ID   HACL_ORYSJ              Reviewed;         577 AA.
AC   Q0JMH0;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 3.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=2-hydroxyacyl-CoA lyase;
DE            EC=4.1.-.-;
DE   AltName: Full=2-hydroxyphytanoyl-CoA lyase;
DE            Short=2-HPCL;
DE   AltName: Full=Oxalyl-CoA decarboxylase;
GN   OrderedLocusNames=Os01g0505400, LOC_Os01g32080;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
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}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF05058.2; Type=Erroneous gene model prediction; Evidence={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; AP008207; BAF05058.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015616825.1; XM_015761339.1.
DR   AlphaFoldDB; Q0JMH0; -.
DR   SMR; Q0JMH0; -.
DR   STRING; 4530.OS01T0505400-01; -.
DR   PaxDb; Q0JMH0; -.
DR   PRIDE; Q0JMH0; -.
DR   GeneID; 4324491; -.
DR   KEGG; osa:4324491; -.
DR   eggNOG; KOG1185; Eukaryota.
DR   HOGENOM; CLU_3194166_0_0_1; -.
DR   InParanoid; Q0JMH0; -.
DR   OrthoDB; 330201at2759; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   Genevisible; Q0JMH0; OS.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
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   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-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.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Magnesium; Metal-binding; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..577
FT                   /note="2-hydroxyacyl-CoA lyase"
FT                   /id="PRO_0000424907"
FT   REGION          412..493
FT                   /note="Thiamine pyrophosphate binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         59
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         462
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         489
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   577 AA;  60826 MW;  21C81E51F10C3689 CRC64;
     MATDTAAPAA MKVDGSALAG RALAAAGARH MFGVVGIPVT SLASRAAAAG VRFLAFRNEQ
     SAGYAAAAYG FLTGSPGLLL TVSGPGCVHG LAGLSHATAN AWPLLMVSGS CSQPDAGRGD
     FQELDQIAAT KPFIKIAVKA TTIADIPRLV FQALAATVSG RPGGCYLDIP SDVLHQTLTE
     SEAAALIDAA AADSAKSDSS PPKHKSLDEG IEKAAELLRR AERPLVVFGK GAAYSRAEDA
     IWKLVDTTGI PFLPTPMGKG VVPDTHPLSA TAARSLAIGQ CDVALVVGAR LNWLLHFGEP
     PKWSKDVKFI LVDVCEEEIE LRKPHVGIVG DAKRVVELIN REIKDQPFCL APSHPWVEAI
     TKKARDNVLK MEAQLAKDVV PFNFLTPLRI IRDAILAEGN PAPVVVSEGA NTMDVGRAVL
     VQNEPRTRLD AGTWGTMGVG LGFCVAAAVA EPDRLVVAVE GDSGFGFSAM EVETLVRYQL
     PVVVIVFNNN GVYGGDRRSP DEITGPYKDD PAPTSFVPAA GYHKMMEAFG GKGYLVETPD
     ELKSALSESF RARKPAVINV IIDPYAGAES GRMQHKN