ID X6N1W4_RETFI Unreviewed; 671 AA.
AC X6N1W4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Thiamine pyrophosphate enzyme, central domain containing protein {ECO:0000313|EMBL:ETO19734.1};
GN ORFNames=RFI_17496 {ECO:0000313|EMBL:ETO19734.1};
OS Reticulomyxa filosa.
OC Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC Reticulomyxidae; Reticulomyxa.
OX NCBI_TaxID=46433 {ECO:0000313|EMBL:ETO19734.1, ECO:0000313|Proteomes:UP000023152};
RN [1] {ECO:0000313|EMBL:ETO19734.1, ECO:0000313|Proteomes:UP000023152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24332546;
RA Glockner G., Hulsmann N., Schleicher M., Noegel A.A., Eichinger L.,
RA Gallinger C., Pawlowski J., Sierra R., Euteneuer U., Pillet L.,
RA Moustafa A., Platzer M., Groth M., Szafranski K., Schliwa M.;
RT "The Genome of the Foraminiferan Reticulomyxa filosa.";
RL Curr. Biol. 0:0-0(2013).
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 -!- 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:ETO19734.1}.
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DR EMBL; ASPP01013344; ETO19734.1; -; Genomic_DNA.
DR AlphaFoldDB; X6N1W4; -.
DR EnsemblProtists; ETO19734; ETO19734; RFI_17496.
DR OrthoDB; 1328249at2759; -.
DR Proteomes; UP000023152; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000023152};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 44..113
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 290..401
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 507..656
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 121..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 671 AA; 74552 MW; C9FEBE914DF9AE49 CRC64;
MKEIVIDWKW AGLLATVSAL LLASPSIAKY SAPFRLKTRP TDRTGGELVA KVLKSHNVEW
LFTLVGGHIS PILVSAKKIG IKVIDVRNEA TAVFAADAIS RLTGTCGVAV VTAENSKDFD
WVQKKNNNNN DKDREGGGIS HQKKKKKEND TNNTQSKTKK DRYIKINSER FKKKKILKKK
KVKAAMGLGE VKSLKTLNTS EDLTDGTLVV PEEFVEEHKT KSASKYIEFM QKSKKTDHFP
IFFDRPKRLP WVVNAYLSYQ VQYLFAGAFD TKCDYSPLAV RQAKARQSDV KKIVSVLVQA
KKPVLIVGSQ ALLNAKDKDA LKDAVDFLSI PTFLSGMARG LTGKDSRYQV RQNRNQALKE
CDCVILLGCM VDFRFDYGRS FSKKSKIIAI NRSYFDLTNN TDLFWKPYLA VQSDPCQTIC
DCVAFIHSQP KLLQDYTKQK EGVIASFVTQ LKHAEIKKEN LNLEKSKEIS FSRSDLWGVK
SKELINPLFL CRKIDELMSD DSIIIVDGGD FAATAAYVLR PRGPLRWMDP GPFGTLGVGA
GFALGAKLAN PDAEIWLIWG DGSSGYGLAE IDTFRKFGIG VIAVIGNDAC WSQIEREQVP
KLGDNVACSL SYCPYELVSQ GFGGSGEVVT NNDELDQALA RAKEYVKKSR APYVINAHIG
TSDFRQGSIS V
//
