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Database: UniProt
Entry: A0A090M8M9_OSTTA
LinkDB: A0A090M8M9_OSTTA
Original site: A0A090M8M9_OSTTA 
ID   A0A090M8M9_OSTTA        Unreviewed;       723 AA.
AC   A0A090M8M9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|ARBA:ARBA00017725};
DE            EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287};
GN   ORFNames=OT_ostta08g02640 {ECO:0000313|EMBL:CEG01513.1};
OS   Ostreococcus tauri.
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Ostreococcus.
OX   NCBI_TaxID=70448 {ECO:0000313|EMBL:CEG01513.1, ECO:0000313|Proteomes:UP000009170};
RN   [1] {ECO:0000313|Proteomes:UP000009170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OTTH0595 {ECO:0000313|Proteomes:UP000009170};
RX   PubMed=16868079; DOI=10.1073/pnas.0604795103;
RA   Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA   Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA   Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P.,
RA   Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA   Van de Peer Y., Moreau H.;
RT   "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT   unveils many unique features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-
CC         bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870,
CC         ChEBI:CHEBI:58272; EC=4.1.1.39;
CC         Evidence={ECO:0000256|ARBA:ARBA00001067};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate +
CC         2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033,
CC         ChEBI:CHEBI:58272; Evidence={ECO:0000256|ARBA:ARBA00000537};
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000256|ARBA:ARBA00006204}.
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:CEG01513.1}.
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DR   EMBL; CAID01000008; CEG01513.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090M8M9; -.
DR   STRING; 70448.A0A090M8M9; -.
DR   InParanoid; A0A090M8M9; -.
DR   OrthoDB; 295391at2759; -.
DR   Proteomes; UP000009170; Chromosome 8.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR   CDD; cd08210; RLP_RrRLP; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 1.
DR   InterPro; IPR013096; Cupin_2.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   InterPro; IPR033966; RuBisCO.
DR   InterPro; IPR000685; RuBisCO_lsu_C.
DR   InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR   InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR   PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR   PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR   Pfam; PF07883; Cupin_2; 1.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   SFLD; SFLDF00158; 5-methylthio-D-ribulose_1-phos; 1.
DR   SFLD; SFLDG00301; RuBisCO-like_proteins; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
DR   SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR   SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1.
PE   3: Inferred from homology;
KW   Calvin cycle {ECO:0000256|ARBA:ARBA00022567};
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW   Coiled coil {ECO:0000256|SAM:Coils}; Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Photorespiration {ECO:0000256|ARBA:ARBA00023238};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009170}.
FT   DOMAIN          128..376
FT                   /note="Ribulose bisphosphate carboxylase large subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00016"
FT   DOMAIN          559..616
FT                   /note="Cupin type-2"
FT                   /evidence="ECO:0000259|Pfam:PF07883"
FT   REGION          696..723
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          460..490
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   723 AA;  78925 MW;  3BE6B7EF7E5786B7 CRC64;
     MSAAHKVRRF VVTYDVEAET ELEARRIVDA LCLEQTIELP EALAPPGTWI NEHVVAKTLE
     LARVSELGWR GRYRARVAFS DDVAGAELTQ LINAIFGNTS IKERVMVRDV EFSEEMQSGF
     GGPRFGAKGL RKLLGVERGP LVMTALKPMG TPSDKLAEMA YAFAKGGIDI IKDDHGLANQ
     RYAPYEERVR ACAAAVKRAN EETGRKCIYA PCINAPAHLV VQRAKFAKAA GAGAVLMIPG
     ITGLDSMRAL AEDPDFGLPI IAHPAILGAM LGGGTEDVCR GFSHEVLLGL LPRLAGADAT
     IFPNFGGRFG FSIDECKDIA RGCRRLMGHH ESILPSPGGG MTLDKVKVMM ETYGQDVLLL
     VGGSLYSHSS DLTANARHIL SMAGRTDTYG PSENGHYTPS RYNHNGNYTP MTGLRPKLRL
     VDESATAQSP YPTTPHNAYP SAPPSTPYTI SLDPEAVAQM SALKEKNSAL ESKVEELTTL
     VKQLMEVESN RYHGNGSKHA SQGPLEGNHS KVLNRKKGEF QWERVPQEMY KMDGASFKEC
     SRIELIGKRG ESPVFHVRYF EVAPGGWTTL EHHQHEHVVV VLRGEGEIQL GLESYHLAHG
     DVGYTAPGDT HQLRCKAGAT EPFGFICVVA SDRDRPIEDE PAELLKMCKV AHVLDDNVRV
     ALETQIKHRA AHKAAHGAVA EGSACEWKPG MKKKAEESVS ACEWKPKAKS NAEPKPTPTR
     YFP
//
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