GenomeNet

Database: UniProt
Entry: M4M1H5_9FLOR
LinkDB: M4M1H5_9FLOR
Original site: M4M1H5_9FLOR 
ID   M4M1H5_9FLOR            Unreviewed;       479 AA.
AC   M4M1H5;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 32.
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:AGG18245.1};
OS   Actinotrichia robusta.
OG   Plastid {ECO:0000313|EMBL:AGG18245.1}.
OC   Eukaryota; Rhodophyta; Florideophyceae; Nemaliophycidae; Nemaliales;
OC   Galaxauraceae; Actinotrichia.
OX   NCBI_TaxID=305682 {ECO:0000313|EMBL:AGG18245.1};
RN   [1] {ECO:0000313|EMBL:AGG18245.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wiriyadamrikul J., Lewmanomont K., Boo S.M.;
RT   "Molecular diversity and morphology of the genus Actinotrichia
RT   (Galaxauraceae, Rhodophyta) from the western Pacific, with a new record of
RT   A. robusta in the Andaman Sea.";
RL   Algae 28:53-62(2013).
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}.
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; KC609389; AGG18241.1; -; Genomic_DNA.
DR   EMBL; KC609393; AGG18245.1; -; Genomic_DNA.
DR   EMBL; KC609400; AGG18252.1; -; Genomic_DNA.
DR   AlphaFoldDB; M4M1H5; -.
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};
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, ECO:0000313|EMBL:AGG18245.1}.
FT   DOMAIN          19..139
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          152..456
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:AGG18245.1"
SQ   SEQUENCE   479 AA;  53118 MW;  033A53AC52DC63F3 CRC64;
     RIKNERYESG VIPYAKMGYW DPDYVVKETD VLALFRVTPQ PGVDPIEASA AVAGESSTAT
     WTVVWTDLLT ACDLYRAKAY KVDAVPSSSD QYFAYIAYDI DLFEEGSIAN LTASIIGNVF
     GFKAVKALRL EDMRLPVAYL KTFQGPATGT IVERERMDKF GRPFLGATVK PKLGLSGKNY
     GRVVYEGLKG GLDFLKDDEN INSQPFMRWR ERYLYSMEGV NRSQAGSGEV KGHYLNVTAG
     TMEDMYERAE FAKELGSVIC MIDLVIGYTA IQTMAVWARK TDMILHLHRA GNSTYSRQKE
     HGMNFRVICK WMRMAGVDHI HAGTVVGKLE GDPLMIRGFY NTLLESHLDV NLPQGIFFEQ
     DWASLRKVTP VASGGIHCGQ MHQLLDYLGD DVVLQFGGGT IGHPDGIQAG ATANRVALES
     MVLARNEGRD YVNEGPQILR DAAKTCGPLQ TALDLWKDIS FNYTSTDTAD FVETPTANV
//
DBGET integrated database retrieval system