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Ribulose bisphosphate carboxylase large chain (EC 4.1.1.39) (Fragment)

 A0A0F6Y5M3_ULEEU        Unreviewed;       468 AA.
A0A0F6Y5M3;
22-JUL-2015, integrated into UniProtKB/TrEMBL.
22-JUL-2015, sequence version 1.
25-OCT-2017, entry version 10.
RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|RuleBase:RU000302};
EC=4.1.1.39 {ECO:0000256|RuleBase:RU000302};
Flags: Fragment;
Name=rbcL {ECO:0000313|EMBL:AKG25380.1};
Ulex europaeus (Furze).
Plastid {ECO:0000313|EMBL:AKG25380.1}.
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Genisteae; Ulex.
NCBI_TaxID=3902 {ECO:0000313|EMBL:AKG25380.1};
[1] {ECO:0000313|EMBL:AKG25380.1}
NUCLEOTIDE SEQUENCE.
PubMed=26018568; DOI=10.1371/journal.pone.0126524;
Pearse W.D., Chase M.W., Crawley M.J., Dolphin K., Fay M.F.,
Joseph J.A., Powney G., Preston C.D., Rapacciuolo G., Roy D.B.,
Purvis A.;
"Beyond the EDGE with EDAM: Prioritising British Plant Species
According to Evolutionary Distinctiveness, and Accuracy and Magnitude
of Decline.";
PLoS ONE 10:e0126524-e0126524(2015).
-!- CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose
1,5-bisphosphate + CO(2) + H(2)O. {ECO:0000256|RuleBase:RU000302}.
-!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
D-ribulose 1,5-bisphosphate + O(2).
{ECO:0000256|RuleBase:RU000302}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|RuleBase:RU000302};
Note=Binds 1 Mg(2+) ion per subunit.
{ECO:0000256|RuleBase:RU000302};
-!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
{ECO:0000256|RuleBase:RU000302}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast
{ECO:0000256|RuleBase:RU000302}.
-!- SIMILARITY: Belongs to the RuBisCO large chain family.
{ECO:0000256|RuleBase:RU000302}.
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EMBL; KM361025; AKG25380.1; -; Genomic_DNA.
GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC.
GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
CDD; cd08212; RuBisCO_large_I; 1.
Gene3D; 3.20.20.110; -; 1.
Gene3D; 3.30.70.150; -; 1.
HAMAP; MF_01338; RuBisCO_L_type1; 1.
InterPro; IPR033966; RuBisCO.
InterPro; IPR020878; RuBisCo_large_chain_AS.
InterPro; IPR000685; RuBisCO_lsu_C.
InterPro; IPR036376; RuBisCO_lsu_C_sf.
InterPro; IPR017443; RuBisCO_lsu_fd_N.
InterPro; IPR036422; RuBisCO_lsu_N_sf.
InterPro; IPR020888; RuBisCO_lsuI.
Pfam; PF00016; RuBisCO_large; 1.
Pfam; PF02788; RuBisCO_large_N; 1.
SFLD; SFLDS00014; RuBisCO; 1.
SUPFAM; SSF51649; SSF51649; 1.
SUPFAM; SSF54966; SSF54966; 1.
PROSITE; PS00157; RUBISCO_LARGE; 1.
3: Inferred from homology;
Calvin cycle {ECO:0000256|RuleBase:RU000302};
Carbon dioxide fixation {ECO:0000256|RuleBase:RU000302};
Chloroplast {ECO:0000256|RuleBase:RU000302};
Lyase {ECO:0000256|RuleBase:RU000302};
Magnesium {ECO:0000256|RuleBase:RU000302};
Metal-binding {ECO:0000256|RuleBase:RU000302};
Monooxygenase {ECO:0000256|RuleBase:RU000302};
Oxidoreductase {ECO:0000256|RuleBase:RU000302};
Photorespiration {ECO:0000256|RuleBase:RU000302};
Photosynthesis {ECO:0000256|RuleBase:RU000302};
Plastid {ECO:0000256|RuleBase:RU000302}.
DOMAIN 17 137 RuBisCO_large_N.
{ECO:0000259|Pfam:PF02788}.
DOMAIN 147 455 RuBisCO_large.
{ECO:0000259|Pfam:PF00016}.
NON_TER 1 1 {ECO:0000313|EMBL:AKG25380.1}.
SEQUENCE 468 AA; 51719 MW; 501088F33548901F CRC64;
KPGVGLKAGV KDYKLTYYTP DYKTKDTDIL AAFRVTPQPG VPPEEAGAAV AAESSTGTWT
TVWTDGLTSL DRYKGRCYHI EPVAGEETQF IAYVAYPLDL FEEGSVTNMF TSIVGNVFGF
KALRALRLED LRIPNAYVKT FQGPPHGIQV ERDKLNKYGR PLLGCTIKPK LGLSAKNYGR
AVYECLRGGL DFTKDDENVN SQPFMRWRDR FLFCAEALYK AQAGTGEIKG HYLNATAGTC
EEMMKRAVFA RELGVPIVMH DYLTGGFTAN TSLSHYCRDN GLLLHIHRAM HAVIDRQKNH
GMHFRVLAKA LRLSGGDHIH AGTVVGKLEG ERDITLGFVD LLRDDFVEKD RSRGIYFTQD
WVSLPGVLPV ASGGIHVWHM PALTEIFGDD SVLQFGGGTL GHPWGNAPGA VANRVALEAC
VQARNEGRDL ASQGNQIIRE ASKWSPELAA ACEVWKEIKF EFEAMDTI


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