ID A0A125S2P5_9FLAO Unreviewed; 581 AA.
AC A0A125S2P5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:AMD84489.1};
GN ORFNames=AXF12_02460 {ECO:0000313|EMBL:AMD84489.1};
OS Capnocytophaga haemolytica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=45243 {ECO:0000313|EMBL:AMD84489.1, ECO:0000313|Proteomes:UP000065822};
RN [1] {ECO:0000313|Proteomes:UP000065822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 32990 {ECO:0000313|Proteomes:UP000065822};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (FEB-2016) 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; CP014227; AMD84489.1; -; Genomic_DNA.
DR RefSeq; WP_066428055.1; NZ_LT906449.1.
DR AlphaFoldDB; A0A125S2P5; -.
DR STRING; 45243.AXF12_02460; -.
DR KEGG; chg:AXF12_02460; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000065822; 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 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; 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.
PE 3: Inferred from homology;
KW Pyruvate {ECO:0000313|EMBL:AMD84489.1};
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 191..321
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 383..529
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 581 AA; 63902 MW; D214F0F83AE8038B CRC64;
MSKNVSDQLV EMLVQAGVKR VYAITGDSLN PVNDAIRRDG RLEWIHVRHE ESAAYAASMD
AELHGIGCCM GSSGPGHVHL INGLYDANRA GNPVIAIAST CATQKFGTHW FQETNPFYLF
EDCSKYVYVA NTPKQFTTMM QRALQTAINE KGVAVLGLPG DVAGADLEEV STATQSFLTR
PVVRPSDAEL DKLATVLNDA KNKRFVLYCG HGCREAVSQV EALAEKLKAP IVSSFRGKIF
FDREDSPYAA GMNGLLGHRS GYDACAKSDV LIMLGTDFPY AEFLPKKNTI IQIDERPEII
GRRAKVDYGY AGDVKDTIEA LLPRLKGNAD DSFLTSIHKE YVELEKSLDH YTSKKTEVDQ
IDPEYAAKLL NKYAAQDAIF TVDTGMNVVW AARFIKGTGE RYLTGSFNHG SMANALPMSI
GAAASEKGRQ VVAMCGDGGL SMLLGDLATI MQYQYPVKIF VFNNRSLAMV KLEMEVSGYL
DWQTNMVNPP FDKIAELMNI KGFEVHKTED LEGVVKQAFE TEGPVLVNIY TNRDTLAMPP
HITFEQMKGF ATNIIKKIGK GDFADAKDAI ANSMGHIKDV F
//
