|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09140 |
PRK09140 |
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed |
1-203 |
2.68e-128 |
|
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed
Pssm-ID: 181670 Cd Length: 206 Bit Score: 359.53 E-value: 2.68e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 1 MQWQTNLPLIAILRGITPDEALAHVGAVIDAGFDAVEIPLNSPQWEKSIPQVVDAYGEQALIGAGTVLQPEQVDRLAAMG 80
Cdd:PRK09140 4 MQPFTKLPLIAILRGITPDEALAHVGALIEAGFRAIEIPLNSPDPFDSIAALVKALGDRALIGAGTVLSPEQVDRLADAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 81 CRLIVTPNIQPEVIRRAVGYGMTVCPGCATASEAFSALDAGAQALKIFPSSAFGPDYIKALKAVLPPEVPVFAVGGVTPE 160
Cdd:PRK09140 84 GRLIVTPNTDPEVIRRAVALGMVVMPGVATPTEAFAALRAGAQALKLFPASQLGPAGIKALRAVLPPDVPVFAVGGVTPE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490246922 161 NLAQWINAGCVGAGLGSDLYRAGQSVERTAQQAAAFVKAYREA 203
Cdd:PRK09140 164 NLAPYLAAGAAGFGLGSALYRPGQSAEEVAERARAFVAAYREA 206
|
|
| Eda |
COG0800 |
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ... |
8-205 |
3.21e-81 |
|
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: 240.76 E-value: 3.21e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 8 PLIAILRGITPDEALAHVGAVIDAGFDAVEIPLNSPQWEKSIPQVVDAYGEQALIGAGTVLQPEQVDRLAAMGCRLIVTP 87
Cdd:COG0800 13 PVVPVLRGDDPEDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEVGPDALVGAGTVLTPEQARAAIAAGARFIVSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 88 NIQPEVIRRAVGYGMTVCPGCATASEAFSALDAGAQALKIFPSSAFGPDYIKALKAVLpPEVPVFAVGGVTPENLAQWIN 167
Cdd:COG0800 93 GLDPEVIKAANRAGLPVLPGVATPTEIMAALEAGADAVKLFPAEALGPAYLKALKGPL-PDVPFMPTGGVSPDNAADYLA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490246922 168 AGCVGAGLGSDLYRAGQSVER----TAQQAAAFVKAYREAVK 205
Cdd:COG0800 172 AGAVAVGGGSWLVPKGAIAAGdwaaITERAREAVAAVRAARA 213
|
|
| KDPG_aldolase |
cd00452 |
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ... |
5-182 |
3.11e-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: 3.11e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 5 TNLPLIAILRGITPDEALAHVGAVIDAGFDAVEIPLNSPQWEKSIPQVVDAYGEqALIGAGTVLQPEQVDRLAAMGCRLI 84
Cdd:cd00452 2 KAQPLVAVLRGDDAEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFPE-ALIGAGTVLTPEQADAAIAAGAQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 85 VTPNIQPEVIRRAVGYGMTVCPGCATASEAFSALDAGAQALKIFPSSAFGPDYIKALKAVLPPeVPVFAVGGVTPENLAQ 164
Cdd:cd00452 81 VSPGLDPEVVKAANRAGIPLLPGVATPTEIMQALELGADIVKLFPAEAVGPAYIKALKGPFPQ-VRFMPTGGVSLDNAAE 159
|
170
....*....|....*...
gi 490246922 165 WINAGCVGAGLGSDLYRA 182
Cdd:cd00452 160 WLAAGVVAVGGGSLLPKD 177
|
|
| eda |
TIGR01182 |
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ... |
4-195 |
4.07e-30 |
|
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: 110.09 E-value: 4.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 4 QTNLPLIAILRGITPDEALAHVGAVIDAGFDAVEIPLNSPQWEKSIPQVVDAYgEQALIGAGTVLQPEQVDRLAAMGCRL 83
Cdd:TIGR01182 5 LREAKIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEV-PDALIGAGTVLNPEQLRQAVAAGAQF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 84 IVTPNIQPEVIRRAVGYGMTVCPGCATASEAFSALDAGAQALKIFPSSAFG-PDYIKALKAVLpPEVPVFAVGGVTPENL 162
Cdd:TIGR01182 84 IVSPGLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAEVSGgVKMLKALAGPF-PQVRFCPTGGINLANA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490246922 163 AQWINAGCVGAGLGS-----DLYRAG--QSVERTAQQAAA 195
Cdd:TIGR01182 163 RDYLALPNVACGGGSwlvpkDLIAAGdwDEITRLAREALE 202
|
|
| Aldolase |
pfam01081 |
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ... |
5-183 |
1.09e-24 |
|
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: 95.62 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 5 TNLPLIAILRGITPDEALAHVGAVIDAGFDAVEIPLNSPQWEKSIpQVVDAYGEQALIGAGTVLQPEQVDRLAAMGCRLI 84
Cdd:pfam01081 6 KEAKIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAI-RLLRKNRPDALVGAGTVLNAQQLAEAAEAGAQFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 85 VTPNIQPEVIRRAVGYGMTVCPGCATASEAFSALDAGAQALKIFPSSAFGPdyIKALKAVLPP--EVPVFAVGGVTPENL 162
Cdd:pfam01081 85 VSPGLTADLLKHAVDVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPAEASGG--VPAIKALAGPfpQVRFCPTGGIHPANV 162
|
170 180
....*....|....*....|.
gi 490246922 163 AQWINAGCVGAGLGSDLYRAG 183
Cdd:pfam01081 163 RDYLALPNILCVGGSWLVPAS 183
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09140 |
PRK09140 |
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed |
1-203 |
2.68e-128 |
|
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed
Pssm-ID: 181670 Cd Length: 206 Bit Score: 359.53 E-value: 2.68e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 1 MQWQTNLPLIAILRGITPDEALAHVGAVIDAGFDAVEIPLNSPQWEKSIPQVVDAYGEQALIGAGTVLQPEQVDRLAAMG 80
Cdd:PRK09140 4 MQPFTKLPLIAILRGITPDEALAHVGALIEAGFRAIEIPLNSPDPFDSIAALVKALGDRALIGAGTVLSPEQVDRLADAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 81 CRLIVTPNIQPEVIRRAVGYGMTVCPGCATASEAFSALDAGAQALKIFPSSAFGPDYIKALKAVLPPEVPVFAVGGVTPE 160
Cdd:PRK09140 84 GRLIVTPNTDPEVIRRAVALGMVVMPGVATPTEAFAALRAGAQALKLFPASQLGPAGIKALRAVLPPDVPVFAVGGVTPE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490246922 161 NLAQWINAGCVGAGLGSDLYRAGQSVERTAQQAAAFVKAYREA 203
Cdd:PRK09140 164 NLAPYLAAGAAGFGLGSALYRPGQSAEEVAERARAFVAAYREA 206
|
|
| Eda |
COG0800 |
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ... |
8-205 |
3.21e-81 |
|
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: 240.76 E-value: 3.21e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 8 PLIAILRGITPDEALAHVGAVIDAGFDAVEIPLNSPQWEKSIPQVVDAYGEQALIGAGTVLQPEQVDRLAAMGCRLIVTP 87
Cdd:COG0800 13 PVVPVLRGDDPEDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEVGPDALVGAGTVLTPEQARAAIAAGARFIVSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 88 NIQPEVIRRAVGYGMTVCPGCATASEAFSALDAGAQALKIFPSSAFGPDYIKALKAVLpPEVPVFAVGGVTPENLAQWIN 167
Cdd:COG0800 93 GLDPEVIKAANRAGLPVLPGVATPTEIMAALEAGADAVKLFPAEALGPAYLKALKGPL-PDVPFMPTGGVSPDNAADYLA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490246922 168 AGCVGAGLGSDLYRAGQSVER----TAQQAAAFVKAYREAVK 205
Cdd:COG0800 172 AGAVAVGGGSWLVPKGAIAAGdwaaITERAREAVAAVRAARA 213
|
|
| KDPG_aldolase |
cd00452 |
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ... |
5-182 |
3.11e-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: 3.11e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 5 TNLPLIAILRGITPDEALAHVGAVIDAGFDAVEIPLNSPQWEKSIPQVVDAYGEqALIGAGTVLQPEQVDRLAAMGCRLI 84
Cdd:cd00452 2 KAQPLVAVLRGDDAEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFPE-ALIGAGTVLTPEQADAAIAAGAQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 85 VTPNIQPEVIRRAVGYGMTVCPGCATASEAFSALDAGAQALKIFPSSAFGPDYIKALKAVLPPeVPVFAVGGVTPENLAQ 164
Cdd:cd00452 81 VSPGLDPEVVKAANRAGIPLLPGVATPTEIMQALELGADIVKLFPAEAVGPAYIKALKGPFPQ-VRFMPTGGVSLDNAAE 159
|
170
....*....|....*...
gi 490246922 165 WINAGCVGAGLGSDLYRA 182
Cdd:cd00452 160 WLAAGVVAVGGGSLLPKD 177
|
|
| PRK06552 |
PRK06552 |
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional |
9-203 |
1.30e-44 |
|
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
Pssm-ID: 180618 Cd Length: 213 Bit Score: 147.45 E-value: 1.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 9 LIAILRGITPDEALAHVGAVIDAGFDAVEIPLNSPQWEKSIPQVVDAYGEQA--LIGAGTVLQPEQVdRLAAM-GCRLIV 85
Cdd:PRK06552 15 VVAVVRGESKEEALKISLAVIKGGIKAIEVTYTNPFASEVIKELVELYKDDPevLIGAGTVLDAVTA-RLAILaGAQFIV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 86 TPNIQPEVIRRAVGYGMTVCPGCATASEAFSALDAGAQALKIFPSSAFGPDYIKALKAVLpPEVPVFAVGGVTPENLAQW 165
Cdd:PRK06552 94 SPSFNRETAKICNLYQIPYLPGCMTVTEIVTALEAGSEIVKLFPGSTLGPSFIKAIKGPL-PQVNVMVTGGVNLDNVKDW 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490246922 166 INAGCVGAGLGSDLYRAGQS--VERTAQQAAAFVKAYREA 203
Cdd:PRK06552 173 FAAGADAVGIGGELNKLASQgdFDLITEKAKKYMSSLRKA 212
|
|
| PRK07455 |
PRK07455 |
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase; |
10-180 |
8.16e-33 |
|
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
Pssm-ID: 180985 Cd Length: 187 Bit Score: 116.29 E-value: 8.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 10 IAILRGITPDEALAHVGAVIDAGFDAVEIPLNSPQWEKSIPQVVDAYgEQALIGAGTVLQPEQVDRLAAMGCRLIVTPNI 89
Cdd:PRK07455 15 IAVIRAPDLELGLQMAEAVAAGGMRLIEITWNSDQPAELISQLREKL-PECIIGTGTILTLEDLEEAIAAGAQFCFTPHV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 90 QPEVIRRAVGYGMTVCPGCATASEAFSALDAGAQALKIFPSSAF-GPDYIKALKAVLpPEVPVFAVGGVTPENLAQWINA 168
Cdd:PRK07455 94 DPELIEAAVAQDIPIIPGALTPTEIVTAWQAGASCVKVFPVQAVgGADYIKSLQGPL-GHIPLIPTGGVTLENAQAFIQA 172
|
170
....*....|..
gi 490246922 169 GCVGAGLGSDLY 180
Cdd:PRK07455 173 GAIAVGLSGQLF 184
|
|
| eda |
TIGR01182 |
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ... |
4-195 |
4.07e-30 |
|
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: 110.09 E-value: 4.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 4 QTNLPLIAILRGITPDEALAHVGAVIDAGFDAVEIPLNSPQWEKSIPQVVDAYgEQALIGAGTVLQPEQVDRLAAMGCRL 83
Cdd:TIGR01182 5 LREAKIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEV-PDALIGAGTVLNPEQLRQAVAAGAQF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 84 IVTPNIQPEVIRRAVGYGMTVCPGCATASEAFSALDAGAQALKIFPSSAFG-PDYIKALKAVLpPEVPVFAVGGVTPENL 162
Cdd:TIGR01182 84 IVSPGLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAEVSGgVKMLKALAGPF-PQVRFCPTGGINLANA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490246922 163 AQWINAGCVGAGLGS-----DLYRAG--QSVERTAQQAAA 195
Cdd:TIGR01182 163 RDYLALPNVACGGGSwlvpkDLIAAGdwDEITRLAREALE 202
|
|
| Aldolase |
pfam01081 |
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ... |
5-183 |
1.09e-24 |
|
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: 95.62 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 5 TNLPLIAILRGITPDEALAHVGAVIDAGFDAVEIPLNSPQWEKSIpQVVDAYGEQALIGAGTVLQPEQVDRLAAMGCRLI 84
Cdd:pfam01081 6 KEAKIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAI-RLLRKNRPDALVGAGTVLNAQQLAEAAEAGAQFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 85 VTPNIQPEVIRRAVGYGMTVCPGCATASEAFSALDAGAQALKIFPSSAFGPdyIKALKAVLPP--EVPVFAVGGVTPENL 162
Cdd:pfam01081 85 VSPGLTADLLKHAVDVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPAEASGG--VPAIKALAGPfpQVRFCPTGGIHPANV 162
|
170 180
....*....|....*....|.
gi 490246922 163 AQWINAGCVGAGLGSDLYRAG 183
Cdd:pfam01081 163 RDYLALPNILCVGGSWLVPAS 183
|
|
| PRK07114 |
PRK07114 |
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase; |
62-203 |
2.95e-24 |
|
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
Pssm-ID: 235939 Cd Length: 222 Bit Score: 95.09 E-value: 2.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 62 IGAGTVLQPEQVDRLAAMGCRLIVTPNIQPEVI----RRAVGYgmtvCPGCATASEAFSALDAGAQALKIFPSSAFGPDY 137
Cdd:PRK07114 73 LGVGSIVDAATAALYIQLGANFIVTPLFNPDIAkvcnRRKVPY----SPGCGSLSEIGYAEELGCEIVKLFPGSVYGPGF 148
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490246922 138 IKALKAVLpPEVPVFAVGGVTP--ENLAQWINAGCVGAGLGSDL-------YRAGQSVERTAQQAAAFVKAYREA 203
Cdd:PRK07114 149 VKAIKGPM-PWTKIMPTGGVEPteENLKKWFGAGVTCVGMGSKLipkealaAKDYAGIEQKVREALAIIKEVRKK 222
|
|
| PRK05718 |
PRK05718 |
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional |
7-198 |
1.00e-22 |
|
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
Pssm-ID: 235577 Cd Length: 212 Bit Score: 91.07 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 7 LPLIAILRgitPDEALAHVGAVIDAGFDAVEIPLNSPQWEKSIPQVVDAYGEqALIGAGTVLQPEQVDRLAAMGCRLIVT 86
Cdd:PRK05718 18 VPVIVINK---LEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIAKEVPE-ALIGAGTVLNPEQLAQAIEAGAQFIVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 87 PNIQPEVIRRAVGYGMTVCPGCATASEAFSALDAGAQALKIFPSSAFGPdyIKALKAVLPP--EVPVFAVGGVTPENLAQ 164
Cdd:PRK05718 94 PGLTPPLLKAAQEGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEASGG--VKMLKALAGPfpDVRFCPTGGISPANYRD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490246922 165 WI---NAGCVGaglGS-----DLYRAGQ--SVERTAQQAAAFVK 198
Cdd:PRK05718 172 YLalpNVLCIG---GSwmvpkDAIENGDwdRITRLAREAVALAK 212
|
|
| PRK06015 |
PRK06015 |
2-dehydro-3-deoxy-phosphogluconate aldolase; |
8-195 |
8.03e-17 |
|
2-dehydro-3-deoxy-phosphogluconate aldolase;
Pssm-ID: 168348 Cd Length: 201 Bit Score: 75.23 E-value: 8.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 8 PLIAILRGITPDEALAHVGAVIDAGFDAVEIPLNSPQWEKSIPQVVDAYgEQALIGAGTVLQPEQVDRLAAMGCRLIVTP 87
Cdd:PRK06015 5 PVIPVLLIDDVEHAVPLARALAAGGLPAIEITLRTPAALDAIRAVAAEV-EEAIVGAGTILNAKQFEDAAKAGSRFIVSP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 88 NIQPEVIRRAVGYGMTVCPGCATASEAFSALDAGAQALKIFPS-SAFGPDYIKALKAVLpPEVPVFAVGGVTPENLAQWI 166
Cdd:PRK06015 84 GTTQELLAAANDSDVPLLPGAATPSEVMALREEGYTVLKFFPAeQAGGAAFLKALSSPL-AGTFFCPTGGISLKNARDYL 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 490246922 167 ---NAGCVGaglGS-----DLYRAGQ--SVERTAQQAAA 195
Cdd:PRK06015 163 slpNVVCVG---GSwvapkELVAAGDwaGITKLAAEAAA 198
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
91-203 |
8.98e-09 |
|
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: 53.27 E-value: 8.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 91 PEVIRRAVGYGMTVCPGCATASEAFSALDAGAQAL---KIFPSS-------AFGPDYIKALKAVLPpeVPVFAVGGVTPE 160
Cdd:COG0352 90 VAEARALLGPDLIIGVSCHSLEEALRAEEAGADYVgfgPVFPTPtkpgappPLGLEGLAWWAELVE--IPVVAIGGITPE 167
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 490246922 161 NLAQWINAGCVGAGLGSDLYRAgqsvERTAQQAAAFVKAYREA 203
Cdd:COG0352 168 NAAEVLAAGADGVAVISAIWGA----PDPAAAARELRAALEAA 206
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
91-191 |
2.38e-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: 49.05 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 91 PEVIRRAVGYGMTVCPGCATASEAFSALDAGAQAL---KIFPSS-------AFGPDYIKALKAVLppEVPVFAVGGVTPE 160
Cdd:cd00564 85 VAEARALLGPDLIIGVSTHSLEEALRAEELGADYVgfgPVFPTPtkpgagpPLGLELLREIAELV--EIPVVAIGGITPE 162
|
90 100 110
....*....|....*....|....*....|.
gi 490246922 161 NLAQWINAGCVGAGLGSDLYRAGQSVERTAQ 191
Cdd:cd00564 163 NAAEVLAAGADGVAVISAITGADDPAAAARE 193
|
|
| TMP-TENI |
pfam02581 |
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ... |
91-172 |
7.67e-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: 44.46 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 91 PEVIRRAVGYGMTVCPGCATASEAFSALDAGAQAL---KIFPS------SAFGPDYIKALKAVLppEVPVFAVGGVTPEN 161
Cdd:pfam02581 85 VAEARELLGPDLIIGVSTHTLEEALEAEALGADYIgfgPIFPTptkpdaPPLGLEGLKAIAEAV--EIPVVAIGGITPEN 162
|
90
....*....|.
gi 490246922 162 LAQWINAGCVG 172
Cdd:pfam02581 163 VPEVIEAGADG 173
|
|
| thiE |
PRK00043 |
thiamine phosphate synthase; |
91-201 |
1.54e-05 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 44.02 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 91 PEVIRRAVGYGMTVCPGCATASEAFSALDAGAQAL---KIFPSS-------AFGPDYIKALKAVLPPeVPVFAVGGVTPE 160
Cdd:PRK00043 94 VADARALLGPDAIIGLSTHTLEEAAAALAAGADYVgvgPIFPTPtkkdakaPQGLEGLREIRAAVGD-IPIVAIGGITPE 172
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 490246922 161 NLAQWINAGCVGAGLGSDLYRAgQSVERTAQQAAAFVKAYR 201
Cdd:PRK00043 173 NAPEVLEAGADGVAVVSAITGA-EDPEAAARALLAAFRAAR 212
|
|
| thiE |
TIGR00693 |
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ... |
90-192 |
1.66e-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: 43.78 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 90 QPEVIRRAVGYGMTVCPGCATASEAFSALDAGAQAL---KIFPSS-------AFGPDYIKALKAVLPpEVPVFAVGGVTP 159
Cdd:TIGR00693 85 PASEARALLGPDKIIGVSTHNLEELAEAEAEGADYIgfgPIFPTPtkkdpapPAGVELLREIAATLI-DIPIVAIGGITL 163
|
90 100 110
....*....|....*....|....*....|...
gi 490246922 160 ENLAQWINAGCVGAGLGSDLYRAgQSVERTAQQ 192
Cdd:TIGR00693 164 ENAAEVLAAGADGVAVVSAIMQA-ADPKAAAKR 195
|
|
| PRK02615 |
PRK02615 |
thiamine phosphate synthase; |
92-178 |
2.71e-05 |
|
thiamine phosphate synthase;
Pssm-ID: 235054 [Multi-domain] Cd Length: 347 Bit Score: 43.72 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 92 EVIRRAVGYGMTVcpGCATAS--EAFSALDAGAQAL---KIFPS------SAFGPDYIKALKAVLPpeVPVFAVGGVTPE 160
Cdd:PRK02615 231 AVARQLLGPEKII--GRSTTNpeEMAKAIAEGADYIgvgPVFPTptkpgkAPAGLEYLKYAAKEAP--IPWFAIGGIDKS 306
|
90 100
....*....|....*....|...
gi 490246922 161 NLAQWINAGC-----VGAGLGSD 178
Cdd:PRK02615 307 NIPEVLQAGAkrvavVRAIMGAE 329
|
|
| PRK07695 |
PRK07695 |
thiazole tautomerase TenI; |
107-205 |
3.80e-05 |
|
thiazole tautomerase TenI;
Pssm-ID: 181086 [Multi-domain] Cd Length: 201 Bit Score: 42.70 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 107 GCATAS--EAFSALDAGAQAL---KIFPSS------AFGPDYIKALKAVLppEVPVFAVGGVTPENLAQWINAGCVGAGL 175
Cdd:PRK07695 99 GYSVHSleEAIQAEKNGADYVvygHVFPTDckkgvpARGLEELSDIARAL--SIPVIAIGGITPENTRDVLAAGVSGIAV 176
|
90 100 110
....*....|....*....|....*....|
gi 490246922 176 GSDLYRAGQSVERtaqqaaafVKAYREAVK 205
Cdd:PRK07695 177 MSGIFSSANPYSK--------AKRYAESIK 198
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
10-176 |
5.73e-05 |
|
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: 42.32 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 10 IAILRGI-TPDEALAHVGAVIDAGFDAVEIPLNspqwekSIPQVVDAYGEQ-----ALIGAGTVLQP-----EQVDRLAA 78
Cdd:cd00945 3 LTLLHPDaTLEDIAKLCDEAIEYGFAAVCVNPG------YVRLAADALAGSdvpviVVVGFPTGLTTtevkvAEVEEAID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246922 79 MGCRLI-VTPNI-------QPEV------IRRAVGYGMTVCPGCAT-----------ASEAfsALDAGAQALKIFPSSAF 133
Cdd:cd00945 77 LGADEIdVVINIgslkegdWEEVleeiaaVVEAADGGLPLKVILETrglktadeiakAARI--AAEAGADFIKTSTGFGG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490246922 134 G---PDYIKALKAVLPPEVPVFAVGGV-TPENLAQWINAGCVGAGLG 176
Cdd:cd00945 155 GgatVEDVKLMKEAVGGRVGVKAAGGIkTLEDALAAIEAGADGIGTS 201
|
|
|