HACL2_BOVIN
ID HACL2_BOVIN Reviewed; 632 AA.
AC A6QQT9; Q5E9W6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 78.
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=AHAS, HACL2 {ECO:0000250|UniProtKB:A1L0T0};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI49990.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAX08821.1; Type=Erroneous initiation; 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; BT020804; AAX08821.1; ALT_INIT; mRNA.
DR EMBL; BC149989; AAI49990.1; ALT_INIT; mRNA.
DR RefSeq; NP_001015535.1; NM_001015535.1.
DR RefSeq; XP_005208552.1; XM_005208495.3.
DR AlphaFoldDB; A6QQT9; -.
DR SMR; A6QQT9; -.
DR STRING; 9913.ENSBTAP00000020206; -.
DR PaxDb; A6QQT9; -.
DR PeptideAtlas; A6QQT9; -.
DR PRIDE; A6QQT9; -.
DR Ensembl; ENSBTAT00000081902; ENSBTAP00000072484; ENSBTAG00000015186.
DR GeneID; 506955; -.
DR KEGG; bta:506955; -.
DR CTD; 10994; -.
DR VEuPathDB; HostDB:ENSBTAG00000015186; -.
DR VGNC; VGNC:30179; ILVBL.
DR eggNOG; KOG1185; Eukaryota.
DR GeneTree; ENSGT00940000158035; -.
DR HOGENOM; CLU_013748_3_3_1; -.
DR InParanoid; A6QQT9; -.
DR OMA; CFGTSGP; -.
DR OrthoDB; 1132247at2759; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000015186; Expressed in liver and 104 other tissues.
DR ExpressionAtlas; A6QQT9; 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: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..632
FT /note="2-hydroxyacyl-CoA lyase 2"
FT /id="PRO_0000314824"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 470..550
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000250|UniProtKB:P40149"
FT BINDING 98
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P40149"
FT BINDING 521
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P40149"
FT BINDING 547
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P40149"
FT CONFLICT 10
FT /note="A -> V (in Ref. 1; AAX08821)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 632 AA; 68110 MW; 13BC87555BF24616 CRC64;
METAVAAAPA WGFFSSFLLL AFGTLVAALL GAAHRLGLFY QLMHKVDTAS TRHGGENVAA
VLKAHGVRFL FTLVGGHISP LLVACEKLGI RVVDTRHEVT AVFAADAVAR LTGTVGVAAV
TAGPGLTNTV TAVKNAQIAQ SPVLLLGGAA STLLQNRGAL QAIDQIALFR PLCKFCASVR
RVRDIIPTLR AAMAAAQSGT PGPVFVELPL DVLYPYFMVQ KEMVPAKPPK GLMSRAVHWY
LANSLANLFA GAWEPQPEGP LPLDIPQASP QQVQRCVEIL SRAKKPLMLI GSQALLPPTS
SDKLRVAVET LGIPCFLAGM ARGLLGRNHP LHFRQNRRAA LKKADVVVLA GAVCDFRLSY
GRVLSRSSKI IVVNRDRKEM LINSDIFWKP QEAVQGDVGS FVVKLVEGLR GQMWASDWAE
ELRQADQQKE QAFREKALMP VAQHLNPVRV LQLVEDTLPD NSILVVDGGD FVGTAAYLVQ
PRGPLRWLDP GAFGTLGVGA GFALGAKLCR PDAEVWCLFG DGAFGYSLIE FDTFVRHKIP
VMALIGNDAG WTQISREQVP SLGSNVACGL AYTDYHKAAQ GLGAQGLLLS RENEDQVVKV
LRDAQQWCQD GHPVVVNILI GRTDFRDGSI AM
