ID Q572U9_9FLOR Unreviewed; 419 AA.
AC Q572U9;
DT 10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2005, sequence version 1.
DT 22-FEB-2023, entry version 52.
DE RecName: Full=ribulose-bisphosphate carboxylase {ECO:0000256|ARBA:ARBA00012287};
DE EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287};
DE Flags: Fragment;
GN Name=rbcL {ECO:0000313|EMBL:CAI30849.1};
OS Grateloupia filicina.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Halymeniales;
OC Halymeniaceae; Grateloupia.
OX NCBI_TaxID=31455 {ECO:0000313|EMBL:CAI30849.1};
RN [1] {ECO:0000313|EMBL:CAI30849.1}
RP NUCLEOTIDE SEQUENCE.
RA De Clerck O., Gavio B., Fredericq S., Barbara I., Coppejans E.;
RT "Systematics of Grateloupia filicina (Halymeniaceae, Rhodophyta), based on
RT rbcL sequence analyses and morphological evidence, including the
RT reinstatement of G. minima and the description of G. capensis sp. nov.";
RL J. Phycol. 41:391-410(2005).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ868480; CAI30849.1; -; Genomic_DNA.
DR AlphaFoldDB; Q572U9; -.
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:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
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; IPR033966; RuBisCO.
DR InterPro; IPR020878; RuBisCo_large_chain_AS.
DR InterPro; IPR000685; RuBisCO_lsu_C.
DR InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR InterPro; IPR017443; RuBisCO_lsu_fd_N.
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; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDG01052; RuBisCO; 1.
DR SFLD; SFLDS00014; RuBisCO; 1.
DR SFLD; SFLDG00301; RuBisCO-like_proteins; 1.
DR SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1.
DR PROSITE; PS00157; RUBISCO_LARGE; 1.
PE 4: Predicted;
KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567};
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Plastid {ECO:0000256|ARBA:ARBA00022640}.
FT DOMAIN 1..112
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 122..407
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAI30849.1"
FT NON_TER 419
FT /evidence="ECO:0000313|EMBL:CAI30849.1"
SQ SEQUENCE 419 AA; 46179 MW; 7811A8E6BF5E02FE CRC64;
DTDVLALFRV TPQPGVDPVE ASAAVAGESS TATWTVVWTD LLTACDLYRA KAYKVDAVPN
SSEQYFAYIA YDIDLFEEGS IANLTASIIG NVFGFKAVKA LRLEDMRIPV AYLKTFQGPA
TGIVVERERM DKFGRPFLGA TVKPKLGLSG KNYGRVVYEG LKGGLDFLKD DENINSQPFM
RWKERFLYSM EAVNRSIAAT GEVKGHYMNV TAATMEDMYE RAEFAKQLGT VIIMIDLVIG
YTAIQTMGIW ARKNDMILHL HRAGNSTYSR QKSHGMNFRV ICKWMRMAGV DHIHAGTVVG
KLEGDPLMIR GFYNTLLLTH LDVNLPQGIF FEQDWASLRK VTPVASGGIH CGQMHQLLDY
LGNDVVLQFG GGTIGHPDGI QAGATANRVA LEAMVMARNE GRDYVGEGPQ ILQDAAKTC
//
