Q93099A8K417B2R8Z0HGD_HUMANHomogentisate 1,2-dioxygenase1.13.11.5Homogentisate oxygenaseHomogentisic acid oxidaseHomogentisicaseHGDHGOHomo sapiensHumanEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomoThe molecular basis of alkaptonuria.NUCLEOTIDE SEQUENCE [MRNA]VARIANTS AKU SER-230 AND GLY-300VARIANT HIS-80CHARACTERIZATION OF VARIANT AKU SER-230FUNCTIONCATALYTIC ACTIVITYHomogentisate 1,2-dioxygenase human cDNA sequence.NUCLEOTIDE SEQUENCE [MRNA]VARIANT HIS-80The human homogentisate 1,2-dioxygenase (HGO) gene.NUCLEOTIDE SEQUENCE [GENOMIC DNA]VARIANT HIS-80Complete sequencing and characterization of 21,243 full-length human cDNAs.NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]VARIANT HIS-80The DNA sequence, annotation and analysis of human chromosome 3.NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]VARIANT HIS-80The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]VARIANT HIS-80Lysine acetylation targets protein complexes and co-regulates major cellular functions.ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-98IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Initial characterization of the human central proteome.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Crystal structure of human homogentisate dioxygenase.X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS)METAL-BINDING SITESSUBUNITCOFACTORMolecular defects in alkaptonuria.VARIANT AKU ARG-161Mutation and polymorphism analysis of the human homogentisate 1, 2-dioxygenase gene in alkaptonuria patients.VARIANTS AKU ALA-42; GLY-97; GLY-153; ILE-189; THR-216; HIS-225; SER-227 AND VAL-368A novel point mutation associated with alkaptonuria.VARIANT AKU LYS-168Analysis of alkaptonuria (AKU) mutations and polymorphisms reveals that the CCC sequence motif is a mutational hot spot in the homogentisate 1,2 dioxygenase gene (HGO).VARIANTS AKU GLY-60; CYS-62; ASP-122; THR-230 AND GLU-291Ocular ochronosis in alkaptonuria patients carrying mutations in the homogentisate 1,2-dioxygenase gene.VARIANTS AKU PRO-25 AND VAL-368Allelic heterogeneity of alkaptonuria in Central Europe.VARIANTS AKU PRO-25; ARG-161; SER-230; ARG-270; GLY-300 AND VAL-368Mutational analysis of the HGO gene in Finnish alkaptonuria patients.VARIANTS AKU SER-330; VAL-368 AND ARG-371Mutation spectrum of homogentisic acid oxidase (HGD) in alkaptonuria.VARIANTS AKU ALA-3; ALA-42; GLY-60; PRO-61; CYS-62; LEU-73; THR-92; ARG-97; PHE-120; TRP-120; VAL-122; ARG-123; PRO-137; LEU-158; ARG-161; ASP-168; LYS-168; ARG-183; GLY-187; TRP-217; LEU-225; SER-230; PRO-258; ARG-269; ARG-270; GLY-300; PRO-321; LEU-359; ARG-360; GLU-362; VAL-368; LEU-373 AND GLN-401Identification of 11 novel homogentisate 1,2 dioxygenase variants in alkaptonuria patients and establishment of a novel LOVD-based HGD mutation database.VARIANTS AKU ARG-33; PHE-44; ARG-115; PRO-116; ALA-123; ALA-152; LEU-169; GLY-178; GLY-197; SER-219; ASN-276; ALA-360; ARG-361 AND HIS-374Novel mutations in the homogentisate 1,2 dioxygenase gene identified in Jordanian patients with alkaptonuria.VARIANTS AKU SER-227 AND ASN-369First report of HGD mutations in a Chinese with alkaptonuria.VARIANT AKU CYS-329An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.VARIANT [LARGE SCALE ANALYSIS] HIS-80IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Analysis of HGD gene mutations in patients with alkaptonuria from the United Kingdom: identification of novel mutations.VARIANTS AKU LYS-13; ASN-18; ALA-42; GLN-53; ARG-115; PHE-120; ARG-123; ARG-161; LEU-169; ASN-171; GLY-197; SER-219; HIS-225; PRO-225; SER-230; PHE-245; ARG-270; ASN-276; GLY-300; ASP-337; LEU-359; ARG-360; ARG-361; VAL-368 AND HIS-374VARIANT THR-172Catalyzes the conversion of homogentisate to maleylacetoacetate.homogentisate + O2 = 4-maleylacetoacetate + H(+)Fe cationAmino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 4/6.Homohexamer arranged as a dimer of trimers.Q93099Q93099false4Q93099Q96HA8false3Q93099P54274false2Highest expression in the prostate, small intestine, colon, kidney and liver.Alkaptonuria
AKU
An autosomal recessive error of metabolism characterized by an increase in the level of homogentisic acid. The clinical manifestations are urine that turns dark on standing and alkalinization, black ochronotic pigmentation of cartilage and collagenous tissues, and spine arthritis.The disease is caused by variants affecting the gene represented in this entry.Belongs to the homogentisate dioxygenase family.3D-structureAcetylationDioxygenaseDisease variantIronMetal-bindingOxidoreductasePhenylalanine catabolismReference proteomeTyrosine catabolismFe cationFe cationFe cationEAEKDNLPQREALFRQWGLPYCFLQHPTWGWRGRLPCFCWADAVGAGRLPGADGPLGREDEKFLKNMTEGQRRGSIRGITGWNSRHRLRPFSPSPTVFQPHRGRKNDEVGRPFCRSNDPLGAGRGRGEMVTNHRPLDHEQKRMAELKYISGFGNECSSEDPRCPGSLPEGQNNPQVCPYNLYAEQLSGSAFTCPRSTNKRSWLYRILPSVSHKPFESIDEGQVTHNWDEVDPDPNQLRWKPFEIPKASQKKVDFVSGLHTLCGAGDIKSNNGLAIHIFLCNTSMENRCFYNSDGDFLIVPQKGNLLIYTEFGKMLVQPNEICVIQRGMRFSIDVFEETRGYILEVYGVHFELPDLGPIGANGLANPRDFLIPIAWYEDRQVPGGYTVINKYQGKLFAAKQDVSPFNVVAWHGNYTPYKYNLKNFMVINSVAFDHADPSIFTVLTAKSVRPGVAIADFVIFPPRWGVADKTFRPPYYHRNCMSEFMGLIRGHYEAKQGGFLPGGGSLHSTMTPHGPDADCFEKASKVKLAPERIADGTMAFMFESSLSLAVTKWGLKASRCLDENYHKCWEPLKSHFTPNSRNPAEPN
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