|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09140 |
PRK09140 |
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed |
1-206 |
6.91e-117 |
|
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed
Pssm-ID: 181670 Cd Length: 206 Bit Score: 330.64 E-value: 6.91e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 1 MPFNTLLQKTGLVAILRGVKPDEIVAIGEKLYAAGFRLIEIPMNSPEALQSISLLRDALPKDCLVGAGTVLSVEQVVAVK 80
Cdd:PRK09140 1 MRLMQPFTKLPLIAILRGITPDEALAHVGALIEAGFRAIEIPLNSPDPFDSIAALVKALGDRALIGAGTVLSPEQVDRLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 81 EAGGQIIVMPHCDTAVIRRARALGMYCAPGVATPTEAFAAIEHGANAIKLFPAEQITPEVTKAWRAVIPQSVPMLPVGGI 160
Cdd:PRK09140 81 DAGGRLIVTPNTDPEVIRRAVALGMVVMPGVATPTEAFAALRAGAQALKLFPASQLGPAGIKALRAVLPPDVPVFAVGGV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447039216 161 TPETMARYLSHGANGFGLGSALYRPGMTPEQVYENAVLFMNAWNNL 206
Cdd:PRK09140 161 TPENLAPYLAAGAAGFGLGSALYRPGQSAEEVAERARAFVAAYREA 206
|
|
| Eda |
COG0800 |
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ... |
1-206 |
1.13e-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: 241.91 E-value: 1.13e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 1 MPFNTLLQKTGLVAILRGVKPDEIVAIGEKLYAAGFRLIEIPMNSPEALQSISLLRDALPKDCLVGAGTVLSVEQVVAVK 80
Cdd:COG0800 3 MELLELLAAAPVVPVLRGDDPEDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEVGPDALVGAGTVLTPEQARAAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 81 EAGGQIIVMPHCDTAVIRRARALGMYCAPGVATPTEAFAAIEHGANAIKLFPAEQITPEVTKAWRAVIPQsVPMLPVGGI 160
Cdd:COG0800 83 AAGARFIVSPGLDPEVIKAANRAGLPVLPGVATPTEIMAALEAGADAVKLFPAEALGPAYLKALKGPLPD-VPFMPTGGV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447039216 161 TPETMARYLSHGANGFGLGSALYRPGMTPEQVY----ENAVLFMNAWNNL 206
Cdd:COG0800 162 SPDNAADYLAAGAVAVGGGSWLVPKGAIAAGDWaaitERAREAVAAVRAA 211
|
|
| KDPG_aldolase |
cd00452 |
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ... |
7-192 |
2.44e-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: 212.38 E-value: 2.44e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 7 LQKTGLVAILRGVKPDEIVAIGEKLYAAGFRLIEIPMNSPEALQSISLLRDALPkDCLVGAGTVLSVEQVVAVKEAGGQI 86
Cdd:cd00452 1 LKAQPLVAVLRGDDAEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFP-EALIGAGTVLTPEQADAAIAAGAQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 87 IVMPHCDTAVIRRARALGMYCAPGVATPTEAFAAIEHGANAIKLFPAEQITPEVTKAWRAVIPQsVPMLPVGGITPETMA 166
Cdd:cd00452 80 IVSPGLDPEVVKAANRAGIPLLPGVATPTEIMQALELGADIVKLFPAEAVGPAYIKALKGPFPQ-VRFMPTGGVSLDNAA 158
|
170 180
....*....|....*....|....*.
gi 447039216 167 RYLSHGANGFGLGSALYRPGMTPEQV 192
Cdd:cd00452 159 EWLAAGVVAVGGGSLLPKDAVAAGDW 184
|
|
| eda |
TIGR01182 |
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ... |
5-182 |
1.55e-38 |
|
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: 131.67 E-value: 1.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 5 TLLQKTGLVAILRGVKPDEIVAIGEKLYAAGFRLIEIPMNSPEALQSISLLRDALPkDCLVGAGTVLSVEQVVAVKEAGG 84
Cdd:TIGR01182 3 ELLREAKIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEVP-DALIGAGTVLNPEQLRQAVAAGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 85 QIIVMPHCDTAVIRRARALGMYCAPGVATPTEAFAAIEHGANAIKLFPAEQI-TPEVTKAWRAVIPQsVPMLPVGGITPE 163
Cdd:TIGR01182 82 QFIVSPGLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAEVSgGVKMLKALAGPFPQ-VRFCPTGGINLA 160
|
170
....*....|....*....
gi 447039216 164 TMARYLSHGANGFGLGSAL 182
Cdd:TIGR01182 161 NARDYLALPNVACGGGSWL 179
|
|
| Aldolase |
pfam01081 |
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ... |
7-182 |
6.08e-26 |
|
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: 99.09 E-value: 6.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 7 LQKTGLVAILRGVKPDEIVAIGEKLYAAGFRLIEIPMNSPEALQSISLLRDALPkDCLVGAGTVLSVEQVVAVKEAGGQI 86
Cdd:pfam01081 5 LKEAKIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAIRLLRKNRP-DALVGAGTVLNAQQLAEAAEAGAQF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 87 IVMPHCDTAVIRRARALGMYCAPGVATPTEAFAAIEHGANAIKLFPAEQITP-EVTKAWRAVIPQsVPMLPVGGITPETM 165
Cdd:pfam01081 84 VVSPGLTADLLKHAVDVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPAEASGGvPAIKALAGPFPQ-VRFCPTGGIHPANV 162
|
170
....*....|....*..
gi 447039216 166 ARYLSHGANGFGLGSAL 182
Cdd:pfam01081 163 RDYLALPNILCVGGSWL 179
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09140 |
PRK09140 |
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed |
1-206 |
6.91e-117 |
|
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed
Pssm-ID: 181670 Cd Length: 206 Bit Score: 330.64 E-value: 6.91e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 1 MPFNTLLQKTGLVAILRGVKPDEIVAIGEKLYAAGFRLIEIPMNSPEALQSISLLRDALPKDCLVGAGTVLSVEQVVAVK 80
Cdd:PRK09140 1 MRLMQPFTKLPLIAILRGITPDEALAHVGALIEAGFRAIEIPLNSPDPFDSIAALVKALGDRALIGAGTVLSPEQVDRLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 81 EAGGQIIVMPHCDTAVIRRARALGMYCAPGVATPTEAFAAIEHGANAIKLFPAEQITPEVTKAWRAVIPQSVPMLPVGGI 160
Cdd:PRK09140 81 DAGGRLIVTPNTDPEVIRRAVALGMVVMPGVATPTEAFAALRAGAQALKLFPASQLGPAGIKALRAVLPPDVPVFAVGGV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447039216 161 TPETMARYLSHGANGFGLGSALYRPGMTPEQVYENAVLFMNAWNNL 206
Cdd:PRK09140 161 TPENLAPYLAAGAAGFGLGSALYRPGQSAEEVAERARAFVAAYREA 206
|
|
| Eda |
COG0800 |
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ... |
1-206 |
1.13e-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: 241.91 E-value: 1.13e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 1 MPFNTLLQKTGLVAILRGVKPDEIVAIGEKLYAAGFRLIEIPMNSPEALQSISLLRDALPKDCLVGAGTVLSVEQVVAVK 80
Cdd:COG0800 3 MELLELLAAAPVVPVLRGDDPEDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEVGPDALVGAGTVLTPEQARAAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 81 EAGGQIIVMPHCDTAVIRRARALGMYCAPGVATPTEAFAAIEHGANAIKLFPAEQITPEVTKAWRAVIPQsVPMLPVGGI 160
Cdd:COG0800 83 AAGARFIVSPGLDPEVIKAANRAGLPVLPGVATPTEIMAALEAGADAVKLFPAEALGPAYLKALKGPLPD-VPFMPTGGV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447039216 161 TPETMARYLSHGANGFGLGSALYRPGMTPEQVY----ENAVLFMNAWNNL 206
Cdd:COG0800 162 SPDNAADYLAAGAVAVGGGSWLVPKGAIAAGDWaaitERAREAVAAVRAA 211
|
|
| KDPG_aldolase |
cd00452 |
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ... |
7-192 |
2.44e-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: 212.38 E-value: 2.44e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 7 LQKTGLVAILRGVKPDEIVAIGEKLYAAGFRLIEIPMNSPEALQSISLLRDALPkDCLVGAGTVLSVEQVVAVKEAGGQI 86
Cdd:cd00452 1 LKAQPLVAVLRGDDAEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFP-EALIGAGTVLTPEQADAAIAAGAQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 87 IVMPHCDTAVIRRARALGMYCAPGVATPTEAFAAIEHGANAIKLFPAEQITPEVTKAWRAVIPQsVPMLPVGGITPETMA 166
Cdd:cd00452 80 IVSPGLDPEVVKAANRAGIPLLPGVATPTEIMQALELGADIVKLFPAEAVGPAYIKALKGPFPQ-VRFMPTGGVSLDNAA 158
|
170 180
....*....|....*....|....*.
gi 447039216 167 RYLSHGANGFGLGSALYRPGMTPEQV 192
Cdd:cd00452 159 EWLAAGVVAVGGGSLLPKDAVAAGDW 184
|
|
| eda |
TIGR01182 |
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ... |
5-182 |
1.55e-38 |
|
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: 131.67 E-value: 1.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 5 TLLQKTGLVAILRGVKPDEIVAIGEKLYAAGFRLIEIPMNSPEALQSISLLRDALPkDCLVGAGTVLSVEQVVAVKEAGG 84
Cdd:TIGR01182 3 ELLREAKIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEVP-DALIGAGTVLNPEQLRQAVAAGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 85 QIIVMPHCDTAVIRRARALGMYCAPGVATPTEAFAAIEHGANAIKLFPAEQI-TPEVTKAWRAVIPQsVPMLPVGGITPE 163
Cdd:TIGR01182 82 QFIVSPGLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAEVSgGVKMLKALAGPFPQ-VRFCPTGGINLA 160
|
170
....*....|....*....
gi 447039216 164 TMARYLSHGANGFGLGSAL 182
Cdd:TIGR01182 161 NARDYLALPNVACGGGSWL 179
|
|
| PRK07455 |
PRK07455 |
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase; |
6-185 |
7.20e-33 |
|
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
Pssm-ID: 180985 Cd Length: 187 Bit Score: 116.68 E-value: 7.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 6 LLQKTGLVAILRGVKPDEIVAIGEKLYAAGFRLIEIPMNSPEALQSISLLRDALPkDCLVGAGTVLSVEQVVAVKEAGGQ 85
Cdd:PRK07455 8 QLQQHRAIAVIRAPDLELGLQMAEAVAAGGMRLIEITWNSDQPAELISQLREKLP-ECIIGTGTILTLEDLEEAIAAGAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 86 IIVMPHCDTAVIRRARALGMYCAPGVATPTEAFAAIEHGANAIKLFPAEQI-TPEVTKAWRAVIPQsVPMLPVGGITPET 164
Cdd:PRK07455 87 FCFTPHVDPELIEAAVAQDIPIIPGALTPTEIVTAWQAGASCVKVFPVQAVgGADYIKSLQGPLGH-IPLIPTGGVTLEN 165
|
170 180
....*....|....*....|.
gi 447039216 165 MARYLSHGANGFGLGSALYRP 185
Cdd:PRK07455 166 AQAFIQAGAIAVGLSGQLFPK 186
|
|
| PRK06552 |
PRK06552 |
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional |
7-204 |
1.31e-30 |
|
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
Pssm-ID: 180618 Cd Length: 213 Bit Score: 111.63 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 7 LQKTGLVAILRGVKPDEIVAIGEKLYAAGFRLIEIPMNSPEALQSISLLRDALP--KDCLVGAGTVLSVEQVVAVKEAGG 84
Cdd:PRK06552 10 LKANGVVAVVRGESKEEALKISLAVIKGGIKAIEVTYTNPFASEVIKELVELYKddPEVLIGAGTVLDAVTARLAILAGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 85 QIIVMPHCDTAVIRRARALGMYCAPGVATPTEAFAAIEHGANAIKLFPAEQITPEVTKAWRAVIPQsVPMLPVGGITPET 164
Cdd:PRK06552 90 QFIVSPSFNRETAKICNLYQIPYLPGCMTVTEIVTALEAGSEIVKLFPGSTLGPSFIKAIKGPLPQ-VNVMVTGGVNLDN 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447039216 165 MARYLSHGANGFGLGSALYRPGMTP--EQVYENAVLFMNAWN 204
Cdd:PRK06552 169 VKDWFAAGADAVGIGGELNKLASQGdfDLITEKAKKYMSSLR 210
|
|
| PRK05718 |
PRK05718 |
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional |
20-170 |
4.65e-30 |
|
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
Pssm-ID: 235577 Cd Length: 212 Bit Score: 109.95 E-value: 4.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 20 KPDEIVAIGEKLYAAGFRLIEIPMNSPEALQSISLLRDALPkDCLVGAGTVLSVEQVVAVKEAGGQIIVMPHCDTAVIRR 99
Cdd:PRK05718 25 KLEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIAKEVP-EALIGAGTVLNPEQLAQAIEAGAQFIVSPGLTPPLLKA 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447039216 100 ARALGMYCAPGVATPTEAFAAIEHGANAIKLFPAEQI-TPEVTKAWRAVIPQsVPMLPVGGITPETMARYLS 170
Cdd:PRK05718 104 AQEGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEASgGVKMLKALAGPFPD-VRFCPTGGISPANYRDYLA 174
|
|
| Aldolase |
pfam01081 |
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ... |
7-182 |
6.08e-26 |
|
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: 99.09 E-value: 6.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 7 LQKTGLVAILRGVKPDEIVAIGEKLYAAGFRLIEIPMNSPEALQSISLLRDALPkDCLVGAGTVLSVEQVVAVKEAGGQI 86
Cdd:pfam01081 5 LKEAKIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAIRLLRKNRP-DALVGAGTVLNAQQLAEAAEAGAQF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 87 IVMPHCDTAVIRRARALGMYCAPGVATPTEAFAAIEHGANAIKLFPAEQITP-EVTKAWRAVIPQsVPMLPVGGITPETM 165
Cdd:pfam01081 84 VVSPGLTADLLKHAVDVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPAEASGGvPAIKALAGPFPQ-VRFCPTGGIHPANV 162
|
170
....*....|....*..
gi 447039216 166 ARYLSHGANGFGLGSAL 182
Cdd:pfam01081 163 RDYLALPNILCVGGSWL 179
|
|
| PRK06015 |
PRK06015 |
2-dehydro-3-deoxy-phosphogluconate aldolase; |
25-170 |
6.92e-16 |
|
2-dehydro-3-deoxy-phosphogluconate aldolase;
Pssm-ID: 168348 Cd Length: 201 Bit Score: 72.54 E-value: 6.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 25 VAIGEKLYAAGFRLIEIPMNSPEALQSISLLRDALPkDCLVGAGTVLSVEQVVAVKEAGGQIIVMPHCDTAVIRRARALG 104
Cdd:PRK06015 19 VPLARALAAGGLPAIEITLRTPAALDAIRAVAAEVE-EAIVGAGTILNAKQFEDAAKAGSRFIVSPGTTQELLAAANDSD 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447039216 105 MYCAPGVATPTEAFAAIEHGANAIKLFPAEQI-TPEVTKAWRAVIPQSVpMLPVGGITPETMARYLS 170
Cdd:PRK06015 98 VPLLPGAATPSEVMALREEGYTVLKFFPAEQAgGAAFLKALSSPLAGTF-FCPTGGISLKNARDYLS 163
|
|
| PRK07114 |
PRK07114 |
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase; |
66-183 |
4.50e-07 |
|
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
Pssm-ID: 235939 Cd Length: 222 Bit Score: 48.48 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 66 GAGTVLSVEQVVAVKEAGGQIIVMPHCDTAVIRRA-RALGMYCaPGVATPTEAFAAIEHGANAIKLFPAEQITPEVTKAW 144
Cdd:PRK07114 74 GVGSIVDAATAALYIQLGANFIVTPLFNPDIAKVCnRRKVPYS-PGCGSLSEIGYAEELGCEIVKLFPGSVYGPGFVKAI 152
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 447039216 145 RAVIPQSVPMlPVGGITP--ETMARYLSHGANGFGLGSALY 183
Cdd:PRK07114 153 KGPMPWTKIM-PTGGVEPteENLKKWFGAGVTCVGMGSKLI 192
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
93-184 |
1.60e-04 |
|
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: 40.94 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 93 DTAVIRRARALGMYCAPGVATPTEAFAAIEHGANAI----------KLFPAEQITPEVTKAWRAVIPqsVPMLPVGGITP 162
Cdd:COG0352 89 PVAEARALLGPDLIIGVSCHSLEEALRAEEAGADYVgfgpvfptptKPGAPPPLGLEGLAWWAELVE--IPVVAIGGITP 166
|
90 100
....*....|....*....|..
gi 447039216 163 ETMARYLSHGANGFGLGSALYR 184
Cdd:COG0352 167 ENAAEVLAAGADGVAVISAIWG 188
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
93-182 |
5.03e-04 |
|
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.
Pssm-ID: 240081 [Multi-domain] Cd Length: 236 Bit Score: 39.77 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 93 DTAVIRRARALGMYCAPGVATPTEAFAAIEHGANAI-------------KLFPAEQITPEVTKAWravipqSVPMLPVGG 159
Cdd:cd04730 91 PAEVVERLKAAGIKVIPTVTSVEEARKAEAAGADALvaqgaeagghrgtFDIGTFALVPEVRDAV------DIPVIAAGG 164
|
90 100
....*....|....*....|....
gi 447039216 160 I-TPETMARYLSHGANGFGLGSAL 182
Cdd:cd04730 165 IaDGRGIAAALALGADGVQMGTRF 188
|
|
| TMP-TENI |
pfam02581 |
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ... |
93-182 |
2.80e-03 |
|
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: 37.14 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 93 DTAVIRRARALGMYCAPGVATPTEAFAAIEHGANAI---KLFP------AEQITPEVTKAWRAVIPqsvpmLPV---GGI 160
Cdd:pfam02581 84 PVAEARELLGPDLIIGVSTHTLEEALEAEALGADYIgfgPIFPtptkpdAPPLGLEGLKAIAEAVE-----IPVvaiGGI 158
|
90 100
....*....|....*....|..
gi 447039216 161 TPETMARYLSHGANGFGLGSAL 182
Cdd:pfam02581 159 TPENVPEVIEAGADGVAVVSAI 180
|
|
| modD_like |
cd01573 |
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ... |
99-183 |
4.67e-03 |
|
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC operons in bacteria, which are involved in molybdate transport. In general, QPRTases are part of the de novo synthesis pathway of NAD in both prokaryotes and eukaryotes. They catalyse the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide.
Pssm-ID: 238807 [Multi-domain] Cd Length: 272 Bit Score: 36.89 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 99 RARALGMYCAPGVATPTEAFAAIEHGANAIKLfpaEQITPEVTKA---WRAVIPQSVPMLPVGGITPETMARYLSHGANG 175
Cdd:cd01573 178 RATAPEKKIVVEVDSLEEALAAAEAGADILQL---DKFSPEELAElvpKLRSLAPPVLLAAAGGINIENAAAYAAAGADI 254
|
....*...
gi 447039216 176 FgLGSALY 183
Cdd:cd01573 255 L-VTSAPY 261
|
|
| IGPS |
cd00331 |
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
97-194 |
4.72e-03 |
|
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, catalyzing the ring closure reaction of 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate (CdRP) to indole-3-glycerol phosphate (IGP), accompanied by the release of carbon dioxide and water. IGPS is active as a separate monomer in most organisms, but is also found fused to other enzymes as part of a bifunctional or multifunctional enzyme involved in tryptophan biosynthesis.
Pssm-ID: 238203 Cd Length: 217 Bit Score: 36.67 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 97 IRRARALGMYCAPGVATPTEAFAAIEHGANAI-------KLFpaeQITPEVTKAWRAVIPQSVPMLPVGGI-TPETMARY 168
Cdd:cd00331 114 YELARELGMEVLVEVHDEEELERALALGAKIIginnrdlKTF---EVDLNTTERLAPLIPKDVILVSESGIsTPEDVKRL 190
|
90 100
....*....|....*....|....*.
gi 447039216 169 LSHGANGFGLGSALyrpgMTPEQVYE 194
Cdd:cd00331 191 AEAGADAVLIGESL----MRAPDPGA 212
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
92-184 |
6.65e-03 |
|
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: 36.34 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 92 CDTAVIRRARALGMYCAPGVATPTEAFAAIEHGANAI---KLFP-------AEQITPEVTKAWRAVIPqsvpmLPV---G 158
Cdd:cd00564 83 LPVAEARALLGPDLIIGVSTHSLEEALRAEELGADYVgfgPVFPtptkpgaGPPLGLELLREIAELVE-----IPVvaiG 157
|
90 100
....*....|....*....|....*.
gi 447039216 159 GITPETMARYLSHGANGFGLGSALYR 184
Cdd:cd00564 158 GITPENAAEVLAAGADGVAVISAITG 183
|
|
| QPRTase_NadC |
cd01568 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
94-183 |
6.88e-03 |
|
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called nicotinate-nucleotide pyrophosphorylase, is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide. QPRTase functions as a homodimer with two active sites, each formed by the C-terminal region of one subunit and the N-terminal region of the other.
Pssm-ID: 238802 [Multi-domain] Cd Length: 269 Bit Score: 36.30 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447039216 94 TAVIRRARALGMYCAP---GVATPTEAFAAIEHGANAIKL--FPAEQIT---PEVTKAWRAVIPQSvpmlpvGGITPETM 165
Cdd:cd01568 168 TEAVKRARAAAPFEKKievEVETLEEAEEALEAGADIIMLdnMSPEELKeavKLLKGLPRVLLEAS------GGITLENI 241
|
90
....*....|....*...
gi 447039216 166 ARYLSHGANGFGLGsALY 183
Cdd:cd01568 242 RAYAETGVDVISTG-ALT 258
|
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