ID Q85UU8_9FLOR Unreviewed; 474 AA.
AC Q85UU8;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|RuleBase:RU000302};
DE EC=4.1.1.39 {ECO:0000256|RuleBase:RU000302};
DE Flags: Fragment;
GN Name=rbcL {ECO:0000313|EMBL:AAP22301.1};
OS Dermocorynus dichotomus.
OG Plastid; Chloroplast {ECO:0000313|EMBL:AAP22301.1}.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Halymeniales;
OC Halymeniaceae; Dermocorynus.
OX NCBI_TaxID=1562370 {ECO:0000313|EMBL:AAP22301.1};
RN [1] {ECO:0000313|EMBL:AAP22301.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=26/V/01 {ECO:0000313|EMBL:AAP22301.1};
RA Gavio B., Fredericq S.;
RT "Grateloupia turuturu (Halymeniaceae, Rhodophyta) is the correct name of
RT the non-native species in the Atlantic known as Grateloupia doryphora.";
RL Eur. J. Phycol. 37:349-359(2002).
RN [2] {ECO:0000313|EMBL:AAP22301.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=26/V/01 {ECO:0000313|EMBL:AAP22301.1};
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 ECO:0000256|RuleBase:RU000302};
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 ECO:0000256|RuleBase:RU000302};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU000302};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|RuleBase:RU000302};
CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC {ECO:0000256|ARBA:ARBA00011371, ECO:0000256|RuleBase:RU000302}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|RuleBase:RU000302}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family.
CC {ECO:0000256|RuleBase:RU000302}.
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DR EMBL; AF488824; AAP22301.1; -; Genomic_DNA.
DR AlphaFoldDB; Q85UU8; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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 CDD; cd08212; RuBisCO_large_I; 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 HAMAP; MF_01338; RuBisCO_L_type1; 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 InterPro; IPR020888; RuBisCO_lsuI.
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 3: Inferred from homology;
KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567,
KW ECO:0000256|RuleBase:RU000302};
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300,
KW ECO:0000256|RuleBase:RU000302};
KW Chloroplast {ECO:0000256|RuleBase:RU000302, ECO:0000313|EMBL:AAP22301.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000302};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU000302};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000302};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU000302};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000302};
KW Photorespiration {ECO:0000256|RuleBase:RU000302};
KW Photosynthesis {ECO:0000256|RuleBase:RU000302};
KW Plastid {ECO:0000256|ARBA:ARBA00022640}.
FT DOMAIN 14..134
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 144..451
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:AAP22301.1"
SQ SEQUENCE 474 AA; 52412 MW; 151F6B1FDC474961 CRC64;
RYESGVIPYA KMGYWDPDYV IKDTDVLALF RVTPQPGVDP VEASAAVAGE SSTATWTVVW
TDLLTACDLY RAKAYKVDAV PNSSEQYFAY IAYDIDLFEE GSIANLTASI IGNVFGFKAV
KALRLEDMRI PVAYLKTFQG PATGVVVERE RMDKFGRPFL GATVKPKLGL SGKNYGRVVY
EGLKGGLDFL KDDENINSQP FMRWKERFLY SMEGVNRSIA ASGEVKGHYM NVTAATMEDM
YERAEFAKQL GTVIIMIDLV IGYTAIQTMG VWARKNDMIL HLHRAGNSTY SRQKSHGMNF
RVICKWMRMA GVDHIHAGTV VGKLEGDPLM IRGFYNTLLL THLDVNLPQG IFFEQDWASL
RKVTPVASGG IHCGQMHQLL DYLGNDVVLQ FGGGTIGHPD GIQAGATANR VALEAMVMAR
NEGREYVAEG PQILQDAAKT CGPLQTALDL WKDITFNYTS TDTADFVETP TANV
//
