ID A0A085NC62_9BILA Unreviewed; 700 AA.
AC A0A085NC62;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=2-hydroxyacyl-CoA lyase 2 {ECO:0000256|ARBA:ARBA00018936};
DE AltName: Full=IlvB-like protein {ECO:0000256|ARBA:ARBA00030510};
GN ORFNames=M513_07369 {ECO:0000313|EMBL:KFD51673.1}, M514_07369
GN {ECO:0000313|EMBL:KFD67058.1};
OS Trichuris suis (pig whipworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD67058.1};
RN [1] {ECO:0000313|EMBL:KFD67058.1, ECO:0000313|Proteomes:UP000030764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD67058.1}, and DCEP-RM93M
RC {ECO:0000313|EMBL:KFD51673.1};
RX PubMed=24929829; DOI=10.1038/ng.3012;
RA Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL Nat. Genet. 46:701-706(2014).
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:0000256|ARBA:ARBA00000244};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55213;
CC Evidence={ECO:0000256|ARBA:ARBA00000244};
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:0000256|ARBA:ARBA00000194};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55197;
CC Evidence={ECO:0000256|ARBA:ARBA00000194};
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; KL363236; KFD51673.1; -; Genomic_DNA.
DR EMBL; KL367518; KFD67058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A085NC62; -.
DR Proteomes; UP000030758; Unassembled WGS sequence.
DR Proteomes; UP000030764; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IEA:InterPro.
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; 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_TPP-bd.
DR PANTHER; PTHR18968:SF166; 2-HYDROXYACYL-COA LYASE 2; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 45..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 102..215
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 342..464
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 537..685
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 700 AA; 76773 MW; 742290236478ACF3 CRC64;
MFQCITGVKE ERNHPIWLSH SSAQRKSILH PIQGRRRRIK LLEKMIMLSL LFMTVALAVM
IVFLVKLLTK GNFSRNLMDV GKGRISVFRL FYSVQSDSRN FGGEIVADVL KAHGVKWVFT
LCGGHISPIL VSCEKNDIRV VDTRNEATAA FAADAVSRLG EPIGVACVTA GPGVTNTLTA
VQNAQMAQSA VLIIGGATSY LLKGRGSLQD IDQIGIMKPV CKHVVSVSRV RDIAPTLRKA
IQIARSDVPG PVFVEMPVDA LHPIHVVEAE MKLNRKPNSI RGYLIHWQAA KFYHCTIHSF
AFQNRFMELY LSRLFSDAWK PTDVAPLPVK YKKASSFQVK SCRDLLTRSK QPLIIIGGQA
MLLPDRIQDL VSALKVINVP CYCNGMARGL LADAEHIQMF HKRREALKEA DLVILAGAAC
DFRLDYGRSL NPEAKIIAIN RSNALLRQNV NVFWKASIFL QADPCDFIIQ LADSLSDVAA
YVQPEDWLRR LKSRDQQAEE DISKLAKTEL TSPGINPIAL LRNIEELIPK DAIIVMDGGD
FVGTAAYVLK ARGPLKWLDP GAFGTLGVGA GFALGAKLCH PDLPVWIIFG DGAFGFSVAE
IDSLVRHQTP VIAIIGNDNG WAQIQRTQIS LFGSSIGCVL SPAIAYEKVA EGFGAIGFAI
DSSNANELNK MITSIKDQPR AAFVNALIGR TNFRDGSVSI
//