ID A0A1B8SCY9_9MYCO Unreviewed; 606 AA.
AC A0A1B8SCY9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:OBY30595.1};
GN ORFNames=ACT18_16730 {ECO:0000313|EMBL:OBY30595.1};
OS Mycolicibacter kumamotonensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacter.
OX NCBI_TaxID=354243 {ECO:0000313|EMBL:OBY30595.1, ECO:0000313|Proteomes:UP000092668};
RN [1] {ECO:0000313|EMBL:OBY30595.1, ECO:0000313|Proteomes:UP000092668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Roo {ECO:0000313|EMBL:OBY30595.1,
RC ECO:0000313|Proteomes:UP000092668};
RA Greninger A.L., Cunningham G., Miller S.;
RT "Genome sequence of Mycobacterium kumamotonense strain Roo.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:OBY30595.1}.
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DR EMBL; LFOE01000028; OBY30595.1; -; Genomic_DNA.
DR RefSeq; WP_065288891.1; NZ_LFOE01000028.1.
DR AlphaFoldDB; A0A1B8SCY9; -.
DR STRING; 354243.BST28_01805; -.
DR PATRIC; fig|354243.3.peg.3462; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000092668; 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; cd02014; TPP_POX; 1.
DR CDD; cd07039; TPP_PYR_POX; 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; IPR047211; POXB-like.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047212; TPP_POXB-like.
DR InterPro; IPR047210; TPP_PYR_POXB-like.
DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 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.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..543
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 583..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 606 AA; 65879 MW; 40EE17D1D4053FBF CRC64;
MPKTADFIID RLRQWGVHRI FGYPGDGILS MLGALDRAGG DPGLIQPRHE EMGAFMATGH
AKFTGELGCC LATSGGGAIH LLNGLYDAKL DHQPVVAIVG QQKRMSLGAA FQQEIDPMSL
FKDVSSDFIQ TCMAPVQARH LVDRACKVAL TNRTVATIIL PEDVAEEDAV PSPPRMHGAV
FSSVGWSRSR MLPAQPELQK AADILNDAEK VAILIGAGAA DASDEVVQVA ELLGAGVAKT
SLGRASLPDD LPYVTGPIGL LGSTASEAMM SGADTLFMIG SSFPYSEWLP KEGQCRGVEI
NHDGRMIGVR YPMDANLIGD SKDTLQELIP LLKRKEDRSW RKKIEGEVQE WWRVLDKRAH
DKADPLNPEL VVHELSKRLP DNSVITTDAG SVANWWARHL RLRPGMAASL AGNLATMGPG
TPYAIAAKLA HPGRPVIALV GDGVFQMNGM AEMITVKRYK ERLSKGPLIF CVFNNQDLNQ
VTFEQRAMGG EKKFEGSQHI PDVPYAEFAK MLGLTGIRCD DPKNIGHAWD QALAASSPVV
LEVVVDPDIA PVPPQIRMDI AKNTAKAMLK DPDRVSIATK NAKQKMHEFT ESARQTVRDL
RDKSDE
//
