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Database: UniProt
Entry: A4BYY0_9FLAO
LinkDB: A4BYY0_9FLAO
Original site: A4BYY0_9FLAO 
ID   A4BYY0_9FLAO            Unreviewed;       329 AA.
AC   A4BYY0;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 57.
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=PI23P_07105 {ECO:0000313|EMBL:EAR12373.1};
OS   Polaribacter irgensii 23-P.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=313594 {ECO:0000313|EMBL:EAR12373.1, ECO:0000313|Proteomes:UP000003053};
RN   [1] {ECO:0000313|EMBL:EAR12373.1, ECO:0000313|Proteomes:UP000003053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=23-P {ECO:0000313|EMBL:EAR12373.1,
RC   ECO:0000313|Proteomes:UP000003053};
RA   Murray A., Staley J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA   Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) 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:EAR12373.1}.
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DR   EMBL; AAOG01000002; EAR12373.1; -; Genomic_DNA.
DR   RefSeq; WP_004570041.1; NZ_CH724148.1.
DR   AlphaFoldDB; A4BYY0; -.
DR   STRING; 313594.PI23P_07105; -.
DR   eggNOG; COG1071; Bacteria.
DR   HOGENOM; CLU_029393_5_0_10; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000003053; 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   Reference proteome {ECO:0000313|Proteomes:UP000003053};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU361139}.
FT   DOMAIN          15..312
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   329 AA;  37273 MW;  1F8163103011D2B5 CRC64;
     MKKITKQTYL DWYKDMLFWR KFEDKLAAVY IQQKVRGFLH LYNGQEAILA GALHAMDLSK
     DRMITAYRNH VQPIGMGEDP KKVMAELFGK VTGTSKGMGG SMHIFSKEFR FYGGHGIVGG
     QIPLGAGLAF ADKYKGSDAV TLTCFGDGAA RQGSLHEAFN MAMLWKLPVV FIVENNGYAM
     GTSVERTANH TDIWKLGLGY EMPCGPVDAM NPIKVAEAVD EAIQRARRGD GPTFLEMKTY
     RYRGHSMSDA QKYRTKDEVE EYKKIDPITQ ILNVIKEKEY ATAEEIAIID KDVKARVKEC
     EKFAEDSPYP EPQQMYDMVY EQKDYPFIS
//
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