ID A1AZQ1_PARDP Unreviewed; 553 AA.
AC A1AZQ1;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Thiamine pyrophosphate enzyme TPP binding domain protein {ECO:0000313|EMBL:ABL68745.1};
GN OrderedLocusNames=Pden_0633 {ECO:0000313|EMBL:ABL68745.1};
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68745.1, 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};
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 chromosome 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, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP000489; ABL68745.1; -; Genomic_DNA.
DR RefSeq; WP_011746978.1; NC_008686.1.
DR AlphaFoldDB; A1AZQ1; -.
DR STRING; 318586.Pden_0633; -.
DR EnsemblBacteria; ABL68745; ABL68745; Pden_0633.
DR GeneID; 75500172; -.
DR KEGG; pde:Pden_0633; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_4_5; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000000361; Chromosome 1.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd00568; TPP_enzymes; 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:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 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:UP000000361};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 187..325
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 380..525
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 553 AA; 58514 MW; ACF021E33954603E CRC64;
MRHGGQILVD ALKTNGVGRV FSVPGESFLA VLDGLYASGI RNVVCRHEGG AAMMAEAHGK
LTGRPGVGFV TRGPGATNAS AGVHVARQDG TPMILFVGQI ARADRDRDAF QEVDYRAMFG
PLAKWVAEID QTERIPEYVS RAFHLAMSGR PGPVVLALPE DMISARAEVP DLPPPAAPLA
AVAAESVEAV AQALAGAERP LVVPGGTLWS QAAADDLARF AESWGLPVAV PFRRQGHIDN
AHPNYVGDLG VGMNPALGQA LSQADCVLSL GSRLGDTLTR GYELMDPVRP HARVIHVHPS
PDELGRLWRP DPGLAADPRV VVAALAALPV PRRWDGWTAG LRAAYEAWQQ PRPTPGAVRM
EAVVRWLSDH LPPDAIITNG AGNYAAFVHR YYRFRRWGTQ LAPTSGSMGY GLPAAIAAKL
EHPGRSVVCM AGDGCLQMTV NELSTAAQHG AAVIVIVANN GHYGTIRMHQ ERSYPGRVSG
TALANPDFVA LARAYGGHGE TVTRQEDFAD AFARAQAAGR LAVLELMLDP EALSTGATLA
ETRAAGAAGL RRA
//
