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
//