ID A0A1I7ET50_9FLAO Unreviewed; 579 AA.
AC A0A1I7ET50;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Pyruvate dehydrogenase (Quinone) {ECO:0000313|EMBL:SFU27124.1};
GN ORFNames=SAMN05216480_10175 {ECO:0000313|EMBL:SFU27124.1};
OS Pustulibacterium marinum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Pustulibacterium.
OX NCBI_TaxID=1224947 {ECO:0000313|EMBL:SFU27124.1, ECO:0000313|Proteomes:UP000199138};
RN [1] {ECO:0000313|EMBL:SFU27124.1, ECO:0000313|Proteomes:UP000199138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12333 {ECO:0000313|EMBL:SFU27124.1,
RC ECO:0000313|Proteomes:UP000199138};
RA de Groot N.N.;
RL Submitted (OCT-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; FPBK01000001; SFU27124.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7ET50; -.
DR STRING; 1224947.SAMN05216480_10175; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000199138; 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:SFU27124.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199138};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..115
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 190..318
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 579 AA; 63226 MW; 6D7C3E64DABE39C5 CRC64;
MSQSVSDKIV KMLVDAGVKR VYAVTGDSLN PVNDAIRREG SIQWIHVRHE EAGAYAASMD
AELNGIGCCM GSSGPGHVHL INGLYDANRS GNPVIAIAST VATHKMGTEN FQETNVTKLF
DDCSKYCFMS NTPKQALTGL QSAIQHAITE KGVAVLGLPG DVASADAEAV VSADKNYFTK
PVITPPQQHI EEFASVINSN KNVMLYVGHG AKDAYSEVID LAETIKAPIG YSFRGKIFFE
KDENPYTVGL NGLLGNKSGF KAMHEADLLI LLGTDFPYSD FLPENNTIIQ IDIKPERIGR
RAKVDYGYCG DIKETLKRVL PLVETKTETK YLDNMLKLHK EVEDNYQSYV EGKGKEDQIH
PEYVASVIDN LADDDAIFTV DTGMSAVWAA RYLKGKKNRY LTGSFNHGSM ANAMPMAIGA
GLSQPERQTI ALCGDGGITM LLGDLMTISQ YNIPVKIIIF NNRTLGMVKL EMEVAGIPDW
QTDMVNPDFA KVAEAMNIRS YTADKPEQVT SVLKEAFVHE GPAVINIFTD PNALAMPPKV
TFEQMKGFAE SMGKLMLNGD AAEVISSAKS NAKYLKELF
//
