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Database: UniProt
Entry: Q1ZNJ6_PHOAS
LinkDB: Q1ZNJ6_PHOAS
Original site: Q1ZNJ6_PHOAS 
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
//
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