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Database: UniProt
Entry: A0A1Q9CLM3_SYMMI
LinkDB: A0A1Q9CLM3_SYMMI
Original site: A0A1Q9CLM3_SYMMI 
ID   A0A1Q9CLM3_SYMMI        Unreviewed;      1051 AA.
AC   A0A1Q9CLM3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00017172};
DE            EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281};
GN   Name=aceE {ECO:0000313|EMBL:OLP83829.1};
GN   ORFNames=AK812_SmicGene35366 {ECO:0000313|EMBL:OLP83829.1};
OS   Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS   microadriatica).
OC   Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC   Symbiodinium.
OX   NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP83829.1, ECO:0000313|Proteomes:UP000186817};
RN   [1] {ECO:0000313|EMBL:OLP83829.1, ECO:0000313|Proteomes:UP000186817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP83829.1,
RC   ECO:0000313|Proteomes:UP000186817};
RA   Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA   Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA   Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT   "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT   adaptations to a symbiotic lifestyle.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:OLP83829.1}.
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DR   EMBL; LSRX01001090; OLP83829.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q9CLM3; -.
DR   OMA; PDEYRTF; -.
DR   OrthoDB; 3638585at2759; -.
DR   Proteomes; UP000186817; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; cd00051; EFh; 1.
DR   CDD; cd02017; TPP_E1_EcPDC_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
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; PF13499; EF-hand_7; 1.
DR   Pfam; PF17831; PDH_E1_M; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:OLP83829.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          101..136
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
SQ   SEQUENCE   1051 AA;  115712 MW;  00066AE3E67FBDE2 CRC64;
     MTLAARLCRG HVFRRPVVLR QVTRGMALHW RHGGTPSGVG IGGNRSPHDL LSELGSIFAK
     EGITTLSSLS ASWFARADQN VSKGLDPEEF RETMASVGLK LSDPESESLF AHFDTDKSGI
     ITYGEFAKGL QGEMPAFSAS LAFMHQHTGH FPSNQERLRA ARPKFDETET HEWLESLDAV
     VQNLGTTRAR FLMHELMEEA SRLGVHISQP VVTPMVNSIP TSAEPAYPGD RAMEDRLSNI
     IRWNAAVMVS DANRRGGGVG GHIGTFASIC DVIEVGMNHF FRGKDYGNGR GDSVWMQGHA
     APGAYSRAFV EGRLSIDQVM NFRREVAGNG VSSYPHPRLM PHFWENPTVS MGLGPLGAVY
     QARFFRYLHL RGLADTSKSR VWAFVGDGEM DEPESITAIS VAGRERLNNM IFIVNCNYQR
     LDGPVRGNSK VMQEYEGTFR GAGFDVIKLI WGGKFNELIE QDHDGKLIEA LESTVDGDCQ
     RLHAKADGAL IRKDIFEKHG LLDRVAHWSD AELLEAFQVP GGHDHSKIYA AFAQAEQNSE
     MGGRPTVILV KTLKGYSLQT FLGRNTVHQK KMMSDSDMKA YRDAMGIPLS DEQLGKADAE
     NFVTLKEDAP EVKYLKERRQ ALGGYLPLRA PAKVSALVEL PKHDVYDMFD TGSKGREIST
     TMCFAQILRK MMQAGEFGQR CTLMVTDESR TFGIDAFFPI FKIHAPFGQN YTPVDADQVM
     KYAESPSGQI LQEGISEGGA IMTWIASATS YSSQHAPTLP FLIYYSMFGF QRVGDSIWQA
     ADARARGFLI GATYGRTTLN GEGLQHQDGH SLLIAHTCPA VKGYDPAFGY EMAAIIENGV
     KEMWGEDKDV IYYVTAYNEN FAMPEKPEGV DEGIVKGLYK FSDAKSADHK VRIIGSGAIM
     KQAMDAIEIL AEYGVGVELW SATSYGELQR EAIACQRLER LGGEAPTSWV EQCLGDGDVT
     VAVSDNMTAY PKLIAPWVGG DFIVLGADGF GRSDTRENLR RFFEVDKEHV AVAALQGLAK
     QGKISADVVA QARAKLGISI ERKDICMEAV C
//
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