ID Q01VH5_SOLUE Unreviewed; 895 AA.
AC Q01VH5;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00017172, ECO:0000256|PIRNR:PIRNR000156};
DE EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281, ECO:0000256|PIRNR:PIRNR000156};
GN OrderedLocusNames=Acid_5391 {ECO:0000313|EMBL:ABJ86340.1};
OS Solibacter usitatus (strain Ellin6076).
OC Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC Solibacter.
OX NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ86340.1};
RN [1] {ECO:0000313|EMBL:ABJ86340.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ86340.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Janssen P.H., Kuske C.R., Richardson P.;
RT "Complete sequence of Solibacter usitatus Ellin6076.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex, that
CC catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
CC {ECO:0000256|PIRNR:PIRNR000156}.
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|ARBA:ARBA00043719,
CC ECO:0000256|PIRNR:PIRNR000156};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000156-1};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|PIRNR:PIRNR000156};
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DR EMBL; CP000473; ABJ86340.1; -; Genomic_DNA.
DR AlphaFoldDB; Q01VH5; -.
DR STRING; 234267.Acid_5391; -.
DR KEGG; sus:Acid_5391; -.
DR eggNOG; COG2609; Bacteria.
DR HOGENOM; CLU_009154_2_0_0; -.
DR InParanoid; Q01VH5; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd02017; TPP_E1_EcPDC_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR035807; PDC_E1_N.
DR InterPro; IPR004660; PDH_E1.
DR InterPro; IPR041621; PDH_E1_M.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005474; Transketolase_N.
DR NCBIfam; TIGR00759; aceE; 1.
DR PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR PANTHER; PTHR43825:SF3; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR Pfam; PF17831; PDH_E1_M; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000156-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000156-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000156}; Pyruvate {ECO:0000256|PIRNR:PIRNR000156};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 142..305
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 493..706
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 268
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 270
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 895 AA; 100844 MW; CCA620FB86332992 CRC64;
MRLSMHQKLN ERVVDLNPQE TSEWIESLDQ VIDEAGPDRA TFLLEHLTER ARATGVELPV
QLNTPYINTI RPEDEVPYPG DRAMERRIKS LIRWNAMAMV VRQNKYDAGI GGHISTYASL
ATLLEVGFNH FFHASYGDQP GDLVYFQGHA SPGVYGRAFL EGRITEEHLK NFRHELRDTP
GLSSYPHPWL MPDFWSFPTV SMGLGPINAI YQARFMRYLE NRGIIPETPR QVWAYLGDGE
MDEPESMGSI TLASREKLDN LKFVINCNLQ RLDGPVRGNG KVIQELEAAF RGAGWNVIKV
IWGSDWDPLL ARDTTGLLQR RMGEVVDGEF QTYVTKDGAY IRQYFFGKYP ELLDLVSHLS
DEEVFKLRRG GHDPRKVYNA YKQAVETKGK PTLILAHSVK GYGLGESGEG RNISHQQKKL
NEQEIANFRS RFEIPIPDEA ARNASFYRPP SDSPEMSYLH ERRRVLGGYM PSRKVPESKI
TAPPLEYLKE SLEGSGEREV SSTMAMVRVL TLLLKHPEIG KRVVPIIPDE ARTFGMESLF
RQFGIYASQG QLYKPHDAEI FLYYKESRDG QILEEGITEA GSISSFTAAG TAYANYGVEM
IPFFIYYSMF GFQRVGDSIW AFGDARGKGF LCGGTAGRTT LSGEGLQHQD GHSILHASTV
PNCKTYDPAF AYEIAIIVQD GIRVMYQEKQ DCFYYLTLYN ENYPMPAMPA GLDPEGVLKG
IYRFKAPEKG KAKVHLFGSG PILNEALRAQ QILAEKYNVP SDVWSVTSYN ELRRDALAVE
RWNRLHPDQP QRVPYLLQAM KGADAPVIAA SDYMKVVADQ IAPWLPGRME TLGTDGFGRS
DNREYLRRHF EINAESIAAA ALSRLARDGK FDAKKAVAAF KDLGVDTEKI DAARA
//
