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Conserved domains on  [gi|937520556|gb|ALI41042|]
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hypothetical protein QQ24_16785 [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

isomerase/hydrolase( domain architecture ID 10013602)

uncharacterized isomerase/hydrolase similar to Escherichia coli YcgM, a member of the fumarylacetate (FAA) hydrolase family

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10691 PRK10691
fumarylacetoacetate hydrolase family protein;
1-219 0e+00

fumarylacetoacetate hydrolase family protein;


:

Pssm-ID: 182650  Cd Length: 219  Bit Score: 498.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556   1 MYQHHNWQGALLDYPVSKVVCVGSNYAKHIKEMGSAVPEEPVLFIKPETALCDLRQPLAIPSDFGSVHHEVELAVLIGAT 80
Cdd:PRK10691   1 MYQHRNWQGALLDYPVSKVVCVGSNYAKHIKEMGSATPEEPVLFIKPETALCDLRQPLAIPKDFGSVHHEVELAVLIGAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556  81 LRQATEEHVRKAIAGYGVALDLTLRDVQGKMKKAGQPWEKAKAFDNSCPLSGFIPAAEFTGDPQNTTLSLSVNGEQRQQG 160
Cdd:PRK10691  81 LRQATEEHVRKAIAGYGVALDLTLRDLQGKMKKAGQPWEKAKAFDNSCPISGFIPVAEFTGDPQNTTLGLSVNGEVRQQG 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 937520556 161 TTADMIHKIVPLIAYMSKFFTLKAGDVVLTGTPDGVGPLQSGDELTVTFDGHSLTTRVL 219
Cdd:PRK10691 161 NTADMIHPIVPLIAYMSRFFTLRAGDVVLTGTPEGVGPLQSGDELTVTFNGHSLTTRVL 219
 
Name Accession Description Interval E-value
PRK10691 PRK10691
fumarylacetoacetate hydrolase family protein;
1-219 0e+00

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 182650  Cd Length: 219  Bit Score: 498.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556   1 MYQHHNWQGALLDYPVSKVVCVGSNYAKHIKEMGSAVPEEPVLFIKPETALCDLRQPLAIPSDFGSVHHEVELAVLIGAT 80
Cdd:PRK10691   1 MYQHRNWQGALLDYPVSKVVCVGSNYAKHIKEMGSATPEEPVLFIKPETALCDLRQPLAIPKDFGSVHHEVELAVLIGAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556  81 LRQATEEHVRKAIAGYGVALDLTLRDVQGKMKKAGQPWEKAKAFDNSCPLSGFIPAAEFTGDPQNTTLSLSVNGEQRQQG 160
Cdd:PRK10691  81 LRQATEEHVRKAIAGYGVALDLTLRDLQGKMKKAGQPWEKAKAFDNSCPISGFIPVAEFTGDPQNTTLGLSVNGEVRQQG 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 937520556 161 TTADMIHKIVPLIAYMSKFFTLKAGDVVLTGTPDGVGPLQSGDELTVTFDGHSLTTRVL 219
Cdd:PRK10691 161 NTADMIHPIVPLIAYMSRFFTLRAGDVVLTGTPEGVGPLQSGDELTVTFNGHSLTTRVL 219
YcgM COG0179
2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) ...
15-218 2.75e-103

2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 439949  Cd Length: 206  Bit Score: 296.98  E-value: 2.75e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556  15 PV--SKVVCVGSNYAKHIKEMGSAVPEEPVLFIKPETALCDLRQPLAIPSDFGSVHHEVELAVLIGATLRQATEEHVRKA 92
Cdd:COG0179    2 PVppGKIICVGLNYADHAAEMGNDVPEEPVLFLKPPSALVGPGDPIPLPAGSGKLDYEGELAVVIGKRARNVSEEDALDH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556  93 IAGYGVALDLTLRDVQgkmKKAGQPWEKAKAFDNSCPLSGFI-PAAEFtGDPQNTTLSLSVNGEQRQQGTTADMIHKIVP 171
Cdd:COG0179   82 VAGYTVANDVTARDLQ---RERGGQWTRGKSFDTFCPLGPWIvTADEI-PDPQDLRIRLRVNGEVRQDGNTSDMIFSVAE 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 937520556 172 LIAYMSKFFTLKAGDVVLTGTPDGVGPLQSGDELTVTFDGH-SLTTRV 218
Cdd:COG0179  158 LIAYLSQFMTLEPGDVILTGTPAGVGPLKPGDVVEVEIEGIgTLRNTV 205
FAA_hydrolase pfam01557
Fumarylacetoacetate (FAA) hydrolase family; This family consists of fumarylacetoacetate (FAA) ...
20-218 3.46e-63

Fumarylacetoacetate (FAA) hydrolase family; This family consists of fumarylacetoacetate (FAA) hydrolase, or fumarylacetoacetate hydrolase (FAH) and it also includes HHDD isomerase/OPET decarboxylase from E. coli strain W. FAA is the last enzyme in the tyrosine catabolic pathway, it hydrolyses fumarylacetoacetate into fumarate and acetoacetate which then join the citric acid cycle. Mutations in FAA cause type I tyrosinemia in humans this is an inherited disorder mainly affecting the liver leading to liver cirrhosis, hepatocellular carcinoma, renal tubular damages and neurologic crises amongst other symptoms. The enzymatic defect causes the toxic accumulation of phenylalanine/tyrosine catabolites. The E. coli W enzyme HHDD isomerase/OPET decarboxylase contains two copies of this domain and functions in fourth and fifth steps of the homoprotocatechuate pathway; here it decarboxylates OPET to HHDD and isomerizes this to OHED. The final products of this pathway are pyruvic acid and succinic semialdehyde. This family also includes various hydratases and 4-oxalocrotonate decarboxylases which are involved in the bacterial meta-cleavage pathways for degradation of aromatic compounds. 2-hydroxypentadienoic acid hydratase encoded by mhpD in E. coli is involved in the phenylpropionic acid pathway of E. coli and catalyzes the conversion of 2-hydroxy pentadienoate to 4-hydroxy-2-keto-pentanoate and uses a Mn2+ co-factor. OHED hydratase encoded by hpcG in E. coli is involved in the homoprotocatechuic acid (HPC) catabolism. XylI in P. putida is a 4-Oxalocrotonate decarboxylase.


Pssm-ID: 460252  Cd Length: 210  Bit Score: 195.20  E-value: 3.46e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556   20 VCVGSNYAKHIKEMGSA--VPEEP---VLFIKPETALCDLRQPLAIPSDFGSVHHEVELAVLIGATLRQATEEHVRKAIA 94
Cdd:pfam01557   1 VCVGLNYAEHAREAGKAepVPDFPiplVLFVKPPSSLIGPGDPIVRPAGVTKLDYEAELAVVIGRPARDVSPEEALDYIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556   95 GYGVALDLTLRDVQGKMKKAgqPWEKAKAFDNSCPLSGFIPAAEFTGDPQNTTLSLSVNGEQRQQGTTADMIHKIVPLIA 174
Cdd:pfam01557  81 GYTLANDVSARDLQRREMPL--QWFRGKSFDGFTPLGPWIVTRDELPDPGDLRLRLRVNGEVRQDGNTSDMIFSPAELIA 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 937520556  175 YMSKFFTLKAGDVVLTGTPDGVG-------PLQSGDELTVTFDG-HSLTTRV 218
Cdd:pfam01557 159 HLSQFMTLRPGDIILTGTPSGVGagrappvFLKPGDTVEVEIEGlGTLRNTV 210
HpaG-C-term TIGR02303
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, C-terminal subunit; ...
15-211 1.34e-47

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, C-terminal subunit; This model represents one of two subunits/domains of the bifunctional isomerase/decarboxylase involved in 4-hydroxyphenylacetate degradation. In E. coli and some other species this enzyme is encoded by a single polypeptide containing both this domain and the closely related N-terminal domain (TIGR02305). In other species such as Pasteurella multocida these domains are found as two separate proteins (usually as tandem genes). Together, these domains carry out the decarboxylation of 5-oxopent-3-ene-1,2,5-tricarboxylic acid (OPET) to 2-hydroxy-2,4-diene-1,7-dioate (HHDD) and the subsequent isomerization to 2-oxohept-3-ene-1,7-dioate (OHED).


Pssm-ID: 131356 [Multi-domain]  Cd Length: 245  Bit Score: 156.90  E-value: 1.34e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556   15 PVS--KVVCVGSNYAKHIKEMGSAVPEEPVLFIKPETALCDLRQPLAIPSDFGSVHHEVELAVLIGATLRQATEEHVRKA 92
Cdd:TIGR02303  39 PFEpgTIFALGLNYADHASELGFSPPEEPLVFLKGNNTLTGHKGVTYRPKDVRFMHYECELAVVVGKTAKNVKREDAMDY 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556   93 IAGYGVALDLTLRDVqgkMKKAGQPWEKAKAFDNSCPLSGFIPAAEFTGDPQNTTLSLSVNGEQRQQGTTADMIHKIVPL 172
Cdd:TIGR02303 119 VLGYTIANDYAIRDY---LENYYRPNLRVKNRDTFTPIGPWIVDKEDVEDPMNLWLRTYVNGELTQEGNTSDMIFSVAEL 195
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 937520556  173 IAYMSKFFTLKAGDVVLTGTPDGVGPLQSGDELTVTFDG 211
Cdd:TIGR02303 196 IEYLSEFMTLEPGDVILTGTPKGLSDVKPGDVVRLEIEG 234
 
Name Accession Description Interval E-value
PRK10691 PRK10691
fumarylacetoacetate hydrolase family protein;
1-219 0e+00

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 182650  Cd Length: 219  Bit Score: 498.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556   1 MYQHHNWQGALLDYPVSKVVCVGSNYAKHIKEMGSAVPEEPVLFIKPETALCDLRQPLAIPSDFGSVHHEVELAVLIGAT 80
Cdd:PRK10691   1 MYQHRNWQGALLDYPVSKVVCVGSNYAKHIKEMGSATPEEPVLFIKPETALCDLRQPLAIPKDFGSVHHEVELAVLIGAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556  81 LRQATEEHVRKAIAGYGVALDLTLRDVQGKMKKAGQPWEKAKAFDNSCPLSGFIPAAEFTGDPQNTTLSLSVNGEQRQQG 160
Cdd:PRK10691  81 LRQATEEHVRKAIAGYGVALDLTLRDLQGKMKKAGQPWEKAKAFDNSCPISGFIPVAEFTGDPQNTTLGLSVNGEVRQQG 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 937520556 161 TTADMIHKIVPLIAYMSKFFTLKAGDVVLTGTPDGVGPLQSGDELTVTFDGHSLTTRVL 219
Cdd:PRK10691 161 NTADMIHPIVPLIAYMSRFFTLRAGDVVLTGTPEGVGPLQSGDELTVTFNGHSLTTRVL 219
YcgM COG0179
2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) ...
15-218 2.75e-103

2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 439949  Cd Length: 206  Bit Score: 296.98  E-value: 2.75e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556  15 PV--SKVVCVGSNYAKHIKEMGSAVPEEPVLFIKPETALCDLRQPLAIPSDFGSVHHEVELAVLIGATLRQATEEHVRKA 92
Cdd:COG0179    2 PVppGKIICVGLNYADHAAEMGNDVPEEPVLFLKPPSALVGPGDPIPLPAGSGKLDYEGELAVVIGKRARNVSEEDALDH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556  93 IAGYGVALDLTLRDVQgkmKKAGQPWEKAKAFDNSCPLSGFI-PAAEFtGDPQNTTLSLSVNGEQRQQGTTADMIHKIVP 171
Cdd:COG0179   82 VAGYTVANDVTARDLQ---RERGGQWTRGKSFDTFCPLGPWIvTADEI-PDPQDLRIRLRVNGEVRQDGNTSDMIFSVAE 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 937520556 172 LIAYMSKFFTLKAGDVVLTGTPDGVGPLQSGDELTVTFDGH-SLTTRV 218
Cdd:COG0179  158 LIAYLSQFMTLEPGDVILTGTPAGVGPLKPGDVVEVEIEGIgTLRNTV 205
FAA_hydrolase pfam01557
Fumarylacetoacetate (FAA) hydrolase family; This family consists of fumarylacetoacetate (FAA) ...
20-218 3.46e-63

Fumarylacetoacetate (FAA) hydrolase family; This family consists of fumarylacetoacetate (FAA) hydrolase, or fumarylacetoacetate hydrolase (FAH) and it also includes HHDD isomerase/OPET decarboxylase from E. coli strain W. FAA is the last enzyme in the tyrosine catabolic pathway, it hydrolyses fumarylacetoacetate into fumarate and acetoacetate which then join the citric acid cycle. Mutations in FAA cause type I tyrosinemia in humans this is an inherited disorder mainly affecting the liver leading to liver cirrhosis, hepatocellular carcinoma, renal tubular damages and neurologic crises amongst other symptoms. The enzymatic defect causes the toxic accumulation of phenylalanine/tyrosine catabolites. The E. coli W enzyme HHDD isomerase/OPET decarboxylase contains two copies of this domain and functions in fourth and fifth steps of the homoprotocatechuate pathway; here it decarboxylates OPET to HHDD and isomerizes this to OHED. The final products of this pathway are pyruvic acid and succinic semialdehyde. This family also includes various hydratases and 4-oxalocrotonate decarboxylases which are involved in the bacterial meta-cleavage pathways for degradation of aromatic compounds. 2-hydroxypentadienoic acid hydratase encoded by mhpD in E. coli is involved in the phenylpropionic acid pathway of E. coli and catalyzes the conversion of 2-hydroxy pentadienoate to 4-hydroxy-2-keto-pentanoate and uses a Mn2+ co-factor. OHED hydratase encoded by hpcG in E. coli is involved in the homoprotocatechuic acid (HPC) catabolism. XylI in P. putida is a 4-Oxalocrotonate decarboxylase.


Pssm-ID: 460252  Cd Length: 210  Bit Score: 195.20  E-value: 3.46e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556   20 VCVGSNYAKHIKEMGSA--VPEEP---VLFIKPETALCDLRQPLAIPSDFGSVHHEVELAVLIGATLRQATEEHVRKAIA 94
Cdd:pfam01557   1 VCVGLNYAEHAREAGKAepVPDFPiplVLFVKPPSSLIGPGDPIVRPAGVTKLDYEAELAVVIGRPARDVSPEEALDYIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556   95 GYGVALDLTLRDVQGKMKKAgqPWEKAKAFDNSCPLSGFIPAAEFTGDPQNTTLSLSVNGEQRQQGTTADMIHKIVPLIA 174
Cdd:pfam01557  81 GYTLANDVSARDLQRREMPL--QWFRGKSFDGFTPLGPWIVTRDELPDPGDLRLRLRVNGEVRQDGNTSDMIFSPAELIA 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 937520556  175 YMSKFFTLKAGDVVLTGTPDGVG-------PLQSGDELTVTFDG-HSLTTRV 218
Cdd:pfam01557 159 HLSQFMTLRPGDIILTGTPSGVGagrappvFLKPGDTVEVEIEGlGTLRNTV 210
HpaG-C-term TIGR02303
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, C-terminal subunit; ...
15-211 1.34e-47

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, C-terminal subunit; This model represents one of two subunits/domains of the bifunctional isomerase/decarboxylase involved in 4-hydroxyphenylacetate degradation. In E. coli and some other species this enzyme is encoded by a single polypeptide containing both this domain and the closely related N-terminal domain (TIGR02305). In other species such as Pasteurella multocida these domains are found as two separate proteins (usually as tandem genes). Together, these domains carry out the decarboxylation of 5-oxopent-3-ene-1,2,5-tricarboxylic acid (OPET) to 2-hydroxy-2,4-diene-1,7-dioate (HHDD) and the subsequent isomerization to 2-oxohept-3-ene-1,7-dioate (OHED).


Pssm-ID: 131356 [Multi-domain]  Cd Length: 245  Bit Score: 156.90  E-value: 1.34e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556   15 PVS--KVVCVGSNYAKHIKEMGSAVPEEPVLFIKPETALCDLRQPLAIPSDFGSVHHEVELAVLIGATLRQATEEHVRKA 92
Cdd:TIGR02303  39 PFEpgTIFALGLNYADHASELGFSPPEEPLVFLKGNNTLTGHKGVTYRPKDVRFMHYECELAVVVGKTAKNVKREDAMDY 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556   93 IAGYGVALDLTLRDVqgkMKKAGQPWEKAKAFDNSCPLSGFIPAAEFTGDPQNTTLSLSVNGEQRQQGTTADMIHKIVPL 172
Cdd:TIGR02303 119 VLGYTIANDYAIRDY---LENYYRPNLRVKNRDTFTPIGPWIVDKEDVEDPMNLWLRTYVNGELTQEGNTSDMIFSVAEL 195
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 937520556  173 IAYMSKFFTLKAGDVVLTGTPDGVGPLQSGDELTVTFDG 211
Cdd:TIGR02303 196 IEYLSEFMTLEPGDVILTGTPKGLSDVKPGDVVRLEIEG 234
PRK15203 PRK15203
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional
1-211 2.79e-44

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional


Pssm-ID: 185125 [Multi-domain]  Cd Length: 429  Bit Score: 152.90  E-value: 2.79e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556   1 MYQHHNWQGalldYPVSKVVCVGSNYAKHIKEMGSAVPEEPVLFIKPETALCDLRQPLAIPSDFGSVHHEVELAVLIGAT 80
Cdd:PRK15203 211 THKSFPTPP----HPHGTLFALGLNYADHASELEFKPPEEPLVFLKAPNTLTGDNQTSVRPNNIEYMHYEAELVVVIGKQ 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556  81 LRQATEEHVRKAIAGYGVALDLTLRDVqgkMKKAGQPWEKAKAFDNSCPLSGFIPAAEFTGDPQNTTLSLSVNGEQRQQG 160
Cdd:PRK15203 287 ARKVSEADAMDYVAGYTVCNDYAIRDY---LENYYRPNLRVKSRDGLTPILSTIVPKEAIPDPHNLTLRTFVNGELRQQG 363
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 937520556 161 TTADMIHKIVPLIAYMSKFFTLKAGDVVLTGTPDGVGPLQSGDELTVTFDG 211
Cdd:PRK15203 364 TTADLIFSVPFLIAYLSEFMTLNPGDMIATGTPKGLSDVVPGDEVVVEVEG 414
HpaG-N-term TIGR02305
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, N-terminal subunit; ...
18-211 3.52e-36

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, N-terminal subunit; This model represents one of two subunits/domains of the bifunctional isomerase/decarboxylase involved in 4-hydroxyphenylacetate degradation. In E. coli and some other species this enzyme is encoded by a single polypeptide containing both this domain and the closely related C-terminal domain (TIGR02303). In other species such as Pasteurella multocida these domains are found as two separate proteins (usually as tandem genes). Together, these domains carry out the decarboxylation of 5-oxopent-3-ene-1,2,5-tricarboxylic acid (OPET) to 2-hydroxy-2,4-diene-1,7-dioate (HHDD) and the subsequent isomerization to 2-oxohept-3-ene-1,7-dioate (OHED).


Pssm-ID: 131358  Cd Length: 205  Bit Score: 126.00  E-value: 3.52e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556   18 KVVCVGSNYAKHIKEMGSAV--------PEEPVLFIKPETALCDLRQPLAIPSDFGSVHHEVELAVLIGATLRQATEEHV 89
Cdd:TIGR02305   2 TVFGVALNYREQLDRLQEAFqqapykapPKTPVLYIKPRNTHNGCGQPIPLPAGVEKLRSGATLALVVGRTACRVREEEA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556   90 RKAIAGYGVALDLTLRDvqgkmKKAGQPWEKAKAFDNSCPLSGFIPAAEFtGDPQNTTLSLSVNGEQRQQGTTADMIHKI 169
Cdd:TIGR02305  82 LDYVAGYALVNDVSLPE-----DSYYRPAIKAKCRDGFCPIGPEVPLSAI-GNPDELTIYTYINGKPAQSNNTSNLVRSA 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 937520556  170 VPLIAYMSKFFTLKAGDVVLTGTPDGVGPLQSGDELTVTFDG 211
Cdd:TIGR02305 156 AQLISELSEFMTLNPGDVLLLGTPEARVEVGPGDRVRVEAEG 197
PRK12764 PRK12764
fumarylacetoacetate hydrolase family protein;
18-218 1.05e-22

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 237193 [Multi-domain]  Cd Length: 500  Bit Score: 95.21  E-value: 1.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556  18 KVVCVGSNYAKHIKEMGSAvPEEPVLFIKPETALCDLRQPLAIPSDFGSVHHEVELAVLIGATLRQATEEHVRKAIAGYG 97
Cdd:PRK12764  23 KVIAVHLNYPSRAAQRGRT-PAQPSYFLKPSSSLALSGGTVERPAGTELLAFEGEIALVIGRPARRVSPEDAWSHVAAVT 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556  98 VALDLTLRDVQGKMKKAGQpweKAKAFDNSCPLS-GFIPAAEFtgDPQNTTLSLSVNGEQRQQGTTADMIHKIVPLIAYM 176
Cdd:PRK12764 102 AANDLGVYDLRYADKGSNL---RSKGGDGFTPIGpALISARGV--DPAQLRVRTWVNGELVQDDTTEDLLFPFAQLVADL 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 937520556 177 SKFFTLKAGDVVLTGTPDGVGPLQSGDELTVTFDGHS--------LTTRV 218
Cdd:PRK12764 177 SQLLTLEEGDVILTGTPAGSSVAAPGDVVEVEVDAPAdgapstgrLVTRV 226
PRK15203 PRK15203
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional
35-211 4.42e-18

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional


Pssm-ID: 185125 [Multi-domain]  Cd Length: 429  Bit Score: 81.63  E-value: 4.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556  35 SAVPEEPVLFIKPETALCDLRQPLAIPSDfGSVHHEVELAVLIGATLRQATEEHVRKAIAGYGVALDLTLRDvqgkmKKA 114
Cdd:PRK15203  29 KAPPKTAVWFIKPRNTVIRCGEPIPFPQG-EKVLSGATVALIVGKTATKVREEDAAEYIAGYALANDVSLPE-----ESF 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556 115 GQPWEKAKAFDNSCPLSGFIPAAeftgDPQNTTLSLSVNGEQRQQGTTADMIHKIVPLIAYMSKFFTLKAGDVVLTGTPD 194
Cdd:PRK15203 103 YRPAIKAKCRDGFCPIGETVALS----NVDNLTIYTEINGRPADHWNTADLQRNAAQLLSALSEFATLNPGDAILLGTPQ 178
                        170
                 ....*....|....*..
gi 937520556 195 GVGPLQSGDELTVTFDG 211
Cdd:PRK15203 179 ARVEIQPGDRVRVLAEG 195
MhpD COG3971
2-keto-4-pentenoate hydratase [Secondary metabolites biosynthesis, transport and catabolism];
70-218 3.82e-11

2-keto-4-pentenoate hydratase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443171  Cd Length: 259  Bit Score: 60.92  E-value: 3.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556  70 EVELAVLIGATL--RQATEEHVRKAIAGYGVAL---DLTLRDvqgkmkkagqpWeKAKAF----DN-SCplSGFI----P 135
Cdd:COG3971  104 EAEIAFVLGRDLpgPGVTLADVLAATDAVAPAIeivDSRIAD-----------W-KIGLAdtiaDNaSS--GGFVlgppP 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937520556 136 AAEFTGDPQNTTLSLSVNGEQRQQGTTADM----IHKIVPLIAYMSKFF-TLKAGDVVLTGTPDGVGPLQSGDELTVTFD 210
Cdd:COG3971  170 VDPDDLDLRNVGVVLEKNGEVVATGAGAAVlghpLNAVAWLANKLAARGiPLKAGDIVLTGSLTPAVPVKPGDTVRADFG 249

                 ....*....
gi 937520556 211 GH-SLTTRV 218
Cdd:COG3971  250 GLgSVSVRF 258
 
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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