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ODO2A_ARATH
ID   ODO2A_ARATH             Reviewed;         464 AA.
AC   Q9FLQ4; Q9ZRQ1;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial;
DE            EC=2.3.1.61;
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E2-1;
DE            Short=OGDC-E2-1;
DE   AltName: Full=Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1;
DE   AltName: Full=E2K-1;
DE   Flags: Precursor;
GN   OrderedLocusNames=At5g55070; ORFNames=MCO15.2;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Machuy N., Klein M., Mueller-Roeber B.;
RT   "Cloning and characterization of 2-oxoglutarate dehydrogenase from
RT   Arabidopsis thaliana.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=14671022; DOI=10.1105/tpc.016055;
RA   Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA   Millar A.H.;
RT   "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT   signaling and regulatory components, provides assessment of targeting
RT   prediction programs, and indicates plant-specific mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP   PHE-86.
RX   PubMed=25732537; DOI=10.1093/jxb/erv064;
RA   Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT   "Identification of cleavage sites and substrate proteins for two
RT   mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL   J. Exp. Bot. 66:2691-2708(2015).
CC   -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the
CC       overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
CC       contains multiple copies of three enzymatic components: 2-oxoglutarate
CC       dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and
CC       lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase
CC         complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)-
CC         succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex
CC         component E2] + CoA; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581,
CC         Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC         ChEBI:CHEBI:83100, ChEBI:CHEBI:83120; EC=2.3.1.61;
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250};
CC       Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC       pathway; glutaryl-CoA from L-lysine: step 6/6.
CC   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022,
CC       ECO:0000305|PubMed:25732537}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ223803; CAA11553.1; -; mRNA.
DR   EMBL; AB010071; BAB08576.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96577.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM68999.1; -; Genomic_DNA.
DR   EMBL; AY042897; AAK68837.1; -; mRNA.
DR   EMBL; AY128726; AAM91126.1; -; mRNA.
DR   RefSeq; NP_001330709.1; NM_001345105.1.
DR   RefSeq; NP_200318.1; NM_124889.5.
DR   AlphaFoldDB; Q9FLQ4; -.
DR   SMR; Q9FLQ4; -.
DR   BioGRID; 20842; 29.
DR   IntAct; Q9FLQ4; 1.
DR   STRING; 3702.AT5G55070.1; -.
DR   MetOSite; Q9FLQ4; -.
DR   PaxDb; Q9FLQ4; -.
DR   PRIDE; Q9FLQ4; -.
DR   ProteomicsDB; 250874; -.
DR   EnsemblPlants; AT5G55070.1; AT5G55070.1; AT5G55070.
DR   EnsemblPlants; AT5G55070.2; AT5G55070.2; AT5G55070.
DR   GeneID; 835598; -.
DR   Gramene; AT5G55070.1; AT5G55070.1; AT5G55070.
DR   Gramene; AT5G55070.2; AT5G55070.2; AT5G55070.
DR   KEGG; ath:AT5G55070; -.
DR   Araport; AT5G55070; -.
DR   TAIR; locus:2161670; AT5G55070.
DR   eggNOG; KOG0559; Eukaryota.
DR   HOGENOM; CLU_016733_0_2_1; -.
DR   InParanoid; Q9FLQ4; -.
DR   OMA; DMAGATF; -.
DR   OrthoDB; 850255at2759; -.
DR   PhylomeDB; Q9FLQ4; -.
DR   BioCyc; ARA:AT5G55070-MON; -.
DR   UniPathway; UPA00868; UER00840.
DR   PRO; PR:Q9FLQ4; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FLQ4; baseline and differential.
DR   Genevisible; Q9FLQ4; AT.
DR   GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IBA:GO_Central.
DR   GO; GO:1901149; F:salicylic acid binding; HDA:TAIR.
DR   GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR   GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   Gene3D; 3.30.559.10; -; 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; IPR011053; Single_hybrid_motif.
DR   InterPro; IPR006255; SucB.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   TIGRFAMs; TIGR01347; sucB; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Lipoyl; Mitochondrion; Reference proteome; Transferase;
KW   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..86
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:25732537"
FT   CHAIN           87..464
FT                   /note="Dihydrolipoyllysine-residue succinyltransferase
FT                   component of 2-oxoglutarate dehydrogenase complex 1,
FT                   mitochondrial"
FT                   /id="PRO_0000399512"
FT   DOMAIN          93..168
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   REGION          168..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..225
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..242
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        435
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        439
FT                   /evidence="ECO:0000250"
FT   MOD_RES         134
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   CONFLICT        30..34
FT                   /note="VAVSA -> LVASS (in Ref. 1; CAA11553)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        70
FT                   /note="I -> V (in Ref. 1; CAA11553)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        74
FT                   /note="Y -> F (in Ref. 1; CAA11553)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218..219
FT                   /note="Missing (in Ref. 1; CAA11553)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   464 AA;  50134 MW;  D5BD3083ACA39879 CRC64;
     MMLRAVFRRA SIRGSSSASG LGKSLQSSRV AVSAQFHSVS ATETLVPRGN HAHSFHHRSC
     PGCPDCSRTI INGYQGTALQ RWVRPFSSDS GDVVEAVVPH MGESITDGTL AAFLKKPGDR
     VEADEAIAQI ETDKVTIDIA SPASGVIQEF LVKEGDTVEP GNKVARISTS ADAVSHVAPS
     EKAPEKPAPK PSPPAEKPKV ESTKVAEKPK APSPPPPPPS KQSAKEPQLP PKDRERRVPM
     TRLRKRVATR LKDSQNTFAL LTTFNEVDMT NLMKLRSQYK DAFLEKHGVK LGLMSGFIKA
     AVSALQHQPV VNAVIDGDDI IYRDYVDISI AVGTSKGLVV PVIRDADKMN FADIEKTING
     LAKKATEGTI SIDEMAGGSF TVSNGGVYGS LISTPIINPP QSAILGMHSI VQRPMVVGGS
     VVPRPMMYVA LTYDHRLIDG REAVYFLRRI KDVVEDPQRL LLDI
 
 
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