(data stored in SCRATCH zone)

SWISSPROT: A4ATT3_MARSH

ID   A4ATT3_MARSH            Unreviewed;       325 AA.
AC   A4ATT3;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|RuleBase:RU364074};
DE            EC=1.2.4.1 {ECO:0000256|RuleBase:RU364074};
GN   OrderedLocusNames=FB2170_17251 {ECO:0000313|EMBL:EAR00853.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00853.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00853.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO2.
CC       {ECO:0000256|RuleBase:RU364074}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[dihydrolipoyllysine-residue acetyltransferase]-(R)-N(6)-
CC         lipoyl-L-lysine + H(+) + pyruvate = [dihydrolipoyllysine-residue
CC         acetyltransferase]-(R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysine
CC         + CO2; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480, Rhea:RHEA-
CC         COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111;
CC         EC=1.2.4.1; Evidence={ECO:0000256|RuleBase:RU364074};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|RuleBase:RU364074};
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DR   EMBL; CP002157; EAR00853.1; -; Genomic_DNA.
DR   RefSeq; WP_013304656.1; NC_014472.1.
DR   STRING; 313603.FB2170_17251; -.
DR   EnsemblBacteria; EAR00853; EAR00853; FB2170_17251.
DR   KEGG; fbc:FB2170_17251; -.
DR   eggNOG; ENOG4107QNT; Bacteria.
DR   eggNOG; COG0022; LUCA.
DR   HOGENOM; HOG000281450; -.
DR   KO; K00162; -.
DR   OMA; EDDWLTY; -.
DR   OrthoDB; 900125at2; -.
DR   BioCyc; MSP313603:G1GNS-226-MONOMER; -.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 3.40.50.920; -; 1.
DR   InterPro; IPR027110; PDHB.
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; PTHR11624; PTHR11624; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   SUPFAM; SSF52922; SSF52922; 1.
PE   4: Predicted;
DR   PRODOM; A4ATT3.
DR   SWISS-2DPAGE; A4ATT3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364074};
KW   Pyruvate {ECO:0000256|RuleBase:RU364074, ECO:0000313|EMBL:EAR00853.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU364074}.
FT   DOMAIN        4    179       Transket_pyr. {ECO:0000259|SMART:
FT                                SM00861}.
SQ   SEQUENCE   325 AA;  35537 MW;  63880CF22A1B6942 CRC64;
     MKTLQFRQAI AEAMSEEMRT DESIYLMGEE VAEYNGAYKA SKGMLDEFGP DRVIDTPISE
     LGFAGIGVGS TLTGNRPIIE FMTFNFALVG IDQIINNAAK IRQMSGGQFS CPIVFRGPTG
     SAGQLAATHS QAFESWFANC PGLKVVVPSN PADAKGLLKS AIRDNDPVIF MESEQMYGDK
     GEVPEGEYTI PLGVADIRRE GSDVTIVSFG KIIKQADKAA DELSKDGISC EIIDLRTVKP
     LDYEAILNSV KKTNRLVILE EAWPYGNVAS EITFHVQSNA FDYLDAPIQK INTADTPAPY
     SPVLLAEWLP DHEDVINAVK KVLYK
//

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