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Conserved domains on  [gi|15599323|ref|NP_252817|]
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2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase [Pseudomonas aeruginosa PAO1]

Protein Classification

HpcH/HpaI aldolase/citrate lyase family protein( domain architecture ID 10020697)

HpcH/HpaI aldolase/citrate lyase family protein similar to Salmonella enterica 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase HpcH (also known as HpaI) which may catalyzes the reversible retro-aldol cleavage of 4-hydroxy-2-ketoheptane-1,7-dioate to pyruvate and succinic semialdehyde

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HpaI TIGR02311
2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase; This model represents the aldolase which ...
6-254 8.08e-150

2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase; This model represents the aldolase which performs the final step unique to the 4-hydroxyphenylacetic acid catabolism pathway in which 2,4-dihydroxyhept-2-ene-1,7-dioic acid is split into pyruvate and succinate-semialdehyde. The gene for enzyme is generally found adjacent to other genes for this pathway organized into an operon.


:

Pssm-ID: 131364  Cd Length: 249  Bit Score: 418.41  E-value: 8.08e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323     6 NRFKQRLRSGEAQIGLWLGLADPYCAELAANAGFDWLLLDGEHAPNDLRSLLGQLQALAPYPGQPVIRPVQGDTALIKQL 85
Cdd:TIGR02311   1 NQFKQALKEGQPQIGLWLGLADPYAAEICAGAGFDWLLIDGEHAPNDVRTILSQLQALAPYPSSPVVRPAIGDPVLIKQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323    86 LDIGAQTLLVPMVDSAAQAEGLVRAVRYPPAGVRGVGSALARASRWNSVAEYLNHADEQMCLLVQVENLEGLANLDAIAA 165
Cdd:TIGR02311  81 LDIGAQTLLVPMIETAEQAEAAVAATRYPPMGIRGVGSALARASRWNRIPDYLQQADEEICVLLQVETREALDNLEEIAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323   166 VEGVDGVFIGPADLSAAMGHRGNPGHPEVQAAIEDAIHRIRTAGKAAGILSADETLARRYLELGCAFVAVGVDTSLLMRS 245
Cdd:TIGR02311 161 VEGVDGVFIGPADLAASMGHLGNPSHPEVQAAIDDAIERIKAAGKAAGILTADPKLARQYLKLGALFVAVGVDTTLLARG 240

                  ....*....
gi 15599323   246 LRELAGRFK 254
Cdd:TIGR02311 241 AEALAARFK 249
 
Name Accession Description Interval E-value
HpaI TIGR02311
2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase; This model represents the aldolase which ...
6-254 8.08e-150

2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase; This model represents the aldolase which performs the final step unique to the 4-hydroxyphenylacetic acid catabolism pathway in which 2,4-dihydroxyhept-2-ene-1,7-dioic acid is split into pyruvate and succinate-semialdehyde. The gene for enzyme is generally found adjacent to other genes for this pathway organized into an operon.


Pssm-ID: 131364  Cd Length: 249  Bit Score: 418.41  E-value: 8.08e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323     6 NRFKQRLRSGEAQIGLWLGLADPYCAELAANAGFDWLLLDGEHAPNDLRSLLGQLQALAPYPGQPVIRPVQGDTALIKQL 85
Cdd:TIGR02311   1 NQFKQALKEGQPQIGLWLGLADPYAAEICAGAGFDWLLIDGEHAPNDVRTILSQLQALAPYPSSPVVRPAIGDPVLIKQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323    86 LDIGAQTLLVPMVDSAAQAEGLVRAVRYPPAGVRGVGSALARASRWNSVAEYLNHADEQMCLLVQVENLEGLANLDAIAA 165
Cdd:TIGR02311  81 LDIGAQTLLVPMIETAEQAEAAVAATRYPPMGIRGVGSALARASRWNRIPDYLQQADEEICVLLQVETREALDNLEEIAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323   166 VEGVDGVFIGPADLSAAMGHRGNPGHPEVQAAIEDAIHRIRTAGKAAGILSADETLARRYLELGCAFVAVGVDTSLLMRS 245
Cdd:TIGR02311 161 VEGVDGVFIGPADLAASMGHLGNPSHPEVQAAIDDAIERIKAAGKAAGILTADPKLARQYLKLGALFVAVGVDTTLLARG 240

                  ....*....
gi 15599323   246 LRELAGRFK 254
Cdd:TIGR02311 241 AEALAARFK 249
HpcH COG3836
2-keto-3-deoxy-L-rhamnonate aldolase RhmA [Carbohydrate transport and metabolism];
3-240 5.58e-124

2-keto-3-deoxy-L-rhamnonate aldolase RhmA [Carbohydrate transport and metabolism];


Pssm-ID: 443047 [Multi-domain]  Cd Length: 237  Bit Score: 352.49  E-value: 5.58e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323   3 LPVNRFKQRLRSGEAQIGLWLGLADPYCAELAANAGFDWLLLDGEHAPNDLRSLLGQLQALAPYPGQPVIRPVQGDTALI 82
Cdd:COG3836   1 MRKNRLKQRLRAGEPVIGTWLSLPSPAVAEILAGAGFDWVLIDLEHGPNDLETLLALLRAAAAAGVAPLVRVPSNDPALI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323  83 KQLLDIGAQTLLVPMVDSAAQAEGLVRAVRYPPAGVRGVGsALARASRWNSVAEYLNHADEQMCLLVQVENLEGLANLDA 162
Cdd:COG3836  81 KRALDAGAQGVLVPMVETAEEARAAVAATRYPPLGIRGVG-GPARAARYGRVADYLARANDETLVIVQIETAEAVENLDE 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599323 163 IAAVEGVDGVFIGPADLSAAMGHRGNPGHPEVQAAIEDAIHRIRTAGKAAGILSADETLARRYLELGCAFVAVGVDTS 240
Cdd:COG3836 160 IAAVPGVDGVFIGPADLSASLGHPGQPDHPEVQAAIERVIAAARAAGKPAGILAGDPEDARRYIALGARFVAVGSDVG 237
PRK10128 PRK10128
2-keto-3-deoxy-L-rhamnonate aldolase; Provisional
2-265 3.91e-117

2-keto-3-deoxy-L-rhamnonate aldolase; Provisional


Pssm-ID: 182257  Cd Length: 267  Bit Score: 336.53  E-value: 3.91e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323    2 DLPVNRFKQRLRSGEAQIGLWLGLADPYCAELAANAGFDWLLLDGEHAPNDLRSLLGQLQALAPYPGQPVIRPVQGDTAL 81
Cdd:PRK10128   3 ALLSNPFKEGLRKGEVQIGLWLSSTTSYMAEIAATSGYDWLLIDGEHAPNTIQDLYHQLQAIAPYASQPVIRPVEGSKPL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323   82 IKQLLDIGAQTLLVPMVDSAAQAEGLVRAVRYPPAGVRGVGSALARASRWNSVAEYLNHADEQMCLLVQVENLEGLANLD 161
Cdd:PRK10128  83 IKQVLDIGAQTLLIPMVDTAEQARQVVSATRYPPYGERGVGASVARAARWGRIENYMAQANDSLCLLVQVESKTALDNLD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323  162 AIAAVEGVDGVFIGPADLSAAMGHRGNPGHPEVQAAIEDAIHRIRTAGKAAGILSADETLARRYLELGCAFVAVGVDTSL 241
Cdd:PRK10128 163 EILDVEGIDGVFIGPADLSASLGYPDNAGHPEVQRIIETSIRRIRAAGKAAGFLAVDPDMAQKCLAWGANFVAVGVDTML 242
                        250       260
                 ....*....|....*....|....
gi 15599323  242 LMRSLRELAGRFKGGAPAPSASSS 265
Cdd:PRK10128 243 YTDALDQRLAMFKSGKNGPRAKGS 266
HpcH_HpaI pfam03328
HpcH/HpaI aldolase/citrate lyase family; This family includes 2,4-dihydroxyhept-2-ene-1, ...
18-242 1.76e-65

HpcH/HpaI aldolase/citrate lyase family; This family includes 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase and 4-hydroxy-2-oxovalerate aldolase.


Pssm-ID: 427247 [Multi-domain]  Cd Length: 221  Bit Score: 203.35  E-value: 1.76e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323    18 QIGLWLGLADPYCAELAANAGFDWLLLDGEHAP---------NDLRSLLGQLQALAPYPGQPVIRPVQGDTALIKQ---L 85
Cdd:pfam03328   1 RSGLFLPGANPAMAEIAAIAGADWVVIDLEDAValaekdaarVLVPTALQQLDALAAAPSEVVVRVNSLDSPFGKQdlaV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323    86 LDIGAQTLLVPMVDSAAQAEGLVRAVRYPPAGVRGvgsalarasrwnsvaeylnhADEQMCLLVQVENLEGLANLDAIAA 165
Cdd:pfam03328  81 LDLGAQVVLVPKVETAEDARAAVSAIRYPPKGIRR--------------------ANGNTCLLAQIESALGVLNADEIAA 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323   166 VEGVDGVFIGPADLSAAMGHRGNPGHPEVQAAIEdaihRIRTAGKAAGI-----LSADETLARRYLELGCAFVAVGVDTS 240
Cdd:pfam03328 141 VEGVDGIFLGAEDLSADLGTLRSPGGPEVLYARE----RIVTAARAAGIaafdtVYSDENDAEGFLAEGALFVALGFDGK 216

                  ..
gi 15599323   241 LL 242
Cdd:pfam03328 217 LL 218
 
Name Accession Description Interval E-value
HpaI TIGR02311
2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase; This model represents the aldolase which ...
6-254 8.08e-150

2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase; This model represents the aldolase which performs the final step unique to the 4-hydroxyphenylacetic acid catabolism pathway in which 2,4-dihydroxyhept-2-ene-1,7-dioic acid is split into pyruvate and succinate-semialdehyde. The gene for enzyme is generally found adjacent to other genes for this pathway organized into an operon.


Pssm-ID: 131364  Cd Length: 249  Bit Score: 418.41  E-value: 8.08e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323     6 NRFKQRLRSGEAQIGLWLGLADPYCAELAANAGFDWLLLDGEHAPNDLRSLLGQLQALAPYPGQPVIRPVQGDTALIKQL 85
Cdd:TIGR02311   1 NQFKQALKEGQPQIGLWLGLADPYAAEICAGAGFDWLLIDGEHAPNDVRTILSQLQALAPYPSSPVVRPAIGDPVLIKQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323    86 LDIGAQTLLVPMVDSAAQAEGLVRAVRYPPAGVRGVGSALARASRWNSVAEYLNHADEQMCLLVQVENLEGLANLDAIAA 165
Cdd:TIGR02311  81 LDIGAQTLLVPMIETAEQAEAAVAATRYPPMGIRGVGSALARASRWNRIPDYLQQADEEICVLLQVETREALDNLEEIAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323   166 VEGVDGVFIGPADLSAAMGHRGNPGHPEVQAAIEDAIHRIRTAGKAAGILSADETLARRYLELGCAFVAVGVDTSLLMRS 245
Cdd:TIGR02311 161 VEGVDGVFIGPADLAASMGHLGNPSHPEVQAAIDDAIERIKAAGKAAGILTADPKLARQYLKLGALFVAVGVDTTLLARG 240

                  ....*....
gi 15599323   246 LRELAGRFK 254
Cdd:TIGR02311 241 AEALAARFK 249
HpcH COG3836
2-keto-3-deoxy-L-rhamnonate aldolase RhmA [Carbohydrate transport and metabolism];
3-240 5.58e-124

2-keto-3-deoxy-L-rhamnonate aldolase RhmA [Carbohydrate transport and metabolism];


Pssm-ID: 443047 [Multi-domain]  Cd Length: 237  Bit Score: 352.49  E-value: 5.58e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323   3 LPVNRFKQRLRSGEAQIGLWLGLADPYCAELAANAGFDWLLLDGEHAPNDLRSLLGQLQALAPYPGQPVIRPVQGDTALI 82
Cdd:COG3836   1 MRKNRLKQRLRAGEPVIGTWLSLPSPAVAEILAGAGFDWVLIDLEHGPNDLETLLALLRAAAAAGVAPLVRVPSNDPALI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323  83 KQLLDIGAQTLLVPMVDSAAQAEGLVRAVRYPPAGVRGVGsALARASRWNSVAEYLNHADEQMCLLVQVENLEGLANLDA 162
Cdd:COG3836  81 KRALDAGAQGVLVPMVETAEEARAAVAATRYPPLGIRGVG-GPARAARYGRVADYLARANDETLVIVQIETAEAVENLDE 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599323 163 IAAVEGVDGVFIGPADLSAAMGHRGNPGHPEVQAAIEDAIHRIRTAGKAAGILSADETLARRYLELGCAFVAVGVDTS 240
Cdd:COG3836 160 IAAVPGVDGVFIGPADLSASLGHPGQPDHPEVQAAIERVIAAARAAGKPAGILAGDPEDARRYIALGARFVAVGSDVG 237
PRK10128 PRK10128
2-keto-3-deoxy-L-rhamnonate aldolase; Provisional
2-265 3.91e-117

2-keto-3-deoxy-L-rhamnonate aldolase; Provisional


Pssm-ID: 182257  Cd Length: 267  Bit Score: 336.53  E-value: 3.91e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323    2 DLPVNRFKQRLRSGEAQIGLWLGLADPYCAELAANAGFDWLLLDGEHAPNDLRSLLGQLQALAPYPGQPVIRPVQGDTAL 81
Cdd:PRK10128   3 ALLSNPFKEGLRKGEVQIGLWLSSTTSYMAEIAATSGYDWLLIDGEHAPNTIQDLYHQLQAIAPYASQPVIRPVEGSKPL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323   82 IKQLLDIGAQTLLVPMVDSAAQAEGLVRAVRYPPAGVRGVGSALARASRWNSVAEYLNHADEQMCLLVQVENLEGLANLD 161
Cdd:PRK10128  83 IKQVLDIGAQTLLIPMVDTAEQARQVVSATRYPPYGERGVGASVARAARWGRIENYMAQANDSLCLLVQVESKTALDNLD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323  162 AIAAVEGVDGVFIGPADLSAAMGHRGNPGHPEVQAAIEDAIHRIRTAGKAAGILSADETLARRYLELGCAFVAVGVDTSL 241
Cdd:PRK10128 163 EILDVEGIDGVFIGPADLSASLGYPDNAGHPEVQRIIETSIRRIRAAGKAAGFLAVDPDMAQKCLAWGANFVAVGVDTML 242
                        250       260
                 ....*....|....*....|....
gi 15599323  242 LMRSLRELAGRFKGGAPAPSASSS 265
Cdd:PRK10128 243 YTDALDQRLAMFKSGKNGPRAKGS 266
PRK10558 PRK10558
alpha-dehydro-beta-deoxy-D-glucarate aldolase; Provisional
6-254 6.99e-98

alpha-dehydro-beta-deoxy-D-glucarate aldolase; Provisional


Pssm-ID: 182547  Cd Length: 256  Bit Score: 287.02  E-value: 6.99e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323    6 NRFKQRLRSGEAQIGLWLGLADPYCAELAANAGFDWLLLDGEHAPNDLRSLLGQLQALAPYPGQPVIRPVQGDTALIKQL 85
Cdd:PRK10558   8 NKFKAALAAKQVQIGCWSALANPITTEVLGLAGFDWLVLDGEHAPNDVSTFIPQLMALKGSASAPVVRVPTNEPVIIKRL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323   86 LDIGAQTLLVPMVDSAAQAEGLVRAVRYPPAGVRGVgSALARASRWNSVAEYLNHADEQMCLLVQVENLEGLANLDAIAA 165
Cdd:PRK10558  88 LDIGFYNFLIPFVETAEEARRAVASTRYPPEGIRGV-SVSHRANMFGTVPDYFAQSNKNITVLVQIESQQGVDNVDAIAA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323  166 VEGVDGVFIGPADLSAAMGHRGNPGHPEVQAAIEDAIHRIRTAGKAAGILSADETLARRYLELGCAFVAVGVDTSLLMRS 245
Cdd:PRK10558 167 TEGVDGIFVGPSDLAAALGHLGNASHPDVQKAIQHIFARAKAHGKPSGILAPVEADARRYLEWGATFVAVGSDLGVFRSA 246

                 ....*....
gi 15599323  246 LRELAGRFK 254
Cdd:PRK10558 247 TQALADTFK 255
GarL TIGR03239
2-dehydro-3-deoxyglucarate aldolase; In E. coli this enzyme (GarL) 2-dehydro-3-deoxyglucarate ...
6-255 1.87e-92

2-dehydro-3-deoxyglucarate aldolase; In E. coli this enzyme (GarL) 2-dehydro-3-deoxyglucarate aldolase acts in the catabolism of several sugars including D-galactarate, D-glucarate and L-idarate. In fact, 5-dehydro-4-deoxy-D-glucarate aldolase is a synonym for this enzyme as it is unclear in the literature whether the enzyme acts on only one of these or, as seems likely, has no preference. (Despite the apparent large difference in substrate stucture indicated by their names, 2-DH-3DO- and 5-DH-4DO-glucarate differ only by the chirality of most central hydroxyl-bearing carbon and is alternately named 2-DH-3DO-galactarate.) The reported product of D-galactarate dehydratase (4.2.1.42) is the 5DH-4DO-glucarate isomer and this enzyme is found proximal to the aldolase in many genomes (GenProp0714) where no epimerase is known. Similarly, the product of D-glucarate dehydratase (4.2.1.40) is again the 5-DH-4DO isomer, so the provenance of the 2-DH-3DO-glucarate isomer for which this enzyme is named is unclear.


Pssm-ID: 132283  Cd Length: 249  Bit Score: 273.25  E-value: 1.87e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323     6 NRFKQRLRSGEAQIGLWLGLADPYCAELAANAGFDWLLLDGEHAPNDLRSLLGQLQALAPYPGQPVIRPVQGDTALIKQL 85
Cdd:TIGR03239   1 NRFRQDLLARETLIGCWSALGNPITTEVLGLAGFDWLLLDGEHAPNDVLTFIPQLMALKGSASAPVVRPPWNEPVIIKRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323    86 LDIGAQTLLVPMVDSAAQAEGLVRAVRYPPAGVRGVgSALARASRWNSVAEYLNHADEQMCLLVQVENLEGLANLDAIAA 165
Cdd:TIGR03239  81 LDIGFYNFLIPFVESAEEAERAVAATRYPPEGIRGV-SVSHRSNRYGTVPDYFATINDNITVLVQIESQKGVDNVDEIAA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323   166 VEGVDGVFIGPADLSAAMGHRGNPGHPEVQAAIEDAIHRIRTAGKAAGILSADETLARRYLELGCAFVAVGVDTSLLMRS 245
Cdd:TIGR03239 160 VDGVDGIFVGPSDLAAALGHLGNPNHPDVQKAIRHIFDRAAAHGKPCGILAPVEADARRYLEWGATFVAVGSDLGVFRSA 239
                         250
                  ....*....|
gi 15599323   246 LRELAGRFKG 255
Cdd:TIGR03239 240 TQALRDKFKK 249
HpcH_HpaI pfam03328
HpcH/HpaI aldolase/citrate lyase family; This family includes 2,4-dihydroxyhept-2-ene-1, ...
18-242 1.76e-65

HpcH/HpaI aldolase/citrate lyase family; This family includes 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase and 4-hydroxy-2-oxovalerate aldolase.


Pssm-ID: 427247 [Multi-domain]  Cd Length: 221  Bit Score: 203.35  E-value: 1.76e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323    18 QIGLWLGLADPYCAELAANAGFDWLLLDGEHAP---------NDLRSLLGQLQALAPYPGQPVIRPVQGDTALIKQ---L 85
Cdd:pfam03328   1 RSGLFLPGANPAMAEIAAIAGADWVVIDLEDAValaekdaarVLVPTALQQLDALAAAPSEVVVRVNSLDSPFGKQdlaV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323    86 LDIGAQTLLVPMVDSAAQAEGLVRAVRYPPAGVRGvgsalarasrwnsvaeylnhADEQMCLLVQVENLEGLANLDAIAA 165
Cdd:pfam03328  81 LDLGAQVVLVPKVETAEDARAAVSAIRYPPKGIRR--------------------ANGNTCLLAQIESALGVLNADEIAA 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323   166 VEGVDGVFIGPADLSAAMGHRGNPGHPEVQAAIEdaihRIRTAGKAAGI-----LSADETLARRYLELGCAFVAVGVDTS 240
Cdd:pfam03328 141 VEGVDGIFLGAEDLSADLGTLRSPGGPEVLYARE----RIVTAARAAGIaafdtVYSDENDAEGFLAEGALFVALGFDGK 216

                  ..
gi 15599323   241 LL 242
Cdd:pfam03328 217 LL 218
CitE COG2301
Citrate lyase beta subunit [Carbohydrate transport and metabolism];
56-218 7.98e-09

Citrate lyase beta subunit [Carbohydrate transport and metabolism];


Pssm-ID: 441876  Cd Length: 288  Bit Score: 55.16  E-value: 7.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323  56 LLGQLQALAPYPGQPVIRPVQGDTAL----IKQLLDIGAQTLLVPMVDSAAQaeglvravryppagVRGVGSALARASRw 131
Cdd:COG2301  51 VAEALAELDFGGPEVFVRINALDTPWglddLAALVGAGLDGIVLPKVESAED--------------VRALAALLTELEA- 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323 132 nsvaeylnhADEQMCLLVQVENLEGLANLDAIAAV-EGVDGVFIGPADLSAAMGHRGNPGhpevQAAIEDAIHRIRTAGK 210
Cdd:COG2301 116 ---------EGGSIPLMALIETARGLLNAAEIAAAsPRVEALVFGAEDLAADLGARRTRD----GDELLYARSRIVLAAR 182

                ....*...
gi 15599323 211 AAGILSAD 218
Cdd:COG2301 183 AAGLAAID 190
PK pfam00224
Pyruvate kinase, barrel domain; This domain of the is actually a small beta-barrel domain ...
127-211 6.34e-03

Pyruvate kinase, barrel domain; This domain of the is actually a small beta-barrel domain nested within a larger TIM barrel. The active site is found in a cleft between the two domains.


Pssm-ID: 395168 [Multi-domain]  Cd Length: 348  Bit Score: 37.35  E-value: 6.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599323   127 RASRWNSVAEYLNHADEQMCLLVQVENLEGLANLDAIaaVEGVDGVFIGPADLSAAMghrgnpGHPEVQAAIEDAIHRIR 206
Cdd:pfam00224 200 KASDVLEIREVLGEAGKNIQIIAKIENQEGVNNFDEI--LEATDGIMVARGDLGIEI------PAEEVFLAQKMLIAKCN 271

                  ....*
gi 15599323   207 TAGKA 211
Cdd:pfam00224 272 LAGKP 276
 
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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