ID   HACL2_DANRE             Reviewed;         621 AA.
AC   Q6NV04;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
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; ORFNames=zgc:66376, zgc:85697;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-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.
CC       {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; BC068362; AAH68362.1; -; mRNA.
DR   RefSeq; NP_956960.2; NM_200666.2.
DR   AlphaFoldDB; Q6NV04; -.
DR   SMR; Q6NV04; -.
DR   STRING; 7955.ENSDARP00000004404; -.
DR   PaxDb; Q6NV04; -.
DR   Ensembl; ENSDART00000016271; ENSDARP00000004404; ENSDARG00000017126.
DR   Ensembl; ENSDART00000177181; ENSDARP00000143612; ENSDARG00000017126.
DR   GeneID; 393639; -.
DR   KEGG; dre:393639; -.
DR   CTD; 10994; -.
DR   ZFIN; ZDB-GENE-040426-1623; ilvbl.
DR   eggNOG; KOG1185; Eukaryota.
DR   GeneTree; ENSGT00940000158035; -.
DR   HOGENOM; CLU_013748_3_3_1; -.
DR   InParanoid; Q6NV04; -.
DR   OMA; CFGTSGP; -.
DR   OrthoDB; 1132247at2759; -.
DR   PhylomeDB; Q6NV04; -.
DR   TreeFam; TF354221; -.
DR   PRO; PR:Q6NV04; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 18.
DR   Bgee; ENSDARG00000017126; Expressed in intestine and 25 other tissues.
DR   ExpressionAtlas; Q6NV04; baseline and differential.
DR   GO; GO:0005948; C:acetolactate synthase complex; IBA:GO_Central.
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:0003984; F:acetolactate synthase activity; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
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:0048701; P:embryonic cranial skeleton morphogenesis; IMP:ZFIN.
DR   GO; GO:0001561; P:fatty acid alpha-oxidation; ISS:UniProtKB.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
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..621
FT                   /note="2-hydroxyacyl-CoA lyase 2"
FT                   /id="PRO_0000314827"
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          459..539
FT                   /note="Thiamine pyrophosphate binding"
FT                   /evidence="ECO:0000250|UniProtKB:P40149"
FT   BINDING         87
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250|UniProtKB:P40149"
FT   BINDING         510
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P40149"
FT   BINDING         536
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P40149"
SQ   SEQUENCE   621 AA;  67036 MW;  B56AF5DB90B4A026 CRC64;
     MDISMYLGCS LGAALGGVIF ASYKLGLLYQ LFHKTERQSP RHGGESVAEV LRSHGVKFVF
     TLVGGHISPI LVACEKLGIR IVDTRHEATA VFAADAVARL SGTVGVAAVT AGPGLTNTVT
     AVKNAQMAES PLLLIGGAAA TLLQGRGALQ DIDQMSLFKP LCKFCASVRT VREIVPTVRK
     ALAIAQSGTP GPVFIEFPID TLYPYHVVEK EFAPKNTPKG LMGKIIAWYL KNHLSNLFAG
     AWESRDLSPL PVHIPHATDD QVQRCVELVS RAKKPVILLG SQATLPPTPA DDIRKALESL
     GIPCFLGGMS RGLLGKNSPL HIRQNRRDAL KDADLVLLAG TVCDFRLSYG RVLNRRSKII
     AVNRDKSQLL KNSDMFWKPT VAIQGDAGSF LLNLSKALKG HRCPEEWPQS LKEGDNVKEK
     ANRAKADEKT ERHLNPLSVL HRVDELLAED SIIVADGGDF VGSAAYIMRP RGPLCWLDPG
     AFGTLGVGGG FALGAKLCRP ESEVWIVYGD GSLGYTVAEF DTFTRHKTPV IALVGNDACW
     SQISREQVPM LGSNVACGLA FTDYHVVADG YGGKGYLIGR EDESQLEDII KKAQKECKEG
     KAVLLNVLIG KTNFREGSIS V