ID A0A1I8IEV9_9PLAT Unreviewed; 579 AA.
AC A0A1I8IEV9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=2-hydroxyacyl-CoA lyase {ECO:0000313|WBParaSite:maker-uti_cns_0012154-snap-gene-0.3-mRNA-1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0012154-snap-gene-0.3-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0012154-snap-gene-0.3-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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 AlphaFoldDB; A0A1I8IEV9; -.
DR WBParaSite; maker-uti_cns_0012154-snap-gene-0.3-mRNA-1; maker-uti_cns_0012154-snap-gene-0.3-mRNA-1; maker-uti_cns_0012154-snap-gene-0.3.
DR Proteomes; UP000095280; 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; 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; 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.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..115
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 190..319
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 389..557
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 579 AA; 61582 MW; DE6C042FD07A280A CRC64;
MDGATVLAQA LRSQGIEYAF GIVGIPVVEV AVAFQSAGIK FVAMRNEQSA SYAASAIGYL
TGKPGVCLVV SGPGVVHALA GLSNANENCW PVLVIGGASD SHLDGSEAFQ EFPQAEAAAK
FCKFSARLPS IARIPHFVHK AVKQATYGRP GAVYLDLPGD FVTSSVDSEE IHFPPPLPQP
PVTLADPQSV SAAARLLRSA RRPLVVIGKG AAQGRAELAV RQLIQSTRLP FLPTPMGKGV
AADDHPGCVS AARTRALKQA DVVVLLGARL NWILHFGRPP RWTPDVKFIQ VDIHPEEFHT
NVTCEVALCG SVAAVVEQLS SELHGFEFSS SSDWWRELNA ASAANRARVD ALIVEGQTVP
MTYYSALNEL AKFVDNSGDD WLIVSEGANS MDIGRAMLPN RLARRRLDAG TFGTMGVGLG
FAAAADLCIG DSRVGHRRVL CLEGDSAVGF SLAELETLAR YRMPVLLVVI NNSGIYSGVP
ADVLRQLLQQ DGAAPSSGAS SASAALRLPA TSLTSECRYD LAAEALGGYG RLVRSVGELR
QAFAEFAGVR DRPCLINAII DTGAERKQQE FDWLSRSKL
//
