ID A0A072U4V2_MEDTR Unreviewed; 568 AA.
AC A0A072U4V2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=2-hydroxyacyl-CoA lyase {ECO:0000313|EMBL:KEH24737.1};
DE SubName: Full=Putative oxalyl-CoA decarboxylase {ECO:0000313|EMBL:RHN49666.1};
DE EC=4.1.1.8 {ECO:0000313|EMBL:RHN49666.1};
GN Name=25495093 {ECO:0000313|EnsemblPlants:KEH24737};
GN OrderedLocusNames=MTR_6g004200 {ECO:0000313|EMBL:KEH24737.1};
GN ORFNames=MtrunA17_Chr6g0449041 {ECO:0000313|EMBL:RHN49666.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000313|EMBL:KEH24737.1, ECO:0000313|Proteomes:UP000002051};
RN [1] {ECO:0000313|EMBL:KEH24737.1, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:KEH24737.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH24737,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [2] {ECO:0000313|EMBL:KEH24737.1, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=A17 {ECO:0000313|EMBL:KEH24737.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH24737,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [3] {ECO:0000313|EnsemblPlants:KEH24737}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:KEH24737};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
RN [4] {ECO:0000313|Proteomes:UP000265566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17 {ECO:0000313|Proteomes:UP000265566};
RX PubMed=30397259; DOI=10.1038/s41477-018-0286-7;
RA Pecrix Y., Staton S.E., Sallet E., Lelandais-Briere C., Moreau S.,
RA Carrere S., Blein T., Jardinaud M.F., Latrasse D., Zouine M., Zahm M.,
RA Kreplak J., Mayjonade B., Satge C., Perez M., Cauet S., Marande W.,
RA Chantry-Darmon C., Lopez-Roques C., Bouchez O., Berard A., Debelle F.,
RA Munos S., Bendahmane A., Berges H., Niebel A., Buitink J., Frugier F.,
RA Benhamed M., Crespi M., Gouzy J., Gamas P.;
RT "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL Nat. Plants 4:1017-1025(2018).
RN [5] {ECO:0000313|EMBL:RHN49666.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:RHN49666.1};
RA Pecrix Y., Gamas P., Carrere S.;
RT "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL Nat. Plants 0:0-0(2018).
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; CM001222; KEH24737.1; -; Genomic_DNA.
DR EMBL; PSQE01000006; RHN49666.1; -; Genomic_DNA.
DR RefSeq; XP_013450709.1; XM_013595255.1.
DR AlphaFoldDB; A0A072U4V2; -.
DR SMR; A0A072U4V2; -.
DR STRING; 3880.A0A072U4V2; -.
DR EnsemblPlants; KEH24737; KEH24737; MTR_6g004200.
DR GeneID; 25495093; -.
DR Gramene; KEH24737; KEH24737; MTR_6g004200.
DR KEGG; mtr:25495093; -.
DR HOGENOM; CLU_013748_3_3_1; -.
DR OrthoDB; 1966690at2759; -.
DR Proteomes; UP000002051; Chromosome 6.
DR Proteomes; UP000265566; Chromosome 6.
DR ExpressionAtlas; A0A072U4V2; differential.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008949; F:oxalyl-CoA decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IBA:GO_Central.
DR GO; GO:0001561; P:fatty acid alpha-oxidation; IBA:GO_Central.
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; IPR000399; TPP-bd_CS.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:KEH24737.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 11..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 201..329
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 402..551
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 488..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 60896 MW; 613D7CFF1D2C5D92 CRC64;
MGEIDGNVLA AKSFSQFGVL HMFGVVGIPV TSLATRAVSL GIRFIAFHNE QSAGYAASAY
GYLTSRPGIF LTVSGPGCVH GLAGLSNGTT NTWPTVMISG SCNQNDVGRG DFQELDQIQA
VKPFTKFAIK AKHISEIPNC VAQVLANSVV NRPGGVYLDL PTDVLHQKVS ESEAESLLTE
AKYLAEKIKK SHVISVESSK IQEAVSLLRK AERPLIVFGK GAAYAKAEDE LKKLVEKTGI
PFLPTPMGKG LLPDDHPLAA SAARSLAIGK CDVAIVIGAR LNWLLHFGEE PKWSKDVKFV
LVDVSKEEIE LRKPFLGLVG DGKEVLEVLN KEIKDDPFCL GSTHPWVEAI SSKVKDNGVK
MEAQLAKDVV PFNFLTPMRI IRDAISEFGG SPAPVVVSEG ANTMDVGRSV LVQKEPRTRL
DAGTWGTMGV GLGYCIAAAV AYPDRLVVAV EGDSGYGFSA MEVETLVRYQ LPVVVIVFNN
GGVYGGDRRS AEEKHGPHKE DPAPTSFVPN AGYHTMMEAF GGKGYLVGTP DELKSALSES
FSARKPAVIN VTIDPYAGSE SGRMQHKN
//
