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Conserved domains on  [gi|502797295|ref|WP_013032271|]
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homogentisate 1,2-dioxygenase [Nitrosococcus halophilus]

Protein Classification

homogentisate 1,2-dioxygenase( domain architecture ID 10007501)

homogentisate 1,2-dioxygenase catalyzes the oxidative ring cleavage of the aromatic ring of homogentisate to yield maleylacetoacetate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HmgA COG3508
Homogentisate 1,2-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
3-372 0e+00

Homogentisate 1,2-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 442731 [Multi-domain]  Cd Length: 382  Bit Score: 520.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502797295   3 HWITLPKIEGVASKQAHADLPPES---YERELGKEGFYGPSTQMYHRHPPTGWSDVQ-----------GPLRPRAFDTTR 68
Cdd:COG3508    1 NEMATYALPGALPRKRHTPQRAPDglyAEELLGGEGFTGPRSWLYHIRPPTAHGDFEpvedgpktaddGPLRPRHLRWNP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502797295  69 LEANQT-SPWNAFRLLSNPHLQFRLWKTDSSMDHLVRNADGDELLFIHQGGGDLYCDYGHLAFREGDYILLPRGTLWRVE 147
Cdd:COG3508   81 LPPDGGdFVDGRRTLLGNGDVAIHLYAANESMDRFFRNADGDELIFVHEGSGRLETEFGHLEVEPGDYVVIPRGTTYRVE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502797295 148 -TENPLCLLLLEATADSYQLPDKGIVGSHAVFDPAVLDTPEIDESFLaqqtESEWRVVVKRRGALSTIIYPFNPLDAVGW 226
Cdd:COG3508  161 lDDGPARGLVIENYGAPFRLPERGQLGEHAPYNERDFRTPVAAYEDD----EGEFEVVVKFRGRLWRATYPHSPLDVVGW 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502797295 227 HGTLLPVRLNWRDIRPVMSHRYHIPPSAHTTFAASRFVVCTFCPRPIESDPGALKVPFFHNNDDYDEVLFYHQGEFFSRD 306
Cdd:COG3508  237 DGNLYPYKFNIRDFEPITGIRFHPPPSIHTTFTAPNFVVCSFVPRWLDVHPGAIRPPYYHSNVDSDEVMFYVDGDFDSRK 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502797295 307 NIHPGMMTLHPSGITHGPHPKAFEAGKKALRKETNEVAVMVDARDALEVAEFPPGVEWTGYVDSWK 372
Cdd:COG3508  317 GIEPGGISLHPCGIPHGPHPGAFEAAINKGKKETDELAVMFDTRRPLRLTEAALEVEDPDYADSWQ 382
 
Name Accession Description Interval E-value
HmgA COG3508
Homogentisate 1,2-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
3-372 0e+00

Homogentisate 1,2-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442731 [Multi-domain]  Cd Length: 382  Bit Score: 520.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502797295   3 HWITLPKIEGVASKQAHADLPPES---YERELGKEGFYGPSTQMYHRHPPTGWSDVQ-----------GPLRPRAFDTTR 68
Cdd:COG3508    1 NEMATYALPGALPRKRHTPQRAPDglyAEELLGGEGFTGPRSWLYHIRPPTAHGDFEpvedgpktaddGPLRPRHLRWNP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502797295  69 LEANQT-SPWNAFRLLSNPHLQFRLWKTDSSMDHLVRNADGDELLFIHQGGGDLYCDYGHLAFREGDYILLPRGTLWRVE 147
Cdd:COG3508   81 LPPDGGdFVDGRRTLLGNGDVAIHLYAANESMDRFFRNADGDELIFVHEGSGRLETEFGHLEVEPGDYVVIPRGTTYRVE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502797295 148 -TENPLCLLLLEATADSYQLPDKGIVGSHAVFDPAVLDTPEIDESFLaqqtESEWRVVVKRRGALSTIIYPFNPLDAVGW 226
Cdd:COG3508  161 lDDGPARGLVIENYGAPFRLPERGQLGEHAPYNERDFRTPVAAYEDD----EGEFEVVVKFRGRLWRATYPHSPLDVVGW 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502797295 227 HGTLLPVRLNWRDIRPVMSHRYHIPPSAHTTFAASRFVVCTFCPRPIESDPGALKVPFFHNNDDYDEVLFYHQGEFFSRD 306
Cdd:COG3508  237 DGNLYPYKFNIRDFEPITGIRFHPPPSIHTTFTAPNFVVCSFVPRWLDVHPGAIRPPYYHSNVDSDEVMFYVDGDFDSRK 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502797295 307 NIHPGMMTLHPSGITHGPHPKAFEAGKKALRKETNEVAVMVDARDALEVAEFPPGVEWTGYVDSWK 372
Cdd:COG3508  317 GIEPGGISLHPCGIPHGPHPGAFEAAINKGKKETDELAVMFDTRRPLRLTEAALEVEDPDYADSWQ 382
PLN02658 PLN02658
homogentisate 1,2-dioxygenase
105-346 5.68e-17

homogentisate 1,2-dioxygenase


Pssm-ID: 215355 [Multi-domain]  Cd Length: 435  Bit Score: 81.68  E-value: 5.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502797295 105 NADGDELLFIHQGGGDLYCDYGHLAFREGDYILLPRGTLWRVEtenplcllLLEATADSY---------QLPDKGIVGSH 175
Cdd:PLN02658 144 NADGDFLIVPQQGRLWIKTELGKLQVSPGEIVVIPRGFRFAVD--------LPDGPSRGYvleifgghfQLPDLGPIGAN 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502797295 176 AVFDPAVLDTPEideSFLAQQTESEWRVVVKRRGALSTIIYPFNPLDAVGWHGTLLPVRLNWRDIRPVMSHRY-HIPPSA 254
Cdd:PLN02658 216 GLANPRDFLHPV---AWFEDGSRPGYTIVQKFGGELFTAKQDFSPFNVVAWHGNYVPYKYDLSKFCPVNTVLFdHADPSI 292
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502797295 255 HTTFAASR---------FVVctFCPRPIESDpGALKVPFFHNNDDYDEV-LFYHQGEFFSrDNIHPGMMTLHPSGITHGP 324
Cdd:PLN02658 293 NTVLTAPTdkpgvaladFVI--FPPRWLVAE-HTFRPPYYHRNCMSEFMgLIYGSYEAKA-DGFLPGGASLHSCMTPHGP 368
                        250       260
                 ....*....|....*....|....*..
gi 502797295 325 HPKAFEA-----GKKALRKETNEVAVM 346
Cdd:PLN02658 369 DTATYEAtiarpCADAPSKLTGTLAFM 395
HgmA_N pfam20510
Homogentisate 1,2-dioxygenase N-terminal; Homogentisate dioxygenase cleaves the aromatic ring ...
98-232 4.57e-12

Homogentisate 1,2-dioxygenase N-terminal; Homogentisate dioxygenase cleaves the aromatic ring during the metabolic degradation of Phe and Tyr. Homogentisate dioxygenase deficiency causes alkaptonuria. The structure of homogentisate dioxygenase shows that the enzyme forms a hexamer arrangement comprised of a dimer of trimers. The active site iron ion is coordinated near the interface between the trimers. This entry represents the N-terminal domain which forms a jelly roll of beta-strands.


Pssm-ID: 466659  Cd Length: 271  Bit Score: 65.84  E-value: 4.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502797295   98 SMDHLV-RNADGDELLFIHQGGGDLYCDYGHLAFREGDYILLPRGTLWRVETEN-PLCLLLLEATADSYQLPDKGIVGSH 175
Cdd:pfam20510 133 SMENRAfYNADGDFLIVPQQGELDITTEFGRLLVEPGEICVIPRGVRFRVEVLDgPARGYICENYGAHFQLPDLGPIGAN 212
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502797295  176 AVFDPAVLDTP----EIDESflaqqteSEWRVVVKRRGALSTIIYPFNPLDAVGWHGTLLP 232
Cdd:pfam20510 213 GLANPRDFLAPvaayEDSEV-------GEYTVINKFQGKLFAAKQDHSPFDVVAWHGNYVP 266
 
Name Accession Description Interval E-value
HmgA COG3508
Homogentisate 1,2-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
3-372 0e+00

Homogentisate 1,2-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442731 [Multi-domain]  Cd Length: 382  Bit Score: 520.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502797295   3 HWITLPKIEGVASKQAHADLPPES---YERELGKEGFYGPSTQMYHRHPPTGWSDVQ-----------GPLRPRAFDTTR 68
Cdd:COG3508    1 NEMATYALPGALPRKRHTPQRAPDglyAEELLGGEGFTGPRSWLYHIRPPTAHGDFEpvedgpktaddGPLRPRHLRWNP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502797295  69 LEANQT-SPWNAFRLLSNPHLQFRLWKTDSSMDHLVRNADGDELLFIHQGGGDLYCDYGHLAFREGDYILLPRGTLWRVE 147
Cdd:COG3508   81 LPPDGGdFVDGRRTLLGNGDVAIHLYAANESMDRFFRNADGDELIFVHEGSGRLETEFGHLEVEPGDYVVIPRGTTYRVE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502797295 148 -TENPLCLLLLEATADSYQLPDKGIVGSHAVFDPAVLDTPEIDESFLaqqtESEWRVVVKRRGALSTIIYPFNPLDAVGW 226
Cdd:COG3508  161 lDDGPARGLVIENYGAPFRLPERGQLGEHAPYNERDFRTPVAAYEDD----EGEFEVVVKFRGRLWRATYPHSPLDVVGW 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502797295 227 HGTLLPVRLNWRDIRPVMSHRYHIPPSAHTTFAASRFVVCTFCPRPIESDPGALKVPFFHNNDDYDEVLFYHQGEFFSRD 306
Cdd:COG3508  237 DGNLYPYKFNIRDFEPITGIRFHPPPSIHTTFTAPNFVVCSFVPRWLDVHPGAIRPPYYHSNVDSDEVMFYVDGDFDSRK 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502797295 307 NIHPGMMTLHPSGITHGPHPKAFEAGKKALRKETNEVAVMVDARDALEVAEFPPGVEWTGYVDSWK 372
Cdd:COG3508  317 GIEPGGISLHPCGIPHGPHPGAFEAAINKGKKETDELAVMFDTRRPLRLTEAALEVEDPDYADSWQ 382
PLN02658 PLN02658
homogentisate 1,2-dioxygenase
105-346 5.68e-17

homogentisate 1,2-dioxygenase


Pssm-ID: 215355 [Multi-domain]  Cd Length: 435  Bit Score: 81.68  E-value: 5.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502797295 105 NADGDELLFIHQGGGDLYCDYGHLAFREGDYILLPRGTLWRVEtenplcllLLEATADSY---------QLPDKGIVGSH 175
Cdd:PLN02658 144 NADGDFLIVPQQGRLWIKTELGKLQVSPGEIVVIPRGFRFAVD--------LPDGPSRGYvleifgghfQLPDLGPIGAN 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502797295 176 AVFDPAVLDTPEideSFLAQQTESEWRVVVKRRGALSTIIYPFNPLDAVGWHGTLLPVRLNWRDIRPVMSHRY-HIPPSA 254
Cdd:PLN02658 216 GLANPRDFLHPV---AWFEDGSRPGYTIVQKFGGELFTAKQDFSPFNVVAWHGNYVPYKYDLSKFCPVNTVLFdHADPSI 292
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502797295 255 HTTFAASR---------FVVctFCPRPIESDpGALKVPFFHNNDDYDEV-LFYHQGEFFSrDNIHPGMMTLHPSGITHGP 324
Cdd:PLN02658 293 NTVLTAPTdkpgvaladFVI--FPPRWLVAE-HTFRPPYYHRNCMSEFMgLIYGSYEAKA-DGFLPGGASLHSCMTPHGP 368
                        250       260
                 ....*....|....*....|....*..
gi 502797295 325 HPKAFEA-----GKKALRKETNEVAVM 346
Cdd:PLN02658 369 DTATYEAtiarpCADAPSKLTGTLAFM 395
HgmA_N pfam20510
Homogentisate 1,2-dioxygenase N-terminal; Homogentisate dioxygenase cleaves the aromatic ring ...
98-232 4.57e-12

Homogentisate 1,2-dioxygenase N-terminal; Homogentisate dioxygenase cleaves the aromatic ring during the metabolic degradation of Phe and Tyr. Homogentisate dioxygenase deficiency causes alkaptonuria. The structure of homogentisate dioxygenase shows that the enzyme forms a hexamer arrangement comprised of a dimer of trimers. The active site iron ion is coordinated near the interface between the trimers. This entry represents the N-terminal domain which forms a jelly roll of beta-strands.


Pssm-ID: 466659  Cd Length: 271  Bit Score: 65.84  E-value: 4.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502797295   98 SMDHLV-RNADGDELLFIHQGGGDLYCDYGHLAFREGDYILLPRGTLWRVETEN-PLCLLLLEATADSYQLPDKGIVGSH 175
Cdd:pfam20510 133 SMENRAfYNADGDFLIVPQQGELDITTEFGRLLVEPGEICVIPRGVRFRVEVLDgPARGYICENYGAHFQLPDLGPIGAN 212
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502797295  176 AVFDPAVLDTP----EIDESflaqqteSEWRVVVKRRGALSTIIYPFNPLDAVGWHGTLLP 232
Cdd:pfam20510 213 GLANPRDFLAPvaayEDSEV-------GEYTVINKFQGKLFAAKQDHSPFDVVAWHGNYVP 266
 
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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