HACL1_DICDI
ID HACL1_DICDI Reviewed; 580 AA.
AC Q54DA9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=2-hydroxyacyl-CoA lyase 1;
DE EC=4.1.2.63 {ECO:0000250|UniProtKB:Q8CHM7};
DE AltName: Full=2-hydroxyphytanoyl-CoA lyase;
DE Short=2-HPCL;
GN Name=hacl1; ORFNames=DDB_G0292402;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Peroxisomal 2-OH acyl-CoA lyase involved in the cleavage (C1
CC removal) reaction in the fatty acid alpha-oxydation in a thiamine
CC pyrophosphate (TPP)-dependent manner. Involved in the degradation of 3-
CC methyl-branched fatty acids and the shortening of 2-hydroxy long-chain
CC fatty acids. {ECO:0000250|UniProtKB:Q9UJ83}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-hydroxy-3-methyl fatty acyl-CoA = a 2-methyl-branched
CC fatty aldehyde + formyl-CoA; Xref=Rhea:RHEA:25375, ChEBI:CHEBI:49188,
CC ChEBI:CHEBI:57376, ChEBI:CHEBI:58783; EC=4.1.2.63;
CC Evidence={ECO:0000250|UniProtKB:Q8CHM7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25376;
CC Evidence={ECO:0000250|UniProtKB:Q8CHM7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an (R)-2-hydroxy-long-chain-fatty acyl-CoA = a long-chain
CC fatty aldehyde + formyl-CoA; Xref=Rhea:RHEA:67444, ChEBI:CHEBI:17176,
CC ChEBI:CHEBI:57376, ChEBI:CHEBI:170012; EC=4.1.2.63;
CC Evidence={ECO:0000250|UniProtKB:Q8CHM7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67445;
CC Evidence={ECO:0000250|UniProtKB:Q8CHM7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxy-3-methylhexadecanoyl-CoA = 2-methylpentadecanal +
CC formyl-CoA; Xref=Rhea:RHEA:25379, ChEBI:CHEBI:49190,
CC ChEBI:CHEBI:57376, ChEBI:CHEBI:58784;
CC Evidence={ECO:0000250|UniProtKB:Q8CHM7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25380;
CC Evidence={ECO:0000250|UniProtKB:Q8CHM7};
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:Q9UJ83};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55197;
CC Evidence={ECO:0000250|UniProtKB:Q9UJ83};
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:Q8CHM7};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000250|UniProtKB:Q8CHM7};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q8CHM7}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q9UJ83}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; AAFI02000190; EAL61180.1; -; Genomic_DNA.
DR RefSeq; XP_629587.1; XM_629585.1.
DR AlphaFoldDB; Q54DA9; -.
DR SMR; Q54DA9; -.
DR STRING; 44689.DDB0305141; -.
DR PaxDb; Q54DA9; -.
DR EnsemblProtists; EAL61180; EAL61180; DDB_G0292402.
DR GeneID; 8628647; -.
DR KEGG; ddi:DDB_G0292402; -.
DR dictyBase; DDB_G0292402; hacl1.
DR eggNOG; KOG1185; Eukaryota.
DR HOGENOM; CLU_013748_3_3_1; -.
DR InParanoid; Q54DA9; -.
DR OMA; FQEWPQV; -.
DR PhylomeDB; Q54DA9; -.
DR Reactome; R-DDI-389599; Alpha-oxidation of phytanate.
DR Reactome; R-DDI-9033241; Peroxisomal protein import.
DR PRO; PR:Q54DA9; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0106360; F:2-hydroxy-3-methylhexadecanoyl-CoA lyase activity; IEA:RHEA.
DR GO; GO:0016830; F:carbon-carbon lyase activity; ISS:UniProtKB.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; ISS:UniProtKB.
DR GO; GO:0001561; P:fatty acid alpha-oxidation; ISS:UniProtKB.
DR GO; GO:0006625; P:protein targeting to peroxisome; ISS:UniProtKB.
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; IPR000399; TPP-bd_CS.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR PANTHER; PTHR43710; PTHR43710; 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 Decarboxylase; Fatty acid metabolism; Lipid metabolism; Lyase; Magnesium;
KW Metal-binding; Peroxisome; Reference proteome; Thiamine pyrophosphate.
FT CHAIN 1..580
FT /note="2-hydroxyacyl-CoA lyase 1"
FT /id="PRO_0000327866"
FT REGION 413..494
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000250|UniProtKB:P40149"
FT BINDING 47
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P40149"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P40149"
FT BINDING 490
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P40149"
SQ SEQUENCE 580 AA; 63165 MW; 1C7F03B455883806 CRC64;
MDGVEIIAKS IKNSAIEKVF GIVGVPITPI AYELQAQGVG FFGFRNEQSC SYAASIVGYL
TGLPGLCMTV SGPGVVHALA GVLNAQSNGW PMILLSSSID QSLVGKGGFQ ECKQFESAEL
YCKKCYYLTE IDHFPEILKD AIETSLSNRP GPVYIQIPAD LIKSKCKESP NIREAAGYGT
IAIKSVVPDM KLIKDAVQLL SEAKRPLVIG GKGAAYCRSE NELLEFIEAT KIPFLPSPMG
KGLLRDDHPL VVGAARSYAL KNADVVLVLG ARLNWMFNFG KAPTFSTDVK FIIVDVDENQ
ASKTKNPNVV PEIAIVGDAR LSIAEMRKLF IGETDEQPQP PQDSLIKSMK MEESWWSNLN
QDIQVKTKSL ATLMSEPQNN DQEYLTYHKV FNALRVGGLF QEDTIFVNEG ANTMDIGRLC
IPQTLPRSRL DAGTLATMGV GVGYSVAAQI CFPDRSVVCI QGDSAFGFSA MEMEVAVRYK
LPIVFIVLNN NGVYEGLESM SDPKYTSSTE SASLHIPPTS LSVDTKYELI MQSFGGTGYS
ISTISNLLDI CKQIKSKQIS LPTLLNIKIK PTGTKPKIVH
