ID PXP1_YEAST Reviewed; 560 AA.
AC P39994; D3DLM9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 27-MAR-2024, entry version 166.
DE RecName: Full=2-hydroxyacyl-CoA lyase {ECO:0000305};
DE EC=4.1.2.63 {ECO:0000250|UniProtKB:Q9UJ83};
DE AltName: Full=Peroxisomal protein 1 {ECO:0000303|PubMed:26928762};
GN Name=PXP1 {ECO:0000303|PubMed:26928762}; OrderedLocusNames=YEL020C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP IDENTIFICATION, AND SUBCELLULAR LOCATION.
RX PubMed=26928762; DOI=10.1038/nmeth.3795;
RA Yofe I., Weill U., Meurer M., Chuartzman S., Zalckvar E., Goldman O.,
RA Ben-Dor S., Schuetze C., Wiedemann N., Knop M., Khmelinskii A.,
RA Schuldiner M.;
RT "One library to make them all: streamlining the creation of yeast libraries
RT via a SWAp-Tag strategy.";
RL Nat. Methods 13:371-378(2016).
RN [5]
RP DOMAIN, SUBCELLULAR LOCATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27392156; DOI=10.1111/tra.12426;
RA Noetzel C., Lingner T., Klingenberg H., Thoms S.;
RT "Identification of new fungal peroxisomal matrix proteins and revision of
RT the PTS1 consensus.";
RL Traffic 17:1110-1124(2016).
CC -!- FUNCTION: Catalyzes a carbon-carbon cleavage reaction; cleaves a 2-
CC hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty
CC aldehyde. {ECO:0000250|UniProtKB:Q9UJ83}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an (R)-2-hydroxy-long-chain-fatty acyl-CoA = a long-chain
CC fatty aldehyde + formyl-CoA; Xref=Rhea:RHEA:67444, ChEBI:CHEBI:17176,
CC ChEBI:CHEBI:57376, ChEBI:CHEBI:170012; EC=4.1.2.63;
CC Evidence={ECO:0000250|UniProtKB:Q9UJ83};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67445;
CC Evidence={ECO:0000250|UniProtKB:Q9UJ83};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-hydroxy-3-methyl fatty acyl-CoA = a 2-methyl-branched
CC fatty aldehyde + formyl-CoA; Xref=Rhea:RHEA:25375, ChEBI:CHEBI:49188,
CC ChEBI:CHEBI:57376, ChEBI:CHEBI:58783; EC=4.1.2.63;
CC Evidence={ECO:0000250|UniProtKB:Q9UJ83};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25376;
CC Evidence={ECO:0000250|UniProtKB:Q9UJ83};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8CHM7};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8CHM7};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250|UniProtKB:Q8CHM7};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000250|UniProtKB:Q8CHM7};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC Peroxisome matrix {ECO:0000269|PubMed:26928762,
CC ECO:0000269|PubMed:27392156}.
CC -!- DOMAIN: Peroxisomal targeting signal 1 (PTS1) is a tripeptide located
CC at the C-terminus of more than 95% of all peroxisomal matrix proteins.
CC The prototypical PTS1 is the terminal tripeptide SKL (serine-lysine-
CC leucine) but the consensus of PTS1 is defined as [S/A/H/C/E/P/Q/V]
CC [K/R/H/Q] [L/F]. However, this description of the PTS1 consensus must
CC probably be expanded beyond the terminal tripeptide.
CC {ECO:0000305|PubMed:27392156}.
CC -!- DISRUPTION PHENOTYPE: Does not affect growth on oleate.
CC {ECO:0000269|PubMed:27392156}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; U18530; AAB64497.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07633.1; -; Genomic_DNA.
DR PIR; S50439; S50439.
DR RefSeq; NP_010895.1; NM_001178835.1.
DR AlphaFoldDB; P39994; -.
DR SMR; P39994; -.
DR BioGRID; 36710; 148.
DR DIP; DIP-5281N; -.
DR IntAct; P39994; 1.
DR STRING; 4932.YEL020C; -.
DR MaxQB; P39994; -.
DR PaxDb; 4932-YEL020C; -.
DR PeptideAtlas; P39994; -.
DR EnsemblFungi; YEL020C_mRNA; YEL020C; YEL020C.
DR GeneID; 856694; -.
DR KEGG; sce:YEL020C; -.
DR AGR; SGD:S000000746; -.
DR SGD; S000000746; PXP1.
DR VEuPathDB; FungiDB:YEL020C; -.
DR eggNOG; KOG1185; Eukaryota.
DR GeneTree; ENSGT00940000156802; -.
DR HOGENOM; CLU_013748_3_3_1; -.
DR InParanoid; P39994; -.
DR OMA; PGPYGCL; -.
DR OrthoDB; 2020042at2759; -.
DR BioCyc; YEAST:G3O-30145-MONOMER; -.
DR Reactome; R-SCE-389599; Alpha-oxidation of phytanate.
DR Reactome; R-SCE-9033241; Peroxisomal protein import.
DR BioGRID-ORCS; 856694; 0 hits in 10 CRISPR screens.
DR PRO; PR:P39994; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39994; Protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IDA:SGD.
DR GO; GO:0016830; F:carbon-carbon lyase activity; ISS:SGD.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IBA:GO_Central.
DR GO; GO:0001561; P:fatty acid alpha-oxidation; IBA:GO_Central.
DR CDD; cd02004; TPP_BZL_OCoD_HPCL; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR045025; HACL1-like.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1.
DR PANTHER; PTHR43710:SF2; 2-HYDROXYACYL-COA LYASE 1; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lyase; Magnesium; Metal-binding; Peroxisome; Reference proteome;
KW Thiamine pyrophosphate.
FT CHAIN 1..560
FT /note="2-hydroxyacyl-CoA lyase"
FT /id="PRO_0000090826"
FT MOTIF 558..560
FT /note="Peroxisomal target signal 1 (PTS1)"
FT /evidence="ECO:0000269|PubMed:27392156"
FT BINDING 49
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P40149"
FT BINDING 446
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P40149"
FT BINDING 473
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P40149"
SQ SEQUENCE 560 AA; 61288 MW; 48523C4E6BCB441F CRC64;
MTTTATQHFA QLLQKYGIDT VFGIVGIPIV QLADTMVANG IKFIPCRNEQ AASYAASAYG
YISDKPGVLL IVGGPGLIHA LAGIYNSMSN RWPLLVIAGS SSQSDIHKGG FQELDQVSLL
SPFLKFTGKL TPDNIDMITQ KALNYCIQGT AGVSYIDVPA DFIEYEKPLE GNDRTGNELP
MILTPNICGP DPSKIKKVVQ LILQHKNKNI LIVIGKGAVK NSHEIRRLVN TFNLPFLPTP
MAKGIVPDSS PLNVSSARSQ ALKIADIVLV LGARLNWILH FGTSPKWNSE SIFIQFDSNP
ETLGDNNVSP GADLSIWGDI GLSVTALVEE LTRQDSCWKY SGVKQEIREK IQLNQTRLLR
KEKTRGAQLN YNQVYGTLRP LIDDYRTILV TEGANTMDIA RISFPTDAPR RRLDAGTNAT
MGIGLGYALA CKASHPELDV VLIQGDSAFG FSAMEIETAV RCQLALVIVV MNNSGIYHGE
KDIEGDLPPT ALSKNCRYDL VGKGLGANDF FVNTISELSR CFQQAVQLSR TKRETSVINV
IIEPGEQKQI AFAWQNKPRL
//
