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Database: UniProt
Entry: A0A0A0HI04_9RHOB
LinkDB: A0A0A0HI04_9RHOB
Original site: A0A0A0HI04_9RHOB 
ID   A0A0A0HI04_9RHOB        Unreviewed;       336 AA.
AC   A0A0A0HI04;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha {ECO:0000256|ARBA:ARBA00014159, ECO:0000256|RuleBase:RU361139};
DE            EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281, ECO:0000256|RuleBase:RU361139};
GN   Name=pdhA {ECO:0000256|RuleBase:RU361139};
GN   ORFNames=rosmuc_02892 {ECO:0000313|EMBL:KGM86601.1};
OS   Roseovarius mucosus DSM 17069.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1288298 {ECO:0000313|EMBL:KGM86601.1, ECO:0000313|Proteomes:UP000030021};
RN   [1] {ECO:0000313|EMBL:KGM86601.1, ECO:0000313|Proteomes:UP000030021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17069 {ECO:0000313|EMBL:KGM86601.1,
RC   ECO:0000313|Proteomes:UP000030021};
RA   Fiebig A., Goeker M., Klenk H.-P.P.;
RL   Submitted (JAN-2013) 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).
CC       {ECO:0000256|RuleBase:RU361139}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-
CC         acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC         Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC         Evidence={ECO:0000256|RuleBase:RU361139};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964,
CC         ECO:0000256|RuleBase:RU361139};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC       {ECO:0000256|ARBA:ARBA00011870, ECO:0000256|RuleBase:RU361139}.
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:KGM86601.1}.
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DR   EMBL; AONH01000016; KGM86601.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A0HI04; -.
DR   STRING; 215743.ROSMUCSMR3_03445; -.
DR   PATRIC; fig|1288298.3.peg.2909; -.
DR   eggNOG; COG1071; Bacteria.
DR   HOGENOM; CLU_029393_5_2_5; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000030021; Unassembled WGS sequence.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:InterPro.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR   CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR   InterPro; IPR029061; THDP-binding.
DR   NCBIfam; TIGR03182; PDH_E1_alph_y; 1.
DR   PANTHER; PTHR11516:SF60; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR11516; PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT BACTERIAL AND ORGANELLAR; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361139};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|RuleBase:RU361139};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU361139}.
FT   DOMAIN          23..320
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   336 AA;  36868 MW;  D5A5A5BE58BDA616 CRC64;
     MVARKSTKKP NVSAEDLKQY YRDMLLIRRF EEKAGQLYGM GLIGGFCHLY IGQEAVVVGL
     EAAAEEGDRR ITTYRDHGHM LACGMDPNGV MAELTGREGG YSRGKGGSMH MFSTEKRFYG
     GHGIVGANVP LGAGLAFADK YLGNDRVTFT YFGDGAANQG QVYETFNMAA LWQLPVIFVI
     ENNQYAMGTS QKRSTSSPDI YTRGQAFGIP GEAVDGMDVL AVKEAGDKAV AHCRSGAGPY
     ILEIKTYRYR GHSMSDPAKY RTREEVQKMR EEKDAIEHVR ELLVSGGHAT EEDLKAIDKE
     IKDVVNASAE FAKESPEPAL EELWTDIIAD AAPQNA
//
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