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Database: UniProt
Entry: A0A0A0KW04_CUCSA
LinkDB: A0A0A0KW04_CUCSA
Original site: A0A0A0KW04_CUCSA 
ID   A0A0A0KW04_CUCSA        Unreviewed;       570 AA.
AC   A0A0A0KW04;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=2-hydroxyacyl-CoA lyase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Csa_4G133700 {ECO:0000313|EMBL:KGN53810.1};
OS   Cucumis sativus (Cucumber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN53810.1, ECO:0000313|Proteomes:UP000029981};
RN   [1] {ECO:0000313|EMBL:KGN53810.1, ECO:0000313|Proteomes:UP000029981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 9930 {ECO:0000313|Proteomes:UP000029981};
RX   PubMed=19881527; DOI=10.1038/ng.475;
RA   Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X.,
RA   Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G.,
RA   Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., Jia Z.,
RA   Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., Li B.,
RA   Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., Zhao B.,
RA   Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., Kim J.Y., Xu Y.,
RA   Heller-Uszynska K., Miao H., Cheng Z., Zhang S., Wu J., Yang Y., Kang H.,
RA   Li M., Liang H., Ren X., Shi Z., Wen M., Jian M., Yang H., Zhang G.,
RA   Yang Z., Chen R., Liu S., Li J., Ma L., Liu H., Zhou Y., Zhao J., Fang X.,
RA   Li G., Fang L., Li Y., Liu D., Zheng H., Zhang Y., Qin N., Li Z., Yang G.,
RA   Yang S., Bolund L., Kristiansen K., Zheng H., Li S., Zhang X., Yang H.,
RA   Wang J., Sun R., Zhang B., Jiang S., Wang J., Du Y., Li S.;
RT   "The genome of the cucumber, Cucumis sativus L.";
RL   Nat. Genet. 41:1275-1281(2009).
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; CM002925; KGN53810.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A0KW04; -.
DR   STRING; 3659.A0A0A0KW04; -.
DR   EnsemblPlants; KGN53810; KGN53810; Csa_4G133700.
DR   Gramene; KGN53810; KGN53810; Csa_4G133700.
DR   eggNOG; KOG1185; Eukaryota.
DR   OMA; PGPYGCL; -.
DR   Proteomes; UP000029981; Chromosome 4.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000029981};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          25..133
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          212..331
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          405..553
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   570 AA;  60997 MW;  7E9E1F9506644423 CRC64;
     MGDSAEALQN DLRFQGPIDG NVLAAMALAR CGVDRMFGVV GIPVTSLATR AVSLGIRFIA
     FHNEQSAGYA ASAYGYLTGR PGVLLTVSGP GCVHGLAGVS NAMVNAWPLV MISGSCDQRD
     FGRGDFQELD QVEAVKPFSK ISVKATDISE IPNCVARVLN SAVSGRPGGC YFDLPSDVLH
     QTISESEAER LLVAAEEFAR REVIPRVPNS QIEEAISLLK HAERPLIVFG KGAALARAEG
     PLKKLVETTG IPFLPTPMGG RAPPAARSLA IGKCDVALVV GARLNWLLHF GEPPKWSKDV
     KFILVDICKE EVELRNPHLG LIGDAKEVLE SINKEIKDDP FCLGKSHPWV EAISQKAKDN
     VAKMEVQLAR DVVPFNFLTP MRIIRDAILA LGSPAPILVS EGANTMDVGR SVLVQTEPRT
     RLDAGTWGTM GVGLGYCIAA AVASPDRLVV AVEGDSGFGF SAMEVETLVR YQLPVVVIVF
     NNSGVYGGDR RTPQEITGPY KHDPAPTSFV PSAGYHKMIE AFGGKGYHVE SPEELKSALA
     ESFSARKPAV VNIKIDPYAG AESGRLQHKN
//
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