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Conserved domains on  [gi|446601745|ref|WP_000679091|]
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MULTISPECIES: 4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase [Enterobacteriaceae]

Protein Classification

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase( domain architecture ID 11487693)

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase decarboxylates OPET (5-oxo-pent-3-ene-1,2,5-tricarboxylic acid) into HHDD (2-hydroxy-hept-2,4-diene-1,7-dioate) and isomerizes it to OHED (2-oxo-hept-3-ene-1,7-dioate)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK15203 PRK15203
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional
 1-429 0e+00

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional


:

Pssm-ID: 185125 [Multi-domain]  Cd Length: 429  Bit Score: 933.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745   1 MKGTIFAVALNHRSQLDAWQEAFQQSPYKAPPKTAVWFIKPRNTVIGCGEPIPFPQGEKVLSGATVALIVGKTATKVREE 80
Cdd:PRK15203   1 MKGTIFAVALNHRSQLDAWQEAFQQSPYKAPPKTAVWFIKPRNTVIRCGEPIPFPQGEKVLSGATVALIVGKTATKVREE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745  81 DAAEYIAGYALANDVSLPEESFYRPAIKAKCRDGFCPIGETVALSNVDNLTIYTEINGRPADHWNTADLQRNAAQLLSAL 160
Cdd:PRK15203  81 DAAEYIAGYALANDVSLPEESFYRPAIKAKCRDGFCPIGETVALSNVDNLTIYTEINGRPADHWNTADLQRNAAQLLSAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745 161 SEFATLNPGDAILLGTPQARVEIQPGDRVRVLAEGFPPLENPVVDEREVTTRKSFPTQPHPHGTLFALGLNYADHASELE 240
Cdd:PRK15203 161 SEFATLNPGDAILLGTPQARVEIQPGDRVRVLAEGFPPLENPVVDEREVTTHKSFPTPPHPHGTLFALGLNYADHASELE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745 241 FKPPEEPLVFLKAPNTLTGDNQTSVRPNNIEYMHYEAELVVVIGKQARNVSEADAMDYVAGYTVCNDYAIRDYLENYYRP 320
Cdd:PRK15203 241 FKPPEEPLVFLKAPNTLTGDNQTSVRPNNIEYMHYEAELVVVIGKQARKVSEADAMDYVAGYTVCNDYAIRDYLENYYRP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745 321 NLRVKSRDGLTPMLSTIVPKEAIPDPHNLTLRTFVNGELRQQGTTADLIFSVPFLIAYLSEFMTLNPGDMIATGTPKGLS 400
Cdd:PRK15203 321 NLRVKSRDGLTPILSTIVPKEAIPDPHNLTLRTFVNGELRQQGTTADLIFSVPFLIAYLSEFMTLNPGDMIATGTPKGLS 400

                        410       420
                 ....*....|....*....|....*....
gi 446601745 401 DVVPGDEVVVEVEGVGRLVNRIVSEDTAK 429
Cdd:PRK15203 401 DVVPGDEVVVEVEGVGRLVNRIVSEETAK 429
 
Name Accession Description Interval E-value
PRK15203 PRK15203
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional
 1-429 0e+00

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional


Pssm-ID: 185125 [Multi-domain]  Cd Length: 429  Bit Score: 933.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745   1 MKGTIFAVALNHRSQLDAWQEAFQQSPYKAPPKTAVWFIKPRNTVIGCGEPIPFPQGEKVLSGATVALIVGKTATKVREE 80
Cdd:PRK15203   1 MKGTIFAVALNHRSQLDAWQEAFQQSPYKAPPKTAVWFIKPRNTVIRCGEPIPFPQGEKVLSGATVALIVGKTATKVREE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745  81 DAAEYIAGYALANDVSLPEESFYRPAIKAKCRDGFCPIGETVALSNVDNLTIYTEINGRPADHWNTADLQRNAAQLLSAL 160
Cdd:PRK15203  81 DAAEYIAGYALANDVSLPEESFYRPAIKAKCRDGFCPIGETVALSNVDNLTIYTEINGRPADHWNTADLQRNAAQLLSAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745 161 SEFATLNPGDAILLGTPQARVEIQPGDRVRVLAEGFPPLENPVVDEREVTTRKSFPTQPHPHGTLFALGLNYADHASELE 240
Cdd:PRK15203 161 SEFATLNPGDAILLGTPQARVEIQPGDRVRVLAEGFPPLENPVVDEREVTTHKSFPTPPHPHGTLFALGLNYADHASELE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745 241 FKPPEEPLVFLKAPNTLTGDNQTSVRPNNIEYMHYEAELVVVIGKQARNVSEADAMDYVAGYTVCNDYAIRDYLENYYRP 320
Cdd:PRK15203 241 FKPPEEPLVFLKAPNTLTGDNQTSVRPNNIEYMHYEAELVVVIGKQARKVSEADAMDYVAGYTVCNDYAIRDYLENYYRP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745 321 NLRVKSRDGLTPMLSTIVPKEAIPDPHNLTLRTFVNGELRQQGTTADLIFSVPFLIAYLSEFMTLNPGDMIATGTPKGLS 400
Cdd:PRK15203 321 NLRVKSRDGLTPILSTIVPKEAIPDPHNLTLRTFVNGELRQQGTTADLIFSVPFLIAYLSEFMTLNPGDMIATGTPKGLS 400

                        410       420
                 ....*....|....*....|....*....
gi 446601745 401 DVVPGDEVVVEVEGVGRLVNRIVSEDTAK 429
Cdd:PRK15203 401 DVVPGDEVVVEVEGVGRLVNRIVSEETAK 429
HpaG-N-term TIGR02305
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, N-terminal subunit; ...
 3-203 7.80e-117

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: 339.79  E-value: 7.80e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745    3 GTIFAVALNHRSQLDAWQEAFQQSPYKAPPKTAVWFIKPRNTVIGCGEPIPFPQG-EKVLSGATVALIVGKTATKVREED 81
Cdd:TIGR02305   1 GTVFGVALNYREQLDRLQEAFQQAPYKAPPKTPVLYIKPRNTHNGCGQPIPLPAGvEKLRSGATLALVVGRTACRVREEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745   82 AAEYIAGYALANDVSLPEESFYRPAIKAKCRDGFCPIG---ETVALSNVDNLTIYTEINGRPADHWNTADLQRNAAQLLS 158
Cdd:TIGR02305  81 ALDYVAGYALVNDVSLPEDSYYRPAIKAKCRDGFCPIGpevPLSAIGNPDELTIYTYINGKPAQSNNTSNLVRSAAQLIS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 446601745  159 ALSEFATLNPGDAILLGTPQARVEIQPGDRVRVLAEGFPPLENPV 203
Cdd:TIGR02305 161 ELSEFMTLNPGDVLLLGTPEARVEVGPGDRVRVEAEGLGELENPV 205
YcgM COG0179
2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) ...
 219-398 4.25e-96

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: 286.58  E-value: 4.25e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745 219 PHPHGTLFALGLNYADHASELEFKPPEEPLVFLKAPNTLTGDNQTSVRPNNIEYMHYEAELVVVIGKQARNVSEADAMDY 298
Cdd:COG0179    2 PVPPGKIICVGLNYADHAAEMGNDVPEEPVLFLKPPSALVGPGDPIPLPAGSGKLDYEGELAVVIGKRARNVSEEDALDH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745 299 VAGYTVCNDYAIRDYLENYYRPNLRVKSRDGLTPMLSTIVPKEAIPDPHNLTLRTFVNGELRQQGTTADLIFSVPFLIAY 378
Cdd:COG0179   82 VAGYTVANDVTARDLQRERGGQWTRGKSFDTFCPLGPWIVTADEIPDPQDLRIRLRVNGEVRQDGNTSDMIFSVAELIAY 161

                        170       180
                 ....*....|....*....|
gi 446601745 379 LSEFMTLNPGDMIATGTPKG 398
Cdd:COG0179  162 LSQFMTLEPGDVILTGTPAG 181
FAA_hydrolase pfam01557
Fumarylacetoacetate (FAA) hydrolase family; This family consists of fumarylacetoacetate (FAA) ...
 226-398 3.17e-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: 202.52  E-value: 3.17e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745  226 FALGLNYADHASELEFK--PPEEP---LVFLKAPNTLTGDNQTSVRPNNIEYMHYEAELVVVIGKQARNVSEADAMDYVA 300
Cdd:pfam01557   1 VCVGLNYAEHAREAGKAepVPDFPiplVLFVKPPSSLIGPGDPIVRPAGVTKLDYEAELAVVIGRPARDVSPEEALDYIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745  301 GYTVCNDYAIRDYLENYYR-PNLRVKSRDGLTPMLSTIVPKEAIPDPHNLTLRTFVNGELRQQGTTADLIFSVPFLIAYL 379
Cdd:pfam01557  81 GYTLANDVSARDLQRREMPlQWFRGKSFDGFTPLGPWIVTRDELPDPGDLRLRLRVNGEVRQDGNTSDMIFSPAELIAHL 160

                         170
                  ....*....|....*....
gi 446601745  380 SEFMTLNPGDMIATGTPKG 398
Cdd:pfam01557 161 SQFMTLRPGDIILTGTPSG 179
MopB_CT_Fdh-Nap-like cd00508
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ...
 136-191 9.42e-04

This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and other related proteins. Formate dehydrogenase H is a component of the anaerobic formate hydrogen lyase complex and catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. Formate dehydrogenase N (alpha subunit) is the major electron donor to the bacterial nitrate respiratory chain and nitrate reductases, Nap and Nas, catalyze the reduction of nitrate to nitrite. This CD (MopB_CT_Fdh-Nap-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.


Pssm-ID: 238282 [Multi-domain]  Cd Length: 120  Bit Score: 39.03  E-value: 9.42e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446601745 136 INGRPADHWNTADLQRNAAQLLSALSE-FATLNPGDAillgtpqARVEIQPGDRVRV 191
Cdd:cd00508    8 TTGRLLEHWHTGTMTRRSPRLAALAPEpFVEIHPEDA-------ARLGIKDGDLVRV 57
 
Name Accession Description Interval E-value
PRK15203 PRK15203
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional
 1-429 0e+00

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional


Pssm-ID: 185125 [Multi-domain]  Cd Length: 429  Bit Score: 933.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745   1 MKGTIFAVALNHRSQLDAWQEAFQQSPYKAPPKTAVWFIKPRNTVIGCGEPIPFPQGEKVLSGATVALIVGKTATKVREE 80
Cdd:PRK15203   1 MKGTIFAVALNHRSQLDAWQEAFQQSPYKAPPKTAVWFIKPRNTVIRCGEPIPFPQGEKVLSGATVALIVGKTATKVREE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745  81 DAAEYIAGYALANDVSLPEESFYRPAIKAKCRDGFCPIGETVALSNVDNLTIYTEINGRPADHWNTADLQRNAAQLLSAL 160
Cdd:PRK15203  81 DAAEYIAGYALANDVSLPEESFYRPAIKAKCRDGFCPIGETVALSNVDNLTIYTEINGRPADHWNTADLQRNAAQLLSAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745 161 SEFATLNPGDAILLGTPQARVEIQPGDRVRVLAEGFPPLENPVVDEREVTTRKSFPTQPHPHGTLFALGLNYADHASELE 240
Cdd:PRK15203 161 SEFATLNPGDAILLGTPQARVEIQPGDRVRVLAEGFPPLENPVVDEREVTTHKSFPTPPHPHGTLFALGLNYADHASELE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745 241 FKPPEEPLVFLKAPNTLTGDNQTSVRPNNIEYMHYEAELVVVIGKQARNVSEADAMDYVAGYTVCNDYAIRDYLENYYRP 320
Cdd:PRK15203 241 FKPPEEPLVFLKAPNTLTGDNQTSVRPNNIEYMHYEAELVVVIGKQARKVSEADAMDYVAGYTVCNDYAIRDYLENYYRP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745 321 NLRVKSRDGLTPMLSTIVPKEAIPDPHNLTLRTFVNGELRQQGTTADLIFSVPFLIAYLSEFMTLNPGDMIATGTPKGLS 400
Cdd:PRK15203 321 NLRVKSRDGLTPILSTIVPKEAIPDPHNLTLRTFVNGELRQQGTTADLIFSVPFLIAYLSEFMTLNPGDMIATGTPKGLS 400

                        410       420
                 ....*....|....*....|....*....
gi 446601745 401 DVVPGDEVVVEVEGVGRLVNRIVSEDTAK 429
Cdd:PRK15203 401 DVVPGDEVVVEVEGVGRLVNRIVSEETAK 429
HpaG-N-term TIGR02305
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, N-terminal subunit; ...
 3-203 7.80e-117

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: 339.79  E-value: 7.80e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745    3 GTIFAVALNHRSQLDAWQEAFQQSPYKAPPKTAVWFIKPRNTVIGCGEPIPFPQG-EKVLSGATVALIVGKTATKVREED 81
Cdd:TIGR02305   1 GTVFGVALNYREQLDRLQEAFQQAPYKAPPKTPVLYIKPRNTHNGCGQPIPLPAGvEKLRSGATLALVVGRTACRVREEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745   82 AAEYIAGYALANDVSLPEESFYRPAIKAKCRDGFCPIG---ETVALSNVDNLTIYTEINGRPADHWNTADLQRNAAQLLS 158
Cdd:TIGR02305  81 ALDYVAGYALVNDVSLPEDSYYRPAIKAKCRDGFCPIGpevPLSAIGNPDELTIYTYINGKPAQSNNTSNLVRSAAQLIS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 446601745  159 ALSEFATLNPGDAILLGTPQARVEIQPGDRVRVLAEGFPPLENPV 203
Cdd:TIGR02305 161 ELSEFMTLNPGDVLLLGTPEARVEVGPGDRVRVEAEGLGELENPV 205
HpaG-C-term TIGR02303
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, C-terminal subunit; ...
 219-425 7.84e-108

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: 318.29  E-value: 7.84e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745  219 PHPHGTLFALGLNYADHASELEFKPPEEPLVFLKAPNTLTGDNQTSVRPNNIEYMHYEAELVVVIGKQARNVSEADAMDY 298
Cdd:TIGR02303  39 PFEPGTIFALGLNYADHASELGFSPPEEPLVFLKGNNTLTGHKGVTYRPKDVRFMHYECELAVVVGKTAKNVKREDAMDY 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745  299 VAGYTVCNDYAIRDYLENYYRPNLRVKSRDGLTPMLSTIVPKEAIPDPHNLTLRTFVNGELRQQGTTADLIFSVPFLIAY 378
Cdd:TIGR02303 119 VLGYTIANDYAIRDYLENYYRPNLRVKNRDTFTPIGPWIVDKEDVEDPMNLWLRTYVNGELTQEGNTSDMIFSVAELIEY 198

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 446601745  379 LSEFMTLNPGDMIATGTPKGLSDVVPGDEVVVEVEGVGRLVNRIVSE 425
Cdd:TIGR02303 199 LSEFMTLEPGDVILTGTPKGLSDVKPGDVVRLEIEGVGALENPIVSE 245
YcgM COG0179
2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) ...
 219-398 4.25e-96

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: 286.58  E-value: 4.25e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745 219 PHPHGTLFALGLNYADHASELEFKPPEEPLVFLKAPNTLTGDNQTSVRPNNIEYMHYEAELVVVIGKQARNVSEADAMDY 298
Cdd:COG0179    2 PVPPGKIICVGLNYADHAAEMGNDVPEEPVLFLKPPSALVGPGDPIPLPAGSGKLDYEGELAVVIGKRARNVSEEDALDH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745 299 VAGYTVCNDYAIRDYLENYYRPNLRVKSRDGLTPMLSTIVPKEAIPDPHNLTLRTFVNGELRQQGTTADLIFSVPFLIAY 378
Cdd:COG0179   82 VAGYTVANDVTARDLQRERGGQWTRGKSFDTFCPLGPWIVTADEIPDPQDLRIRLRVNGEVRQDGNTSDMIFSVAELIAY 161

                        170       180
                 ....*....|....*....|
gi 446601745 379 LSEFMTLNPGDMIATGTPKG 398
Cdd:COG0179  162 LSQFMTLEPGDVILTGTPAG 181
FAA_hydrolase pfam01557
Fumarylacetoacetate (FAA) hydrolase family; This family consists of fumarylacetoacetate (FAA) ...
 226-398 3.17e-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: 202.52  E-value: 3.17e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745  226 FALGLNYADHASELEFK--PPEEP---LVFLKAPNTLTGDNQTSVRPNNIEYMHYEAELVVVIGKQARNVSEADAMDYVA 300
Cdd:pfam01557   1 VCVGLNYAEHAREAGKAepVPDFPiplVLFVKPPSSLIGPGDPIVRPAGVTKLDYEAELAVVIGRPARDVSPEEALDYIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745  301 GYTVCNDYAIRDYLENYYR-PNLRVKSRDGLTPMLSTIVPKEAIPDPHNLTLRTFVNGELRQQGTTADLIFSVPFLIAYL 379
Cdd:pfam01557  81 GYTLANDVSARDLQRREMPlQWFRGKSFDGFTPLGPWIVTRDELPDPGDLRLRLRVNGEVRQDGNTSDMIFSPAELIAHL 160

                         170
                  ....*....|....*....
gi 446601745  380 SEFMTLNPGDMIATGTPKG 398
Cdd:pfam01557 161 SQFMTLRPGDIILTGTPSG 179
YcgM COG0179
2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) ...
 3-204 7.31e-57

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: 186.04  E-value: 7.31e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745   3 GTIFAVALN---HRSQLDawqeafqqspyKAPPKTAVWFIKPRNTVIGCGEPIPFPQG-EKVLSGATVALIVGKTATKVR 78
Cdd:COG0179    6 GKIICVGLNyadHAAEMG-----------NDVPEEPVLFLKPPSALVGPGDPIPLPAGsGKLDYEGELAVVIGKRARNVS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745  79 EEDAAEYIAGYALANDVSLPE--ESFYRPAIKAKCRDGFCPIGETV----ALSNVDNLTIYTEINGRPADHWNTADLQRN 152
Cdd:COG0179   75 EEDALDHVAGYTVANDVTARDlqRERGGQWTRGKSFDTFCPLGPWIvtadEIPDPQDLRIRLRVNGEVRQDGNTSDMIFS 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446601745 153 AAQLLSALSEFATLNPGDAILLGTPQARVEIQPGDRVRVLAEGFPPLENPVV 204
Cdd:COG0179  155 VAELIAYLSQFMTLEPGDVILTGTPAGVGPLKPGDVVEVEIEGIGTLRNTVV 206
HpaG-N-term TIGR02305
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, N-terminal subunit; ...
 223-398 1.34e-49

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: 167.22  E-value: 1.34e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745  223 GTLFALGLNYADHASELEF--------KPPEEPLVFLKAPNTLTGDNQTSVRPNNIEYMHYEAELVVVIGKQARNVSEAD 294
Cdd:TIGR02305   1 GTVFGVALNYREQLDRLQEafqqapykAPPKTPVLYIKPRNTHNGCGQPIPLPAGVEKLRSGATLALVVGRTACRVREEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745  295 AMDYVAGYTVCNDYAIRDylENYYRPNLRVKSRDGLTPmLSTIVPKEAIPDPHNLTLRTFVNGELRQQGTTADLIFSVPF 374
Cdd:TIGR02305  81 ALDYVAGYALVNDVSLPE--DSYYRPAIKAKCRDGFCP-IGPEVPLSAIGNPDELTIYTYINGKPAQSNNTSNLVRSAAQ 157

                         170       180
                  ....*....|....*....|....
gi 446601745  375 LIAYLSEFMTLNPGDMIATGTPKG 398
Cdd:TIGR02305 158 LISELSEFMTLNPGDVLLLGTPEA 181
PRK12764 PRK12764
fumarylacetoacetate hydrolase family protein;
198-400 1.96e-43

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 237193 [Multi-domain]  Cd Length: 500  Bit Score: 158.76  E-value: 1.96e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745 198 PLENPVVDEREVTTRKSFPtqphphGTLFALGLNYADHASElEFKPPEEPLVFLKAPNTLTGDNQTSVRPNNIEYMHYEA 277
Cdd:PRK12764   3 SAPVPTVVAIVVAPLLARP------GKVIAVHLNYPSRAAQ-RGRTPAQPSYFLKPSSSLALSGGTVERPAGTELLAFEG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745 278 ELVVVIGKQARNVSEADAMDYVAGYTVCNDYAIRDYLENYYRPNLRVKSRDGLTPMLSTIVPKEAIpDPHNLTLRTFVNG 357
Cdd:PRK12764  76 EIALVIGRPARRVSPEDAWSHVAAVTAANDLGVYDLRYADKGSNLRSKGGDGFTPIGPALISARGV-DPAQLRVRTWVNG 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446601745 358 ELRQQGTTADLIFSVPFLIAYLSEFMTLNPGDMIATGTPKGLS 400
Cdd:PRK12764 155 ELVQDDTTEDLLFPFAQLVADLSQLLTLEEGDVILTGTPAGSS 197
HpaG-C-term TIGR02303
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, C-terminal subunit; ...
 3-206 2.02e-43

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: 152.27  E-value: 2.02e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745    3 GTIFAVALN---HRSQLDawqeafqqspyKAPPKTAVWFIKPRNTVIGCGEPIPFPQG-EKVLSGATVALIVGKTATKVR 78
Cdd:TIGR02303  43 GTIFALGLNyadHASELG-----------FSPPEEPLVFLKGNNTLTGHKGVTYRPKDvRFMHYECELAVVVGKTAKNVK 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745   79 EEDAAEYIAGYALANDVSLPE--ESFYRPAIKAKCRDGFCPIGETVA----LSNVDNLTIYTEINGRPADHWNTADLQRN 152
Cdd:TIGR02303 112 REDAMDYVLGYTIANDYAIRDylENYYRPNLRVKNRDTFTPIGPWIVdkedVEDPMNLWLRTYVNGELTQEGNTSDMIFS 191

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446601745  153 AAQLLSALSEFATLNPGDAILLGTPQARVEIQPGDRVRVLAEGFPPLENPVVDE 206
Cdd:TIGR02303 192 VAELIEYLSEFMTLEPGDVILTGTPKGLSDVKPGDVVRLEIEGVGALENPIVSE 245
FAA_hydrolase pfam01557
Fumarylacetoacetate (FAA) hydrolase family; This family consists of fumarylacetoacetate (FAA) ...
 6-203 5.06e-43

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: 150.13  E-value: 5.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745    6 FAVALNHRSQLDAWQeAFQQSPYKAPPKtaVWFIKPRNTVIGCGEPIPFPQGEKVLS-GATVALIVGKTATKVREEDAAE 84
Cdd:pfam01557   1 VCVGLNYAEHAREAG-KAEPVPDFPIPL--VLFVKPPSSLIGPGDPIVRPAGVTKLDyEAELAVVIGRPARDVSPEEALD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745   85 YIAGYALANDVS---LPEESFYRPAIKAKCRDGFCPIGETV----ALSNVDNLTIYTEINGRPADHWNTADLQRNAAQLL 157
Cdd:pfam01557  78 YIFGYTLANDVSardLQRREMPLQWFRGKSFDGFTPLGPWIvtrdELPDPGDLRLRLRVNGEVRQDGNTSDMIFSPAELI 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446601745  158 SALSEFATLNPGDAILLGTPQARVE-------IQPGDRVRVLAEGFPPLENPV 203
Cdd:pfam01557 158 AHLSQFMTLRPGDIILTGTPSGVGAgrappvfLKPGDTVEVEIEGLGTLRNTV 210
PRK10691 PRK10691
fumarylacetoacetate hydrolase family protein;
229-398 4.27e-37

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 182650  Cd Length: 219  Bit Score: 134.83  E-value: 4.27e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745 229 GLNYADHASELEFKPPEEPLVFLKAPNTLTGDNQTSVRPNNIEYMHYEAELVVVIGKQARNVSEADAMDYVAGYTVCNDY 308
Cdd:PRK10691  23 GSNYAKHIKEMGSATPEEPVLFIKPETALCDLRQPLAIPKDFGSVHHEVELAVLIGATLRQATEEHVRKAIAGYGVALDL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745 309 AIRDY---LENYYRPNLRVKSRDGLTPMLSTIVPKEAIPDPHNLTLRTFVNGELRQQGTTADLIFSVPFLIAYLSEFMTL 385
Cdd:PRK10691 103 TLRDLqgkMKKAGQPWEKAKAFDNSCPISGFIPVAEFTGDPQNTTLGLSVNGEVRQQGNTADMIHPIVPLIAYMSRFFTL 182

                        170
                 ....*....|...
gi 446601745 386 NPGDMIATGTPKG 398
Cdd:PRK10691 183 RAGDVVLTGTPEG 195
PRK12764 PRK12764
fumarylacetoacetate hydrolase family protein;
3-205 7.66e-23

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 237193 [Multi-domain]  Cd Length: 500  Bit Score: 100.60  E-value: 7.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745   3 GTIFAVALNHRSQldawqeAFQQSpykAPPKTAVWFIKPRNTVIGCGEPIPFPQGEKVLS-GATVALIVGKTATKVREED 81
Cdd:PRK12764  22 GKVIAVHLNYPSR------AAQRG---RTPAQPSYFLKPSSSLALSGGTVERPAGTELLAfEGEIALVIGRPARRVSPED 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745  82 AAEYIAGYALANDVSLPEesfYRPA-----IKAKCRDGFCPIG-ETVALSNVD--NLTIYTEINGRPADHWNTADLQRNA 153
Cdd:PRK12764  93 AWSHVAAVTAANDLGVYD---LRYAdkgsnLRSKGGDGFTPIGpALISARGVDpaQLRVRTWVNGELVQDDTTEDLLFPF 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446601745 154 AQLLSALSEFATLNPGDAILLGTPQARVEIQPGDRVRVLAEGFPP-------LENPVVD 205
Cdd:PRK12764 170 AQLVADLSQLLTLEEGDVILTGTPAGSSVAAPGDVVEVEVDAPADgapstgrLVTRVVE 228
PRK10691 PRK10691
fumarylacetoacetate hydrolase family protein;
30-212 1.09e-18

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 182650  Cd Length: 219  Bit Score: 84.37  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745  30 APPKTAVWFIKPRNTVIGCGEPIPFPQG-EKVLSGATVALIVGKTATKVREEDAAEYIAGYALANDVSLPE-----ESFY 103
Cdd:PRK10691  36 ATPEEPVLFIKPETALCDLRQPLAIPKDfGSVHHEVELAVLIGATLRQATEEHVRKAIAGYGVALDLTLRDlqgkmKKAG 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745 104 RPAIKAKCRDGFCPIGETVALSNVD----NLTIYTEINGRPADHWNTADLQRNAAQLLSALSEFATLNPGDAILLGTPQA 179
Cdd:PRK10691 116 QPWEKAKAFDNSCPISGFIPVAEFTgdpqNTTLGLSVNGEVRQQGNTADMIHPIVPLIAYMSRFFTLRAGDVVLTGTPEG 195

                        170       180       190
                 ....*....|....*....|....*....|...
gi 446601745 180 RVEIQPGDRVRVlaegfpplenpVVDEREVTTR 212
Cdd:PRK10691 196 VGPLQSGDELTV-----------TFNGHSLTTR 217
MhpD COG3971
2-keto-4-pentenoate hydratase [Secondary metabolites biosynthesis, transport and catabolism];
276-395 1.17e-04

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


Pssm-ID: 443171  Cd Length: 259  Bit Score: 43.58  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601745 276 EAELVVVIGK--QARNVSEADAMDYVAGYTVC---NDYAIRDYlenyyrpnlrvksrdGLTPMlSTI---------VPKE 341
Cdd:COG3971  104 EAEIAFVLGRdlPGPGVTLADVLAATDAVAPAieiVDSRIADW---------------KIGLA-DTIadnassggfVLGP 167

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446601745 342 AIPDPHNLTLRT-----FVNGELRQQGTTADL----IFSVPFLIAYLSEF-MTLNPGDMIATGT 395
Cdd:COG3971  168 PPVDPDDLDLRNvgvvlEKNGEVVATGAGAAVlghpLNAVAWLANKLAARgIPLKAGDIVLTGS 231
MopB_CT_Fdh-Nap-like cd00508
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ...
 136-191 9.42e-04

This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and other related proteins. Formate dehydrogenase H is a component of the anaerobic formate hydrogen lyase complex and catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. Formate dehydrogenase N (alpha subunit) is the major electron donor to the bacterial nitrate respiratory chain and nitrate reductases, Nap and Nas, catalyze the reduction of nitrate to nitrite. This CD (MopB_CT_Fdh-Nap-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.


Pssm-ID: 238282 [Multi-domain]  Cd Length: 120  Bit Score: 39.03  E-value: 9.42e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446601745 136 INGRPADHWNTADLQRNAAQLLSALSE-FATLNPGDAillgtpqARVEIQPGDRVRV 191
Cdd:cd00508    8 TTGRLLEHWHTGTMTRRSPRLAALAPEpFVEIHPEDA-------ARLGIKDGDLVRV 57
Molydop_binding pfam01568
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ...
 136-191 1.58e-03

Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules.


Pssm-ID: 426328 [Multi-domain]  Cd Length: 110  Bit Score: 38.02  E-value: 1.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446601745  136 INGRPADHWNTADLQRNAAQLLSALSEFATLNPGDAILLGtpqarveIQPGDRVRV 191
Cdd:pfam01568   4 ITGRVLGQYHSQTRTRRVLRLAKPEPEVVEIHPEDAAALG-------IKDGDLVEV 52
MopB_CT_Formate-Dh_H cd02790
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ...
 136-191 6.96e-03

Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. This CD (MopB_CT_Formate-Dh_H) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.


Pssm-ID: 239191 [Multi-domain]  Cd Length: 116  Bit Score: 36.45  E-value: 6.96e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446601745 136 INGRPADHWNTADLQRNAAQLLS-ALSEFATLNPGDAILLGtpqarveIQPGDRVRV 191
Cdd:cd02790    8 TTGRVLYHYHTGTMTRRAEGLDAiAPEEYVEINPEDAKRLG-------IEDGEKVRV 57
 
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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