|
Name |
Accession |
Description |
Interval |
E-value |
| salvage_mtnB |
TIGR03328 |
methylthioribulose-1-phosphate dehydratase; Members of this family are the ... |
30-228 |
3.81e-92 |
|
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: 269.14 E-value: 3.81e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 30 IPELCRLFYQLGWVTGTGGGISLKRGEQ-IYIAPSGVQKERIQPEDMFVCDLEERDIScppawKKLKKSQCTPLFMNAYI 108
Cdd:TIGR03328 1 LIEAGRDLYKRGWVPGTGGNLSARLDEDeILITPSGVDKGRLTPEDFLVVDLQGKPVS-----GGLKPSAETLLHTQLYR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 109 LRGAQAVIHTHSKAAVMATLLYPG-KEFRITHQEMIKGIRKGTSgtnyrYDEILVVPIIENTPEEKDLKDRMAWAMEEYP 187
Cdd:TIGR03328 76 LTGAGAVLHTHSVEATVLSRLYPSnGGFELEGYEMLKGLPGITT-----HEDTLVVPIIENTQDIARLADSVAPALNAYP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1951406446 188 DSCAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAVQMKQ 228
Cdd:TIGR03328 151 DVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLK 191
|
|
| Aldolase_II |
pfam00596 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
28-224 |
6.47e-51 |
|
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: 163.87 E-value: 6.47e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 28 ALIPELCRLFYQLGWVTGTGGGISLKR-GEQIYIAPSGVQKERIQPEDMFVCDLEERDISCPPawkklKKSQCTPLFMNA 106
Cdd:pfam00596 1 EELAAAGRLLARRGLVEGTGGNISVRLpGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGL-----KPSSETPLHLAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 107 YILR-GAQAVIHTHSKAAVMATLLYPGkeFRITHQEMIKgirkgtsgtnYRYDEIlvvPIIEN-TPEEKDLKDRMAWAME 184
Cdd:pfam00596 76 YRARpDAGAVVHTHSPYATALSLAKEG--LPPITQEAAD----------FLGGDI---PIIPYyTPGTEELGERIAEALG 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1951406446 185 EypDSCAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAV 224
Cdd:pfam00596 141 G--DRKAVLLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
|
|
| Aldolase_II |
smart01007 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
30-224 |
5.01e-49 |
|
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: 159.34 E-value: 5.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 30 IPELCRLFYQLGWVTGTGGGISLKRGEQ--IYIAPSGVQKERIQPEDMFVCDLEERDIscpPAWKKLKKSQCTPLFMNAY 107
Cdd:smart01007 1 LAAACRLLARRGLVEGTGGNISARVGEEdlFLITPSGVDFGELTASDLVVVDLDGNVV---EGGGGPKPSSETPLHLAIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 108 ILR-GAQAVIHTHSKAAVMATLLypGKEFRITHQEMIKGIRKGTSG-TNYRydeilvVPIIENTPEEKDLKDRMAWAMEE 185
Cdd:smart01007 78 RARpDVGAVVHTHSPYATALAAL--GKPLPLLPTEQAAAFLGGEIPyAPYA------GPGTELAEEGAELAEALAEALPD 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 1951406446 186 YPdscAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAV 224
Cdd:smart01007 150 RP---AVLLRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
|
|
| AraD |
COG0235 |
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ... |
24-240 |
2.30e-34 |
|
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: 122.25 E-value: 2.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 24 EHPRALIPELCRLFYQLGWVTGTGGGISLK-RGEQIYIAPSGVQKERIQPEDMFVCDLEERDIscppaWKKLKKSQCTPL 102
Cdd:COG0235 4 EELREELAAAGRRLARRGLVDGTAGNISVRlDDDRFLITPSGVDFGELTPEDLVVVDLDGNVV-----EGDLKPSSETPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 103 FMNAYILR-GAQAVIHTHSKAAVMATLLypGKEFRITHQEMIKgirkgtsgtnYRYDEILVVPiiENTPEEKDLKDRMAW 181
Cdd:COG0235 79 HLAIYRARpDVGAVVHTHSPYATALSAL--GEPLPPLEQTEAA----------AFLGDVPVVP--YAGPGTEELAEAIAE 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1951406446 182 AMEEYPdscAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAVQMKQCGlDPAALPVEE 240
Cdd:COG0235 145 ALGDRP---AVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALG-GPLVLSDEE 199
|
|
| Aldolase_II |
cd00398 |
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ... |
24-240 |
5.76e-28 |
|
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: 105.91 E-value: 5.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 24 EHPRALIPELCRLFYQLGWVTGTGGGISLKRGEQIY--IAPSGVQKERIQPEDMFVCDLEERDIscppawKKLKKSQCTP 101
Cdd:cd00398 1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYflITPSGVDYEEMTASDLVVVDAQGKVV------EGKKPSSETP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 102 LFMNAYILR-GAQAVIHTHSKAAVMATLLypgkefritHQEMIKGIrkGTSGTNYRYDEIlvvPIIENTPEEKDLKDRMA 180
Cdd:cd00398 75 LHLALYRARpDIGCIVHTHSTHATAVSQL---------KEGLIPAG--HTACAVYFTGDI---PCTPYMTPETGEDEIGT 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 181 WAMEEYPDSCAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAVQMKQCGLDPAALPVEE 240
Cdd:cd00398 141 QRALGFPNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLEL 200
|
|
| PRK09220 |
PRK09220 |
methylthioribulose 1-phosphate dehydratase; |
28-228 |
3.62e-21 |
|
methylthioribulose 1-phosphate dehydratase;
Pssm-ID: 236415 [Multi-domain] Cd Length: 204 Bit Score: 87.69 E-value: 3.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 28 ALIPELCRLFYQLGWVTGTGGGISLKRGEQ-IYIAPSGVQKERIQPEDMFVCDLEERdiSCPPAwkkLKKSQCTPLFMNA 106
Cdd:PRK09220 8 QQLIAAGRWIGARGWVPATSGNMSVRLDEQhCAITVSGKDKGSLTAEDFLQVDIAGN--AVPSG---RKPSAETLLHTQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 107 YILR-GAQAVIHTHSKAAVMATLLYPGKEFRITHQEMIKGIRKGTSgtnyrYDEILVVPIIENTPEEKDLKDRMAWAMEE 185
Cdd:PRK09220 83 YRLFpEIGAVLHTHSVNATVLSRVEKSDALVLEGYELQKAFAGQTT-----HETAVVVPIFDNDQDIARLAARVAPYLDA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1951406446 186 YPDSCAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAVQMKQ 228
Cdd:PRK09220 158 QPLRYGYLIRGHGLYCWGRDMAEARRHLEGLEFLFECELERRL 200
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| salvage_mtnB |
TIGR03328 |
methylthioribulose-1-phosphate dehydratase; Members of this family are the ... |
30-228 |
3.81e-92 |
|
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: 269.14 E-value: 3.81e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 30 IPELCRLFYQLGWVTGTGGGISLKRGEQ-IYIAPSGVQKERIQPEDMFVCDLEERDIScppawKKLKKSQCTPLFMNAYI 108
Cdd:TIGR03328 1 LIEAGRDLYKRGWVPGTGGNLSARLDEDeILITPSGVDKGRLTPEDFLVVDLQGKPVS-----GGLKPSAETLLHTQLYR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 109 LRGAQAVIHTHSKAAVMATLLYPG-KEFRITHQEMIKGIRKGTSgtnyrYDEILVVPIIENTPEEKDLKDRMAWAMEEYP 187
Cdd:TIGR03328 76 LTGAGAVLHTHSVEATVLSRLYPSnGGFELEGYEMLKGLPGITT-----HEDTLVVPIIENTQDIARLADSVAPALNAYP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1951406446 188 DSCAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAVQMKQ 228
Cdd:TIGR03328 151 DVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLK 191
|
|
| Aldolase_II |
pfam00596 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
28-224 |
6.47e-51 |
|
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: 163.87 E-value: 6.47e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 28 ALIPELCRLFYQLGWVTGTGGGISLKR-GEQIYIAPSGVQKERIQPEDMFVCDLEERDISCPPawkklKKSQCTPLFMNA 106
Cdd:pfam00596 1 EELAAAGRLLARRGLVEGTGGNISVRLpGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGL-----KPSSETPLHLAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 107 YILR-GAQAVIHTHSKAAVMATLLYPGkeFRITHQEMIKgirkgtsgtnYRYDEIlvvPIIEN-TPEEKDLKDRMAWAME 184
Cdd:pfam00596 76 YRARpDAGAVVHTHSPYATALSLAKEG--LPPITQEAAD----------FLGGDI---PIIPYyTPGTEELGERIAEALG 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1951406446 185 EypDSCAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAV 224
Cdd:pfam00596 141 G--DRKAVLLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
|
|
| Aldolase_II |
smart01007 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
30-224 |
5.01e-49 |
|
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: 159.34 E-value: 5.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 30 IPELCRLFYQLGWVTGTGGGISLKRGEQ--IYIAPSGVQKERIQPEDMFVCDLEERDIscpPAWKKLKKSQCTPLFMNAY 107
Cdd:smart01007 1 LAAACRLLARRGLVEGTGGNISARVGEEdlFLITPSGVDFGELTASDLVVVDLDGNVV---EGGGGPKPSSETPLHLAIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 108 ILR-GAQAVIHTHSKAAVMATLLypGKEFRITHQEMIKGIRKGTSG-TNYRydeilvVPIIENTPEEKDLKDRMAWAMEE 185
Cdd:smart01007 78 RARpDVGAVVHTHSPYATALAAL--GKPLPLLPTEQAAAFLGGEIPyAPYA------GPGTELAEEGAELAEALAEALPD 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 1951406446 186 YPdscAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAV 224
Cdd:smart01007 150 RP---AVLLRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
|
|
| AraD |
COG0235 |
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ... |
24-240 |
2.30e-34 |
|
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: 122.25 E-value: 2.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 24 EHPRALIPELCRLFYQLGWVTGTGGGISLK-RGEQIYIAPSGVQKERIQPEDMFVCDLEERDIscppaWKKLKKSQCTPL 102
Cdd:COG0235 4 EELREELAAAGRRLARRGLVDGTAGNISVRlDDDRFLITPSGVDFGELTPEDLVVVDLDGNVV-----EGDLKPSSETPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 103 FMNAYILR-GAQAVIHTHSKAAVMATLLypGKEFRITHQEMIKgirkgtsgtnYRYDEILVVPiiENTPEEKDLKDRMAW 181
Cdd:COG0235 79 HLAIYRARpDVGAVVHTHSPYATALSAL--GEPLPPLEQTEAA----------AFLGDVPVVP--YAGPGTEELAEAIAE 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1951406446 182 AMEEYPdscAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAVQMKQCGlDPAALPVEE 240
Cdd:COG0235 145 ALGDRP---AVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALG-GPLVLSDEE 199
|
|
| Aldolase_II |
cd00398 |
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ... |
24-240 |
5.76e-28 |
|
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: 105.91 E-value: 5.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 24 EHPRALIPELCRLFYQLGWVTGTGGGISLKRGEQIY--IAPSGVQKERIQPEDMFVCDLEERDIscppawKKLKKSQCTP 101
Cdd:cd00398 1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYflITPSGVDYEEMTASDLVVVDAQGKVV------EGKKPSSETP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 102 LFMNAYILR-GAQAVIHTHSKAAVMATLLypgkefritHQEMIKGIrkGTSGTNYRYDEIlvvPIIENTPEEKDLKDRMA 180
Cdd:cd00398 75 LHLALYRARpDIGCIVHTHSTHATAVSQL---------KEGLIPAG--HTACAVYFTGDI---PCTPYMTPETGEDEIGT 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 181 WAMEEYPDSCAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAVQMKQCGLDPAALPVEE 240
Cdd:cd00398 141 QRALGFPNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLEL 200
|
|
| PRK09220 |
PRK09220 |
methylthioribulose 1-phosphate dehydratase; |
28-228 |
3.62e-21 |
|
methylthioribulose 1-phosphate dehydratase;
Pssm-ID: 236415 [Multi-domain] Cd Length: 204 Bit Score: 87.69 E-value: 3.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 28 ALIPELCRLFYQLGWVTGTGGGISLKRGEQ-IYIAPSGVQKERIQPEDMFVCDLEERdiSCPPAwkkLKKSQCTPLFMNA 106
Cdd:PRK09220 8 QQLIAAGRWIGARGWVPATSGNMSVRLDEQhCAITVSGKDKGSLTAEDFLQVDIAGN--AVPSG---RKPSAETLLHTQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 107 YILR-GAQAVIHTHSKAAVMATLLYPGKEFRITHQEMIKGIRKGTSgtnyrYDEILVVPIIENTPEEKDLKDRMAWAMEE 185
Cdd:PRK09220 83 YRLFpEIGAVLHTHSVNATVLSRVEKSDALVLEGYELQKAFAGQTT-----HETAVVVPIFDNDQDIARLAARVAPYLDA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1951406446 186 YPDSCAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAVQMKQ 228
Cdd:PRK09220 158 QPLRYGYLIRGHGLYCWGRDMAEARRHLEGLEFLFECELERRL 200
|
|
| mtnB |
PRK06754 |
methylthioribulose 1-phosphate dehydratase; |
32-230 |
1.45e-19 |
|
methylthioribulose 1-phosphate dehydratase;
Pssm-ID: 180679 [Multi-domain] Cd Length: 208 Bit Score: 83.56 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 32 ELCRLFYQLGWVTGTGGGISLKRGE---QIYIAPSGVQKERIQPEDMFVCDLEERdiscpPAWK-KLKKSQCTPLFMNAY 107
Cdd:PRK06754 13 EIKKELAARDWFPATSGNLSIKVSDdplTFLVTASGKDKRKTTPEDFLLVDHDGK-----PVEEtELKPSAETLLHTHIY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 108 ILRGAQAVIHTHSKAAVMATLLYPG-KEFRITHQEMIK--GIrkgtsgtnYRYDEILVVPIIENTPEEKDLKDRMAWAME 184
Cdd:PRK06754 88 NNTNAGCVLHVHTVDNNVISELYGDdGAVTFQGQEIIKalGI--------WEENAEIHIPIIENHADIPTLAEEFAKHIQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1951406446 185 eyPDSCAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAVQMKQCG 230
Cdd:PRK06754 160 --GDSGAVLIRNHGITVWGRDAFEAKKHLEAYEFLFSYHIKLLSIQ 203
|
|
| PRK06557 |
PRK06557 |
L-ribulose-5-phosphate 4-epimerase; Validated |
32-240 |
3.63e-08 |
|
L-ribulose-5-phosphate 4-epimerase; Validated
Pssm-ID: 235829 [Multi-domain] Cd Length: 221 Bit Score: 52.32 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 32 ELCRLFYQL---GWVTGTGGGISLKRGEQ--IYIAPSGVQKERIQPEDMFVCDLEERDIScppawKKLKKSQCTPlfMNA 106
Cdd:PRK06557 14 EVCKLHLELpkyGLVVWTSGNVSARDPGTdlVVIKPSGVSYDDLTPEDMVVVDLDGNVVE-----GDLKPSSDTA--SHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 107 YILR---GAQAVIHTHSK-AAVMATLLYP------------GKEFRITHQEMIKG--IRKGtsgtnyrydeilVVPIIEN 168
Cdd:PRK06557 87 YVYRhmpDVGGVVHTHSTyATAWAARGEPipcvltamadefGGPIPVGPFALIGDeaIGKG------------IVETLKG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1951406446 169 tpeekdlkdrmawameeyPDSCAVLVRRHGVYVWGESWE---KAKTMCEcydylfDIAVQM---KQCGlDPAALPVEE 240
Cdd:PRK06557 155 ------------------GRSPAVLMQNHGVFTIGKDAEdavKAAVMVE------EVARTVhiaRQLG-EPIPIPQEE 207
|
|
| PRK08130 |
PRK08130 |
putative aldolase; Validated |
32-209 |
8.26e-08 |
|
putative aldolase; Validated
Pssm-ID: 181241 [Multi-domain] Cd Length: 213 Bit Score: 51.03 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 32 ELCRL---FYQLGWVTGTGGGISLKRGEQ-IYIAPSGVQKERIQPEDMFVCDLEERDISCPPAWKKLkksqctPLFMNAY 107
Cdd:PRK08130 9 EIVRLgrsLFQRGYTVGSAGNISARLDDGgWLVTPTGSCLGRLDPARLSKVDADGNWLSGDKPSKEV------PLHRAIY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 108 ILRG-AQAVIHTHSKAAVMATLLyPGkefrITHQEMIKGIrkgtsgTNY---RYDEILVVPIIEntPEEKDLKDRMAwam 183
Cdd:PRK08130 83 RNNPeCGAVVHLHSTHLTALSCL-GG----LDPTNVLPPF------TPYyvmRVGHVPLIPYYR--PGDPAIAEALA--- 146
|
170 180
....*....|....*....|....*.
gi 1951406446 184 EEYPDSCAVLVRRHGVYVWGESWEKA 209
Cdd:PRK08130 147 GLAARYRAVLLANHGPVVWGSSLEAA 172
|
|
| araD |
PRK08193 |
L-ribulose-5-phosphate 4-epimerase AraD; |
38-209 |
2.00e-07 |
|
L-ribulose-5-phosphate 4-epimerase AraD;
Pssm-ID: 236181 Cd Length: 231 Bit Score: 50.22 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 38 YQLGWVTGTGG---GISLKRGeQIYIAPSGVQKERIQPEDMFVCDLEERDIscppaWKKLKKSQCTP---LFMNAYilRG 111
Cdd:PRK08193 17 PKHGLVTFTWGnvsAIDRERG-LFVIKPSGVDYDKMTAEDMVVVDLEGNVV-----EGKLKPSSDTPthlVLYKAF--PE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 112 AQAVIHTHSKAAV-----------MATllypgkefriTH---------------QEMIKGirkgtsgtNYRYDEILVvpI 165
Cdd:PRK08193 89 IGGIVHTHSRHATawaqagrdipaLGT----------THadyfygdipctrkmtDEEING--------EYEWETGKV--I 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1951406446 166 IEnTPEEKDLkdrmawameEYPDSCAVLVRRHGVYVWGESWEKA 209
Cdd:PRK08193 149 VE-TFEKRGI---------DPAAVPGVLVHSHGPFTWGKDAEDA 182
|
|
| PRK06833 |
PRK06833 |
L-fuculose-phosphate aldolase; |
45-240 |
7.74e-07 |
|
L-fuculose-phosphate aldolase;
Pssm-ID: 180717 [Multi-domain] Cd Length: 214 Bit Score: 48.21 E-value: 7.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 45 GTGGGISLKRGEQIYIA--PSGVQKERIQPEDMFVCDLEERDIScppawKKLKKSQCTPLFMNAYILR-GAQAVIHTHSK 121
Cdd:PRK06833 25 GTGGNISIFNREQGLMAitPSGIDYFEIKPEDIVIMDLDGKVVE-----GERKPSSELDMHLIFYRNReDINAIVHTHSP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 122 -AAVMATLlypGKEFRITHQeMIkgirkGTSGTNYRYDEIlvvpiieNTPEEKDLKDRMAWAMEeypDSCAVLVRRHGVY 200
Cdd:PRK06833 100 yATTLACL---GWELPAVHY-LI-----AVAGPNVRCAEY-------ATFGTKELAENAFEAME---DRRAVLLANHGLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1951406446 201 VWGESWEKAKTMCECYDYLFDIAVQMKQCGlDPAALPVEE 240
Cdd:PRK06833 161 AGANNLKNAFNIAEEIEFCAEIYYQTKSIG-EPKLLPEDE 199
|
|
| PRK08660 |
PRK08660 |
aldolase; |
35-218 |
5.47e-06 |
|
aldolase;
Pssm-ID: 181527 [Multi-domain] Cd Length: 181 Bit Score: 45.33 E-value: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 35 RLFYQlGWVTGTGGGISLKRGEQIYIAPSGVQKERIQPEDMFVCDLEERDISCPPAwkklkkSQCTPLFMNAYILRGAQA 114
Cdd:PRK08660 11 KLFAH-GLVSSHFGNISVRTGDGLLITRTGSMLDEITEGDVIEVGIDDDGSVDPLA------SSETPVHRAIYRRTSAKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 115 VIHTHSKAAVMATLLypgkefrithqemIKGIRKGTSGTNYRYDEIlvvPIIENTPEEKDLKDRMAWAMEEYPdscAVLV 194
Cdd:PRK08660 84 IVHAHPPYAVALSLL-------------EDEIVPLDSEGLYFLGTI---PVVGGDIGSGELAENVARALSEHK---GVVV 144
|
170 180
....*....|....*....|....
gi 1951406446 195 RRHGVYVWGeswekaKTMCECYDY 218
Cdd:PRK08660 145 RGHGTFAIG------KTLEEAYIY 162
|
|
| araD |
PRK13145 |
L-ribulose-5-phosphate 4-epimerase; Provisional |
41-209 |
7.24e-06 |
|
L-ribulose-5-phosphate 4-epimerase; Provisional
Pssm-ID: 183870 [Multi-domain] Cd Length: 234 Bit Score: 45.59 E-value: 7.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 41 GWVTGTGGGISL--KRGEQIYIAPSGVQKERIQPEDMFVCDLEERDIScppawKKLKKSQCTPLFMNAYILRG-AQAVIH 117
Cdd:PRK13145 21 GLVKFTWGNVSEvcRELGRIVIKPSGVDYDELTPENMVVTDLDGNVVE-----GDLNPSSDLPTHVELYKAWPeVGGIVH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 118 THSKAAVmaTLLYPGKE---FRITHQEMIKG----IRKGTSG-TNYRYDEILVVPIIENTpEEKDLkDRMAWAmeeypds 189
Cdd:PRK13145 96 THSTEAV--GWAQAGRDipfYGTTHADYFYGpipcARSLTKDeVNGAYEKETGSVIIEEF-EKRGL-DPMAVP------- 164
|
170 180
....*....|....*....|
gi 1951406446 190 cAVLVRRHGVYVWGESWEKA 209
Cdd:PRK13145 165 -GIVVRNHGPFTWGKNPEQA 183
|
|
| PRK08333 |
PRK08333 |
aldolase; |
35-209 |
1.56e-05 |
|
aldolase;
Pssm-ID: 181393 [Multi-domain] Cd Length: 184 Bit Score: 44.04 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 35 RLFYQLGWVTGTGGGISLKRGEQIYIAPSGVQKERIQPEDMFVCDLEERDIScppawkKLKKSQCTPLFMNAYILR-GAQ 113
Cdd:PRK08333 13 KLAHERGLTAAFGGNLSIRVGNLVFIKATGSVMDELTREQVAVIDLNGNQLS------SVRPSSEYRLHLAVYRNRpDVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 114 AVIHTHSKAAVMATLLYPGKEFRITHQEMIKgIRKgtsgtnyrydeilvVPIIENTPE-EKDLKDRMAWAMEEYPdscAV 192
Cdd:PRK08333 87 AIAHLHPPYSIVASTLLEEELPIITPEAELY-LKK--------------IPILPFRPAgSVELAEQVAEAMKEYD---AV 148
|
170
....*....|....*..
gi 1951406446 193 LVRRHGVYVWGESWEKA 209
Cdd:PRK08333 149 IMERHGIVTVGRSLREA 165
|
|
| PRK06755 |
PRK06755 |
hypothetical protein; Validated |
42-226 |
2.60e-05 |
|
hypothetical protein; Validated
Pssm-ID: 102532 Cd Length: 209 Bit Score: 43.87 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 42 WVTGTGGGISL---KRGEQIYIAPSGVQKERIQPEDMFVCDleerdISCPPAWKKLKKSQCTPlFMNAYILR--GAQAVI 116
Cdd:PRK06755 23 WFYGTKISLSLctsKEPLTFLVNVEGRDKGLFSEEDFIVVN-----CMCEPVFENEEKPAAES-FMHADIYKksSAECIL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 117 HTHSKAAVMATLLYpGKEFRITHQEmiKGIRK--GTSGTnyrydEILVVPIIENTPEEKDLKDRMAWAMEEypDSCAVLV 194
Cdd:PRK06755 97 QVQTVDSHLISELY-GEEGEVTFDK--RSVERvfGKEGI-----TEMTIPIVEDEKKFADLLENNVPNFIE--GGGVVLV 166
|
170 180 190
....*....|....*....|....*....|..
gi 1951406446 195 RRHGVYVWGESWEKAKTMCECYDYLFDIAVQM 226
Cdd:PRK06755 167 HNYGMIVWGKTPEEAKKWLEGIEYLMNYHVKL 198
|
|
| sgaE |
PRK12348 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
41-123 |
3.10e-04 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 183460 Cd Length: 228 Bit Score: 40.94 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 41 GWVTGTGGGISLKRGEQ--IYIAPSGVQKERIQPEDMFVCDLEERDIScppawKKLKKSQCTPLFMNAY----ILRGaqa 114
Cdd:PRK12348 19 GLVTFTWGNVSAIDRERglVVIKPSGVAYETMKADDMVVVDMSGKVVE-----GEYRPSSDTATHLELYrrypSLGG--- 90
|
....*....
gi 1951406446 115 VIHTHSKAA 123
Cdd:PRK12348 91 IVHTHSTHA 99
|
|
|