ID   HACL2_XENLA             Reviewed;         649 AA.
AC   Q6DDK5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=2-hydroxyacyl-CoA lyase 2;
DE            EC=4.1.2.- {ECO:0000250|UniProtKB:A1L0T0};
DE   AltName: Full=Acetolactate synthase-like protein;
DE   AltName: Full=IlvB-like protein;
GN   Name=ilvbl; Synonyms=hacl2 {ECO:0000250|UniProtKB:A1L0T0};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endoplasmic reticulum 2-OH acyl-CoA lyase involved in the
CC       cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a
CC       thiamine pyrophosphate (TPP)-dependent manner. Involved in the
CC       phytosphingosine degradation pathway. {ECO:0000250|UniProtKB:A1L0T0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-hydroxyoctadecanoyl-CoA = formyl-CoA + heptadecanal;
CC         Xref=Rhea:RHEA:55196, ChEBI:CHEBI:57376, ChEBI:CHEBI:74116,
CC         ChEBI:CHEBI:138631; Evidence={ECO:0000250|UniProtKB:A1L0T0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55197;
CC         Evidence={ECO:0000250|UniProtKB:A1L0T0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-hydroxyhexadecanoyl-CoA = formyl-CoA + pentadecanal;
CC         Xref=Rhea:RHEA:55212, ChEBI:CHEBI:17302, ChEBI:CHEBI:57376,
CC         ChEBI:CHEBI:138654; Evidence={ECO:0000250|UniProtKB:A1L0T0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55213;
CC         Evidence={ECO:0000250|UniProtKB:A1L0T0};
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:A1L0T0};
CC       Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:A1L0T0}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; BC077553; AAH77553.1; -; mRNA.
DR   RefSeq; NP_001086850.1; NM_001093381.1.
DR   AlphaFoldDB; Q6DDK5; -.
DR   SMR; Q6DDK5; -.
DR   DNASU; 446685; -.
DR   GeneID; 446685; -.
DR   CTD; 10994; -.
DR   Xenbase; XB-GENE-6255656; ilvbl.L.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0001561; P:fatty acid alpha-oxidation; ISS:UniProtKB.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
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; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   PANTHER; PTHR18968; PTHR18968; 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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Fatty acid metabolism; Lipid metabolism; Lyase;
KW   Magnesium; Membrane; Metal-binding; Reference proteome;
KW   Thiamine pyrophosphate; Transmembrane; Transmembrane helix.
FT   CHAIN           1..649
FT                   /note="2-hydroxyacyl-CoA lyase 2"
FT                   /id="PRO_0000314828"
FT   TRANSMEM        2..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          474..554
FT                   /note="Thiamine pyrophosphate binding"
FT                   /evidence="ECO:0000250|UniProtKB:P40149"
FT   BINDING         84
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250|UniProtKB:P40149"
FT   BINDING         525
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P40149"
FT   BINDING         551
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P40149"
SQ   SEQUENCE   649 AA;  71429 MW;  4A369CF0FE3B1D1F CRC64;
     MFHLIPFVVA FLLVFLTWFL IKKLRKVIIF ELDQNSKHFG GELVADVLKA HDVRFLFTLC
     GGHISPILVA AERQNIRVID VRHEASAVFA ADAVSRLSGT VGVAAVTAGP GLTNTVTAVK
     NAQMAESPIV LLAGAAAGLL RGRGSLQDID QLSLFRPLCK WSGRVNCVKD IVPMLCKAFY
     LARSGTPGPV LVEFPIDTLY PYSLVRQHLR ISDNPQSWRQ RFTNWYLRFY LFRLFANGFR
     IQPCLPGQVP TQIPVEIPSI PWPSTKSIDQ LVWLLSQAKR PVIVVSSQAL LPPVPATQTA
     EHVKSLRIPV YLTGMARGLL GRHHPCVFRH ARRAALRVAD LIILAGSVCD FRMDYGRVLN
     RKAKIVIINR DKKQLYLNSD IFWRPYLAIR GDVGTALKEL SISLNDRFPC LSDFRCPTEW
     VGELLAREHH RDEEIRQSSL TQPAERINPL SVLWQLEHNG LTDQESIIVA DGGDFVGSAA
     YILRPRGPLS WLDPGPFGTL GVGGGFALGA KLCRPQAHVW VVYGDGSAGY SLAEWDTMAR
     HKAPAIGVIG NDACWSQIAR DQLGLFGSNV ACGLQSTRYD LVGAAYAGAD PLNSTLSVED
     SGAFLVTEKN LDNLSDYMAH ARELSDRGLP SIINCNIAAS GFREGSISL