ID C1MVI5_MICPC Unreviewed; 326 AA.
AC C1MVI5;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EEH55996.1};
GN ORFNames=MICPUCDRAFT_59391 {ECO:0000313|EMBL:EEH55996.1};
OS Micromonas pusilla (strain CCMP1545) (Picoplanktonic green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Mamiellaceae; Micromonas.
OX NCBI_TaxID=564608 {ECO:0000313|Proteomes:UP000001876};
RN [1] {ECO:0000313|EMBL:EEH55996.1, ECO:0000313|Proteomes:UP000001876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1545 {ECO:0000313|EMBL:EEH55996.1,
RC ECO:0000313|Proteomes:UP000001876};
RX PubMed=19359590; DOI=10.1126/science.1167222;
RA Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA Grigoriev I.V.;
RT "Green evolution and dynamic adaptations revealed by genomes of the marine
RT picoeukaryotes Micromonas.";
RL Science 324:268-272(2009).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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DR EMBL; GG663741; EEH55996.1; -; Genomic_DNA.
DR RefSeq; XP_003060044.1; XM_003059998.1.
DR AlphaFoldDB; C1MVI5; -.
DR STRING; 564608.C1MVI5; -.
DR GeneID; 9685482; -.
DR KEGG; mpp:MICPUCDRAFT_59391; -.
DR eggNOG; KOG4166; Eukaryota.
DR OrthoDB; 318356at2759; -.
DR Proteomes; UP000001876; Unassembled WGS sequence.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR PANTHER; PTHR18968:SF86; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVX-RELATED; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001876}.
FT DOMAIN 24..136
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 326 AA; 34482 MW; 6BCDCA5973321978 CRC64;
MPRFAPSAAK QPVEKRVERP KAPTGAESMM KALADRGVEA CFANPGTTEM WLVGALDAEP
RVRPVLGLHE TVCAGAVDGY ARMARKPACT ILHLGPGLAN ALANLHNARR ANVPVLNIVG
DMSTWHRGAD ALLEMDVEAR SISHWPFAGA SLRPPLDFNP RPRCLTTPTD AFELHPDVAS
YGLALNVEAL AAAVSSHVHT STVPGAMRSD AIDALKATDR SETNADGRGR VATLIVPHDR
TWERTGSLLA SIMDSDDEDD VDDAKRAAPA SYVPPTPAPH PAPSSVINAG DDATAFVTAA
VHDAVRGALA LRCVLYTGPH TTPSAW
//
