ID C3PJA0_CORA7 Unreviewed; 581 AA.
AC C3PJA0;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Pyruvate:quinone oxidoreductase {ECO:0000313|EMBL:ACP33786.1};
GN Name=pqo {ECO:0000313|EMBL:ACP33786.1};
GN OrderedLocusNames=cauri_2195 {ECO:0000313|EMBL:ACP33786.1};
OS Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CIP 107346 /
OS CN-1) (Corynebacterium nigricans).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=548476 {ECO:0000313|EMBL:ACP33786.1, ECO:0000313|Proteomes:UP000002077};
RN [1] {ECO:0000313|EMBL:ACP33786.1, ECO:0000313|Proteomes:UP000002077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700975 / DSM 44827 / CIP 107346 / CN-1
RC {ECO:0000313|Proteomes:UP000002077};
RX PubMed=20137072; DOI=10.1186/1471-2164-11-91;
RA Trost E., Gotker S., Schneider J., Schneiker-Bekel S., Szczepanowski R.,
RA Tilker A., Viehoever P., Arnold W., Bekel T., Blom J., Gartemann K.H.,
RA Linke B., Goesmann A., Puhler A., Shukla S.K., Tauch A.;
RT "Complete genome sequence and lifestyle of black-pigmented Corynebacterium
RT aurimucosum ATCC 700975 (formerly C. nigricans CN-1) isolated from a
RT vaginal swab of a woman with spontaneous abortion.";
RL BMC Genomics 11:91-91(2010).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP001601; ACP33786.1; -; Genomic_DNA.
DR RefSeq; WP_010188918.1; NZ_ACLH01000050.1.
DR AlphaFoldDB; C3PJA0; -.
DR STRING; 548476.cauri_2195; -.
DR GeneID; 31924846; -.
DR KEGG; car:cauri_2195; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_11; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000002077; 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 CDD; cd02014; TPP_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 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:ACP33786.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002077};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..114
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 193..317
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 381..527
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 581 AA; 62642 MW; 95FDADD6A59C86E5 CRC64;
MARNYATQLV ETLEAQGVKR IYGLVGDSLN PIVDAVRQSS IEWVHVRNEE AAAFAAEADS
LTTGNLAVCA ASCGPGNTHL IQGLYDAHRN GAKVLALASH IPSRQIGSKF FQETHPEAIF
QECSGYCEMV NSAEQGGVVL HHAIQSTMAG KGVSVLVIPG DVSTQEAEED TFTSSVISSG
RPVVYPDPAE AAALTQAINE AKTVALFVGA GVKNAREQVL ALAEKIKAPI GHALGGKMYI
QYDNPFDVGM SGLLGYGAAH EATHEADLLI LLGTDFPYND FLPDANVAQV DIDGSHIGRR
TRIKYPVTGD VAATIENILP HVDEKKDRSF LDKMLKKHYD KLHHVVEAYT SGVEKHTPIH
PEYIADLIDQ QADEDAIFTV DTGMCNVWGA RYITANGKRE QIGSFRHGTM ANALPMAIGA
QAAHPGRQVI TFSGDGGLSM LMGELLTVKL HNLPVKMFVF NNSSLGMVKL EMLVQGLPEH
ETDHEHVNYA KIAEGAGIKH FRIEDPKDAP RLIKEALAYD GPALIDVVTD PNALSLPPTL
TFEQLLGFSK AATRTVFGGG VGQMLSMAKS NLRNIPRPQD F
//
