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Conserved domains on  [gi|490246922|ref|WP_004145082|]
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MULTISPECIES: 2-dehydro-3-deoxy-6-phosphogalactonate aldolase [Klebsiella]

Protein Classification

2-dehydro-3-deoxy-6-phosphogalactonate aldolase( domain architecture ID 10793147)

2-dehydro-3-deoxy-6-phosphogalactonate aldolase catalyzes the reversible, stereospecific retro-aldol cleavage of 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) to pyruvate and D-glyceraldehyde-3-phosphate

EC:  4.1.2.21
Gene Ontology:  GO:0034194|GO:0008674

Graphical summary

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List of domain hits

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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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