ID A0A437MD73_9PROT Unreviewed; 542 AA.
AC A0A437MD73;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Thiamine pyrophosphate-requiring protein {ECO:0000313|EMBL:RVT95614.1};
GN ORFNames=EOD42_15535 {ECO:0000313|EMBL:RVT95614.1};
OS Rhodovarius crocodyli.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Rhodovarius.
OX NCBI_TaxID=1979269 {ECO:0000313|EMBL:RVT95614.1, ECO:0000313|Proteomes:UP000282957};
RN [1] {ECO:0000313|EMBL:RVT95614.1, ECO:0000313|Proteomes:UP000282957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP-6 {ECO:0000313|EMBL:RVT95614.1,
RC ECO:0000313|Proteomes:UP000282957};
RA Chen W.-M.;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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:RVT95614.1}.
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DR EMBL; SACL01000005; RVT95614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A437MD73; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000282957; 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:UP000282957};
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 384..530
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 542 AA; 59196 MW; E0C4368DEB4A0C45 CRC64;
MKVGDAIAEI MRREGIRTLT GYPVNHLIES AAAIDIRPVM VRQERIGLHM ADAISRVTSG
QEIGAFCMQH GPGAENSYGG VAQCFGESIP VLVLPMGYPR RIAHVPPNYN STVQMRGITK
STEAIMNAAE VPNIMRRAFA RLKNGRGGPV LVEIPTDMFN EEMPANWEYT PAVKTRAAPD
PLDVKRAAEM LAHARRPVIY AGTGVHWARA WPQLRALAEL LGAPVTSSLG GKSSFPEDHP
LALGSGGLAI SAPVRHFLDN SDVIFGIGCS FTETNFGVAM PKGKKIIHAT LDPDHLDKDV
RCEIGLVGDA ALVLDALLEE LRGRIKETRD IPGVQQEIEA IRAPWLRQWA PKRDSNDAPL
NPYRVLRDLW RTVDVDNTII THDAGSPRDQ LSPFWVSRTP LSYLGWGKTT QLGYGLGLAM
GAKLAAPDKL CINVWGDAAI GFTGMDFETA VRERIPILSI LLNNFSMAIE LKVMPVSTEK
YRSTDISGDY AAMARAFGGF GERVERPEDI IPAIQRGIAA TKEGKPALLE FITSKETQVS
RL
//
