HACL_ARATH
ID HACL_ARATH Reviewed; 572 AA.
AC Q9LF46; Q682H7; Q9FNY6;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=2-hydroxyacyl-CoA lyase;
DE EC=4.1.-.-;
DE AltName: Full=2-hydroxyphytanoyl-CoA lyase;
DE Short=2-HPCL;
DE AltName: Full=Oxalyl-CoA decarboxylase;
GN Name=HACL; Synonyms=HPCL, OCD; OrderedLocusNames=At5g17380;
GN ORFNames=T10B6.40;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Van Veldhoven P.P.;
RT "Cloning of Arabidopsis oxalyl-CoA decarboxylase.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 511-572.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Catalyzes a carbon-carbon cleavage reaction; cleaves a 2-
CC hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty
CC aldehyde. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; AJ278629; CAC19854.1; -; mRNA.
DR EMBL; AL391142; CAC01733.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92419.1; -; Genomic_DNA.
DR EMBL; AY099774; AAM20625.1; -; mRNA.
DR EMBL; BT000284; AAN15603.1; -; mRNA.
DR EMBL; AK175390; BAD43153.1; -; mRNA.
DR PIR; T51575; T51575.
DR RefSeq; NP_197240.1; NM_121744.4.
DR AlphaFoldDB; Q9LF46; -.
DR SMR; Q9LF46; -.
DR BioGRID; 16880; 7.
DR STRING; 3702.AT5G17380.1; -.
DR iPTMnet; Q9LF46; -.
DR PaxDb; Q9LF46; -.
DR PRIDE; Q9LF46; -.
DR ProteomicsDB; 247216; -.
DR EnsemblPlants; AT5G17380.1; AT5G17380.1; AT5G17380.
DR GeneID; 831604; -.
DR Gramene; AT5G17380.1; AT5G17380.1; AT5G17380.
DR KEGG; ath:AT5G17380; -.
DR Araport; AT5G17380; -.
DR TAIR; locus:2167205; AT5G17380.
DR eggNOG; KOG1185; Eukaryota.
DR HOGENOM; CLU_013748_3_3_1; -.
DR InParanoid; Q9LF46; -.
DR OMA; DIGSHYI; -.
DR OrthoDB; 330201at2759; -.
DR PhylomeDB; Q9LF46; -.
DR BioCyc; ARA:AT5G17380-MON; -.
DR BioCyc; MetaCyc:AT5G17380-MON; -.
DR PRO; PR:Q9LF46; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LF46; baseline and differential.
DR Genevisible; Q9LF46; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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; IBA:GO_Central.
DR GO; GO:0001561; P:fatty acid alpha-oxidation; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acetylation; Decarboxylase; Lyase; Magnesium; Metal-binding;
KW Reference proteome; Thiamine pyrophosphate.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..572
FT /note="2-hydroxyacyl-CoA lyase"
FT /id="PRO_0000399509"
FT REGION 407..488
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 457
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 484
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 103
FT /note="M -> L (in Ref. 1; CAC19854)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="P -> S (in Ref. 1; CAC19854)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="R -> T (in Ref. 1; CAC19854)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 61470 MW; E422655F1EB58CFF CRC64;
MADKSETTPP SIDGNVLVAK SLSHLGVTHM FGVVGIPVTS LASRAMALGI RFIAFHNEQS
AGYAASAYGY LTGKPGILLT VSGPGCVHGL AGLSNAWVNT WPMVMISGSC DQRDVGRGDF
QELDQIEAVK AFSKLSEKAK DVREIPDCVS RVLDRAVSGR PGGCYLDIPT DVLRQKISES
EADKLVDEVE RSRKEEPIRG SLRSEIESAV SLLRKAERPL IVFGKGAAYS RAEDELKKLV
EITGIPFLPT PMGKGLLPDT HEFSATAARS LAIGKCDVAL VVGARLNWLL HFGESPKWDK
DVKFILVDVS EEEIELRKPH LGIVGDAKTV IGLLNREIKD DPFCLGKSNS WVESISKKAK
ENGEKMEIQL AKDVVPFNFL TPMRIIRDAI LAVEGPSPVV VSEGANTMDV GRSVLVQKEP
RTRLDAGTWG TMGVGLGYCI AAAVASPDRL VVAVEGDSGF GFSAMEVETL VRYNLAVVII
VFNNGGVYGG DRRGPEEISG PHKEDPAPTS FVPNAGYHKL IEAFGGKGYI VETPDELKSA
LAESFAARKP AVVNVIIDPF AGAESGRLQH KN
