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Database: UniProt
Entry: A0A0D6TJH7_9FLAO
LinkDB: A0A0D6TJH7_9FLAO
Original site: A0A0D6TJH7_9FLAO 
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
//
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