You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Human Metabolome Database.
Identification
HMDB Protein ID HMDBP08729
Secondary Accession Numbers
  • 14452
Name 2-hydroxyacyl-CoA lyase 1
Synonyms
  1. 2-HPCL
  2. 2-hydroxyphytanoyl-CoA lyase
  3. Phytanoyl-CoA 2-hydroxylase 2
Gene Name HACL1
Protein Type Unknown
Biological Properties
General Function Involved in magnesium ion binding
Specific Function Catalyzes a carbon-carbon cleavage reaction; cleaves a 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde.
Pathways
  • fatty acid metabolism
  • Oxidation of Branched Chain Fatty Acids
  • Peroxisome
  • Phytanic Acid Peroxisomal Oxidation
  • Refsum Disease
Reactions
2-Hydroxyphytanoyl-CoA → Pristanal + Formyl-CoA details
GO Classification
Biological Process
fatty acid alpha-oxidation
protein oligomerization
Cellular Component
peroxisomal matrix
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
magnesium ion binding
vitamin binding
thiamin pyrophosphate binding
Molecular Function
magnesium ion binding
carbon-carbon lyase activity
thiamine pyrophosphate binding
Cellular Location
  1. Peroxisome
Gene Properties
Chromosome Location 3
Locus 3p25.1
SNPs HACL1
Gene Sequence
>1737 bp
ATGCCGGACAGTAACTTCGCAGAGCGCAGCGAGGAGCAGGTGTCTGGTGCTAAAGTCATC
GCTCAGGCCCTGAAAACGCAAGATGTGGAGTACATATTTGGCATCGTAGGCATCCCAGTG
ACCGAAATCGCCATTGCTGCCCAGCAGCTAGGCATCAAGTACATCGGGATGAGGAATGAG
CAAGCGGCTTGTTATGCTGCCTCCGCGATTGGATATCTGACAAGCAGGCCAGGAGTCTGC
CTTGTTGTTTCTGGCCCAGGTCTCATCCATGCCTTGGGCGGTATGGCAAATGCAAACATG
AACTGCTGGCCCTTGCTTGTGATTGGTGGTTCCTCTGAAAGAAACCAAGAAACAATGGGA
GCTTTCCAGGAGTTTCCTCAGGTTGAAGCTTGTAGATTATATACCAAGTTCTCTGCCCGC
CCAAGCAGCATAGAAGCTATTCCTTTTGTTATTGAAAAGGCAGTGAGAAGCAGTATCTAT
GGTCGTCCAGGTGCTTGCTATGTTGACATACCAGCAGATTTTGTGAACCTTCAGGTGAAT
GTGAATTCTATAAAGTACATGGAACGCTGCATGTCACCTCCTATTAGCATGGCAGAAACC
TCTGCTGTGTGCACGGCGGCTTCTGTTATTAGGAATGCCAAACAACCCCTTCTTATCATC
GGGAAAGGTGCTGCTTACGCTCATGCAGAAGAGAGTATCAAGAAATTGGTGGAGCAATAT
AAACTGCCATTTTTGCCCACCCCTATGGGGAAGGGTGTTGTCCCTGACAACCATCCATAC
TGTGTAGGTGCAGCCAGATCCAGGGCTTTGCAATTTGCTGATGTAATTGTGTTATTTGGT
GCCAGACTAAATTGGATTTTACATTTTGGACTGCCTCCAAGATATCAGCCAGATGTGAAG
TTTATCCAGGTTGATATCTGTGCAGAAGAATTGGGGAATAATGTAAAGCCCGCTGTTACT
TTGCTAGGAAACATACATGCTGTCACTAAGCAGCTTTTAGAGGAACTTGATAAAACACCA
TGGCAGTATCCTCCAGAGAGCAAGTGGTGGAAAACTCTGAGAGAAAAAATGAAGAGCAAT
GAAGCTGCATCCAAGGAACTAGCTTCTAAAAAATCCCTGCCTATGAATTATTACACAGTA
TTCTACCATGTTCAAGAACAACTACCTAGAGACTGTTTCGTGGTAAGTGAAGGAGCAAAT
ACTATGGACATTGGACGGACTGTGCTTCAGAACTACCTTCCTCGTCACAGGCTTGATGCT
GGTACTTTCGGAACAATGGGAGTTGGTTTGGGATTTGCTATTGCAGCTGCCGTGGTGGCT
AAAGATAGAAGCCCTGGGCAATGGATCATCTGTGTGGAAGGAGACAGTGCATTTGGGTTT
TCTGGCATGGAGGTAGAAACCATCTGCAGGTACAACTTGCCAATCATACTGTTGGTAGTG
AATAACAATGGAATTTACCAAGGTTTTGATACAGATACTTGGAAAGAAATGTTAAAATTT
CAAGATGCTACTGCAGTGGTCCCTCCAATGTGTTTGCTGCCAAATTCACATTATGAGCAA
GTCATGACTGCATTTGGAGGCAAAGGGTATTTTGTACAAACACCAGAAGAACTCCAAAAA
TCCCTGAGGCAGAGCCTAGCAGACACAACTAAACCTTCTCTTATCAACATCATGATTGAG
CCACAAGCCACACGGAAGGCCCAGGATTTTCATTGGCTGACCCGCTCTAATATGTAA
Protein Properties
Number of Residues 578
Molecular Weight 63728.095
Theoretical pI 7.354
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>2-hydroxyacyl-CoA lyase 1
MPDSNFAERSEEQVSGAKVIAQALKTQDVEYIFGIVGIPVTEIAIAAQQLGIKYIGMRNE
QAACYAASAIGYLTSRPGVCLVVSGPGLIHALGGMANANMNCWPLLVIGGSSERNQETMG
AFQEFPQVEACRLYTKFSARPSSIEAIPFVIEKAVRSSIYGRPGACYVDIPADFVNLQVN
VNSIKYMERCMSPPISMAETSAVCTAASVIRNAKQPLLIIGKGAAYAHAEESIKKLVEQY
KLPFLPTPMGKGVVPDNHPYCVGAARSRALQFADVIVLFGARLNWILHFGLPPRYQPDVK
FIQVDICAEELGNNVKPAVTLLGNIHAVTKQLLEELDKTPWQYPPESKWWKTLREKMKSN
EAASKELASKKSLPMNYYTVFYHVQEQLPRDCFVVSEGANTMDIGRTVLQNYLPRHRLDA
GTFGTMGVGLGFAIAAAVVAKDRSPGQWIICVEGDSAFGFSGMEVETICRYNLPIILLVV
NNNGIYQGFDTDTWKEMLKFQDATAVVPPMCLLPNSHYEQVMTAFGGKGYFVQTPEELQK
SLRQSLADTTKPSLINIMIEPQATRKAQDFHWLTRSNM
GenBank ID Protein 93004078
UniProtKB/Swiss-Prot ID Q9UJ83
UniProtKB/Swiss-Prot Entry Name HACL1_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_012260.2
GeneCard ID HACL1
GenAtlas ID HACL1
HGNC ID HGNC:17856
References
General References
  1. 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. [PubMed:15489334 ]
  2. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  3. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed:11042152 ]
  4. Foulon V, Antonenkov VD, Croes K, Waelkens E, Mannaerts GP, Van Veldhoven PP, Casteels M: Purification, molecular cloning, and expression of 2-hydroxyphytanoyl-CoA lyase, a peroxisomal thiamine pyrophosphate-dependent enzyme that catalyzes the carbon-carbon bond cleavage during alpha-oxidation of 3-methyl-branched fatty acids. Proc Natl Acad Sci U S A. 1999 Aug 31;96(18):10039-44. [PubMed:10468558 ]