ID   A0A0N5ATZ0_9BILA        Unreviewed;       594 AA.
AC   A0A0N5ATZ0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=2-hydroxyacyl-CoA lyase 2 {ECO:0000256|ARBA:ARBA00018936};
DE   AltName: Full=IlvB-like protein {ECO:0000256|ARBA:ARBA00030510};
OS   Syphacia muris.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX   NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000831101-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMUV_0000831101-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A0N5ATZ0; -.
DR   STRING; 451379.A0A0N5ATZ0; -.
DR   WBParaSite; SMUV_0000831101-mRNA-1; SMUV_0000831101-mRNA-1; SMUV_0000831101.
DR   Proteomes; UP000046393; Unplaced.
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   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          11..125
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          231..363
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          429..567
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   594 AA;  64391 MW;  ED92BAEC7B079523 CRC64;
     MCDADESSKR NGGELVASVL KAHNVKEIFA LCGGHISAIL VAAEKLGIRV VDTRSEANAV
     FAADAVARLR QTIGVAAVTA GPGVTNTITA VKNAQMAEIP LLLLGGAAPT MLKNCGALQD
     IDQISLFKPI CKYVTSVKRI RDITETLRKA ISVARSGTPG PVFVELPVDL LYPYAVIEKE
     LGFISEPKNF MQRMTNFYLR YYISQLFSEA WIERDVTEIL PSIPKPQPDQ VEELAQLIMS
     AKRPLLLIGS QAVLPPVKPT DLQSSIMKMK LPTYLGGMAR GLLGRNCKYQ MRQNRRAALK
     KADLVVLAGM VCDFRLSYGR SLPAQGEVIS INRNRTQMCK NKGVFWKAKL LIEADVGLTL
     QELSNALSAK GYSGCSTQWI DELTEQEVMK NAENERKAEE FTSGTGFNPI KVLSLFNKFL
     PDDAILVVDG GDFVGTAAYV VQPRGPLGWL DPGPFGTLGV GGGFAIGAKV VYPNRPVYII
     YGDGACGYSV LEFDTFVRHN LPVGALIGND ACWSQIARDQ VPLFNNDVGV MLSHSKYEKI
     AEAFGAKGNY IDKGSCSQLD KTIQEFTTTV ANGTAMVANV IIGKSDFRAG SISV
//