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Conserved domains on  [gi|148298760|ref|NP_694498|]
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homogentisate 1,2-dioxygenase [Danio rerio]

Protein Classification

homogentisate 1,2-dioxygenase( domain architecture ID 10017572)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
hmgA TIGR01015
homogentisate 1,2-dioxygenase; Missing in human disease alkaptonuria. [Energy metabolism, ...
4-434 0e+00

homogentisate 1,2-dioxygenase; Missing in human disease alkaptonuria. [Energy metabolism, Amino acids and amines]


:

Pssm-ID: 273395  Cd Length: 429  Bit Score: 853.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760    4 LKYMSGFGNEFSSEdpRCPGSLPEGQNNPQVCPYGLYAEQLSGSAFTCPRSSNKRSWLYRILPSVRHKPFTRM--SCGDL 81
Cdd:TIGR01015   2 LKYLSGFGNEFESE--RVPGALPVGQNSPQKCPYGLYAEQLSGSAFTAPRHENKRSWLYRIRPSAAHEPFEPRdgNPGHV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760   82 TENWNEVEPDPNQLRWKPFNIPksSEKKVDFVSGLHTVCGAGDSKSRNGIAIHMYSCNTSMTDKCFQNADGDFLIVPQQG 161
Cdd:TIGR01015  80 TANFDEQAPDPNQLRWSPFPIP--SDEAVDFVDGLHTLCGAGDATSRTGLAIHIYLCNASMENRAFYNADGDFLIVPQQG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760  162 EILITTEFGKMMVEPNEICVIQQGMRFSVDVFGETRGYILEVFGAHFELPDLGPIGANGLANPRDFQTPVAWYEDRTIAT 241
Cdd:TIGR01015 158 ALLITTEFGRLLVEPNEICVIPRGVRFRVTVLEPARGYICEVYGAHFQLPDLGPIGANGLANPRDFEAPVAAFEDREVPG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760  242 GYTIVNKYQGKLFSCQQDFSPFNVVAWHGNYAPYKYNLENFMVINCVAFDHADPSIFTVLTAKSTRPGVAIADFVIFPPR 321
Cdd:TIGR01015 238 PYTVINKFQGSLFAAKQDHSPFDVVAWHGNYVPYKYDLKRFNVINSVSFDHPDPSIFTVLTAPSDRPGTAIADFVIFPPR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760  322 WGVADHTFRPPYYHRNCMSEFMGLIKGHYEAKEEGFQPGGGSLHSIMTPHGPDVDCFEKNSTALLKPERVAEGTMAFMFE 401
Cdd:TIGR01015 318 WLVAEKTFRPPYYHRNCMSEFMGLITGAYDAKEGGFVPGGGSLHNMMTPHGPDFDCFEKASNAKLKPERIADGTMAFMFE 397
                         410       420       430
                  ....*....|....*....|....*....|...
gi 148298760  402 SSFSMAVTKWGLeTCQRLDKNYYKCWEALKSHF 434
Cdd:TIGR01015 398 SSLSLAVTKWGA-TCQKLQEDYYKCWQPLKRHF 429
 
Name Accession Description Interval E-value
hmgA TIGR01015
homogentisate 1,2-dioxygenase; Missing in human disease alkaptonuria. [Energy metabolism, ...
4-434 0e+00

homogentisate 1,2-dioxygenase; Missing in human disease alkaptonuria. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273395  Cd Length: 429  Bit Score: 853.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760    4 LKYMSGFGNEFSSEdpRCPGSLPEGQNNPQVCPYGLYAEQLSGSAFTCPRSSNKRSWLYRILPSVRHKPFTRM--SCGDL 81
Cdd:TIGR01015   2 LKYLSGFGNEFESE--RVPGALPVGQNSPQKCPYGLYAEQLSGSAFTAPRHENKRSWLYRIRPSAAHEPFEPRdgNPGHV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760   82 TENWNEVEPDPNQLRWKPFNIPksSEKKVDFVSGLHTVCGAGDSKSRNGIAIHMYSCNTSMTDKCFQNADGDFLIVPQQG 161
Cdd:TIGR01015  80 TANFDEQAPDPNQLRWSPFPIP--SDEAVDFVDGLHTLCGAGDATSRTGLAIHIYLCNASMENRAFYNADGDFLIVPQQG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760  162 EILITTEFGKMMVEPNEICVIQQGMRFSVDVFGETRGYILEVFGAHFELPDLGPIGANGLANPRDFQTPVAWYEDRTIAT 241
Cdd:TIGR01015 158 ALLITTEFGRLLVEPNEICVIPRGVRFRVTVLEPARGYICEVYGAHFQLPDLGPIGANGLANPRDFEAPVAAFEDREVPG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760  242 GYTIVNKYQGKLFSCQQDFSPFNVVAWHGNYAPYKYNLENFMVINCVAFDHADPSIFTVLTAKSTRPGVAIADFVIFPPR 321
Cdd:TIGR01015 238 PYTVINKFQGSLFAAKQDHSPFDVVAWHGNYVPYKYDLKRFNVINSVSFDHPDPSIFTVLTAPSDRPGTAIADFVIFPPR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760  322 WGVADHTFRPPYYHRNCMSEFMGLIKGHYEAKEEGFQPGGGSLHSIMTPHGPDVDCFEKNSTALLKPERVAEGTMAFMFE 401
Cdd:TIGR01015 318 WLVAEKTFRPPYYHRNCMSEFMGLITGAYDAKEGGFVPGGGSLHNMMTPHGPDFDCFEKASNAKLKPERIADGTMAFMFE 397
                         410       420       430
                  ....*....|....*....|....*....|...
gi 148298760  402 SSFSMAVTKWGLeTCQRLDKNYYKCWEALKSHF 434
Cdd:TIGR01015 398 SSLSLAVTKWGA-TCQKLQEDYYKCWQPLKRHF 429
PLN02658 PLN02658
homogentisate 1,2-dioxygenase
6-434 0e+00

homogentisate 1,2-dioxygenase


Pssm-ID: 215355 [Multi-domain]  Cd Length: 435  Bit Score: 709.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760   6 YMSGFGNEFSSEdpRCPGSLPEGQNNPQVCPYGLYAEQLSGSAFTCPRSSNKRSWLYRILPSVRHKPFTRMS------CG 79
Cdd:PLN02658   1 YQSGFGNHFSSE--ALPGALPRGQNNPLLCPYGLYAEQLSGTAFTAPRKLNRRSWLYRIKPSVTHEPFKPRVpaheklVG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760  80 DLTENWNeVEPDPNQLRWKPFNIPkssEKKVDFVSGLHTVCGAGDSKSRNGIAIHMYSCNTSMTDKCFQNADGDFLIVPQ 159
Cdd:PLN02658  79 EFDPSNS-CETTPTQLRWRPFPVP---DSPVDFVDGLFTVCGAGSPFLRHGYAIHMYVANKSMDDCAFCNADGDFLIVPQ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760 160 QGEILITTEFGKMMVEPNEICVIQQGMRFSVDVF-GETRGYILEVFGAHFELPDLGPIGANGLANPRDFQTPVAWYEDRT 238
Cdd:PLN02658 155 QGRLWIKTELGKLQVSPGEIVVIPRGFRFAVDLPdGPSRGYVLEIFGGHFQLPDLGPIGANGLANPRDFLHPVAWFEDGS 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760 239 IAtGYTIVNKYQGKLFSCQQDFSPFNVVAWHGNYAPYKYNLENFMVINCVAFDHADPSIFTVLTAKSTRPGVAIADFVIF 318
Cdd:PLN02658 235 RP-GYTIVQKFGGELFTAKQDFSPFNVVAWHGNYVPYKYDLSKFCPVNTVLFDHADPSINTVLTAPTDKPGVALADFVIF 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760 319 PPRWGVADHTFRPPYYHRNCMSEFMGLIKGHYEAKEEGFQPGGGSLHSIMTPHGPDVDCFEKN-STALLKPERVAEGTMA 397
Cdd:PLN02658 314 PPRWLVAEHTFRPPYYHRNCMSEFMGLIYGSYEAKADGFLPGGASLHSCMTPHGPDTATYEATiARPCADAPSKLTGTLA 393
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 148298760 398 FMFESSFSMAVTKWGLEtCQRLDKNYYKCWEALKSHF 434
Cdd:PLN02658 394 FMFESSLIPRVCPWALE-SPFRDRDYYQCWIGLKSHF 429
HgmA_N pfam20510
Homogentisate 1,2-dioxygenase N-terminal; Homogentisate dioxygenase cleaves the aromatic ring ...
5-279 0e+00

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: 525.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760    5 KYMSGFGNEFSSEdpRCPGSLPEGQNNPQVCPYGLYAEQLSGSAFTCPRSSNKRSWLYRILPSVRHKPFTRMSCGDLTEN 84
Cdd:pfam20510   1 KYQSGFGNEFESE--AIPGALPVGQNSPQKCPYGLYAEQLSGTAFTAPRHENQRSWLYRIRPSVAHEPFFPRDGEHLTAP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760   85 WNEVEPDPNQLRWKPFNIPksSEKKVDFVSGLHTVCGAGDSKSRNGIAIHMYSCNTSMTDKCFQNADGDFLIVPQQGEIL 164
Cdd:pfam20510  79 FNGEAPDPNQLRWKPLPLP--SQEPVDFVEGLHTIAGAGDALVRTGLAIHIYLANKSMENRAFYNADGDFLIVPQQGELD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760  165 ITTEFGKMMVEPNEICVIQQGMRFSVDVF-GETRGYILEVFGAHFELPDLGPIGANGLANPRDFQTPVAWYEDRTiATGY 243
Cdd:pfam20510 157 ITTEFGRLLVEPGEICVIPRGVRFRVEVLdGPARGYICENYGAHFQLPDLGPIGANGLANPRDFLAPVAAYEDSE-VGEY 235
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 148298760  244 TIVNKYQGKLFSCQQDFSPFNVVAWHGNYAPYKYNL 279
Cdd:pfam20510 236 TVINKFQGKLFAAKQDHSPFDVVAWHGNYVPYKYDL 271
HmgA COG3508
Homogentisate 1,2-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
12-427 8.48e-162

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


Pssm-ID: 442731 [Multi-domain]  Cd Length: 382  Bit Score: 461.12  E-value: 8.48e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760  12 NEFSSEdpRCPGSLPEGQNNPQVCPYGLYAE-QLSGSAFTCPRSsnkrsWLYRILPSVRHKPFTRMscGDLTENWNEVEP 90
Cdd:COG3508    1 NEMATY--ALPGALPRKRHTPQRAPDGLYAEeLLGGEGFTGPRS-----WLYHIRPPTAHGDFEPV--EDGPKTADDGPL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760  91 DPNQLRWKPfnIPKSSekkVDFVSGLHTVCGAGDsksrngIAIHMYSCNTSMtDKCFQNADGDFLIVPQQGEILITTEFG 170
Cdd:COG3508   72 RPRHLRWNP--LPPDG---GDFVDGRRTLLGNGD------VAIHLYAANESM-DRFFRNADGDELIFVHEGSGRLETEFG 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760 171 KMMVEPNEICVIQQGMRFSVDVF-GETRGYILEVFGAHFELPDLGPIGANGLANPRDFQTPVAWYEDRtiATGYTIVNKY 249
Cdd:COG3508  140 HLEVEPGDYVVIPRGTTYRVELDdGPARGLVIENYGAPFRLPERGQLGEHAPYNERDFRTPVAAYEDD--EGEFEVVVKF 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760 250 QGKLFSCQQDFSPFNVVAWHGNYAPYKYNLENFMVINCVAFdHADPSIFTVLTAkstrPGVaiaDFVIFPPRW-GVADHT 328
Cdd:COG3508  218 RGRLWRATYPHSPLDVVGWDGNLYPYKFNIRDFEPITGIRF-HPPPSIHTTFTA----PNF---VVCSFVPRWlDVHPGA 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760 329 FRPPYYHRN-CMSEFMGLIKGHYEAKeEGFQPGGGSLHSIMTPHGPDVDCFEKnstALLKPERvAEGTMAFMFESSFSMA 407
Cdd:COG3508  290 IRPPYYHSNvDSDEVMFYVDGDFDSR-KGIEPGGISLHPCGIPHGPHPGAFEA---AINKGKK-ETDELAVMFDTRRPLR 364
                        410       420
                 ....*....|....*....|
gi 148298760 408 VTKWGLETcqrLDKNYYKCW 427
Cdd:COG3508  365 LTEAALEV---EDPDYADSW 381
cupin_HGO_N cd07000
homogentisate 1,2-dioxygenase and related proteins, N-terminal cupin domain; This family ...
95-205 1.17e-72

homogentisate 1,2-dioxygenase and related proteins, N-terminal cupin domain; This family includes homogentisate 1,2-dioxygenase (also known as homogentisate oxygenase, homogentisic acid oxidase, homogentisicase, HGO, HGD, HGDO, or HmgA; EC 1.13.11.5), which is involved in the metabolic degradation of phenylalanine and tyrosine. It catalyzes the crucial aromatic ring opening reaction, utilizing nonheme Fe2+ to incorporate both atoms of molecular oxygen into homogentisate (2,5-dihydroxyphenylacetate) to yield 4-maleylacetoacetate as part of the homogentisate pathway. HGO deficiency caused by critical mutations and polymorphic sites, causes the metabolic disease alkaptonuria (AKU), a rare disorder of autosomal recessive inheritance. Homogentisate accumulation causes insoluble ochronotic pigments to deposit in connective tissues, resulting in degenerative arthritis. These enzymes are found in prokaryotes, eukaryotes, and archaea. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380404 [Multi-domain]  Cd Length: 109  Bit Score: 223.55  E-value: 1.17e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760  95 LRWKPFNIPkssEKKVDFVSGLHTVCGAGDSKSRNGIAIHMYSCNTSMTDKCFQNADGDFLIVPQQGEILITTEFGKMMV 174
Cdd:cd07000    1 LRWKPFPIP---EEPTDFVDGLRTICGAGDPAARHGLAIHVYAANKSMDDRAFYNSDGDFLIVPQQGTLRIQTEFGKLEV 77
                         90       100       110
                 ....*....|....*....|....*....|..
gi 148298760 175 EPNEICVIQQGMRFSVDVF-GETRGYILEVFG 205
Cdd:cd07000   78 EPGEIAVIPRGIRFRVELPdGPARGYICEVYG 109
 
Name Accession Description Interval E-value
hmgA TIGR01015
homogentisate 1,2-dioxygenase; Missing in human disease alkaptonuria. [Energy metabolism, ...
4-434 0e+00

homogentisate 1,2-dioxygenase; Missing in human disease alkaptonuria. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273395  Cd Length: 429  Bit Score: 853.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760    4 LKYMSGFGNEFSSEdpRCPGSLPEGQNNPQVCPYGLYAEQLSGSAFTCPRSSNKRSWLYRILPSVRHKPFTRM--SCGDL 81
Cdd:TIGR01015   2 LKYLSGFGNEFESE--RVPGALPVGQNSPQKCPYGLYAEQLSGSAFTAPRHENKRSWLYRIRPSAAHEPFEPRdgNPGHV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760   82 TENWNEVEPDPNQLRWKPFNIPksSEKKVDFVSGLHTVCGAGDSKSRNGIAIHMYSCNTSMTDKCFQNADGDFLIVPQQG 161
Cdd:TIGR01015  80 TANFDEQAPDPNQLRWSPFPIP--SDEAVDFVDGLHTLCGAGDATSRTGLAIHIYLCNASMENRAFYNADGDFLIVPQQG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760  162 EILITTEFGKMMVEPNEICVIQQGMRFSVDVFGETRGYILEVFGAHFELPDLGPIGANGLANPRDFQTPVAWYEDRTIAT 241
Cdd:TIGR01015 158 ALLITTEFGRLLVEPNEICVIPRGVRFRVTVLEPARGYICEVYGAHFQLPDLGPIGANGLANPRDFEAPVAAFEDREVPG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760  242 GYTIVNKYQGKLFSCQQDFSPFNVVAWHGNYAPYKYNLENFMVINCVAFDHADPSIFTVLTAKSTRPGVAIADFVIFPPR 321
Cdd:TIGR01015 238 PYTVINKFQGSLFAAKQDHSPFDVVAWHGNYVPYKYDLKRFNVINSVSFDHPDPSIFTVLTAPSDRPGTAIADFVIFPPR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760  322 WGVADHTFRPPYYHRNCMSEFMGLIKGHYEAKEEGFQPGGGSLHSIMTPHGPDVDCFEKNSTALLKPERVAEGTMAFMFE 401
Cdd:TIGR01015 318 WLVAEKTFRPPYYHRNCMSEFMGLITGAYDAKEGGFVPGGGSLHNMMTPHGPDFDCFEKASNAKLKPERIADGTMAFMFE 397
                         410       420       430
                  ....*....|....*....|....*....|...
gi 148298760  402 SSFSMAVTKWGLeTCQRLDKNYYKCWEALKSHF 434
Cdd:TIGR01015 398 SSLSLAVTKWGA-TCQKLQEDYYKCWQPLKRHF 429
PLN02658 PLN02658
homogentisate 1,2-dioxygenase
6-434 0e+00

homogentisate 1,2-dioxygenase


Pssm-ID: 215355 [Multi-domain]  Cd Length: 435  Bit Score: 709.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760   6 YMSGFGNEFSSEdpRCPGSLPEGQNNPQVCPYGLYAEQLSGSAFTCPRSSNKRSWLYRILPSVRHKPFTRMS------CG 79
Cdd:PLN02658   1 YQSGFGNHFSSE--ALPGALPRGQNNPLLCPYGLYAEQLSGTAFTAPRKLNRRSWLYRIKPSVTHEPFKPRVpaheklVG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760  80 DLTENWNeVEPDPNQLRWKPFNIPkssEKKVDFVSGLHTVCGAGDSKSRNGIAIHMYSCNTSMTDKCFQNADGDFLIVPQ 159
Cdd:PLN02658  79 EFDPSNS-CETTPTQLRWRPFPVP---DSPVDFVDGLFTVCGAGSPFLRHGYAIHMYVANKSMDDCAFCNADGDFLIVPQ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760 160 QGEILITTEFGKMMVEPNEICVIQQGMRFSVDVF-GETRGYILEVFGAHFELPDLGPIGANGLANPRDFQTPVAWYEDRT 238
Cdd:PLN02658 155 QGRLWIKTELGKLQVSPGEIVVIPRGFRFAVDLPdGPSRGYVLEIFGGHFQLPDLGPIGANGLANPRDFLHPVAWFEDGS 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760 239 IAtGYTIVNKYQGKLFSCQQDFSPFNVVAWHGNYAPYKYNLENFMVINCVAFDHADPSIFTVLTAKSTRPGVAIADFVIF 318
Cdd:PLN02658 235 RP-GYTIVQKFGGELFTAKQDFSPFNVVAWHGNYVPYKYDLSKFCPVNTVLFDHADPSINTVLTAPTDKPGVALADFVIF 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760 319 PPRWGVADHTFRPPYYHRNCMSEFMGLIKGHYEAKEEGFQPGGGSLHSIMTPHGPDVDCFEKN-STALLKPERVAEGTMA 397
Cdd:PLN02658 314 PPRWLVAEHTFRPPYYHRNCMSEFMGLIYGSYEAKADGFLPGGASLHSCMTPHGPDTATYEATiARPCADAPSKLTGTLA 393
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 148298760 398 FMFESSFSMAVTKWGLEtCQRLDKNYYKCWEALKSHF 434
Cdd:PLN02658 394 FMFESSLIPRVCPWALE-SPFRDRDYYQCWIGLKSHF 429
HgmA_N pfam20510
Homogentisate 1,2-dioxygenase N-terminal; Homogentisate dioxygenase cleaves the aromatic ring ...
5-279 0e+00

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: 525.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760    5 KYMSGFGNEFSSEdpRCPGSLPEGQNNPQVCPYGLYAEQLSGSAFTCPRSSNKRSWLYRILPSVRHKPFTRMSCGDLTEN 84
Cdd:pfam20510   1 KYQSGFGNEFESE--AIPGALPVGQNSPQKCPYGLYAEQLSGTAFTAPRHENQRSWLYRIRPSVAHEPFFPRDGEHLTAP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760   85 WNEVEPDPNQLRWKPFNIPksSEKKVDFVSGLHTVCGAGDSKSRNGIAIHMYSCNTSMTDKCFQNADGDFLIVPQQGEIL 164
Cdd:pfam20510  79 FNGEAPDPNQLRWKPLPLP--SQEPVDFVEGLHTIAGAGDALVRTGLAIHIYLANKSMENRAFYNADGDFLIVPQQGELD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760  165 ITTEFGKMMVEPNEICVIQQGMRFSVDVF-GETRGYILEVFGAHFELPDLGPIGANGLANPRDFQTPVAWYEDRTiATGY 243
Cdd:pfam20510 157 ITTEFGRLLVEPGEICVIPRGVRFRVEVLdGPARGYICENYGAHFQLPDLGPIGANGLANPRDFLAPVAAYEDSE-VGEY 235
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 148298760  244 TIVNKYQGKLFSCQQDFSPFNVVAWHGNYAPYKYNL 279
Cdd:pfam20510 236 TVINKFQGKLFAAKQDHSPFDVVAWHGNYVPYKYDL 271
HmgA COG3508
Homogentisate 1,2-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
12-427 8.48e-162

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


Pssm-ID: 442731 [Multi-domain]  Cd Length: 382  Bit Score: 461.12  E-value: 8.48e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760  12 NEFSSEdpRCPGSLPEGQNNPQVCPYGLYAE-QLSGSAFTCPRSsnkrsWLYRILPSVRHKPFTRMscGDLTENWNEVEP 90
Cdd:COG3508    1 NEMATY--ALPGALPRKRHTPQRAPDGLYAEeLLGGEGFTGPRS-----WLYHIRPPTAHGDFEPV--EDGPKTADDGPL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760  91 DPNQLRWKPfnIPKSSekkVDFVSGLHTVCGAGDsksrngIAIHMYSCNTSMtDKCFQNADGDFLIVPQQGEILITTEFG 170
Cdd:COG3508   72 RPRHLRWNP--LPPDG---GDFVDGRRTLLGNGD------VAIHLYAANESM-DRFFRNADGDELIFVHEGSGRLETEFG 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760 171 KMMVEPNEICVIQQGMRFSVDVF-GETRGYILEVFGAHFELPDLGPIGANGLANPRDFQTPVAWYEDRtiATGYTIVNKY 249
Cdd:COG3508  140 HLEVEPGDYVVIPRGTTYRVELDdGPARGLVIENYGAPFRLPERGQLGEHAPYNERDFRTPVAAYEDD--EGEFEVVVKF 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760 250 QGKLFSCQQDFSPFNVVAWHGNYAPYKYNLENFMVINCVAFdHADPSIFTVLTAkstrPGVaiaDFVIFPPRW-GVADHT 328
Cdd:COG3508  218 RGRLWRATYPHSPLDVVGWDGNLYPYKFNIRDFEPITGIRF-HPPPSIHTTFTA----PNF---VVCSFVPRWlDVHPGA 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760 329 FRPPYYHRN-CMSEFMGLIKGHYEAKeEGFQPGGGSLHSIMTPHGPDVDCFEKnstALLKPERvAEGTMAFMFESSFSMA 407
Cdd:COG3508  290 IRPPYYHSNvDSDEVMFYVDGDFDSR-KGIEPGGISLHPCGIPHGPHPGAFEA---AINKGKK-ETDELAVMFDTRRPLR 364
                        410       420
                 ....*....|....*....|
gi 148298760 408 VTKWGLETcqrLDKNYYKCW 427
Cdd:COG3508  365 LTEAALEV---EDPDYADSW 381
HgmA_C pfam04209
Homogentisate 1,2-dioxygenase C-terminal; Homogentisate dioxygenase cleaves the aromatic ring ...
281-434 7.95e-103

Homogentisate 1,2-dioxygenase C-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 C-terminal active site domain.


Pssm-ID: 461227 [Multi-domain]  Cd Length: 153  Bit Score: 302.37  E-value: 7.95e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760  281 NFMVINCVAFDHADPSIFTVLTAKSTRPGVAIADFVIFPPRWGVADHTFRPPYYHRNCMSEFMGLIKGHYEAKEEGFQPG 360
Cdd:pfam04209   2 RFNVINTVSFDHPDPSIFTVLTAPSDRPGTANADFVIFPPRWLVAEHTFRPPYYHRNCMSEFMGLIYGAYDAKAGGFVPG 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148298760  361 GGSLHSIMTPHGPDVDCFEKNSTALLKPERVAEgTMAFMFESSFSMAVTKWGLEtCQRLDKNYYKCWEALKSHF 434
Cdd:pfam04209  82 GASLHSCMTPHGPDAESFEKASNADLKPHRIAD-TMAFMFESSLVLAVTEWALE-SPKLQEDYYKCWQGLKRHF 153
cupin_HGO_N cd07000
homogentisate 1,2-dioxygenase and related proteins, N-terminal cupin domain; This family ...
95-205 1.17e-72

homogentisate 1,2-dioxygenase and related proteins, N-terminal cupin domain; This family includes homogentisate 1,2-dioxygenase (also known as homogentisate oxygenase, homogentisic acid oxidase, homogentisicase, HGO, HGD, HGDO, or HmgA; EC 1.13.11.5), which is involved in the metabolic degradation of phenylalanine and tyrosine. It catalyzes the crucial aromatic ring opening reaction, utilizing nonheme Fe2+ to incorporate both atoms of molecular oxygen into homogentisate (2,5-dihydroxyphenylacetate) to yield 4-maleylacetoacetate as part of the homogentisate pathway. HGO deficiency caused by critical mutations and polymorphic sites, causes the metabolic disease alkaptonuria (AKU), a rare disorder of autosomal recessive inheritance. Homogentisate accumulation causes insoluble ochronotic pigments to deposit in connective tissues, resulting in degenerative arthritis. These enzymes are found in prokaryotes, eukaryotes, and archaea. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380404 [Multi-domain]  Cd Length: 109  Bit Score: 223.55  E-value: 1.17e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148298760  95 LRWKPFNIPkssEKKVDFVSGLHTVCGAGDSKSRNGIAIHMYSCNTSMTDKCFQNADGDFLIVPQQGEILITTEFGKMMV 174
Cdd:cd07000    1 LRWKPFPIP---EEPTDFVDGLRTICGAGDPAARHGLAIHVYAANKSMDDRAFYNSDGDFLIVPQQGTLRIQTEFGKLEV 77
                         90       100       110
                 ....*....|....*....|....*....|..
gi 148298760 175 EPNEICVIQQGMRFSVDVF-GETRGYILEVFG 205
Cdd:cd07000   78 EPGEIAVIPRGIRFRVELPdGPARGYICEVYG 109
 
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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