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Database: UniProt
Entry: G0PNB2_CAEBE
LinkDB: G0PNB2_CAEBE
Original site: G0PNB2_CAEBE 
ID   G0PNB2_CAEBE            Unreviewed;       485 AA.
AC   G0PNB2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGT41141.1};
GN   ORFNames=CAEBREN_28812 {ECO:0000313|EMBL:EGT41141.1};
OS   Caenorhabditis brenneri (Nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN   [1] {ECO:0000313|Proteomes:UP000008068}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG   Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA   Wilson R.K.;
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; GL381790; EGT41141.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0PNB2; -.
DR   STRING; 135651.G0PNB2; -.
DR   EnsemblMetazoa; CBN28812.1; CBN28812.1; WBGene00190777.
DR   eggNOG; KOG1185; Eukaryota.
DR   HOGENOM; CLU_013748_3_3_1; -.
DR   InParanoid; G0PNB2; -.
DR   Proteomes; UP000008068; Unassembled WGS sequence.
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; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000008068}.
FT   DOMAIN          112..242
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          312..463
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   485 AA;  53444 MW;  D58CDF02AFED549D CRC64;
     MEVSPNATVN CWPVVCIGGT ADVDLENRGA FQEWSQQESV RNSCKHVSRP TSLHTIPAHI
     EKAVRCAMYG RPGAVYVDLP GNLVLTSTEE EISFPEPVPL PPPVSIPPIA EIEKAINTLK
     NAKKPLVIVG KGAAWSERGA TQVQQFLTKS KLPWLATPGG KGVASDLHPR FIGQARSLAL
     READTVFLIG ARFNWILHFG LPPRFQKDVK VVQIDICPEE FHQNVKTEVP LLGDIGETLA
     ELTPRLGEWA YDESTEWFKK LRENAEKNRK AVEKLVDDHS TPLNYYAAYQ PIREFLANND
     VIVVNEGANT MDIGRTMMPS RLPKRRLDAG TFGTMGVGQG FALAAALWAR DHSPKTKVLV
     VQGDSAFGFS AMELETIARY NLPVVTVIIN NSGIYRGLLP EDDKAIEGDR TLALPVLSLT
     AECRYEQMCQ AFGGEGTVVR TVPEIKAALE KAFQKTDGPT VINALISTDS ERKPQADHWL
     TRSKM
//
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