ID A0A2K3D6Z2_CHLRE Unreviewed; 572 AA.
AC A0A2K3D6Z2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Dehydrogenase E1 component domain-containing protein {ECO:0000259|Pfam:PF00676};
GN ORFNames=CHLRE_12g539900v5 {ECO:0000313|EMBL:PNW76303.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055 {ECO:0000313|EMBL:PNW76303.1, ECO:0000313|Proteomes:UP000006906};
RN [1] {ECO:0000313|EMBL:PNW76303.1, ECO:0000313|Proteomes:UP000006906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503 {ECO:0000313|Proteomes:UP000006906};
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
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DR EMBL; CM008973; PNW76303.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K3D6Z2; -.
DR STRING; 3055.A0A2K3D6Z2; -.
DR EnsemblPlants; PNW76303; PNW76303; CHLRE_12g539900v5.
DR Gramene; PNW76303; PNW76303; CHLRE_12g539900v5.
DR InParanoid; A0A2K3D6Z2; -.
DR OMA; RPTNEIE; -.
DR OrthoDB; 952at2759; -.
DR Proteomes; UP000006906; Chromosome 12.
DR ExpressionAtlas; A0A2K3D6Z2; baseline.
DR GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; IBA:GO_Central.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR029061; THDP-binding.
DR PANTHER; PTHR43380; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43380:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00676; E1_dh; 2.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006906}.
FT DOMAIN 139..351
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT DOMAIN 413..496
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 385..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 572 AA; 59219 MW; 8494D93FCC30441F CRC64;
MHLPALAAAR QRHSLSELLC ALARAATPVA ALGSGHGGPC ATVAPCRSHT AAAASGARRY
AVSTRSESVA AARSTVDAYL EVPGGRVPYT PELRFLGGPD APIPTMPCYR TIDSTGQDVP
GAHIPHPLSQ ELSLRLYGAM ARLQTMDTMF YEAQRQGRFS FYLTCQGEEA TNIGSAAGLG
GQDMVFAQYR EQGVLLWRGY TLDQFANQLL GNALEPGKGR QMPIHYGSPE LAYQTISSPL
ATQMPHAVGT AYGYKMDRLP RVAVTYFGDG ASSEGDAHAA FNFAAVLGAP CLFVCRNNGY
AISTPAHEQY KGDGIAGRGP MYGIPSIRVD GGDVRAVYNA VVEARRRALG GQPAAAAAAA
AGAAGAAAAP GQHCSGSGSS GGLLTEPAVG AVGKGAGQGQ GQGQGQGQQQ AAEPGPVLIE
CMSYRSGHHS TSDDSTRYRT SEEMGAWRAR DPVARFRSWL VRQGWWDEAR EAELRRSTRQ
EVLAALDRAA QVPKPPLSDM FTDVYAPLTA AAGGGGATAG GGGAGGAAAA AGGADDTGAG
LGLPPHLAAQ RAATLDFARR HPAVCPPDVP LR
//