HACL2_CAEEL
ID HACL2_CAEEL Reviewed; 640 AA.
AC O61856;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=2-hydroxyacyl-CoA lyase 2;
DE EC=4.1.2.- {ECO:0000250|UniProtKB:A1L0T0};
DE AltName: Full=IlvB-like protein;
GN ORFNames=T26C12.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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; FO081749; CCD74004.1; -; Genomic_DNA.
DR PIR; T33164; T33164.
DR RefSeq; NP_500306.1; NM_067905.3.
DR AlphaFoldDB; O61856; -.
DR SMR; O61856; -.
DR BioGRID; 42235; 2.
DR IntAct; O61856; 1.
DR STRING; 6239.T26C12.1; -.
DR EPD; O61856; -.
DR PaxDb; O61856; -.
DR PeptideAtlas; O61856; -.
DR EnsemblMetazoa; T26C12.1.1; T26C12.1.1; WBGene00020831.
DR GeneID; 177095; -.
DR KEGG; cel:CELE_T26C12.1; -.
DR UCSC; T26C12.1.1; c. elegans.
DR CTD; 177095; -.
DR WormBase; T26C12.1; CE26009; WBGene00020831; -.
DR eggNOG; KOG1185; Eukaryota.
DR GeneTree; ENSGT00940000158035; -.
DR HOGENOM; CLU_013748_3_3_1; -.
DR InParanoid; O61856; -.
DR OMA; CFGTSGP; -.
DR OrthoDB; 1132247at2759; -.
DR PhylomeDB; O61856; -.
DR PRO; PR:O61856; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00020831; Expressed in adult organism and 4 other tissues.
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: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 3: Inferred from homology;
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..640
FT /note="2-hydroxyacyl-CoA lyase 2"
FT /id="PRO_0000314829"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 477..557
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000250|UniProtKB:P40149"
FT BINDING 102
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P40149"
FT BINDING 528
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P40149"
FT BINDING 554
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P40149"
SQ SEQUENCE 640 AA; 69263 MW; D5F793843BF923C8 CRC64;
MVLFLIIAAI IIGLLLWKWL DVRSTDELTS MVKLLGSGNG QHVLSNAFQV DEKSKRHGGE
LVASVLKAHD VEEIFVLCGG HISPILVAAE KLGIKIVDTR HEVTAVFAAD AVARLRQSIG
VAAVTAGPGL TNTITAVKNA QMAESPLLLI GGAAPTLLKG RGALQDIDQM VLFRPLCKYV
ARVERLRDIV PTVREAIKAA KSGCPGPVFV EFPVDVLYPY ELVVKEIGFN PNAKGFIQRA
LNFYLRCHVS RQFGNAWAPQ TITPLPTNIP MPKSEKIQEI VQLVKSAKRP VLLIGSQATL
PPVKPADLVK AVEALGCPVF LGGMARGLLG KDHPLQMRQV RRDALKDADL TILAGTVCDF
RLSYGRTLSK KSKIVALNRN SSQLTKNEKA FWNSDVSVQA DVATSLVQVA NALGANHTTT
PTEWVKSLRE KDDEKESANA KKMEQKLTNG FLNPLNFLRT LDQSLPDDAI LVADGGDFVG
SAAYIVRPRG PLQWLDPGAF GTLGVGGGFA LGAKTVYPKR PVYIIWGDGS CGYSLMEYDT
FARHKLPVIG IVGNDACWTQ IAREQVPMFQ SSVAVDLART RYDNVAKSLG SWGETIDESN
ADSARKILDE ALAVCRSGEQ SALVNVLIGK TDFREGSISV
