|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09140 |
PRK09140 |
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed |
1-203 |
5.96e-126 |
|
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed
Pssm-ID: 181670 Cd Length: 206 Bit Score: 353.36 E-value: 5.96e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 1 MQWQTNLPLIAILRGITPEEALAHVGAAIDAGFDAVEIPLNSPQWEKSIPAVVEAYGDKALIGAGTVLNAERVDQLARMG 80
Cdd:PRK09140 4 MQPFTKLPLIAILRGITPDEALAHVGALIEAGFRAIEIPLNSPDPFDSIAALVKALGDRALIGAGTVLSPEQVDRLADAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 81 CRLIVTPNIQPEVIRRAVSYGMTVCPGCATATEAFAALDAGAQALKVFPSSAFGPDYIKALKAVLPPEVPVFAVGGVTPE 160
Cdd:PRK09140 84 GRLIVTPNTDPEVIRRAVALGMVVMPGVATPTEAFAALRAGAQALKLFPASQLGPAGIKALRAVLPPDVPVFAVGGVTPE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503993336 161 NLAQWIKAGCTGAGLGSDLYRAGQSVERTQRQAAAFVKAYREA 203
Cdd:PRK09140 164 NLAPYLAAGAAGFGLGSALYRPGQSAEEVAERARAFVAAYREA 206
|
|
| Eda |
COG0800 |
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ... |
8-203 |
4.10e-80 |
|
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; 2-keto-3-deoxy-6-phosphogluconate aldolase is part of the Pathway/BioSystem: Entner-Doudoroff pathway
Pssm-ID: 440563 Cd Length: 213 Bit Score: 237.67 E-value: 4.10e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 8 PLIAILRGITPEEALAHVGAAIDAGFDAVEIPLNSPQWEKSIPAVVEAYGDKALIGAGTVLNAERVDQLARMGCRLIVTP 87
Cdd:COG0800 13 PVVPVLRGDDPEDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEVGPDALVGAGTVLTPEQARAAIAAGARFIVSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 88 NIQPEVIRRAVSYGMTVCPGCATATEAFAALDAGAQALKVFPSSAFGPDYIKALKAVLpPEVPVFAVGGVTPENLAQWIK 167
Cdd:COG0800 93 GLDPEVIKAANRAGLPVLPGVATPTEIMAALEAGADAVKLFPAEALGPAYLKALKGPL-PDVPFMPTGGVSPDNAADYLA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503993336 168 AGCTGAGLGSDLYRAGQSVER----TQRQAAAFVKAYREA 203
Cdd:COG0800 172 AGAVAVGGGSWLVPKGAIAAGdwaaITERAREAVAAVRAA 211
|
|
| KDPG_aldolase |
cd00452 |
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ... |
5-182 |
3.04e-70 |
|
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases whose reaction mechanism involves Schiff base formation between a substrate carbonyl and lysine residue in the active site. 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase, is best known for its role in the Entner-Doudoroff pathway of bacteria, where it catalyzes the reversible cleavage of KDPG to pyruvate and glyceraldehyde-3-phosphate. 2-keto-4-hydroxyglutarate (KHG) aldolase, which has enzymatic specificity toward glyoxylate, forming KHG in the presence of pyruvate, and is capable of regulating glyoxylate levels in the glyoxylate bypass, an alternate pathway when bacteria are grown on acetate carbon sources.
Pssm-ID: 188632 Cd Length: 190 Bit Score: 211.99 E-value: 3.04e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 5 TNLPLIAILRGITPEEALAHVGAAIDAGFDAVEIPLNSPQWEKSIPAVVEAYGDkALIGAGTVLNAERVDQLARMGCRLI 84
Cdd:cd00452 2 KAQPLVAVLRGDDAEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFPE-ALIGAGTVLTPEQADAAIAAGAQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 85 VTPNIQPEVIRRAVSYGMTVCPGCATATEAFAALDAGAQALKVFPSSAFGPDYIKALKAVLPPeVPVFAVGGVTPENLAQ 164
Cdd:cd00452 81 VSPGLDPEVVKAANRAGIPLLPGVATPTEIMQALELGADIVKLFPAEAVGPAYIKALKGPFPQ-VRFMPTGGVSLDNAAE 159
|
170
....*....|....*...
gi 503993336 165 WIKAGCTGAGLGSDLYRA 182
Cdd:cd00452 160 WLAAGVVAVGGGSLLPKD 177
|
|
| eda |
TIGR01182 |
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ... |
4-179 |
1.03e-29 |
|
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an enzyme of the Entner-Doudoroff pathway. This aldolase has another function, 4-hydroxy-2-oxoglutarate aldolase (EC 4.1.3.16) shown experimentally in Escherichia coli and Pseudomonas putida [Amino acid biosynthesis, Glutamate family, Energy metabolism, Entner-Doudoroff]
Pssm-ID: 273490 Cd Length: 204 Bit Score: 108.94 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 4 QTNLPLIAILRGITPEEALAHVGAAIDAGFDAVEIPLNSPQWEKSIPAVVEAYGDkALIGAGTVLNAERVDQLARMGCRL 83
Cdd:TIGR01182 5 LREAKIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEVPD-ALIGAGTVLNPEQLRQAVAAGAQF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 84 IVTPNIQPEVIRRAVSYGMTVCPGCATATEAFAALDAGAQALKVFPSSAFG-PDYIKALKAVLpPEVPVFAVGGVTPENL 162
Cdd:TIGR01182 84 IVSPGLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAEVSGgVKMLKALAGPF-PQVRFCPTGGINLANA 162
|
170
....*....|....*..
gi 503993336 163 AQWIKAGCTGAGLGSDL 179
Cdd:TIGR01182 163 RDYLALPNVACGGGSWL 179
|
|
| Aldolase |
pfam01081 |
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ... |
5-183 |
1.50e-23 |
|
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate aldolase (KHG-aldolase) Phospho-2-dehydro-3-deoxygluconate aldolase (KDPG-aldolase)
Pssm-ID: 395858 Cd Length: 196 Bit Score: 92.54 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 5 TNLPLIAILRGITPEEALAHVGAAIDAGFDAVEIPLNSPQWEKSIPAVVEAYGDkALIGAGTVLNAERVDQLARMGCRLI 84
Cdd:pfam01081 6 KEAKIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAIRLLRKNRPD-ALVGAGTVLNAQQLAEAAEAGAQFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 85 VTPNIQPEVIRRAVSYGMTVCPGCATATEAFAALDAGAQALKVFPSSAFGPdyIKALKAVLPP--EVPVFAVGGVTPENL 162
Cdd:pfam01081 85 VSPGLTADLLKHAVDVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPAEASGG--VPAIKALAGPfpQVRFCPTGGIHPANV 162
|
170 180
....*....|....*....|.
gi 503993336 163 AQWIKAGCTGAGLGSDLYRAG 183
Cdd:pfam01081 163 RDYLALPNILCVGGSWLVPAS 183
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09140 |
PRK09140 |
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed |
1-203 |
5.96e-126 |
|
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed
Pssm-ID: 181670 Cd Length: 206 Bit Score: 353.36 E-value: 5.96e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 1 MQWQTNLPLIAILRGITPEEALAHVGAAIDAGFDAVEIPLNSPQWEKSIPAVVEAYGDKALIGAGTVLNAERVDQLARMG 80
Cdd:PRK09140 4 MQPFTKLPLIAILRGITPDEALAHVGALIEAGFRAIEIPLNSPDPFDSIAALVKALGDRALIGAGTVLSPEQVDRLADAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 81 CRLIVTPNIQPEVIRRAVSYGMTVCPGCATATEAFAALDAGAQALKVFPSSAFGPDYIKALKAVLPPEVPVFAVGGVTPE 160
Cdd:PRK09140 84 GRLIVTPNTDPEVIRRAVALGMVVMPGVATPTEAFAALRAGAQALKLFPASQLGPAGIKALRAVLPPDVPVFAVGGVTPE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503993336 161 NLAQWIKAGCTGAGLGSDLYRAGQSVERTQRQAAAFVKAYREA 203
Cdd:PRK09140 164 NLAPYLAAGAAGFGLGSALYRPGQSAEEVAERARAFVAAYREA 206
|
|
| Eda |
COG0800 |
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ... |
8-203 |
4.10e-80 |
|
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; 2-keto-3-deoxy-6-phosphogluconate aldolase is part of the Pathway/BioSystem: Entner-Doudoroff pathway
Pssm-ID: 440563 Cd Length: 213 Bit Score: 237.67 E-value: 4.10e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 8 PLIAILRGITPEEALAHVGAAIDAGFDAVEIPLNSPQWEKSIPAVVEAYGDKALIGAGTVLNAERVDQLARMGCRLIVTP 87
Cdd:COG0800 13 PVVPVLRGDDPEDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEVGPDALVGAGTVLTPEQARAAIAAGARFIVSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 88 NIQPEVIRRAVSYGMTVCPGCATATEAFAALDAGAQALKVFPSSAFGPDYIKALKAVLpPEVPVFAVGGVTPENLAQWIK 167
Cdd:COG0800 93 GLDPEVIKAANRAGLPVLPGVATPTEIMAALEAGADAVKLFPAEALGPAYLKALKGPL-PDVPFMPTGGVSPDNAADYLA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503993336 168 AGCTGAGLGSDLYRAGQSVER----TQRQAAAFVKAYREA 203
Cdd:COG0800 172 AGAVAVGGGSWLVPKGAIAAGdwaaITERAREAVAAVRAA 211
|
|
| KDPG_aldolase |
cd00452 |
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ... |
5-182 |
3.04e-70 |
|
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases whose reaction mechanism involves Schiff base formation between a substrate carbonyl and lysine residue in the active site. 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase, is best known for its role in the Entner-Doudoroff pathway of bacteria, where it catalyzes the reversible cleavage of KDPG to pyruvate and glyceraldehyde-3-phosphate. 2-keto-4-hydroxyglutarate (KHG) aldolase, which has enzymatic specificity toward glyoxylate, forming KHG in the presence of pyruvate, and is capable of regulating glyoxylate levels in the glyoxylate bypass, an alternate pathway when bacteria are grown on acetate carbon sources.
Pssm-ID: 188632 Cd Length: 190 Bit Score: 211.99 E-value: 3.04e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 5 TNLPLIAILRGITPEEALAHVGAAIDAGFDAVEIPLNSPQWEKSIPAVVEAYGDkALIGAGTVLNAERVDQLARMGCRLI 84
Cdd:cd00452 2 KAQPLVAVLRGDDAEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFPE-ALIGAGTVLTPEQADAAIAAGAQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 85 VTPNIQPEVIRRAVSYGMTVCPGCATATEAFAALDAGAQALKVFPSSAFGPDYIKALKAVLPPeVPVFAVGGVTPENLAQ 164
Cdd:cd00452 81 VSPGLDPEVVKAANRAGIPLLPGVATPTEIMQALELGADIVKLFPAEAVGPAYIKALKGPFPQ-VRFMPTGGVSLDNAAE 159
|
170
....*....|....*...
gi 503993336 165 WIKAGCTGAGLGSDLYRA 182
Cdd:cd00452 160 WLAAGVVAVGGGSLLPKD 177
|
|
| PRK06552 |
PRK06552 |
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional |
9-203 |
9.31e-45 |
|
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
Pssm-ID: 180618 Cd Length: 213 Bit Score: 147.83 E-value: 9.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 9 LIAILRGITPEEALAHVGAAIDAGFDAVEIPLNSPQWEKSIPAVVEAYGDKA--LIGAGTVLNAERvdqlARM----GCR 82
Cdd:PRK06552 15 VVAVVRGESKEEALKISLAVIKGGIKAIEVTYTNPFASEVIKELVELYKDDPevLIGAGTVLDAVT----ARLailaGAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 83 LIVTPNIQPEVIRRAVSYGMTVCPGCATATEAFAALDAGAQALKVFPSSAFGPDYIKALKAVLpPEVPVFAVGGVTPENL 162
Cdd:PRK06552 91 FIVSPSFNRETAKICNLYQIPYLPGCMTVTEIVTALEAGSEIVKLFPGSTLGPSFIKAIKGPL-PQVNVMVTGGVNLDNV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503993336 163 AQWIKAGCTGAGLGSDLYRAGQS--VERTQRQAAAFVKAYREA 203
Cdd:PRK06552 170 KDWFAAGADAVGIGGELNKLASQgdFDLITEKAKKYMSSLRKA 212
|
|
| PRK07455 |
PRK07455 |
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase; |
10-180 |
7.71e-31 |
|
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
Pssm-ID: 180985 Cd Length: 187 Bit Score: 111.29 E-value: 7.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 10 IAILRGITPEEALAHVGAAIDAGFDAVEIPLNSPQWEKSIPAVVEAYGDkALIGAGTVLNAERVDQLARMGCRLIVTPNI 89
Cdd:PRK07455 15 IAVIRAPDLELGLQMAEAVAAGGMRLIEITWNSDQPAELISQLREKLPE-CIIGTGTILTLEDLEEAIAAGAQFCFTPHV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 90 QPEVIRRAVSYGMTVCPGCATATEAFAALDAGAQALKVFPSSAF-GPDYIKALKAVLpPEVPVFAVGGVTPENLAQWIKA 168
Cdd:PRK07455 94 DPELIEAAVAQDIPIIPGALTPTEIVTAWQAGASCVKVFPVQAVgGADYIKSLQGPL-GHIPLIPTGGVTLENAQAFIQA 172
|
170
....*....|..
gi 503993336 169 GCTGAGLGSDLY 180
Cdd:PRK07455 173 GAIAVGLSGQLF 184
|
|
| eda |
TIGR01182 |
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ... |
4-179 |
1.03e-29 |
|
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an enzyme of the Entner-Doudoroff pathway. This aldolase has another function, 4-hydroxy-2-oxoglutarate aldolase (EC 4.1.3.16) shown experimentally in Escherichia coli and Pseudomonas putida [Amino acid biosynthesis, Glutamate family, Energy metabolism, Entner-Doudoroff]
Pssm-ID: 273490 Cd Length: 204 Bit Score: 108.94 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 4 QTNLPLIAILRGITPEEALAHVGAAIDAGFDAVEIPLNSPQWEKSIPAVVEAYGDkALIGAGTVLNAERVDQLARMGCRL 83
Cdd:TIGR01182 5 LREAKIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEVPD-ALIGAGTVLNPEQLRQAVAAGAQF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 84 IVTPNIQPEVIRRAVSYGMTVCPGCATATEAFAALDAGAQALKVFPSSAFG-PDYIKALKAVLpPEVPVFAVGGVTPENL 162
Cdd:TIGR01182 84 IVSPGLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAEVSGgVKMLKALAGPF-PQVRFCPTGGINLANA 162
|
170
....*....|....*..
gi 503993336 163 AQWIKAGCTGAGLGSDL 179
Cdd:TIGR01182 163 RDYLALPNVACGGGSWL 179
|
|
| PRK07114 |
PRK07114 |
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase; |
62-203 |
7.39e-24 |
|
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
Pssm-ID: 235939 Cd Length: 222 Bit Score: 94.32 E-value: 7.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 62 IGAGTVLNAERVDQLARMGCRLIVTPNIQPEVI----RRAVSYgmtvCPGCATATEAFAALDAGAQALKVFPSSAFGPDY 137
Cdd:PRK07114 73 LGVGSIVDAATAALYIQLGANFIVTPLFNPDIAkvcnRRKVPY----SPGCGSLSEIGYAEELGCEIVKLFPGSVYGPGF 148
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503993336 138 IKALKAVLpPEVPVFAVGGVTP--ENLAQWIKAGCTGAGLGSDL-------YRAGQSVERTQRQAAAFVKAYREA 203
Cdd:PRK07114 149 VKAIKGPM-PWTKIMPTGGVEPteENLKKWFGAGVTCVGMGSKLipkealaAKDYAGIEQKVREALAIIKEVRKK 222
|
|
| Aldolase |
pfam01081 |
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ... |
5-183 |
1.50e-23 |
|
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate aldolase (KHG-aldolase) Phospho-2-dehydro-3-deoxygluconate aldolase (KDPG-aldolase)
Pssm-ID: 395858 Cd Length: 196 Bit Score: 92.54 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 5 TNLPLIAILRGITPEEALAHVGAAIDAGFDAVEIPLNSPQWEKSIPAVVEAYGDkALIGAGTVLNAERVDQLARMGCRLI 84
Cdd:pfam01081 6 KEAKIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAIRLLRKNRPD-ALVGAGTVLNAQQLAEAAEAGAQFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 85 VTPNIQPEVIRRAVSYGMTVCPGCATATEAFAALDAGAQALKVFPSSAFGPdyIKALKAVLPP--EVPVFAVGGVTPENL 162
Cdd:pfam01081 85 VSPGLTADLLKHAVDVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPAEASGG--VPAIKALAGPfpQVRFCPTGGIHPANV 162
|
170 180
....*....|....*....|.
gi 503993336 163 AQWIKAGCTGAGLGSDLYRAG 183
Cdd:pfam01081 163 RDYLALPNILCVGGSWLVPAS 183
|
|
| PRK05718 |
PRK05718 |
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional |
7-163 |
7.42e-22 |
|
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
Pssm-ID: 235577 Cd Length: 212 Bit Score: 88.76 E-value: 7.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 7 LPLIAILRgitPEEALAHVGAAIDAGFDAVEIPLNSPQWEKSIPAVVEAYGDkALIGAGTVLNAERVDQLARMGCRLIVT 86
Cdd:PRK05718 18 VPVIVINK---LEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIAKEVPE-ALIGAGTVLNPEQLAQAIEAGAQFIVS 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503993336 87 PNIQPEVIRRAVSYGMTVCPGCATATEAFAALDAGAQALKVFPSSAFGPdyIKALKAVLPP--EVPVFAVGGVTPENLA 163
Cdd:PRK05718 94 PGLTPPLLKAAQEGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEASGG--VKMLKALAGPfpDVRFCPTGGISPANYR 170
|
|
| PRK06015 |
PRK06015 |
2-dehydro-3-deoxy-phosphogluconate aldolase; |
8-166 |
3.09e-14 |
|
2-dehydro-3-deoxy-phosphogluconate aldolase;
Pssm-ID: 168348 Cd Length: 201 Bit Score: 68.30 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 8 PLIAILRGITPEEALAHVGAAIDAGFDAVEIPLNSPQWEKSIPAVVEAYgDKALIGAGTVLNAERVDQLARMGCRLIVTP 87
Cdd:PRK06015 5 PVIPVLLIDDVEHAVPLARALAAGGLPAIEITLRTPAALDAIRAVAAEV-EEAIVGAGTILNAKQFEDAAKAGSRFIVSP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 88 NIQPEVIRRAVSYGMTVCPGCATATEAFAALDAGAQALKVFPS-SAFGPDYIKALKAVLpPEVPVFAVGGVTPENLAQWI 166
Cdd:PRK06015 84 GTTQELLAAANDSDVPLLPGAATPSEVMALREEGYTVLKFFPAeQAGGAAFLKALSSPL-AGTFFCPTGGISLKNARDYL 162
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
91-199 |
2.85e-08 |
|
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440121 [Multi-domain] Cd Length: 206 Bit Score: 51.72 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 91 PEVIRRAVSYGMTVCPGCATATEAFAALDAGAQAL---KVFPSS-------AFGPDYIKALKAVLPpeVPVFAVGGVTPE 160
Cdd:COG0352 90 VAEARALLGPDLIIGVSCHSLEEALRAEEAGADYVgfgPVFPTPtkpgappPLGLEGLAWWAELVE--IPVVAIGGITPE 167
|
90 100 110
....*....|....*....|....*....|....*....
gi 503993336 161 NLAQWIKAGCTGAGLGSDLYRAGQSVERTQRQAAAFVKA 199
Cdd:COG0352 168 NAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
91-191 |
5.11e-07 |
|
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.
Pssm-ID: 238317 [Multi-domain] Cd Length: 196 Bit Score: 47.90 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 91 PEVIRRAVSYGMTVCPGCATATEAFAALDAGAQAL---KVFPSS-------AFGPDYIKALKAVLppEVPVFAVGGVTPE 160
Cdd:cd00564 85 VAEARALLGPDLIIGVSTHSLEEALRAEELGADYVgfgPVFPTPtkpgagpPLGLELLREIAELV--EIPVVAIGGITPE 162
|
90 100 110
....*....|....*....|....*....|.
gi 503993336 161 NLAQWIKAGCTGAGLGSDLYRAGQSVERTQR 191
Cdd:cd00564 163 NAAEVLAAGADGVAVISAITGADDPAAAARE 193
|
|
| PRK07695 |
PRK07695 |
thiazole tautomerase TenI; |
112-205 |
3.66e-06 |
|
thiazole tautomerase TenI;
Pssm-ID: 181086 [Multi-domain] Cd Length: 201 Bit Score: 45.78 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 112 TEAFAALDAGAQAL---KVFPSS------AFGPDYIKALKAVLppEVPVFAVGGVTPENLAQWIKAGCTGAGLGSDLYRA 182
Cdd:PRK07695 106 EEAIQAEKNGADYVvygHVFPTDckkgvpARGLEELSDIARAL--SIPVIAIGGITPENTRDVLAAGVSGIAVMSGIFSS 183
|
90 100
....*....|....*....|...
gi 503993336 183 GQSVERTQRqaaafvkaYREAVQ 205
Cdd:PRK07695 184 ANPYSKAKR--------YAESIK 198
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
10-176 |
4.60e-06 |
|
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.
Pssm-ID: 188634 [Multi-domain] Cd Length: 201 Bit Score: 45.40 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 10 IAILRGI-TPEEALAHVGAAIDAGFDAVEIPLNspqwekSIPAVVEAYGDkALIGAGTVLNA-----------ERVDQLA 77
Cdd:cd00945 3 LTLLHPDaTLEDIAKLCDEAIEYGFAAVCVNPG------YVRLAADALAG-SDVPVIVVVGFptgltttevkvAEVEEAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 78 RMGCRLI-VTPNI-------QPEV------IRRAVSYGMTVCPGCATA---TEAF------AALDAGAQALKVFPSSAFG 134
Cdd:cd00945 76 DLGADEIdVVINIgslkegdWEEVleeiaaVVEAADGGLPLKVILETRglkTADEiakaarIAAEAGADFIKTSTGFGGG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503993336 135 ---PDYIKALKAVLPPEVPVFAVGGV-TPENLAQWIKAGCTGAGLG 176
Cdd:cd00945 156 gatVEDVKLMKEAVGGRVGVKAAGGIkTLEDALAAIEAGADGIGTS 201
|
|
| TMP-TENI |
pfam02581 |
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ... |
91-172 |
9.60e-06 |
|
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl)thiazole phosphate to yield thiamine phosphate. This Pfam family also includes the regulatory protein TENI, a protein from Bacillus subtilis that regulates the production of several extracellular enzymes by reducing alkaline protease production. While TenI shows high sequence similarity with thiamin phosphate synthase, the purified protein has no thiamin phosphate synthase activity. Instead, it is a thiazole tautomerase.
Pssm-ID: 426849 [Multi-domain] Cd Length: 180 Bit Score: 44.08 E-value: 9.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 91 PEVIRRAVSYGMTVCPGCATATEAFAALDAGAQAL---KVFPS------SAFGPDYIKALKAVLppEVPVFAVGGVTPEN 161
Cdd:pfam02581 85 VAEARELLGPDLIIGVSTHTLEEALEAEALGADYIgfgPIFPTptkpdaPPLGLEGLKAIAEAV--EIPVVAIGGITPEN 162
|
90
....*....|.
gi 503993336 162 LAQWIKAGCTG 172
Cdd:pfam02581 163 VPEVIEAGADG 173
|
|
| thiE |
TIGR00693 |
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ... |
90-191 |
1.13e-05 |
|
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate pyrophosphorylase, ThiE, of a number of bacteria, and N-terminal domains of bifunctional thiamine proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe, in which the C-terminal domain corresponds to the bacterial hydroxyethylthiazole kinase (EC 2.7.1.50), ThiM. This model includes ThiE from Bacillus subtilis but excludes its paralog, the regulatory protein TenI (SP:P25053), and neighbors of TenI. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
Pssm-ID: 273222 [Multi-domain] Cd Length: 196 Bit Score: 44.16 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 90 QPEVIRRAVSYGMTVCPGCATATEAFAALDAGAQAL---KVFPSS-------AFGPDYIKALKAVLPpEVPVFAVGGVTP 159
Cdd:TIGR00693 85 PASEARALLGPDKIIGVSTHNLEELAEAEAEGADYIgfgPIFPTPtkkdpapPAGVELLREIAATLI-DIPIVAIGGITL 163
|
90 100 110
....*....|....*....|....*....|..
gi 503993336 160 ENLAQWIKAGCTGAGLGSDLYRAGQSVERTQR 191
Cdd:TIGR00693 164 ENAAEVLAAGADGVAVVSAIMQAADPKAAAKR 195
|
|
| thiE |
PRK00043 |
thiamine phosphate synthase; |
108-201 |
5.89e-05 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 42.48 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 108 CATATEAFAALDAGAQAL---KVFPSS-------AFGPDYIKALKAVLPPeVPVFAVGGVTPENLAQWIKAGCTGAGLGS 177
Cdd:PRK00043 111 THTLEEAAAALAAGADYVgvgPIFPTPtkkdakaPQGLEGLREIRAAVGD-IPIVAIGGITPENAPEVLEAGADGVAVVS 189
|
90 100
....*....|....*....|....
gi 503993336 178 DLYRAgQSVERTQRQAAAFVKAYR 201
Cdd:PRK00043 190 AITGA-EDPEAAARALLAAFRAAR 212
|
|
| PRK02615 |
PRK02615 |
thiamine phosphate synthase; |
127-171 |
4.45e-04 |
|
thiamine phosphate synthase;
Pssm-ID: 235054 [Multi-domain] Cd Length: 347 Bit Score: 40.25 E-value: 4.45e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 503993336 127 VFPS------SAFGPDYIKALKAVLPpeVPVFAVGGVTPENLAQWIKAGCT 171
Cdd:PRK02615 269 VFPTptkpgkAPAGLEYLKYAAKEAP--IPWFAIGGIDKSNIPEVLQAGAK 317
|
|
| BtpA |
COG0434 |
Membrane biogenesis protein, BtpA/SgcQ family [Cell wall/membrane/envelope biogenesis]; |
135-203 |
3.63e-03 |
|
Membrane biogenesis protein, BtpA/SgcQ family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440203 Cd Length: 268 Bit Score: 37.07 E-value: 3.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503993336 135 PDYIKALKAVLPpEVPVFAVGGVTPENLAQWIKAgCTGAGLGSDLYRAGQ-----SVERtqrqAAAFVKAYREA 203
Cdd:COG0434 200 LEDLKRVKEAAP-DVPVLVGSGVTPENVAELLSV-ADGAIVGSSLKRDGKtwnpvDPER----VRRFMEAVRRL 267
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
4-177 |
9.64e-03 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 35.64 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 4 QTNLPLIAILRGITPEEALAH-VGAAIDAGFDAVEIPLNSPQ----WEKSIPAVVEAYGDKALIGAGTVLNAERVDQLAR 78
Cdd:cd04722 55 ETDLPLGVQLAINDAAAAVDIaAAAARAAGADGVEIHGAVGYlareDLELIRELREAVPDVKVVVKLSPTGELAAAAAEE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993336 79 MGcrlivtpniqpevirravsygmtvcpgcatATEAFAALDAGAQAlkvfPSSAFGPDYIKALKAVLPPEVPVFAVGGV- 157
Cdd:cd04722 135 AG------------------------------VDEVGLGNGGGGGG----GRDAVPIADLLLILAKRGSKVPVIAGGGIn 180
|
170 180
....*....|....*....|
gi 503993336 158 TPENLAQWIKAGCTGAGLGS 177
Cdd:cd04722 181 DPEDAAEALALGADGVIVGS 200
|
|
| |
