ID   PXP1_SCHPO              Reviewed;         568 AA.
AC   Q9Y7M1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Putative 2-hydroxyacyl-CoA lyase {ECO:0000305};
DE            EC=4.1.-.- {ECO:0000305};
GN   ORFNames=SPBC725.04;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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   -!- 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:16823372}.
CC       Peroxisome matrix {ECO:0000250|UniProtKB:P39994}.
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:0000250|UniProtKB:P39994}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU329671; CAA22176.2; -; Genomic_DNA.
DR   PIR; T40656; T40656.
DR   RefSeq; NP_595484.1; NM_001021395.2.
DR   AlphaFoldDB; Q9Y7M1; -.
DR   SMR; Q9Y7M1; -.
DR   BioGRID; 277657; 30.
DR   IntAct; Q9Y7M1; 1.
DR   STRING; 4896.SPBC725.04.1; -.
DR   iPTMnet; Q9Y7M1; -.
DR   MaxQB; Q9Y7M1; -.
DR   PaxDb; Q9Y7M1; -.
DR   EnsemblFungi; SPBC725.04.1; SPBC725.04.1:pep; SPBC725.04.
DR   GeneID; 2541142; -.
DR   KEGG; spo:SPBC725.04; -.
DR   PomBase; SPBC725.04; -.
DR   VEuPathDB; FungiDB:SPBC725.04; -.
DR   eggNOG; KOG1185; Eukaryota.
DR   HOGENOM; CLU_013748_3_3_1; -.
DR   InParanoid; Q9Y7M1; -.
DR   OMA; DIGSHYI; -.
DR   PhylomeDB; Q9Y7M1; -.
DR   Reactome; R-SPO-389599; Alpha-oxidation of phytanate.
DR   Reactome; R-SPO-9033241; Peroxisomal protein import.
DR   PRO; PR:Q9Y7M1; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0106360; F:2-hydroxy-3-methylhexadecanoyl-CoA lyase activity; TAS:PomBase.
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; ISS:PomBase.
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; IPR011766; TPP_enzyme-bd_C.
DR   PANTHER; PTHR43710; PTHR43710; 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; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
PE   3: Inferred from homology;
KW   Cytoplasm; Decarboxylase; Lyase; Peroxisome; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..568
FT                   /note="Putative 2-hydroxyacyl-CoA lyase"
FT                   /id="PRO_0000315628"
FT   MOTIF           566..568
FT                   /note="Peroxisomal target signal 1 (PTS1)"
FT                   /evidence="ECO:0000250|UniProtKB:P39994"
SQ   SEQUENCE   568 AA;  61937 MW;  FFEDB9673A3CB066 CRC64;
     MSISFSELVA KTLLDLEVKV VFGIVGIPVI EICEAIQASG IRFVGFRNEQ SAAYAATAYG
     YLTQRPGVCV VVGGPGVVHA MAGVFNSKTN RWPLLLLAGS SETFQQNCGA FQELDQVSYL
     SPHTKLAVRP PSPKMVVDSI RRAYRVSMTG TPGTCYVDLP ANYIESTVDD FPKDPLPPIP
     SSPKCAPDPT QLQKAAYYLK NAKAPLLVVG KGAAYACAEK QLLEFVEHTG IPFLPSPMGK
     GLLPESHPLN VSSARSAALR NADVVLLAGA RLNWIFQYGL PPKWSPNAKF IQIDTNAETL
     GNNAADLDLA IWADVGLTID CLFKLVQTWK YSVGISTPYL RTLNETRSKN EKKALESRKS
     SIPLQMNYAL YVVNEELQSL SLKSKRNITW VSEGANTMDR GRQLLEVTHP RGRLDAGTMS
     TMGVGMGYAI ASAFAHSSDK IVVVEGDSAF GFSAMELETA IRNQLDLLVI VINNNGVYHG
     LDTDAYETLR DNHQLPTTAL GTSIRYDQIC EACGGKGFFV KNEEDLRSSL RKAWQTSSVS
     LINVMVDPEA ARKLTFAWMS STKVKPKL