ID A0A0J1BPW2_9SPHI Unreviewed; 578 AA.
AC A0A0J1BPW2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:KLT67543.1};
GN ORFNames=AB669_02285 {ECO:0000313|EMBL:KLT67543.1};
OS Pedobacter sp. BMA.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1663685 {ECO:0000313|EMBL:KLT67543.1, ECO:0000313|Proteomes:UP000036014};
RN [1] {ECO:0000313|EMBL:KLT67543.1, ECO:0000313|Proteomes:UP000036014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BMA {ECO:0000313|EMBL:KLT67543.1,
RC ECO:0000313|Proteomes:UP000036014};
RA Anderson B.M., Pipes S.E., Miller J.R., Newman J.D.;
RT "Pedobacter sp. BMA.";
RL Submitted (JUN-2015) 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:KLT67543.1}.
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DR EMBL; LECU01000001; KLT67543.1; -; Genomic_DNA.
DR RefSeq; WP_047797632.1; NZ_LECU01000001.1.
DR AlphaFoldDB; A0A0J1BPW2; -.
DR STRING; 1663685.AB669_02285; -.
DR PATRIC; fig|1663685.3.peg.481; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000036014; Unassembled WGS sequence.
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; 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:KLT67543.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036014};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..318
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 380..526
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 578 AA; 63108 MW; 4D62D1A3456B626D CRC64;
MSKNVAEQLV EMLVEAGVKR IYAVTGDSLN YFNEAVRKNG KIKWIHVRNE EAGAFAAAAE
AELDGIACCA GSCGPGHVHL INGLYDAHRS HVPVIAIAST IPTGEFGMDF FQETNTIKLF
DDCSFYNQIA TTPEQAPRML QTALQHAIHQ KGVAVFGLPG DVSQMDAVES VTSMQFFSNK
PVVRPSEEEL GELALLLNSE KKITLYCGIG AAEAHDEVVA LASRLKSPVS FSFRGKMSIQ
HNNPYEVGMT GLLGQPSGYH AMHEADVVLL LGTDFPYVNF MPVKNKIVQI DERPERLGRR
AKLTMGLCGN IADSIAALLP LLEEKTDDDF LKSQLEFYEK VKENQQVYIK DQGEENRIQP
EFVADTLNRI ASSDAIFTVD TGMCCVWGAR FIDGTGKRKM LGSFNHGSMA NAMPMAIGAA
LAHPEKQVIA LCGDGGLSML LGDIATIKQY NLPVKLIVFN NRALGMVKLE MEVDGLPDNE
TDMINPDFAL VAQAMGFKGM TVSKPEDVET AIAHALSEDG PVLLNIMTNP NALAMPPKIE
WKQIKGMTES MTKLMLGGKM SEVFDTIKSN YKHLGEVL
//
