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Conserved domains on  [gi|1403507349|emb|SQH26355|]
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ketohydroxyglutarate aldolase [Streptococcus pyogenes]

Protein Classification

bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase( domain architecture ID 10792805)

bifunctional 4-hydroxy-2-oxoglutarate (KHG) aldolase/2-dehydro-3-deoxy-phosphogluconate (KDPG) aldolase is involved in the degradation of glucose via the Entner-Doudoroff pathway; catalyzes the reversible, stereospecific retro-aldol cleavage of KDPG to pyruvate and D-glyceraldehyde-3-phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK06552 PRK06552
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
 1-211 9.02e-133

keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional


:

Pssm-ID: 180618  Cd Length: 213  Bit Score: 371.25  E-value: 9.02e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349   1 MGKIEILTKLKANRLVLVVRGESSEEALACSLASIEGGIKTIEVTYTNPFASEVIGQLAERFKEDPEVLIGAGTVLDDVT 80
Cdd:PRK06552    1 MKKSEILTKLKANGVVAVVRGESKEEALKISLAVIKGGIKAIEVTYTNPFASEVIKELVELYKDDPEVLIGAGTVLDAVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349  81 ARQAILAGAQFIVGPNFNRAVALICHRYSIPYLPGCMTVNEVVTALESGVDMVKIFPGSTVGMSFIRAIKSPLPQVEVMV 160
Cdd:PRK06552   81 ARLAILAGAQFIVSPSFNRETAKICNLYQIPYLPGCMTVTEIVTALEAGSEIVKLFPGSTLGPSFIKAIKGPLPQVNVMV 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1403507349 161 TGGVSSDNLKDWLAAGVDVLGIGGEFNQLASQKQYNLITKKAAHYIKSLRQ 211
Cdd:PRK06552  161 TGGVNLDNVKDWFAAGADAVGIGGELNKLASQGDFDLITEKAKKYMSSLRK 211
 
Name Accession Description Interval E-value
PRK06552 PRK06552
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
 1-211 9.02e-133

keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional


Pssm-ID: 180618  Cd Length: 213  Bit Score: 371.25  E-value: 9.02e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349   1 MGKIEILTKLKANRLVLVVRGESSEEALACSLASIEGGIKTIEVTYTNPFASEVIGQLAERFKEDPEVLIGAGTVLDDVT 80
Cdd:PRK06552    1 MKKSEILTKLKANGVVAVVRGESKEEALKISLAVIKGGIKAIEVTYTNPFASEVIKELVELYKDDPEVLIGAGTVLDAVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349  81 ARQAILAGAQFIVGPNFNRAVALICHRYSIPYLPGCMTVNEVVTALESGVDMVKIFPGSTVGMSFIRAIKSPLPQVEVMV 160
Cdd:PRK06552   81 ARLAILAGAQFIVSPSFNRETAKICNLYQIPYLPGCMTVTEIVTALEAGSEIVKLFPGSTLGPSFIKAIKGPLPQVNVMV 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1403507349 161 TGGVSSDNLKDWLAAGVDVLGIGGEFNQLASQKQYNLITKKAAHYIKSLRQ 211
Cdd:PRK06552  161 TGGVNLDNVKDWFAAGADAVGIGGELNKLASQGDFDLITEKAKKYMSSLRK 211
Eda COG0800
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ...
 3-211 1.61e-84

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: 249.23  E-value: 1.61e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349   3 KIEILTKLKANRLVLVVRGESSEEALACSLASIEGGIKTIEVTYTNPFASEVIGQLAERFkeDPEVLIGAGTVLDDVTAR 82
Cdd:COG0800     2 KMELLELLAAAPVVPVLRGDDPEDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEV--GPDALVGAGTVLTPEQAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349  83 QAILAGAQFIVGPNFNRAVALICHRYSIPYLPGCMTVNEVVTALESGVDMVKIFPGSTVGMSFIRAIKSPLPQVEVMVTG 162
Cdd:COG0800    80 AAIAAGARFIVSPGLDPEVIKAANRAGLPVLPGVATPTEIMAALEAGADAVKLFPAEALGPAYLKALKGPLPDVPFMPTG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1403507349 163 GVSSDNLKDWLAAGVDVLGIGGEF--NQLASQKQYNLITKKAAHYIKSLRQ 211
Cdd:COG0800   160 GVSPDNAADYLAAGAVAVGGGSWLvpKGAIAAGDWAAITERAREAVAAVRA 210
KDPG_aldolase cd00452
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ...
 10-201 2.52e-81

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: 240.11  E-value: 2.52e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349  10 LKANRLVLVVRGESSEEALACSLASIEGGIKTIEVTYTNPFASEVIGQLAERFkedPEVLIGAGTVLDDVTARQAILAGA 89
Cdd:cd00452     1 LKAQPLVAVLRGDDAEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEF---PEALIGAGTVLTPEQADAAIAAGA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349  90 QFIVGPNFNRAVALICHRYSIPYLPGCMTVNEVVTALESGVDMVKIFPGSTVGMSFIRAIKSPLPQVEVMVTGGVSSDNL 169
Cdd:cd00452    78 QFIVSPGLDPEVVKAANRAGIPLLPGVATPTEIMQALELGADIVKLFPAEAVGPAYIKALKGPFPQVRFMPTGGVSLDNA 157

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1403507349 170 KDWLAAGVDVLGIGGE-FNQLASQKQYNLITKK 201
Cdd:cd00452   158 AEWLAAGVVAVGGGSLlPKDAVAAGDWAAITAL 190
eda TIGR01182
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ...
 6-202 1.31e-50

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: 162.87  E-value: 1.31e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349   6 ILTKLKANRLVLVVRGESSEEALACSLASIEGGIKTIEVTYTNPFASEVIGQLAerfKEDPEVLIGAGTVLDDVTARQAI 85
Cdd:TIGR01182   1 IEELLREAKIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLR---KEVPDALIGAGTVLNPEQLRQAV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349  86 LAGAQFIVGPNFNRAVALICHRYSIPYLPGCMTVNEVVTALESGVDMVKIFPGSTVG-MSFIRAIKSPLPQVEVMVTGGV 164
Cdd:TIGR01182  78 AAGAQFIVSPGLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAEVSGgVKMLKALAGPFPQVRFCPTGGI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1403507349 165 SSDNLKDWLAAGVDVLGIGGEF--NQLASQKQYNLITKKA 202
Cdd:TIGR01182 158 NLANARDYLALPNVACGGGSWLvpKDLIAAGDWDEITRLA 197
Aldolase pfam01081
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ...
 6-184 9.12e-38

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: 129.52  E-value: 9.12e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349   6 ILTKLKANRLVLVVRGESSEEALACSLASIEGGIKTIEVTYTNPFASEVIGQLaerFKEDPEVLIGAGTVLDDVTARQAI 85
Cdd:pfam01081   1 IESILKEAKIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAIRLL---RKNRPDALVGAGTVLNAQQLAEAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349  86 LAGAQFIVGPNFNRAVALICHRYSIPYLPGCMTVNEVVTALESGVDMVKIFP-GSTVGMSFIRAIKSPLPQVEVMVTGGV 164
Cdd:pfam01081  78 EAGAQFVVSPGLTADLLKHAVDVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPaEASGGVPAIKALAGPFPQVRFCPTGGI 157

                         170       180
                  ....*....|....*....|
gi 1403507349 165 SSDNLKDWLAAGvDVLGIGG 184
Cdd:pfam01081 158 HPANVRDYLALP-NILCVGG 176
 
Name Accession Description Interval E-value
PRK06552 PRK06552
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
 1-211 9.02e-133

keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional


Pssm-ID: 180618  Cd Length: 213  Bit Score: 371.25  E-value: 9.02e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349   1 MGKIEILTKLKANRLVLVVRGESSEEALACSLASIEGGIKTIEVTYTNPFASEVIGQLAERFKEDPEVLIGAGTVLDDVT 80
Cdd:PRK06552    1 MKKSEILTKLKANGVVAVVRGESKEEALKISLAVIKGGIKAIEVTYTNPFASEVIKELVELYKDDPEVLIGAGTVLDAVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349  81 ARQAILAGAQFIVGPNFNRAVALICHRYSIPYLPGCMTVNEVVTALESGVDMVKIFPGSTVGMSFIRAIKSPLPQVEVMV 160
Cdd:PRK06552   81 ARLAILAGAQFIVSPSFNRETAKICNLYQIPYLPGCMTVTEIVTALEAGSEIVKLFPGSTLGPSFIKAIKGPLPQVNVMV 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1403507349 161 TGGVSSDNLKDWLAAGVDVLGIGGEFNQLASQKQYNLITKKAAHYIKSLRQ 211
Cdd:PRK06552  161 TGGVNLDNVKDWFAAGADAVGIGGELNKLASQGDFDLITEKAKKYMSSLRK 211
Eda COG0800
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ...
 3-211 1.61e-84

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: 249.23  E-value: 1.61e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349   3 KIEILTKLKANRLVLVVRGESSEEALACSLASIEGGIKTIEVTYTNPFASEVIGQLAERFkeDPEVLIGAGTVLDDVTAR 82
Cdd:COG0800     2 KMELLELLAAAPVVPVLRGDDPEDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEV--GPDALVGAGTVLTPEQAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349  83 QAILAGAQFIVGPNFNRAVALICHRYSIPYLPGCMTVNEVVTALESGVDMVKIFPGSTVGMSFIRAIKSPLPQVEVMVTG 162
Cdd:COG0800    80 AAIAAGARFIVSPGLDPEVIKAANRAGLPVLPGVATPTEIMAALEAGADAVKLFPAEALGPAYLKALKGPLPDVPFMPTG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1403507349 163 GVSSDNLKDWLAAGVDVLGIGGEF--NQLASQKQYNLITKKAAHYIKSLRQ 211
Cdd:COG0800   160 GVSPDNAADYLAAGAVAVGGGSWLvpKGAIAAGDWAAITERAREAVAAVRA 210
KDPG_aldolase cd00452
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ...
 10-201 2.52e-81

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: 240.11  E-value: 2.52e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349  10 LKANRLVLVVRGESSEEALACSLASIEGGIKTIEVTYTNPFASEVIGQLAERFkedPEVLIGAGTVLDDVTARQAILAGA 89
Cdd:cd00452     1 LKAQPLVAVLRGDDAEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEF---PEALIGAGTVLTPEQADAAIAAGA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349  90 QFIVGPNFNRAVALICHRYSIPYLPGCMTVNEVVTALESGVDMVKIFPGSTVGMSFIRAIKSPLPQVEVMVTGGVSSDNL 169
Cdd:cd00452    78 QFIVSPGLDPEVVKAANRAGIPLLPGVATPTEIMQALELGADIVKLFPAEAVGPAYIKALKGPFPQVRFMPTGGVSLDNA 157

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1403507349 170 KDWLAAGVDVLGIGGE-FNQLASQKQYNLITKK 201
Cdd:cd00452   158 AEWLAAGVVAVGGGSLlPKDAVAAGDWAAITAL 190
PRK07114 PRK07114
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
1-211 3.18e-55

bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;


Pssm-ID: 235939  Cd Length: 222  Bit Score: 175.21  E-value: 3.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349   1 MGKIEILTKLKANRLVLVVRGESSEEALACSLASIEGGIKTIEVTYTNPFASEVIGQLAERF-KEDPEVLIGAGTVLDDV 79
Cdd:PRK07114    3 FDRIAVLTAMKATGMVPVFYHADVEVAKKVIKACYDGGARVFEFTNRGDFAHEVFAELVKYAaKELPGMILGVGSIVDAA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349  80 TARQAILAGAQFIVGPNFNRAVALICHRYSIPYLPGCMTVNEVVTALESGVDMVKIFPGSTVGMSFIRAIKSPLPQVEVM 159
Cdd:PRK07114   83 TAALYIQLGANFIVTPLFNPDIAKVCNRRKVPYSPGCGSLSEIGYAEELGCEIVKLFPGSVYGPGFVKAIKGPMPWTKIM 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1403507349 160 VTGGVS--SDNLKDWLAAGVDVLGIGGEF--NQLASQKQYNLITKK---AAHYIKSLRQ 211
Cdd:PRK07114  163 PTGGVEptEENLKKWFGAGVTCVGMGSKLipKEALAAKDYAGIEQKvreALAIIKEVRK 221
eda TIGR01182
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ...
 6-202 1.31e-50

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: 162.87  E-value: 1.31e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349   6 ILTKLKANRLVLVVRGESSEEALACSLASIEGGIKTIEVTYTNPFASEVIGQLAerfKEDPEVLIGAGTVLDDVTARQAI 85
Cdd:TIGR01182   1 IEELLREAKIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLR---KEVPDALIGAGTVLNPEQLRQAV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349  86 LAGAQFIVGPNFNRAVALICHRYSIPYLPGCMTVNEVVTALESGVDMVKIFPGSTVG-MSFIRAIKSPLPQVEVMVTGGV 164
Cdd:TIGR01182  78 AAGAQFIVSPGLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAEVSGgVKMLKALAGPFPQVRFCPTGGI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1403507349 165 SSDNLKDWLAAGVDVLGIGGEF--NQLASQKQYNLITKKA 202
Cdd:TIGR01182 158 NLANARDYLALPNVACGGGSWLvpKDLIAAGDWDEITRLA 197
PRK05718 PRK05718
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
 3-203 6.32e-41

keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional


Pssm-ID: 235577  Cd Length: 212  Bit Score: 138.06  E-value: 6.32e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349   3 KIEILTKLKANRLVLVVRGESSEEALACSLASIEGGIKTIEVTYTNPFASEVIGQLAerfKEDPEVLIGAGTVLDDVTAR 82
Cdd:PRK05718    5 KTSIEEILRAGPVVPVIVINKLEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIA---KEVPEALIGAGTVLNPEQLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349  83 QAILAGAQFIVGPNFNRAVALICHRYSIPYLPGCMTVNEVVTALESGVDMVKIFPGSTV-GMSFIRAIKSPLPQVEVMVT 161
Cdd:PRK05718   82 QAIEAGAQFIVSPGLTPPLLKAAQEGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEASgGVKMLKALAGPFPDVRFCPT 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1403507349 162 GGVSSDNLKDWLAAGvDVLGIGGEF---NQLASQKQYNLITKKAA 203
Cdd:PRK05718  162 GGISPANYRDYLALP-NVLCIGGSWmvpKDAIENGDWDRITRLAR 205
PRK07455 PRK07455
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
7-185 7.99e-38

bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;


Pssm-ID: 180985  Cd Length: 187  Bit Score: 129.39  E-value: 7.99e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349   7 LTKLKANRLVLVVRGESSEEALACSLASIEGGIKTIEVTYTNPFASEVIGQLAERFkedPEVLIGAGTVLDDVTARQAIL 86
Cdd:PRK07455    6 LAQLQQHRAIAVIRAPDLELGLQMAEAVAAGGMRLIEITWNSDQPAELISQLREKL---PECIIGTGTILTLEDLEEAIA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349  87 AGAQFIVGPNFNRAVALICHRYSIPYLPGCMTVNEVVTALESGVDMVKIFPGSTV-GMSFIRAIKSPLPQVEVMVTGGVS 165
Cdd:PRK07455   83 AGAQFCFTPHVDPELIEAAVAQDIPIIPGALTPTEIVTAWQAGASCVKVFPVQAVgGADYIKSLQGPLGHIPLIPTGGVT 162

                         170       180
                  ....*....|....*....|
gi 1403507349 166 SDNLKDWLAAGVDVLGIGGE 185
Cdd:PRK07455  163 LENAQAFIQAGAIAVGLSGQ 182
Aldolase pfam01081
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ...
 6-184 9.12e-38

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: 129.52  E-value: 9.12e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349   6 ILTKLKANRLVLVVRGESSEEALACSLASIEGGIKTIEVTYTNPFASEVIGQLaerFKEDPEVLIGAGTVLDDVTARQAI 85
Cdd:pfam01081   1 IESILKEAKIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAIRLL---RKNRPDALVGAGTVLNAQQLAEAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349  86 LAGAQFIVGPNFNRAVALICHRYSIPYLPGCMTVNEVVTALESGVDMVKIFP-GSTVGMSFIRAIKSPLPQVEVMVTGGV 164
Cdd:pfam01081  78 EAGAQFVVSPGLTADLLKHAVDVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPaEASGGVPAIKALAGPFPQVRFCPTGGI 157

                         170       180
                  ....*....|....*....|
gi 1403507349 165 SSDNLKDWLAAGvDVLGIGG 184
Cdd:pfam01081 158 HPANVRDYLALP-NILCVGG 176
PRK09140 PRK09140
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed
 15-185 1.40e-37

2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed


Pssm-ID: 181670  Cd Length: 206  Bit Score: 129.56  E-value: 1.40e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349  15 LVLVVRGESSEEALACSLASIEGGIKTIEVTYTNPFASEVIGQLAERFKEDpeVLIGAGTVL--DDVTARQAilAGAQFI 92
Cdd:PRK09140   12 LIAILRGITPDEALAHVGALIEAGFRAIEIPLNSPDPFDSIAALVKALGDR--ALIGAGTVLspEQVDRLAD--AGGRLI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349  93 VGPNFNRAVALICHRYSIPYLPGCMTVNEVVTALESGVDMVKIFPGSTVGMSFIRAIKSPLP-QVEVMVTGGVSSDNLKD 171
Cdd:PRK09140   88 VTPNTDPEVIRRAVALGMVVMPGVATPTEAFAALRAGAQALKLFPASQLGPAGIKALRAVLPpDVPVFAVGGVTPENLAP 167

                         170
                  ....*....|....
gi 1403507349 172 WLAAGVDVLGIGGE 185
Cdd:PRK09140  168 YLAAGAAGFGLGSA 181
PRK06015 PRK06015
2-dehydro-3-deoxy-phosphogluconate aldolase;
10-203 1.43e-24

2-dehydro-3-deoxy-phosphogluconate aldolase;


Pssm-ID: 168348  Cd Length: 201  Bit Score: 95.65  E-value: 1.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349  10 LKANRLVLVVRGESSEEALACSLASIEGGIKTIEVTYTNPFASEVIGQLAErfkEDPEVLIGAGTVLDDVTARQAILAGA 89
Cdd:PRK06015    1 LKLQPVIPVLLIDDVEHAVPLARALAAGGLPAIEITLRTPAALDAIRAVAA---EVEEAIVGAGTILNAKQFEDAAKAGS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349  90 QFIVGPNFNRAVALICHRYSIPYLPGCMTVNEVVTALESGVDMVKIFPGSTV-GMSFIRAIKSPLPQVEVMVTGGVSSDN 168
Cdd:PRK06015   78 RFIVSPGTTQELLAAANDSDVPLLPGAATPSEVMALREEGYTVLKFFPAEQAgGAAFLKALSSPLAGTFFCPTGGISLKN 157

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1403507349 169 LKDWLAAGvDVLGIGGEF---NQLASQKQYNLITKKAA 203
Cdd:PRK06015  158 ARDYLSLP-NVVCVGGSWvapKELVAAGDWAGITKLAA 194
QRPTase_C pfam01729
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ...
 116-183 2.18e-03

Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl transferase (QPRTase) or nicotinate-nucleotide pyrophosphorylase EC:2.4.2.19 is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyzes the reaction of quinolinic acid with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to give rise to nicotinic acid mononucleotide (NaMN), pyrophosphate and carbon dioxide. The QA substrate is bound between the C-terminal domain of one subunit, and the N-terminal domain of the other. The C-terminal domain has a 7 beta-stranded TIM barrel-like fold.


Pssm-ID: 396337  Cd Length: 169  Bit Score: 37.29  E-value: 2.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349 116 CMTVNEVVTALESGVDMVKI--FPGSTVGMsFIRAIKSPLPQVEVMVTGGVSSDNLKDWLAAGVDVLGIG 183
Cdd:pfam01729  87 VESLEEAEEALEAGADIIMLdnFSPEEVKK-AVEELDERNPRVLLEVSGGVTLDNVLEYAKTGVDVISVG 155
Aldolase_Class_I cd00945
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ...
 35-183 3.57e-03

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: 36.92  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349  35 IEGGIKTIEVTYtnpfasEVIGQLAERFKEDPEVL---IGAGTVLDDV-----TARQAILAGAQFI-VGPNF-------- 97
Cdd:cd00945    23 IEYGFAAVCVNP------GYVRLAADALAGSDVPVivvVGFPTGLTTTevkvaEVEEAIDLGADEIdVVINIgslkegdw 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403507349  98 ------NRAVALIChRYSIP-----YLPGCMTVNEVVTA----LESGVDMVKIFPGSTVGM----SFIRAIKSPLPQVEV 158
Cdd:cd00945    97 eevleeIAAVVEAA-DGGLPlkvilETRGLKTADEIAKAariaAEAGADFIKTSTGFGGGGatveDVKLMKEAVGGRVGV 175

                         170       180
                  ....*....|....*....|....*.
gi 1403507349 159 MVTGGVSS-DNLKDWLAAGVDVLGIG 183
Cdd:cd00945   176 KAAGGIKTlEDALAAIEAGADGIGTS 201
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 121-183 8.89e-03

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 36.49  E-value: 8.89e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1403507349 121 EVVTAL-ESGVDM--VKIFPG-STVGMSFIRAIKSPLPQVEVMVTGGVSSDNLKDWLAAGVDVLGIG 183
Cdd:PTZ00314  244 ERAAALiEAGVDVlvVDSSQGnSIYQIDMIKKLKSNYPHVDIIAGNVVTADQAKNLIDAGADGLRIG 310
 
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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