ID A0A0U3JYG1_9BACT Unreviewed; 575 AA.
AC A0A0U3JYG1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:ALW85391.1};
GN ORFNames=AUC43_09970 {ECO:0000313|EMBL:ALW85391.1};
OS Hymenobacter sedentarius.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1411621 {ECO:0000313|EMBL:ALW85391.1, ECO:0000313|Proteomes:UP000059542};
RN [1] {ECO:0000313|EMBL:ALW85391.1, ECO:0000313|Proteomes:UP000059542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG5B {ECO:0000313|EMBL:ALW85391.1,
RC ECO:0000313|Proteomes:UP000059542};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) 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; CP013909; ALW85391.1; -; Genomic_DNA.
DR RefSeq; WP_068192566.1; NZ_CP013909.1.
DR AlphaFoldDB; A0A0U3JYG1; -.
DR STRING; 1411621.AUC43_09970; -.
DR KEGG; hyg:AUC43_09970; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000059542; 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:ALW85391.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000059542};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..319
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 382..527
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 575 AA; 61109 MW; 85273ABE0639C860 CRC64;
MPKKSVAEII VDTLQAAGVR RVFGVVGDSL NGITDAIRTR EGIEFVAVRH EEGGAFAAGA
EAALTGDLAV CAGSCGPGNT HLINGLFDCH RSRVPVLALA AQIPNVEIGT GYFQETHPER
LFRECSHYCE LISVPEQAVR TIESAVAAAI GLRGVAVVVL PGDVAYLETD APEVRLPTQG
RNSALVPAEA DIRQAAALLN AGDKVTILAG IGCAGAHAEL LQTAAALHAP VVHALRGKEW
VEPNNPYDVG LTGLLGMPAG YHALLDADTV LMLGTDFPYR QFYPDDARVV QVDSRPEHIG
RRTRVEIGLV GTVADTLRLL LPHLAPRTDA AHLEDAQQRH ADDEAHLAEL ATGEPGDTSL
HPQHVARLLD ELASEDAIFT CDVGTPTIWA ARYLHMNGQR RLIGSFVHGS MANAVSQAYG
AALAQPSRQV VAMCGDGGVA MLLSELLTIR QHKVPVKLIV FNNSALSFVE LEMKAAGILE
YGTELDNPDF GAVAEAAGLR GFRVSDPGQL EGVLREALAH DGPVLVDAVV KRQELSMPPS
IDRKQVAGFS LYAVKALIDG RGGELLELAK TNLFR
//
