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
//