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Database: UniProt
Entry: A0A085NC62_9BILA
LinkDB: A0A085NC62_9BILA
Original site: A0A085NC62_9BILA 
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
//
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