2-Hydroxyacid oxidase 1
Details
- Name
- 2-Hydroxyacid oxidase 1
- Kind
- protein
- Synonyms
- 1.1.3.15
- Glycolate oxidase
- Glyoxylate oxidase
- GO
- GOX
- GOX1
- HAOX1
- Gene Name
- HAO1
- UniProtKB Entry
- Q9UJM8Swiss-Prot
- Organism
- Humans
- NCBI Taxonomy ID
- 9606
- Amino acid sequence
>lcl|BSEQ0012630|2-Hydroxyacid oxidase 1 MLPRLICINDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAET DLSTSVLGQRVSMPICVGATAMQRMAHVDGELATVRACQSLGTGMMLSSWATSSIEEVAE AGPEALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYLGNRLDDVRNRFKLPPQ LRMKNFETSTLSFSPEENFGDDSGLAAYVAKAIDPSISWEDIKWLRRLTSLPIVAKGILR GDDAREAVKHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDV LKALALGAKAVFVGRPIVWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLV RKNPLAVSKI
- Number of residues
- 370
- Molecular Weight
- 40923.945
- Theoretical pI
- 8.29
- GO Classification
- Processesglycine biosynthetic processComponentscytosol / intracellular membrane-bounded organelle
- General Function
- Broad substrate specificity (S)-2-hydroxy-acid oxidase that preferentially oxidizes glycolate (PubMed:10777549, PubMed:10978532, PubMed:17669354, PubMed:18215067). The glyoxylate produced by the oxidation of glycolate can then be utilized by alanine-glyoxylate aminotransferase for the peroxisomal synthesis of glycine; this pathway appears to be an important step for the detoxification of glyoxylate which, if allowed to accumulate, may be metabolized to oxalate with formation of kidney stones (PubMed:10978532, PubMed:17669354). Can also catalyze the oxidation of glyoxylate, and long chain hydroxyacids such as 2-hydroxyhexadecanoate and 2-hydroxyoctanoate, albeit with much lower catalytic efficiency (PubMed:10777549, PubMed:17669354, PubMed:18215067). Active in vitro with the artificial electron acceptor 2,6-dichlorophenolindophenol (DCIP), but O2 is believed to be the physiological electron acceptor, leading to the production of H2O2 (PubMed:10777549, PubMed:10978532, PubMed:17669354, PubMed:18215067). Is not active on L-lactate and 2-hydroxybutanoate (PubMed:10777549)
- Specific Function
- (S)-2-hydroxy-acid oxidase activity
- Pfam Domain Function
- FMN_dh (PF01070)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Peroxisome matrix
- Gene sequence
>lcl|BSEQ0012631|Hydroxyacid oxidase 1 (HAO1) ATGCTCCCCCGGCTAATTTGTATCAATGATTATGAACAACATGCTAAATCAGTACTTCCA AAGTCTATATATGACTATTACAGGTCTGGGGCAAATGATGAAGAAACTTTGGCTGATAAT ATTGCAGCATTTTCCAGATGGAAGCTGTATCCAAGGATGCTCCGGAATGTTGCTGAAACA GATCTGTCGACTTCTGTTTTAGGACAGAGGGTCAGCATGCCAATATGTGTGGGGGCTACG GCCATGCAGCGCATGGCTCATGTGGACGGCGAGCTTGCCACTGTGAGAGCCTGTCAGTCC CTGGGAACGGGCATGATGTTGAGTTCCTGGGCCACCTCCTCAATTGAAGAAGTGGCGGAA GCTGGTCCTGAGGCACTTCGTTGGCTGCAACTGTATATCTACAAGGACCGAGAAGTCACC AAGAAGCTAGTGCGGCAGGCAGAGAAGATGGGCTACAAGGCCATATTTGTGACAGTGGAC ACACCTTACCTGGGCAACCGTCTGGATGATGTGCGTAACAGATTCAAACTGCCGCCACAA CTCAGGATGAAAAATTTTGAAACCAGTACTTTATCATTTTCTCCTGAGGAAAATTTTGGA GACGACAGTGGACTTGCTGCATATGTGGCTAAAGCAATAGACCCATCTATCAGCTGGGAA GATATCAAATGGCTGAGAAGACTGACATCATTGCCAATTGTTGCAAAGGGCATTTTGAGA GGTGATGATGCCAGGGAGGCTGTTAAACATGGCTTGAATGGGATCTTGGTGTCGAATCAT GGGGCTCGACAACTCGATGGGGTGCCAGCCACTATTGATGTTCTGCCAGAAATTGTGGAG GCTGTGGAAGGGAAGGTGGAAGTCTTCCTGGACGGGGGTGTGCGGAAAGGCACTGATGTT CTGAAAGCTCTGGCTCTTGGCGCCAAGGCTGTGTTTGTGGGGAGACCAATCGTTTGGGGC TTAGCTTTCCAGGGGGAGAAAGGTGTTCAAGATGTCCTCGAGATACTAAAGGAAGAATTC CGGTTGGCCATGGCTCTGAGTGGGTGCCAGAATGTGAAAGTCATCGACAAGACATTGGTG AGGAAAAATCCTTTGGCCGTTTCCAAGATCTGA
- Chromosome Location
- 20
- Locus
- 20p12.3
- External Identifiers
Resource Link UniProtKB ID Q9UJM8 UniProtKB Entry Name HAOX1_HUMAN GenBank Protein ID 7530485 GenBank Gene ID AF244134 GeneCard ID HAO1 HGNC ID HGNC:4809 PDB ID(s) 2NZL, 2RDT, 2RDU, 2RDW, 2W0U, 5QIB, 5QIC, 5QID, 5QIE, 5QIF, 5QIG, 5QIH, 6GMB, 6GMC, 6W44, 6W45, 6W4C, 7M2O, 7R4N, 7R4O, 7R4P KEGG ID hsa:54363 NCBI Gene ID 54363 - General References
- Williams E, Cregeen D, Rumsby G: Identification and expression of a cDNA for human glycolate oxidase. Biochim Biophys Acta. 2000 Sep 7;1493(1-2):246-8. [Article]
- Jones JM, Morrell JC, Gould SJ: Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases. J Biol Chem. 2000 Apr 28;275(17):12590-7. [Article]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [Article]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
- Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
- Murray MS, Holmes RP, Lowther WT: Active site and loop 4 movements within human glycolate oxidase: implications for substrate specificity and drug design. Biochemistry. 2008 Feb 26;47(8):2439-49. doi: 10.1021/bi701710r. Epub 2008 Jan 24. [Article]
- Bourhis JM, Vignaud C, Pietrancosta N, Gueritte F, Guenard D, Lederer F, Lindqvist Y: Structure of human glycolate oxidase in complex with the inhibitor 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1,2,3-thiadiazole. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Dec 1;65(Pt 12):1246-53. doi: 10.1107/S1744309109041670. Epub 2009 Nov 27. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details N-sulfo-flavin mononucleotide experimental unknown target Details Benzoylformic Acid experimental unknown target Details Flavin mononucleotide approved, investigational unknown target Details 5-(dodecylthio)-1H-1,2,3-triazole-4-carboxylic acid experimental unknown target Details 3-(INDOL-3-YL) LACTATE experimental unknown target Details 3-Decyl-2,5-Dioxo-4-Hydroxy-3-Pyrroline experimental unknown target Details (2S)-2-HYDROXYOCTANOIC ACID experimental unknown target Details 4-Carboxy-5-(1-Pentyl)Hexylsulfanyl-1,2,3-Triazole experimental unknown target Details Phenylpyruvic acid experimental unknown target Details Lumasiran approved, investigational yes target antisense oligonucleotide Details