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Conserved domains on  [gi|1468758365|gb|AXT28916|]
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2-dehydro-3-deoxy-6-phosphogalactonate aldolase (plasmid) [Ruegeria sp. AD91A]

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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK09140 PRK09140
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed
 1-199 1.55e-103

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


:

Pssm-ID: 181670  Cd Length: 206  Bit Score: 296.74  E-value: 1.55e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365   1 MSRPIIAILRGLKPQEAKAVGRTIIDAGIDRIEVPLNSPDPLDSIGTLVDAFGNQALIGAGTVLTVDQVDAVSAAGGKLI 80
Cdd:PRK09140    8 TKLPLIAILRGITPDEALAHVGALIEAGFRAIEIPLNSPDPFDSIAALVKALGDRALIGAGTVLSPEQVDRLADAGGRLI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365  81 VSPNYDAEVIKRSVALGLQSWPGVYTPTEAFAALKAGATGLKLFPGVMAGPAGLAALRPVLPTSSLVFAVGGAGPDNFAQ 160
Cdd:PRK09140   88 VTPNTDPEVIRRAVALGMVVMPGVATPTEAFAALRAGAQALKLFPASQLGPAGIKALRAVLPPDVPVFAVGGVTPENLAP 167

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1468758365 161 WIKAGADGFGIGSALYKPGIDVAEIAERARHIVTAFDEA 199
Cdd:PRK09140  168 YLAAGAAGFGLGSALYRPGQSAEEVAERARAFVAAYREA 206
 
Name Accession Description Interval E-value
PRK09140 PRK09140
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed
 1-199 1.55e-103

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


Pssm-ID: 181670  Cd Length: 206  Bit Score: 296.74  E-value: 1.55e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365   1 MSRPIIAILRGLKPQEAKAVGRTIIDAGIDRIEVPLNSPDPLDSIGTLVDAFGNQALIGAGTVLTVDQVDAVSAAGGKLI 80
Cdd:PRK09140    8 TKLPLIAILRGITPDEALAHVGALIEAGFRAIEIPLNSPDPFDSIAALVKALGDRALIGAGTVLSPEQVDRLADAGGRLI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365  81 VSPNYDAEVIKRSVALGLQSWPGVYTPTEAFAALKAGATGLKLFPGVMAGPAGLAALRPVLPTSSLVFAVGGAGPDNFAQ 160
Cdd:PRK09140   88 VTPNTDPEVIRRAVALGMVVMPGVATPTEAFAALRAGAQALKLFPASQLGPAGIKALRAVLPPDVPVFAVGGVTPENLAP 167

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1468758365 161 WIKAGADGFGIGSALYKPGIDVAEIAERARHIVTAFDEA 199
Cdd:PRK09140  168 YLAAGAAGFGLGSALYRPGQSAEEVAERARAFVAAYREA 206
Eda COG0800
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ...
 1-201 2.10e-74

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: 223.04  E-value: 2.10e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365   1 MSRPIIAILRGLKPQEAKAVGRTIIDAGIDRIEVPLNSPDPLDSIGTLVDAFGNQALIGAGTVLTVDQVDAVSAAGGKLI 80
Cdd:COG0800    10 AAAPVVPVLRGDDPEDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEVGPDALVGAGTVLTPEQARAAIAAGARFI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365  81 VSPNYDAEVIKRSVALGLQSWPGVYTPTEAFAALKAGATGLKLFPGVMAGPAGLAALRPVLPTSSLVfAVGGAGPDNFAQ 160
Cdd:COG0800    90 VSPGLDPEVIKAANRAGLPVLPGVATPTEIMAALEAGADAVKLFPAEALGPAYLKALKGPLPDVPFM-PTGGVSPDNAAD 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1468758365 161 WIKAGADGFGIGSALYKPGI----DVAEIAERARHIVTAFDEAAG 201
Cdd:COG0800   169 YLAAGAVAVGGGSWLVPKGAiaagDWAAITERAREAVAAVRAARA 213
KDPG_aldolase cd00452
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ...
 4-188 2.87e-54

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: 171.16  E-value: 2.87e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365   4 PIIAILRGLKPQEAKAVGRTIIDAGIDRIEVPLNSPDPLDSIGTLVDAFGNqALIGAGTVLTVDQVDAVSAAGGKLIVSP 83
Cdd:cd00452     5 PLVAVLRGDDAEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFPE-ALIGAGTVLTPEQADAAIAAGAQFIVSP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365  84 NYDAEVIKRSVALGLQSWPGVYTPTEAFAALKAGATGLKLFPGVMAGPAGLAALRPVLPTSSLVfAVGGAGPDNFAQWIK 163
Cdd:cd00452    84 GLDPEVVKAANRAGIPLLPGVATPTEIMQALELGADIVKLFPAEAVGPAYIKALKGPFPQVRFM-PTGGVSLDNAAEWLA 162

                         170       180
                  ....*....|....*....|....*...
gi 1468758365 164 AGADGFGIGSALYKPGI---DVAEIAER 188
Cdd:cd00452   163 AGVVAVGGGSLLPKDAVaagDWAAITAL 190
eda TIGR01182
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ...
 4-190 2.73e-29

Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an enzyme of the Entner-Doudoroff pathway. This aldolase has another function, 4-hydroxy-2-oxoglutarate aldolase (EC 4.1.3.16) shown experimentally in Escherichia coli and Pseudomonas putida [Amino acid biosynthesis, Glutamate family, Energy metabolism, Entner-Doudoroff]


Pssm-ID: 273490  Cd Length: 204  Bit Score: 107.78  E-value: 2.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365   4 PIIAILRGLKPQEAKAVGRTIIDAGIDRIEVPLNSPDPLDSIGTLVDAFGNqALIGAGTVLTVDQVDAVSAAGGKLIVSP 83
Cdd:TIGR01182   9 KIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEVPD-ALIGAGTVLNPEQLRQAVAAGAQFIVSP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365  84 NYDAEVIKRSVALGLQSWPGVYTPTEAFAALKAGATGLKLFPG-VMAGPAGLAALRPVLPTSSLVfAVGGAGPDNFAQWI 162
Cdd:TIGR01182  88 GLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAeVSGGVKMLKALAGPFPQVRFC-PTGGINLANARDYL 166

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1468758365 163 KAGADGFGIGSALYKPGI----DVAEIAERAR 190
Cdd:TIGR01182 167 ALPNVACGGGSWLVPKDLiaagDWDEITRLAR 198
Aldolase pfam01081
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ...
 4-175 1.19e-19

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: 82.52  E-value: 1.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365   4 PIIAILRGLKPQEAKAVGRTIIDAGIDRIEVPLNSPDPLDSIGTLVdAFGNQALIGAGTVLTVDQVDAVSAAGGKLIVSP 83
Cdd:pfam01081   9 KIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAIRLLR-KNRPDALVGAGTVLNAQQLAEAAEAGAQFVVSP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365  84 NYDAEVIKRSVALGLQSWPGVYTPTEAFAALKAGATGLKLFPGVMAGpaGLAALRPVL-PTSSLVFA-VGGAGPDNFAQW 161
Cdd:pfam01081  88 GLTADLLKHAVDVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPAEASG--GVPAIKALAgPFPQVRFCpTGGIHPANVRDY 165

                         170
                  ....*....|....
gi 1468758365 162 IKAGADGFGIGSAL 175
Cdd:pfam01081 166 LALPNILCVGGSWL 179
 
Name Accession Description Interval E-value
PRK09140 PRK09140
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed
 1-199 1.55e-103

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


Pssm-ID: 181670  Cd Length: 206  Bit Score: 296.74  E-value: 1.55e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365   1 MSRPIIAILRGLKPQEAKAVGRTIIDAGIDRIEVPLNSPDPLDSIGTLVDAFGNQALIGAGTVLTVDQVDAVSAAGGKLI 80
Cdd:PRK09140    8 TKLPLIAILRGITPDEALAHVGALIEAGFRAIEIPLNSPDPFDSIAALVKALGDRALIGAGTVLSPEQVDRLADAGGRLI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365  81 VSPNYDAEVIKRSVALGLQSWPGVYTPTEAFAALKAGATGLKLFPGVMAGPAGLAALRPVLPTSSLVFAVGGAGPDNFAQ 160
Cdd:PRK09140   88 VTPNTDPEVIRRAVALGMVVMPGVATPTEAFAALRAGAQALKLFPASQLGPAGIKALRAVLPPDVPVFAVGGVTPENLAP 167

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1468758365 161 WIKAGADGFGIGSALYKPGIDVAEIAERARHIVTAFDEA 199
Cdd:PRK09140  168 YLAAGAAGFGLGSALYRPGQSAEEVAERARAFVAAYREA 206
Eda COG0800
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ...
 1-201 2.10e-74

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: 223.04  E-value: 2.10e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365   1 MSRPIIAILRGLKPQEAKAVGRTIIDAGIDRIEVPLNSPDPLDSIGTLVDAFGNQALIGAGTVLTVDQVDAVSAAGGKLI 80
Cdd:COG0800    10 AAAPVVPVLRGDDPEDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEVGPDALVGAGTVLTPEQARAAIAAGARFI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365  81 VSPNYDAEVIKRSVALGLQSWPGVYTPTEAFAALKAGATGLKLFPGVMAGPAGLAALRPVLPTSSLVfAVGGAGPDNFAQ 160
Cdd:COG0800    90 VSPGLDPEVIKAANRAGLPVLPGVATPTEIMAALEAGADAVKLFPAEALGPAYLKALKGPLPDVPFM-PTGGVSPDNAAD 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1468758365 161 WIKAGADGFGIGSALYKPGI----DVAEIAERARHIVTAFDEAAG 201
Cdd:COG0800   169 YLAAGAVAVGGGSWLVPKGAiaagDWAAITERAREAVAAVRAARA 213
KDPG_aldolase cd00452
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ...
 4-188 2.87e-54

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: 171.16  E-value: 2.87e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365   4 PIIAILRGLKPQEAKAVGRTIIDAGIDRIEVPLNSPDPLDSIGTLVDAFGNqALIGAGTVLTVDQVDAVSAAGGKLIVSP 83
Cdd:cd00452     5 PLVAVLRGDDAEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFPE-ALIGAGTVLTPEQADAAIAAGAQFIVSP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365  84 NYDAEVIKRSVALGLQSWPGVYTPTEAFAALKAGATGLKLFPGVMAGPAGLAALRPVLPTSSLVfAVGGAGPDNFAQWIK 163
Cdd:cd00452    84 GLDPEVVKAANRAGIPLLPGVATPTEIMQALELGADIVKLFPAEAVGPAYIKALKGPFPQVRFM-PTGGVSLDNAAEWLA 162

                         170       180
                  ....*....|....*....|....*...
gi 1468758365 164 AGADGFGIGSALYKPGI---DVAEIAER 188
Cdd:cd00452   163 AGVVAVGGGSLLPKDAVaagDWAAITAL 190
PRK06552 PRK06552
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
 5-199 3.29e-38

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


Pssm-ID: 180618  Cd Length: 213  Bit Score: 130.89  E-value: 3.29e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365   5 IIAILRGLKPQEAKAVGRTIIDAGIDRIEVPLNSPDPLDSIGTLVDAFGNQA--LIGAGTVLtvdqvDAVSA-----AGG 77
Cdd:PRK06552   15 VVAVVRGESKEEALKISLAVIKGGIKAIEVTYTNPFASEVIKELVELYKDDPevLIGAGTVL-----DAVTArlailAGA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365  78 KLIVSPNYDAEVIKRSVALGLQSWPGVYTPTEAFAALKAGATGLKLFPGVMAGPAGLAALRPVLPTSSlVFAVGGAGPDN 157
Cdd:PRK06552   90 QFIVSPSFNRETAKICNLYQIPYLPGCMTVTEIVTALEAGSEIVKLFPGSTLGPSFIKAIKGPLPQVN-VMVTGGVNLDN 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1468758365 158 FAQWIKAGADGFGIGSALYKPGI--DVAEIAERARHIVTAFDEA 199
Cdd:PRK06552  169 VKDWFAAGADAVGIGGELNKLASqgDFDLITEKAKKYMSSLRKA 212
eda TIGR01182
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ...
 4-190 2.73e-29

Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an enzyme of the Entner-Doudoroff pathway. This aldolase has another function, 4-hydroxy-2-oxoglutarate aldolase (EC 4.1.3.16) shown experimentally in Escherichia coli and Pseudomonas putida [Amino acid biosynthesis, Glutamate family, Energy metabolism, Entner-Doudoroff]


Pssm-ID: 273490  Cd Length: 204  Bit Score: 107.78  E-value: 2.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365   4 PIIAILRGLKPQEAKAVGRTIIDAGIDRIEVPLNSPDPLDSIGTLVDAFGNqALIGAGTVLTVDQVDAVSAAGGKLIVSP 83
Cdd:TIGR01182   9 KIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEVPD-ALIGAGTVLNPEQLRQAVAAGAQFIVSP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365  84 NYDAEVIKRSVALGLQSWPGVYTPTEAFAALKAGATGLKLFPG-VMAGPAGLAALRPVLPTSSLVfAVGGAGPDNFAQWI 162
Cdd:TIGR01182  88 GLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAeVSGGVKMLKALAGPFPQVRFC-PTGGINLANARDYL 166

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1468758365 163 KAGADGFGIGSALYKPGI----DVAEIAERAR 190
Cdd:TIGR01182 167 ALPNVACGGGSWLVPKDLiaagDWDEITRLAR 198
PRK07455 PRK07455
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
5-178 9.67e-25

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


Pssm-ID: 180985  Cd Length: 187  Bit Score: 95.49  E-value: 9.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365   5 IIAILRGLKPQEAKAVGRTIIDAGIDRIEVPLNSPDPLDSIGTLVDAFgNQALIGAGTVLTVDQVDAVSAAGGKLIVSPN 84
Cdd:PRK07455   14 AIAVIRAPDLELGLQMAEAVAAGGMRLIEITWNSDQPAELISQLREKL-PECIIGTGTILTLEDLEEAIAAGAQFCFTPH 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365  85 YDAEVIKRSVALGLQSWPGVYTPTEAFAALKAGATGLKLFP-GVMAGPAGLAALRPVLPTSSLvFAVGGAGPDNFAQWIK 163
Cdd:PRK07455   93 VDPELIEAAVAQDIPIIPGALTPTEIVTAWQAGASCVKVFPvQAVGGADYIKSLQGPLGHIPL-IPTGGVTLENAQAFIQ 171

                         170
                  ....*....|....*
gi 1468758365 164 AGADGFGIGSALYKP 178
Cdd:PRK07455  172 AGAIAVGLSGQLFPK 186
Aldolase pfam01081
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ...
 4-175 1.19e-19

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: 82.52  E-value: 1.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365   4 PIIAILRGLKPQEAKAVGRTIIDAGIDRIEVPLNSPDPLDSIGTLVdAFGNQALIGAGTVLTVDQVDAVSAAGGKLIVSP 83
Cdd:pfam01081   9 KIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAIRLLR-KNRPDALVGAGTVLNAQQLAEAAEAGAQFVVSP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365  84 NYDAEVIKRSVALGLQSWPGVYTPTEAFAALKAGATGLKLFPGVMAGpaGLAALRPVL-PTSSLVFA-VGGAGPDNFAQW 161
Cdd:pfam01081  88 GLTADLLKHAVDVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPAEASG--GVPAIKALAgPFPQVRFCpTGGIHPANVRDY 165

                         170
                  ....*....|....
gi 1468758365 162 IKAGADGFGIGSAL 175
Cdd:pfam01081 166 LALPNILCVGGSWL 179
PRK05718 PRK05718
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
 4-157 2.18e-19

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


Pssm-ID: 235577  Cd Length: 212  Bit Score: 81.83  E-value: 2.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365   4 PIIAILrglKPQEAKAVGRTIIDAGIDRIEVPLNSPDPLDSIGTLVDAFGNqALIGAGTVLTVDQVDAVSAAGGKLIVSP 83
Cdd:PRK05718   19 PVIVIN---KLEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIAKEVPE-ALIGAGTVLNPEQLAQAIEAGAQFIVSP 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1468758365  84 NYDAEVIKRSVALGLQSWPGVYTPTEAFAALKAGATGLKLFPGVMAGpaGLAALRPVL-PTSSLVFA-VGGAGPDN 157
Cdd:PRK05718   95 GLTPPLLKAAQEGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEASG--GVKMLKALAgPFPDVRFCpTGGISPAN 168
PRK06015 PRK06015
2-dehydro-3-deoxy-phosphogluconate aldolase;
3-132 1.13e-12

2-dehydro-3-deoxy-phosphogluconate aldolase;


Pssm-ID: 168348  Cd Length: 201  Bit Score: 63.68  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365   3 RPIIAILRGLKPQEAKAVGRTIIDAGIDRIEVPLNSPDPLDSIGTLVDAFgNQALIGAGTVLTVDQVDAVSAAGGKLIVS 82
Cdd:PRK06015    4 QPVIPVLLIDDVEHAVPLARALAAGGLPAIEITLRTPAALDAIRAVAAEV-EEAIVGAGTILNAKQFEDAAKAGSRFIVS 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1468758365  83 PNYDAEVIKRSVALGLQSWPGVYTPTEAFAALKAGATGLKLFPGVMAGPA 132
Cdd:PRK06015   83 PGTTQELLAAANDSDVPLLPGAATPSEVMALREEGYTVLKFFPAEQAGGA 132
PRK07114 PRK07114
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
58-199 3.09e-10

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


Pssm-ID: 235939  Cd Length: 222  Bit Score: 57.34  E-value: 3.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365  58 IGAGTVltvdqVDAVSAA-----GGKLIVSPNYDAEVIK----RSVAlglqsW-PGVYTPTEAFAALKAGATGLKLFPGV 127
Cdd:PRK07114   73 LGVGSI-----VDAATAAlyiqlGANFIVTPLFNPDIAKvcnrRKVP-----YsPGCGSLSEIGYAEELGCEIVKLFPGS 142

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1468758365 128 MAGPAGLAALRPVLPTSSLVfAVGGAGP--DNFAQWIKAGADGFGIGSALYKPGI----DVAEIAERARHIVTAFDEA 199
Cdd:PRK07114  143 VYGPGFVKAIKGPMPWTKIM-PTGGVEPteENLKKWFGAGVTCVGMGSKLIPKEAlaakDYAGIEQKVREALAIIKEV 219
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 104-199 1.57e-05

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: 44.02  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365 104 VYTPTEAFAALKAGA----------TGLKLFPGVMAGPAGLAALRPVLPTSslVFAVGGAGPDNFAQWIKAGADGFGIGS 173
Cdd:COG0352   107 CHSLEEALRAEEAGAdyvgfgpvfpTPTKPGAPPPLGLEGLAWWAELVEIP--VVAIGGITPENAAEVLAAGADGVAVIS 184

                          90       100
                  ....*....|....*....|....*.
gi 1468758365 174 ALYkpgiDVAEIAERARHIVTAFDEA 199
Cdd:COG0352   185 AIW----GAPDPAAAARELRAALEAA 206
thiE PRK00043
thiamine phosphate synthase;
104-200 6.98e-05

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 42.09  E-value: 6.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365 104 VYTPTEAFAALKAGA----------TGLKLFPGVMAGPAGLAALR---PVLPtsslVFAVGGAGPDNFAQWIKAGADGFG 170
Cdd:PRK00043  111 THTLEEAAAALAAGAdyvgvgpifpTPTKKDAKAPQGLEGLREIRaavGDIP----IVAIGGITPENAPEVLEAGADGVA 186

                          90       100       110
                  ....*....|....*....|....*....|
gi 1468758365 171 IGSALYkpgiDVAEIAERARHIVTAFDEAA 200
Cdd:PRK00043  187 VVSAIT----GAEDPEAAARALLAAFRAAR 212
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 104-177 2.43e-04

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: 40.19  E-value: 2.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365 104 VYTPTEAFAALKAGA----------TGLKlfPGVMAgPAGLAALRPVLPTSSL-VFAVGGAGPDNFAQWIKAGADGFGIG 172
Cdd:cd00564   102 THSLEEALRAEELGAdyvgfgpvfpTPTK--PGAGP-PLGLELLREIAELVEIpVVAIGGITPENAAEVLAAGADGVAVI 178


                  ....*
gi 1468758365 173 SALYK 177
Cdd:cd00564   179 SAITG 183
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
 104-175 1.82e-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: 37.53  E-value: 1.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1468758365 104 VYTPTEAFAALKAGATGL---KLFPG---VMAGPAGLAALRPVLPTSSL-VFAVGGAGPDNFAQWIKAGADGFGIGSAL 175
Cdd:pfam02581 102 THTLEEALEAEALGADYIgfgPIFPTptkPDAPPLGLEGLKAIAEAVEIpVVAIGGITPENVPEVIEAGADGVAVVSAI 180
PRK07695 PRK07695
thiazole tautomerase TenI;
104-176 5.32e-03

thiazole tautomerase TenI;


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 36.54  E-value: 5.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468758365 104 VYTPTEAFAALKAGA----------TGLKlfPGVMagPAGLAALRPVLPTSSL-VFAVGGAGPDNFAQWIKAGADGFGIG 172
Cdd:PRK07695  102 VHSLEEAIQAEKNGAdyvvyghvfpTDCK--KGVP--ARGLEELSDIARALSIpVIAIGGITPENTRDVLAAGVSGIAVM 177


                  ....
gi 1468758365 173 SALY 176
Cdd:PRK07695  178 SGIF 181
modD_like cd01573
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ...
 104-176 8.02e-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: 36.12  E-value: 8.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1468758365 104 VYTPTEAFAALKAGATGLKL--FPgvmagPAGLAALRPVL---PTSSLVFAVGGAGPDNFAQWIKAGADGFgIGSALY 176
Cdd:cd01573   190 VDSLEEALAAAEAGADILQLdkFS-----PEELAELVPKLrslAPPVLLAAAGGINIENAAAYAAAGADIL-VTSAPY 261
 
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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