ID A0A0A0B9A9_9CELL Unreviewed; 600 AA.
AC A0A0A0B9A9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Thiamine pyrophosphate protein {ECO:0000313|EMBL:KGM03435.1};
GN ORFNames=Q760_03125 {ECO:0000313|EMBL:KGM03435.1};
OS Cellulomonas cellasea DSM 20118.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1408250 {ECO:0000313|EMBL:KGM03435.1, ECO:0000313|Proteomes:UP000029833};
RN [1] {ECO:0000313|EMBL:KGM03435.1, ECO:0000313|Proteomes:UP000029833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20118 {ECO:0000313|EMBL:KGM03435.1,
RC ECO:0000313|Proteomes:UP000029833};
RA Wang G., Zhuang W.;
RL Submitted (OCT-2013) 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:KGM03435.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AXNT01000013; KGM03435.1; -; Genomic_DNA.
DR RefSeq; WP_034625426.1; NZ_AXNT01000013.1.
DR AlphaFoldDB; A0A0A0B9A9; -.
DR STRING; 1408250.Q760_03125; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000029833; 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:UP000029833};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..327
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 386..540
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 547..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 600 AA; 63774 MW; 3A901E5268FD8920 CRC64;
MATVADGIVA RLAEWGVGRV FGFAGDGIDP LLAALHRASG TVELVTARHE EMAAFMATGH
AKYGGGVGVC LATQGPGAIH LLTGLYDAKL DRKPVVAIVG QVVSTALGSG YLQEVDLQTL
FKDVCGQYVQ TVHSPEQLPL VLDNAIRTAL ATSSPTCVIV PHDVQKEDLP EDAQHTHGVV
ASSATWAPSR VLPDEASLDR AVEVLDAGER VALLVGQGAA GAAEQVRAVA ERLGAGITTS
LLGKPVLDEG LPYHCGVMGH LGTTASADLL ARCDTLLIVG SSDPWTEFYP PPGTVRTVQI
DVAARNLGAK YPVQVGLAGD AAETLDLLLP RLRAREGWRA DVERSVAAWH EVARRRAAEP
ADPLNPQLVL RALSDHLPAD AQVSLDVGSV VYWYARFLRL PRGVPAHLSS TLASMGSAMP
YGIAAKLLHP DRPVVALAGD GAMQMNGLSE LITVAARWRD WADPRFVVLV LHNGDLAEVS
WEQREMEGDP RFPTSQTVPP FPYAAYAEML GLTGIRVDDP ADVHAAWRTA LGADRPCLIE
AVVDPDTPLL APRQPTEKVE QMRRGLAQEP GAGRATDHLD RQRAHEAEHD PAGVSAENDA
//
