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Database: UniProt
Entry: A0A1B7ZCX5_9FLAO
LinkDB: A0A1B7ZCX5_9FLAO
Original site: A0A1B7ZCX5_9FLAO 
ID   A0A1B7ZCX5_9FLAO        Unreviewed;       803 AA.
AC   A0A1B7ZCX5;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN   ORFNames=A9200_14165 {ECO:0000313|EMBL:OBR40975.1};
OS   Maribacter hydrothermalis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=1836467 {ECO:0000313|EMBL:OBR40975.1, ECO:0000313|Proteomes:UP000092164};
RN   [1] {ECO:0000313|Proteomes:UP000092164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T28 {ECO:0000313|Proteomes:UP000092164};
RA   Zhan P.;
RL   Submitted (JUN-2016) 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:OBR40975.1}.
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DR   EMBL; LZFP01000004; OBR40975.1; -; Genomic_DNA.
DR   RefSeq; WP_068482964.1; NZ_LZFP01000004.1.
DR   AlphaFoldDB; A0A1B7ZCX5; -.
DR   STRING; 1836467.BTR34_15865; -.
DR   KEGG; mart:BTR34_15865; -.
DR   OrthoDB; 9769337at2; -.
DR   Proteomes; UP000092164; 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:UP000092164}.
FT   DOMAIN          469..643
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   803 AA;  90069 MW;  D315DE165330E710 CRC64;
     MDVSSKTSND ISFDDFKEQI ISDYEIAFLS RTCSLLGRKE VLTGKAKFGI FGDGKELPQL
     AMARSFKNGD FRSGYYRDQT FMMALGLLKP KDFFHALYAT TDIEKEPMSA GRQMGGHFLT
     HSLNTDGSWK DLTKQKNSSA DISCTAGQMP RLLGLAQASK VYRNQKGLDS AKFSVNGNEI
     AWGTIGNAST SEGMFFETIN AAGVLQVPMV ISIWDDEYGI SVPAKHHTTK EDISKVLKGF
     QRTDDENGYE IFKVNGWDYT ALMHAYENAA DIARQEHVPV MIHVKELTQP QGHSTSGSHE
     RYKDNNRLAW ERDNDCNKRF KEWILESGIA NNEELESIEK RIKRTVREAK KQAWEEYLEG
     LLSAKNTLVS LIDQAAAKSP NKNFLNKLKN DLIATEEPIK KDLAISARKS LRFLLGETST
     EKTALVNWTT NFLKESQDTY SKHLYSENEN KATNINAIAP IFKDDAEEVD GRVILRDNFD
     KLFEKYPNTL IFGEDTGAIG DVNQGLEGMQ EKYGDIRVSD TGIRETTIIG QGLGMALRGL
     RPIAEIQYLD YIFYALPTLT DDLASLLYRT AGKQKAPLII RTRGHRLEGI WHSGSEMGGL
     IHLLRGMYIL APRNMTQAAG FYNTLLKSDE PALVIESLNG YRLKEKKPSN LGEYCTPIGK
     IETIKEGNDI TLVSYGSTLR IVEKAAKELL EVGIDAEIID AQTLLPFDIT KDVLESIKKT
     NRLLVIDEDV PGGCSAYLLN EIIEKQGAFK YLDSPPQTLS AKAHRPAYGS DGDYFSKPNR
     EDIFEKVYAI MHEVSPNDYP KLR
//
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