ID A1BAW3_PARDP Unreviewed; 514 AA.
AC A1BAW3;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Thiamine pyrophosphate enzyme domain protein TPP-binding protein {ECO:0000313|EMBL:ABL72657.1};
GN OrderedLocusNames=Pden_4594 {ECO:0000313|EMBL:ABL72657.1};
OS Paracoccus denitrificans (strain Pd 1222).
OG Plasmid pPD1222 {ECO:0000313|Proteomes:UP000000361}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL72657.1, ECO:0000313|Proteomes:UP000000361};
RN [1] {ECO:0000313|Proteomes:UP000000361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RC PLASMID=pPD1222 {ECO:0000313|Proteomes:UP000000361};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of plasmid 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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DR EMBL; CP000491; ABL72657.1; -; Genomic_DNA.
DR RefSeq; WP_011750816.1; NC_008688.1.
DR AlphaFoldDB; A1BAW3; -.
DR EnsemblBacteria; ABL72657; ABL72657; Pden_4594.
DR GeneID; 75503962; -.
DR KEGG; pde:Pden_4594; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_8_0_5; -.
DR OrthoDB; 9773408at2; -.
DR Proteomes; UP000000361; Plasmid pPD1222.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02002; TPP_BFDC; 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; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF86; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVX-RELATED; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 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 Plasmid {ECO:0000313|EMBL:ABL72657.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000361}.
FT DOMAIN 1..102
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 382..511
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 514 AA; 53628 MW; B2360637D11F62ED CRC64;
MNGADLLCET LLANGIDTCF ANPGTSEMHF VAALDRQPRM RCVLGLFEGV VTGAADGYAR
MAEKPAATLL HLGPGLANGL ANMHNARRAR SPMVNVVGDH ATCHLALDAP LTSDIDSLAR
PMSHWIGRAE TAEAVGQRTA EAIAAARAGA GGIATLILHA DAAWTETSAP VPAAVVPAAP
AAPDPARIRE AAEALRNGKR TTILVTGRAL RAPQTEMLDR IAQKTDARVM AQQANARMQR
GAGRVALDRV PYVIDQALAT FAETEQLVLI GANAPVGFFA YPGKPGSMLP EGCRVIAMAD
ADDDLPAAIA ALAGETGLAP APRLAEHGAP DMPGGALTPD AIAIALAHLM PQDAIVCDES
ITSGRDFFRS THGAAPHDFL QLTGGSIGEG IPMATGAAVA CPDRKVIGLQ ADGSGMYTVQ
GLWTQARERL DVVTIVFANR LYKILHGELQ NVGAGAPGEN ARRMLDLDDP ALDWVRIANG
MGVEAARADT AEAFFDLLRS AMSRKGPFLI EAVV
//
