ID A0A0D6TJH7_9FLAO Unreviewed; 801 AA.
AC A0A0D6TJH7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=SY27_14720 {ECO:0000313|EMBL:KIX20360.1};
OS Flavobacterium sp. 316.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1603293 {ECO:0000313|EMBL:KIX20360.1, ECO:0000313|Proteomes:UP000032747};
RN [1] {ECO:0000313|EMBL:KIX20360.1, ECO:0000313|Proteomes:UP000032747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=316 {ECO:0000313|EMBL:KIX20360.1,
RC ECO:0000313|Proteomes:UP000032747};
RA Karczewska-Golec J., Kochanowska-Lyzen M., Balut M., Golec P.,
RA Madanecki P., Markert S., Piotrowski A., Schweder T., Szalewska-Palasz A.;
RT "Three Bacterial Inhabitants of the Baltic Sea under Osmotic Stress: a
RT Genomic and a Proteomic Perspective.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (E3). {ECO:0000256|ARBA:ARBA00025211}.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|ARBA:ARBA00011870}.
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:KIX20360.1}.
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DR EMBL; JYGZ01000006; KIX20360.1; -; Genomic_DNA.
DR RefSeq; WP_045971656.1; NZ_JYGZ01000006.1.
DR AlphaFoldDB; A0A0D6TJH7; -.
DR STRING; 1603293.SY27_14720; -.
DR PATRIC; fig|1603293.4.peg.3034; -.
DR OrthoDB; 9769337at2; -.
DR Proteomes; UP000032747; Unassembled WGS sequence.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR43257; PYRUVATE DEHYDROGENASE E1 COMPONENT BETA SUBUNIT; 1.
DR PANTHER; PTHR43257:SF2; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000032747}.
FT DOMAIN 467..641
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 801 AA; 89591 MW; 7DF9BAD3DA8A5F2D CRC64;
MSNSVAKETL SFQDFKTEVI NDYKIAVTSR ECSLLGRREV LTGKAKFGIF GDGKEVPQLA
LAKAFKNGDF RSGYYRDQTF MMAIGAMNIE QFFAGLYGHT DINHDPMSAG RQMGGHFATH
SLDENGNWNN LTAQKNSSAD ISPTAGQMPR LLGLAQASKI YRNVKGLENK THFSNQGDEI
AWGTIGNAST SEGLFFETIN AAGVLQVPMV MSVWDDEYGI SVHAKYQTTK ENISEILKGF
QRDEDNNGYE ILRVKGWDYP ALVETYQKAS QIARKEHIPV LIHVNELTQP QGHSTSGSHE
RYKSTERLEW ETEFDCLAQM KLWIIANNIA TEEELTDINL TAKKAVLEGK KAAWTAFTSP
IKTEQEELIT LLKSIAETST NKVFIEKHIN DLAVLKEPIR KDVLTTARKA LRLLINESGK
TTLGNWITTY QEKTQPKFSS HLFSQSDKNI FSVKEVKPTY DETAEDVDAR LVLRDNFDAI
FSKYPETLIF GEDSGNIGDV NQGLEGMQEK YGEFRVADAG IREATILGQG IGMAMRGLRP
IAEIQYLDYL LYAIQIMSDD LATLQYRTKG RQKAPLIIRT RGHRLEGVWH SGSPMGMIIN
AIRGIHVLVP RNMTKAAGFY NTLLETDEPA LVIECLNGYR LKEKMPTNLA EFKTPIGVVE
TIKEGNDITL VSYGSTLRLI EQAAKELLEI GIDAEIIDVQ SLLPFDINHD IVKSLAKTNR
LLVIDEDVPG GASAYILQEI IENQKGYKHL DSEPQTLASQ AHRPAYGTDG DYFSKPSAED
IFEKVYAIMH ESNPTKYPSL Y
//