ID A0A0D0VMZ8_9ACTN Unreviewed; 599 AA.
AC A0A0D0VMZ8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:KIR62118.1};
GN ORFNames=TK50_25065 {ECO:0000313|EMBL:KIR62118.1};
OS Micromonospora haikouensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=686309 {ECO:0000313|EMBL:KIR62118.1, ECO:0000313|Proteomes:UP000032254};
RN [1] {ECO:0000313|EMBL:KIR62118.1, ECO:0000313|Proteomes:UP000032254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JXNU-1 {ECO:0000313|EMBL:KIR62118.1,
RC ECO:0000313|Proteomes:UP000032254};
RA Long Z., Huang Y., Jiang Y.;
RT "Sequencing and annotation of Micromonospora carbonacea strain JXNU-1
RT genome.";
RL Submitted (JAN-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:KIR62118.1}.
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DR EMBL; JXSX01000003; KIR62118.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0VMZ8; -.
DR PATRIC; fig|47853.6.peg.5252; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000032254; 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; IPR000399; TPP-bd_CS.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000032254};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..123
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 202..332
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 393..547
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 599 AA; 64223 MW; 94AF561198FDDD2E CRC64;
MPRDATVADH IVARLAQWGV RRYFGYPGDG INGMTSALQR AGDRAEFVQV RHEETAGFAA
SAHVKYGGGP LGCALATSGP GAIHLLNGLY DAKLDHQPVV ALVGHTALTA EGGGYYQEVD
LLALYKDVAS AFLAQLDDPS QVRHLVDRAC RTALARRTVT ALVLPSDVQD EAAVPDPPHA
HGYYHTSAVP SSATTVPPEA DVRRAAEVLR GGERVAMLVG QGALGAEAEV RQVADRLGAG
VATALLGFTA VDHREPWVTG AIGLLGTRPS WQLMRDCDRL LIVGSNMPYS EFYPPQGQAR
GVQIDVDGSR LGLRYPTEVN LTGDAGPTLR ALLRELGPGT APTAWRQRIA DATAGWHRAQ
REIAGQSADP VNPQALFAAL DDQLPGDVML AVDCGTCTAW YARHLRLRPG MLASLSGTLL
SMGGAMPYGI AAKLAHPDRP LVALLGDGAM QMNGVNELIT VAKHWRSWPD PRFVVLVLNN
RDLAFVSWEQ RSGEGTPMFP ASQDLPDVAY HRWAEVLGLH GILVDSPDQV PDAWRRALAA
DRPTVINAMV DPAELMLPPH FTAAQARKTA AAVLRDPDRA GIVRRGLPAA VSTWRPRLR
//
