ID   W3RFX9_9BRAD            Unreviewed;       544 AA.
AC   W3RFX9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Thiamine pyrophosphate-requiring protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=X566_23465 {ECO:0000313|EMBL:ETR75642.1};
OS   Afipia sp. P52-10.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Afipia.
OX   NCBI_TaxID=1429916 {ECO:0000313|EMBL:ETR75642.1, ECO:0000313|Proteomes:UP000018975};
RN   [1] {ECO:0000313|Proteomes:UP000018975}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P52-10 {ECO:0000313|Proteomes:UP000018975};
RX   PubMed=25874801;
RA   Pickering B.S., Tyler S., Smith G., Burton L., Li M., Dallaire A.,
RA   Weingartl H.;
RT   "Identification of a novel afipia species isolated from an Indian flying
RT   fox.";
RL   PLoS ONE 10:E0121274-E0121274(2015).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:ETR75642.1}.
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DR   EMBL; AZSJ01000007; ETR75642.1; -; Genomic_DNA.
DR   AlphaFoldDB; W3RFX9; -.
DR   STRING; 1429916.X566_23465; -.
DR   PATRIC; fig|1429916.3.peg.4747; -.
DR   eggNOG; COG0028; Bacteria.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000018975; 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:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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:UP000018975};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          1..104
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          184..317
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          383..530
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   544 AA;  59025 MW;  800C33D874CB72B8 CRC64;
     MKLGAAIAEI MKREGIEILC GYPVNHLIEY AAAADIRPVM VRQERIGVHM ADAISRVTSG
     QTIGAFCMQH GPGAENAMGG VAQCYGESVP VLVLPMGYPR RLAHIDPNFS STYAMKPFAK
     STEPIILASE VCNIFRRAFT RLKNGRGGPV VVEIPSDMWN EEVAEPLNYT PVLRTRSGPD
     PQHVRDAAAL LISARRPVLY VGQGVHYAKA WPQLRKLAER LAIPVVTSLG GKSAFPETHP
     LSLGAGGLAL PRAVTKFLAD ADVIFGVGCS FTETSFGVAM PKGKTIIHAT IDPDHLNKDV
     EAKVGLVGDA GLVLDALLDE IGKTVTDDRD HKPVAAEIAA LHAEWLKTWM PKLTSNDAPL
     NPYRVLWDLQ NTVDIRNTII THDAGSPRDQ LSPFWKSVEP LSYIGWGKTT QLGYGLGLAM
     GAKLAKPDKL CINVWGDAAI GFTGMDFETA VRERIPIMSI LLNNFSMAIE LKVMPVSTEK
     YRSTDISGDY AAMARAFGGY GERVTKPEDI IPAIQRGIQK TKEGIPVLLE FITSKEVEVA
     RPGT
//