ID M1V566_CYAM1 Unreviewed; 677 AA.
AC M1V566;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN ORFNames=CYME_CMI273C {ECO:0000313|EMBL:BAM80135.1};
OS Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC Cyanidioschyzon.
OX NCBI_TaxID=280699 {ECO:0000313|EMBL:BAM80135.1, ECO:0000313|Proteomes:UP000007014};
RN [1] {ECO:0000313|EMBL:BAM80135.1, ECO:0000313|Proteomes:UP000007014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10D {ECO:0000313|EMBL:BAM80135.1,
RC ECO:0000313|Proteomes:UP000007014};
RX PubMed=15071595; DOI=10.1038/nature02398;
RA Matsuzaki M., Misumi O., Shin-i T., Maruyama S., Takahara M.,
RA Miyagishima S., Mori T., Nishida K., Yagisawa F., Nishida K., Yoshida Y.,
RA Nishimura Y., Nakao S., Kobayashi T., Momoyama Y., Higashiyama T.,
RA Minoda A., Sano M., Nomoto H., Oishi K., Hayashi H., Ohta F., Nishizaka S.,
RA Haga S., Miura S., Morishita T., Kabeya Y., Terasawa K., Suzuki Y.,
RA Ishii Y., Asakawa S., Takano H., Ohta N., Kuroiwa H., Tanaka K.,
RA Shimizu N., Sugano S., Sato N., Nozaki H., Ogasawara N., Kohara Y.,
RA Kuroiwa T.;
RT "Genome sequence of the ultrasmall unicellular red alga Cyanidioschyzon
RT merolae 10D.";
RL Nature 428:653-657(2004).
RN [2] {ECO:0000313|EMBL:BAM80135.1, ECO:0000313|Proteomes:UP000007014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10D {ECO:0000313|EMBL:BAM80135.1,
RC ECO:0000313|Proteomes:UP000007014};
RX PubMed=17623057; DOI=10.1186/1741-7007-5-28;
RA Nozaki H., Takano H., Misumi O., Terasawa K., Matsuzaki M., Maruyama S.,
RA Nishida K., Yagisawa F., Yoshida Y., Fujiwara T., Takio S., Tamura K.,
RA Chung S.J., Nakamura S., Kuroiwa H., Tanaka K., Sato N., Kuroiwa T.;
RT "A 100%-complete sequence reveals unusually simple genomic features in the
RT hot-spring red alga Cyanidioschyzon merolae.";
RL BMC Biol. 5:28-28(2007).
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|RuleBase:RU003423};
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP006491; BAM80135.1; -; Genomic_DNA.
DR RefSeq; XP_005536421.1; XM_005536364.1.
DR AlphaFoldDB; M1V566; -.
DR STRING; 280699.M1V566; -.
DR EnsemblPlants; CMI273CT; CMI273CT; CMI273C.
DR GeneID; 16993667; -.
DR Gramene; CMI273CT; CMI273CT; CMI273C.
DR KEGG; cme:CYME_CMI273C; -.
DR eggNOG; KOG0557; Eukaryota.
DR HOGENOM; CLU_016733_10_2_1; -.
DR OMA; NEWLVKP; -.
DR OrthoDB; 5483022at2759; -.
DR Proteomes; UP000007014; Chromosome 9.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR045257; E2/Pdx1.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR23151:SF9; PYRUVATE DEHYDROGENASE PROTEIN X COMPONENT, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000007014};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:BAM80135.1};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 180..256
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 38..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 677 AA; 73370 MW; E615D31F9BCC72BC CRC64;
MEPPGTGSPT STAAISTTTS VRGVGCPTFR FEGIAGAARS GATVSDTNSR RPERFGARAS
TSVEEATKAM LRLQTKSWWW RCGIQRRSVG AWFGGHNLIR SGDGSRALRR PEQPRSDPAG
RYVQQRPAWG LVHRLCQVVD QQQRTECVAA GTRLSCVDRW RPRGALRRRS SAAADSLPPH
VPIKMPALSP TMKAGNLLAW KRREGEPVTA GDVLAEIETD KATIEFESQE EGILAKILVP
DGTQDVPVGT LIAVLAEDEE HVSALQRMDW NSATKPESTS VQRQRYALAT EMQQQQQQQQ
ASSGSTEADT SMTQQLEQES EPLPWRYGPA VATMLANHEL PAALVQRLQP SGPRGHVLKG
DLLRVLAAAK GSGAASTRRD SQSAAEVQRS SSSFVSSTPH GPGTGTAAEG SRVLPSREHQ
QVPTSSSPSP AAATPTTTTT QFRDIPLSQV RRVIAERLLE SKQKAPHAYQ SIVVNFEALL
ELRQTINMLA ANSLQALRTP KLTVNDLLLR AVAIALREHR SLNTNAERVD LAFAVATPTG
LITPIIHDAD TKSVSVIAAE SQDLVQRARQ NKLKLHEFQG GSFSISNLGM VPAIARFTAI
INPPQAGILA IGAPQRRLVP RAANLTSQSS VEPLDTERLR FATLTLSYDA GRVQRTASLA
FLQDLQRLIE SPSWLLV
//
