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Database: UniProt
Entry: Q3KCN2_PSEPF
LinkDB: Q3KCN2_PSEPF
Original site: Q3KCN2_PSEPF 
ID   Q3KCN2_PSEPF            Unreviewed;       596 AA.
AC   Q3KCN2;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   SubName: Full=Pyruvate dehydrogenase, cytochrome {ECO:0000313|EMBL:ABA74473.1};
GN   OrderedLocusNames=Pfl01_2732 {ECO:0000313|EMBL:ABA74473.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA74473.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA74473.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA74473.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP000094; ABA74473.1; -; Genomic_DNA.
DR   RefSeq; WP_011334145.1; NC_007492.2.
DR   AlphaFoldDB; Q3KCN2; -.
DR   KEGG; pfo:Pfl01_2732; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_0_6; -.
DR   Proteomes; UP000002704; Chromosome.
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   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
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:ABA74473.1};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          4..121
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          198..328
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          388..543
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   596 AA;  64517 MW;  AFB5351D86C62CBE CRC64;
     MTVTVGDFLV ERLSQWGVTR IFGYPGDGIN GVFGTLSRAG GKIEFVQARH EEMAAFMASA
     HAKFTGELGV CIATSGPGAS HLITGLYDAR LDHMPVLAIV GQQARTALGS HYQQELDLVS
     MFKDVAGAFV QQASAPSQVR HLLDRAVRTA IGERRVTALI LPNDLQDLEY KAPARAHGTA
     HSGVGYSKPK VLPYDADLQR AADVLNAGEK VAILVGAGAL HASEQVFAIA EKLGAGVAKA
     LLGKAVLPDE LPWVTGCIGL LGTEPSYKLM TECDTLLMIG SGFPYAEFLP KEGQARGVQI
     DLQPDMLSLR YPMEVNLAGD AAETLAALAP LLEHKPLRKW RKKIEGWRAS WDKTLEKRAM
     AKADPVNPQR VVYELSPRLP EQAIITSDSG SCANWFARDL KIRKGMKCSL SGGLASMGAA
     VPYAIAAKFA FPQRPVIALV GDGAMQMNNM AELITVAKYW RQWDSPKWIC AVFNNEDLNQ
     VTWEQRVMEG DPKFGASQSI PDVPYHLFAI SIGLKGIFVD REEDVAAAWE QALASEVPVV
     IEFKTDPNVP PLPPHIKLEQ AKKFASTLLK GDPDEAGVIV QTAKQVLGTV LPGKRK
//
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