ID Q1ZNJ6_PHOAS Unreviewed; 888 AA.
AC Q1ZNJ6;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 90.
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 ORFNames=VAS14_19986 {ECO:0000313|EMBL:EAS63733.1};
OS Photobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain S14 /
OS CCUG 15956)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=314292 {ECO:0000313|EMBL:EAS63733.1, ECO:0000313|Proteomes:UP000001603};
RN [1] {ECO:0000313|EMBL:EAS63733.1, ECO:0000313|Proteomes:UP000001603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14 {ECO:0000313|EMBL:EAS63733.1,
RC ECO:0000313|Proteomes:UP000001603};
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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|ARBA:ARBA00003157, 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:ARBA00033635,
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};
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:EAS63733.1}.
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DR EMBL; AAOJ01000005; EAS63733.1; -; Genomic_DNA.
DR RefSeq; WP_005371273.1; NZ_CH902602.1.
DR AlphaFoldDB; Q1ZNJ6; -.
DR CarbonylDB; Q1ZNJ6; -.
DR eggNOG; COG2609; Bacteria.
DR HOGENOM; CLU_009154_2_0_6; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000001603; Unassembled WGS sequence.
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; IPR001849; PH_domain.
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; 2.
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.
DR PROSITE; PS50003; PH_DOMAIN; 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};
KW Pyruvate {ECO:0000256|PIRNR:PIRNR000156, ECO:0000313|EMBL:EAS63733.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 1..26
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 888 AA; 99136 MW; 95756687A55B2AE2 CRC64;
MSEVMKSDVD VLETQDWLEA LESVVREEGV ERAQFLLEQV LEKARLDGVD MPTGVNTNYI
NTIPAAQEPA YPGDVTLERR IRSIIRWNAI MIVLRASKKD LDLGGHMASY QSASAFYEVC
FNHFFRAPND VDGGDLVYYQ GHISPGIYSR AFVEGRLTEE QLDNFRQEVD GKGIPSYPHP
KLMPEFWQFP TVSMGLGPIS AIYQARFLKY LEGRGLKDTS AQRVYAFLGD GEMDEPESRG
AISFAAREKL DNLCFLINCN LQRLDGPVMG NGKIIQELEG LFKGAGWNVV KVIWGNNWDA
LLAKDTSGKL LQLMNETIDG DYQTFKSKDG AYVREHFFGK YPETAALVSD MTDEQIFELK
RGGHDSSKLF AAFNNAKETS GKPTVILAKT VKGYGMGEAA EGKNIAHGVK KMDMTHVQYL
RDRLGLQDLI SEEELKTLPY LKLEEGSAEY NYLHARRDAL HGYTPKRSPK FTQEFKVPEL
DAFAPLLSEQ KREISTTMAY VRTLNILLKD KAIGKNIVPI ICDEARTFGM EGLFRQVGIY
NPDGQTYTPE DKGIVSFYKE ATSGQVLQEG INELGSMASW VAAATSYSTN DLPMIPFYIY
YSMFGFQRIG DMAWLAGDQQ ARGFLLGATA GRTTLNGEGL QHEDGHSHIL ANTVPNCISY
DPTFAYELAV IMQDGIRRMY GENQENVYYY LTVMNENYAM PAMPEGAEAG IRKGIYKLES
HAGDKSKVQL MSSGTIMNEV RKAAQILSEE YGVASDVYSV TSFNELTRDG QDCERYNMLH
PTAEKKVPYL TTAMGSEPAI AATDYMKNYA EQVRAFMPSE SYKVLGTDGF GRSDSRANLR
RHFEVNAGYV VVAALSELAK RGDIDNAVVV DAIAKFDIDA DKINPLYA
//