ID   J9AZA2_WUCBA            Unreviewed;       408 AA.
AC   J9AZA2;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Thiamine pyrophosphate enzyme {ECO:0000313|EMBL:EJW79945.1};
DE   Flags: Fragment;
GN   ORFNames=WUBG_09145 {ECO:0000313|EMBL:EJW79945.1};
OS   Wuchereria bancrofti.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Wuchereria.
OX   NCBI_TaxID=6293 {ECO:0000313|EMBL:EJW79945.1, ECO:0000313|Proteomes:UP000004810};
RN   [1] {ECO:0000313|Proteomes:UP000004810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA {ECO:0000313|Proteomes:UP000004810};
RA   Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Hepburn T.,
RA   Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M.,
RA   Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA   Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Wuchereria bancrofti.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJW79945.1}.
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DR   EMBL; ADBV01004966; EJW79945.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9AZA2; -.
DR   Proteomes; UP000004810; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd07035; TPP_PYR_POX_like; 1.
DR   Gene3D; 3.40.50.970; -; 1.
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; IPR045229; TPP_enz.
DR   PANTHER; PTHR18968:SF166; 2-HYDROXYACYL-COA LYASE 2; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 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); 1.
PE   3: Inferred from homology;
FT   DOMAIN          59..174
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          281..408
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   NON_TER         408
FT                   /evidence="ECO:0000313|EMBL:EJW79945.1"
SQ   SEQUENCE   408 AA;  45175 MW;  2F0434CEE0F64B9E CRC64;
     MCLLSGILFV LIGFLLWLTK IFGIDSIQTF HQILLDLYTR KRSHWILELF QVDEESDHHG
     GELVAAVLKA HNINEIFTLC GGHISPILVA AKNIGIRVYD TRHEVNAVFA ADAVARLRQS
     VGVAVVTAGP GLTNTITAVK NAQLAETAVV IIAGAAPILS KNRGALQDID QISLMRPLCK
     YVARITCIRN IITVLKKAMH IAQSDTPGPV FVEIPIDVLY SYKMVLKEMN IAEARNFKQT
     VINSYLLAYI SRQFSGGWVI RESMLPIPVR TTFPKDNDII KLMHMVLKSK KPVLIIGSQA
     VLAPVSVYEL KKAVKTIGIP TFLTGMSRGL LGQRSPIHMR YNRKDTLKEA DLIILAGAVC
     DFRLSYGRVL SPNANVVSIN RDRTQMLKNE GIFWRVNLAV QADVATTL
//