ID A0A452EEK8_CAPHI Unreviewed; 609 AA.
AC A0A452EEK8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=2-hydroxyacyl-CoA lyase 1 {ECO:0000313|Ensembl:ENSCHIP00000010596.1};
GN Name=HACL1 {ECO:0000313|Ensembl:ENSCHIP00000010596.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000010596.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000010596.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000010596.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000194};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55197;
CC Evidence={ECO:0000256|ARBA:ARBA00000194};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; LWLT01000001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452EEK8; -.
DR SMR; A0A452EEK8; -.
DR STRING; 9925.ENSCHIP00000010596; -.
DR Ensembl; ENSCHIT00000018377.1; ENSCHIP00000010596.1; ENSCHIG00000013034.1.
DR GeneTree; ENSGT00940000156802; -.
DR Proteomes; UP000291000; Chromosome 1.
DR Bgee; ENSCHIG00000013034; Expressed in liver and 17 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005777; C:peroxisome; IEA:Ensembl.
DR GO; GO:0106359; F:2-hydroxyacyl-CoA lyase activity; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:Ensembl.
DR GO; GO:0001561; P:fatty acid alpha-oxidation; IEA:Ensembl.
DR GO; GO:1903512; P:phytanic acid metabolic process; IEA:Ensembl.
DR GO; GO:0006625; P:protein targeting to peroxisome; IEA:Ensembl.
DR CDD; cd02004; TPP_BZL_OCoD_HPCL; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
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_TPP-bd.
DR PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1.
DR PANTHER; PTHR43710:SF2; 2-HYDROXYACYL-COA LYASE 1; 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; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..131
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 207..335
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 432..588
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 609 AA; 66712 MW; 665570DCB37AD7FD CRC64;
MSESNLAARS DGLEGQVSGA RVIAQALKTQ DVNYMFGIVG IPVTEIALAA QEVGIRYIGM
RNEQAACYAA SAVGYLTGRP GVCLVVSGPG LIHGLGGMAN ANMNCWPLIV IGGSSERSQE
TMGAFQEFPQ VEACRLYSKF SARPSSIEAI PSIIEKAVRS SIYGRPGACY VDIPADFVNL
QVNVNSIKYV ECCMPPPISM AETSAVRMAA SVIRNAKQPL VIIGKGAAYA RAEESIRKLV
EQCKLPFLPT PMGKGVIRDN HPNCVAAARS RALQFADVIV LLGARLNWIL HFGLPPRYQP
DVKFIQADIC AEELGNNVRP AVTLLGDINA VTKQLLEQFD KTPWQYPPES EWWKVLREKM
KSNEALSKAL VSFAKFPVPP LQCTFVSSSW AKRTDVELAS KKSLPMNYYT VFYHVQEQLP
RDCFVVSEGA NTMDIGRTVL QNYLPRHRLD AGTFGTMGVG LGFAIAAAIV AKDRNPGKRV
ICVEGDSAFG FSGMEVETIC RYNLPIVLLV VNNNGIYQGF DTDSWKEMLK FGDATTVAPP
MSLLPHSHYE HVMTAFGGKG YFVQTPEELQ KSLRQSLADT TNPSLINIMI EPQATRKAQD
FHWLTQSNL
//
