ID A0A1M6CTW0_9FLAO Unreviewed; 573 AA.
AC A0A1M6CTW0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Pyruvate dehydrogenase (Quinone) {ECO:0000313|EMBL:SHI64467.1};
GN ORFNames=SAMN05443429_1034 {ECO:0000313|EMBL:SHI64467.1};
OS Cruoricaptor ignavus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Cruoricaptor.
OX NCBI_TaxID=1118202 {ECO:0000313|EMBL:SHI64467.1, ECO:0000313|Proteomes:UP000184335};
RN [1] {ECO:0000313|EMBL:SHI64467.1, ECO:0000313|Proteomes:UP000184335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25479 {ECO:0000313|EMBL:SHI64467.1,
RC ECO:0000313|Proteomes:UP000184335};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQYI01000003; SHI64467.1; -; Genomic_DNA.
DR RefSeq; WP_073178662.1; NZ_FQYI01000003.1.
DR AlphaFoldDB; A0A1M6CTW0; -.
DR STRING; 1118202.SAMN05443429_1034; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000184335; 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; 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:SHI64467.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184335};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..112
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 189..317
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 379..525
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 573 AA; 62613 MW; 3C6A05BE576648E4 CRC64;
MNVSDQLVLM LKDAGVKRIY AITGDSLNPV NDAIRRDGEI EWIHVRHEEA AAYAASMDAE
LHGIGCCMGS SGPGHVHLVN GLYDANRAGN PVIAIASTVP TGKVGTDYFQ ETFPQFLFEG
CSKYNQAANT PQQFVTMFQQ AIQVAKNERG VAVVSLPGDV AAASYDEVVT SEHTYHPKPL
YRPQDSELAE LAAILNQNEK IAIYAGYGAK DAVGEVEALV EKLQAPLSFS FRGKIFFDKT
ESKYTCGMNG LLGNPGGFKS LHDADVVLML GTDFPYAEFV PQDNILIQID AKPSQIGRRG
KVDHGYAGDI KDTIAALLPL VQPKDDYSFA EKYHKEYVRE HAHHRDKVNK QTKTDHIHPE
AVAVLLDDMA DEDAIFTVDV GMTCVWAARL LSPKKGRYMT SSMNHGSMAS ALPQAIGAAA
STKNRQVIAL CGDGGLSMSL SELATVMQYQ YPIKIVVFNN RSLGMVKLEM EVQGFVDWQT
DMVNPPFEKV AELFNIKGYA VRERGELDST MKEFLAHEGP ALLHIYTDPG TLAMPPQVTF
DQVKGFAKSA IRKVALGRFS DVGDMVKAGL DAL
//
