ID A0A074JB36_9RHOB Unreviewed; 571 AA.
AC A0A074JB36;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:KEO52793.1};
GN ORFNames=TP2_07585 {ECO:0000313|EMBL:KEO52793.1};
OS Thioclava pacifica DSM 10166.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1353537 {ECO:0000313|EMBL:KEO52793.1, ECO:0000313|Proteomes:UP000027432};
RN [1] {ECO:0000313|EMBL:KEO52793.1, ECO:0000313|Proteomes:UP000027432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10166 {ECO:0000313|EMBL:KEO52793.1,
RC ECO:0000313|Proteomes:UP000027432};
RA Lai Q., Shao Z.;
RT "Thioclava pacifica DSM 10166 Genome Sequencing.";
RL Submitted (JUL-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:KEO52793.1}.
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DR EMBL; AUND01000023; KEO52793.1; -; Genomic_DNA.
DR RefSeq; WP_038077002.1; NZ_AUND01000023.1.
DR AlphaFoldDB; A0A074JB36; -.
DR STRING; 1353537.TP2_07585; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000027432; Unassembled WGS sequence.
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; 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 Pyruvate {ECO:0000313|EMBL:KEO52793.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027432};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 189..317
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 378..524
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 571 AA; 61656 MW; 434848E6CAD3F9E6 CRC64;
MSKTVSDIIA DTLVSAGARR VYGIVGDTIN HFTDAVRRSD LDWVHVRHEE VGALAAGGES
YMTGELSVCA GTTGPGSLHF VNGIFESHRN GAPVVLIASN IARAEEGLGF PQEVDQKKIY
EQCSVFCEKI SHPDQARRIV AKAAQAALTL HGVAVVIVNG DMFREISSDD LPWAVHRPAP
VIRPSEAEIE ALAAMIAGAE RITIYAGIGA RGAAAQIRAL SERLAAPVAH TTRAKEFIEP
DMPNNVGMTG ILGNRAGMQA VGDCDLLLCL GSDFAYTQFY PGKARIVQVD IEPTRLGRRM
PVDLGLVGDV GDTIDALLPR LAPREHGKHL NRALKGYAED LKGYLESAEE PDPSLIHPQH
LTEMLDRLAA QDAIFTADGG SPMVWLLRHL SANGERRFLT SLLHGTMANA YPQALGIQNA
YPDRQVIAMC GDGGMTMLMG DLLTLVQEKL PVKLLIFNNA SLGFVEMEQR VEGMLDAFTE
LHNPDFGAMA RAIGMQGARV ETADDLETAM HEWLAAPGPA LLDVKVNRME LVMPPKIEPS
QIASTALFGV KAVLNGRADE VVSLMRDNFL R
//
