARFGFDEGLAGHITAR-DpelpDHFWVNPLGVHFSQIKVSDLLLVDHDGEVVeGDRPLNRAAFaiHSAIHEARPDV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 92 DVVLHCHSIYATTLACHHKTIpsfHYMTGIAggttirCAEY---ATFGTQA-----LSDNALLA--LKDRLACLLGQHGQ 161
Cdd:PRK06208 130 VAAAHTHSTYGKAWSTLGRPL---DPITQDA------CAFYedhALFDDFTgvvvdTSEGRRIAaaLGTHKAVILQNHGL 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1550132976 162 ISLGKTLEQALWLAIEVETLSRIYVQALTLGEPPILPdDEMERVIAQMRRMSYG 215
Cdd:PRK06208 201 LTVGPSVDAAAWWFIALERACQTQLLAEAAGPPQPID-HETARHTRSQVGSEYG 253
|
|
| PRK06661 |
PRK06661 |
hypothetical protein; Provisional |
11-202 |
1.03e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 168637 Cd Length: 231 Bit Score: 53.68 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 11 LRREMVDICRRMNLSGINQGTAGNLSVRTDDG--FLITPSSMPYDTMQPDDLVEMGFDGTYVGHRP----SSEWRFHRDI 84
Cdd:PRK06661 3 IKYNLAAAYRIMAYLSLDDHTYTHLSARPKNAdfYYIYPFGLRFEEVTTENLLKVSLDGQILEGEEyqynKTGYFIHGSI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 85 LRARTDIDVVLHCH---SIYATTLACHHKTIPSF--HYMTGIAggttircaeYATFGTQAL-----SDNALLALKDRLAC 154
Cdd:PRK06661 83 YKTRPDISAIFHYHtpaSIAVSALKCGLLPISQWalHFYDRIS---------YHNYNSLALdadkqSSRLVNDLKQNYVM 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1550132976 155 LLGQHGQISLGKTLEQALWLAIEVETLSRIYVQAL-TLGEPPILPDDEM 202
Cdd:PRK06661 154 LLRNHGAITCGKTIHEAMFYTYHLEQACKTQCLLNsTKKQELIIPSVEI 202
|
|
| PRK07044 |
PRK07044 |
aldolase II superfamily protein; Provisional |
35-222 |
1.68e-08 |
|
aldolase II superfamily protein; Provisional
Pssm-ID: 235916 Cd Length: 252 Bit Score: 53.31 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 35 LSVR---TDDGFLITPSSMPYDTMQPDDLVEMGFDGTYVGHrpsSEWR-------FHRDILRARTDIDVVLHCHSIYATT 104
Cdd:PRK07044 41 ISARvpgEEHHFLINPYGLLFDEITASNLVKIDLDGNVVDD---SPYPvnpagftIHSAIHAARPDAHCVMHTHTTAGVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 105 LACHHKTI-P-SFHYM---TGIA----GGTTIRCAEYATfgtqalsdnaLLA-LKDRLACLLGQHGQISLGKTLEQALWL 174
Cdd:PRK07044 118 VSAQRDGLlPlSQHALqfyGRLAyhdyEGIALDLDEGER----------LVAdLGDKPAMLLRNHGLLTVGRTVAEAFLL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1550132976 175 AIEVETLSRIYVQALTLGEPPILPDDEmerVIAQMRRMSYGQAPDPEG 222
Cdd:PRK07044 188 MYTLERACEIQVAAQAGGGELVLPPPE---VAERTARQSLFDPGAGAG 232
|
|
| PRK07090 |
PRK07090 |
class II aldolase/adducin domain protein; Provisional |
8-199 |
7.89e-08 |
|
class II aldolase/adducin domain protein; Provisional
Pssm-ID: 180832 Cd Length: 260 Bit Score: 51.56 E-value: 7.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 8 KLALRREMVDICRRMNLSGINQGTAGNLSVRTDDG--FLITPSSMPYDTMQPDDLVEMGFD-GTYVGH-RPSSEWRFHRD 83
Cdd:PRK07090 28 GWTLRQKLALTCRILFDAGHDSGLAGQITARAEAPgtYYTQRLGLGFDEITASNLLLVDEDlNVLDGEgMPNPANRFHSW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 84 ILRARTDIDVVLHCHSIYATTLA--------CHHKTIPSFHymtgiaggttiRCAEYATF-GTQALSDNALL---ALKDR 151
Cdd:PRK07090 108 IYRARPDVNCIIHTHPPHVAALSmlevplvvSHMDTCPLYD-----------DCAFLKDWpGVPVGNEEGEIisaALGDK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1550132976 152 LACLLGQHGQISLGKTLEQALWLAIEVETLSRIYVQALTLGE-PPILPD 199
Cdd:PRK07090 177 RAILLSHHGQLVAGKSIEEACVLALLIERAARLQLLAMAAGPiKPIPPE 225
|
|
| araD |
PRK13145 |
L-ribulose-5-phosphate 4-epimerase; Provisional |
11-184 |
1.82e-07 |
|
L-ribulose-5-phosphate 4-epimerase; Provisional
Pssm-ID: 183870 [Multi-domain] Cd Length: 234 Bit Score: 50.22 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 11 LRREMVDICRRMNLSGINQGTAGNLSV--RTDDGFLITPSSMPYDTMQPDDLVEMGFDGTYVGH--RPSSEWRFHRDILR 86
Cdd:PRK13145 6 MRERVCAANKSLPKHGLVKFTWGNVSEvcRELGRIVIKPSGVDYDELTPENMVVTDLDGNVVEGdlNPSSDLPTHVELYK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 87 ARTDIDVVLHCHSIYATTLACHHKTIPSFhymtgiagGTT--------IRCAEYAT-----------FGTQALSDNALLA 147
Cdd:PRK13145 86 AWPEVGGIVHTHSTEAVGWAQAGRDIPFY--------GTThadyfygpIPCARSLTkdevngayekeTGSVIIEEFEKRG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1550132976 148 LkDRLAC---LLGQHGQISLGKTLEQALWLAIEVETLSRI 184
Cdd:PRK13145 158 L-DPMAVpgiVVRNHGPFTWGKNPEQAVYHSVVLEEVAKM 196
|
|
| sgbE |
PRK12347 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
31-199 |
1.79e-06 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 183459 Cd Length: 231 Bit Score: 47.51 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 31 TAGNLSV--RTDDGFLITPSSMPYDTMQPDDLVEMG-FDGTYV--GHRPSSEWRFHRDILRARTDIDVVLHCHSIYATTL 105
Cdd:PRK12347 25 TWGNVSAvdETRQLMVIKPSGVEYDVMTADDMVVVEiASGKVVegSKKPSSDTPTHLALYRRYPEIGGIVHTHSRHATIW 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 106 A-----------CH----HKTIPSFHYMTG--IAGGTTIRCAEY--ATFGTQALSDNALLALkdrlacLLGQHGQISLGK 166
Cdd:PRK12347 105 SqagldlpawgtTHadyfYGAIPCTRLMTAeeINGEYEYQTGEViiETFEERGISPAQIPAV------LVHSHGPFAWGK 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1550132976 167 TLEQALWLAIEVETLS--RIYVQALTLGEPPILPD 199
Cdd:PRK12347 179 NAADAVHNAVVLEECAymGLFSRQLAPQLPAMQNE 213
|
|
| mtnB |
PRK06754 |
methylthioribulose 1-phosphate dehydratase; |
30-100 |
1.28e-05 |
|
methylthioribulose 1-phosphate dehydratase;
Pssm-ID: 180679 [Multi-domain] Cd Length: 208 Bit Score: 44.66 E-value: 1.28e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1550132976 30 GTAGNLSVRTDDG---FLITPSSMPYDTMQPDDLVEMGFDGTYVGH---RPSSEWRFHRDILRaRTDIDVVLHCHSI 100
Cdd:PRK06754 26 ATSGNLSIKVSDDpltFLVTASGKDKRKTTPEDFLLVDHDGKPVEEtelKPSAETLLHTHIYN-NTNAGCVLHVHTV 101
|
|
| PRK06486 |
PRK06486 |
aldolase; |
6-210 |
4.61e-05 |
|
aldolase;
Pssm-ID: 235814 Cd Length: 262 Bit Score: 43.16 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 6 TDKLALRREMVDICRRM-NLSGINQGTAGNLSVRT---DDGFLITPSSMPYDTMQPDDLVEMGFDGTYVG--HRPSS--- 76
Cdd:PRK06486 21 SDAVAQARVDLAACFRAaARHGLEEGICNHFSAVLpghDDLFLVNPYGYAFSEITASDLLICDFDGNVLAgrGEPEAtaf 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 77 --EWRFHRDILRARtdidVVLHCHSIYATTLAchhktipsfhyMTGIAGGTTircaeyatfgtqaLSDNAL--------- 145
Cdd:PRK06486 101 fiHARIHRAIPRAK----AAFHTHMPYATALS-----------LTEGRPLTT-------------LGQTALkfygrtavd 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 146 -----LALK----DRLA--------CLLGQHGQISLGKTLEQA------LWLAIEVETLsriyvqALTLGEPPILPDDEM 202
Cdd:PRK06486 153 edyngLALDaaegDRIAramgdadiVFLKNHGVMVCGPRIAEAwddlyyLERACEVQVL------AMSTGRPLVPVDPAI 226
|
....*....
gi 1550132976 203 -ERVIAQMR 210
Cdd:PRK06486 227 aAAVARQMR 235
|
|
| araD |
PRK13213 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
31-115 |
4.18e-03 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 106181 Cd Length: 231 Bit Score: 37.40 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550132976 31 TAGNLS-VRTDDGFL-ITPSSMPYDTMQPDDLVEMGFDGTYV---GHRPSSEWRFHRDILRARTDIDVVLHCHSIYATTL 105
Cdd:PRK13213 25 TWGNVSgIDREHGLVvIKPSGVEYDVMSVNDMVVVDLATGKVvegDKKPSSDTDTHLVLYRAFAEIGGIVHTHSRHATIW 104
|
90
....*....|
gi 1550132976 106 ACHHKTIPSF 115
Cdd:PRK13213 105 AQAGKSLSAL 114
|
|
|