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Database: UniProt
Entry: G5EK04_9CHLO
LinkDB: G5EK04_9CHLO
Original site: G5EK04_9CHLO 
ID   G5EK04_9CHLO            Unreviewed;       436 AA.
AC   G5EK04;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   22-FEB-2023, entry version 31.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|ARBA:ARBA00017725};
DE            EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287};
DE   Flags: Fragment;
GN   Name=rbcL {ECO:0000313|EMBL:BAL14442.1};
OS   Ulva sp. RH039.
OC   Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; OUU clade; Ulvales;
OC   Ulvaceae; Ulva.
OX   NCBI_TaxID=915488 {ECO:0000313|EMBL:BAL14442.1};
RN   [1] {ECO:0000313|EMBL:BAL14442.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RH039 {ECO:0000313|EMBL:BAL14442.1};
RA   Horimoto R., Masakiyo Y., Ichihara K., Shimada S.;
RT   "Enteromorpha-like Ulva (Ulvophyceae, Chlorophyta) Growing in the Todoroki
RT   River, Ishigaki Island, Japan, with Special Reference to Ulva meridionalis
RT   Horimoto et Shimada, sp. nov.";
RL   Bull Natl Mus Nat Sci Ser B Bot 37:155-167(2011).
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   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000256|ARBA:ARBA00006204}.
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DR   EMBL; AB598811; BAL14442.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5EK04; -.
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; 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   Acetylation {ECO:0000256|ARBA:ARBA00022990};
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   Photorespiration {ECO:0000256|ARBA:ARBA00023238};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640}.
FT   DOMAIN          15..134
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          144..428
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:BAL14442.1"
FT   NON_TER         436
FT                   /evidence="ECO:0000313|EMBL:BAL14442.1"
SQ   SEQUENCE   436 AA;  48097 MW;  46061A57234E6C00 CRC64;
     GTGFKAGVKD YRLTYYTPDY QVKDTDILAA FRMTPQPGVP AEEAGAAVAA ESSTGTWTTV
     WTDGLTSLDR YKGRCYDIEP LGEDDQYIAY IAYPLDLFEE GSVTNLFTSI VGNVFGFKAL
     RALRLEDLRI PPAYVKTFQG PPHGIQVERD KLNKYGRGLL GCTIKPKLGL SAKNYGRAVY
     ECLRGGLDFT KDDENVNSQP FMRWRDRFLF TAEAIYKSQA ETGEVKGHYL NATAGTCEEM
     MERGQFAKDL GVPIIMHDYI TGGFTANTSL AHFCRASGLL LHIHRAMHAV IDRQRNHGIH
     FRVLAKILRM SGGDHLHSGT VVGKLEGERE ITLGFVDLMR DDYIEKDRSR GIYFTQDWVS
     LPGTMPVASG GIHVWHMPAL VEIFGDDACL QFGGGTLGHP WGNAPGAAAN RVALEACTQA
     RNEGRDLASE GGDVIR
//
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