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Database: UniProt/SWISS-PROT
Entry: RBL_HELAN
LinkDB: RBL_HELAN
Original site: RBL_HELAN 
ID   RBL_HELAN               Reviewed;         485 AA.
AC   P45738; Q9ZSR9;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   23-MAY-2018, entry version 98.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000255|HAMAP-Rule:MF_01338};
DE            Short=RuBisCO large subunit {ECO:0000255|HAMAP-Rule:MF_01338};
DE            EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338};
DE   Flags: Precursor;
GN   Name=rbcL {ECO:0000255|HAMAP-Rule:MF_01338};
OS   Helianthus annuus (Common sunflower).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; asterids; campanulids; Asterales; Asteraceae;
OC   Asteroideae; Heliantheae alliance; Heliantheae; Helianthus.
OX   NCBI_TaxID=4232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9880354; DOI=10.1104/pp.119.1.133;
RA   Kanevski I., Maliga P., Rhoades D.F., Gutteridge S.;
RT   "Plastome engineering of ribulose-1,5-bisphosphate
RT   carboxylase/oxygenase in tobacco to form a sunflower large subunit and
RT   tobacco small subunit hybrid.";
RL   Plant Physiol. 119:133-142(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Michaels H.J.;
RT   "Interfamilial relationships of the Asteraceae.";
RL   Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HA383;
RA   Timme R.E., Kuehl J.V., Boore J.L., Jansen R.K.;
RT   "A comparison of the first two published chloroplast genomes in
RT   Asteraceae: Lactuca and Helianthus.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC       ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC       fixation, as well as the oxidative fragmentation of the pentose
CC       substrate in the photorespiration process. Both reactions occur
CC       simultaneously and in competition at the same active site.
CC       {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose
CC       1,5-bisphosphate + CO(2) + H(2)O. {ECO:0000255|HAMAP-
CC       Rule:MF_01338}.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
CC       D-ribulose 1,5-bisphosphate + O(2). {ECO:0000255|HAMAP-
CC       Rule:MF_01338}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01338};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01338};
CC   -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains;
CC       disulfide-linked. The disulfide link is formed within the large
CC       subunit homodimers. {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- PTM: The disulfide bond which can form in the large chain dimeric
CC       partners within the hexadecamer appears to be associated with
CC       oxidative stress and protein turnover. {ECO:0000255|HAMAP-
CC       Rule:MF_01338}.
CC   -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC       chain homodimer in a "head-to-tail" conformation. In form I
CC       RuBisCO this homodimer is arranged in a barrel-like tetramer with
CC       the small subunits forming a tetrameric "cap" on each end of the
CC       "barrel". {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}.
DR   EMBL; AF097517; AAD13766.1; -; Genomic_DNA.
DR   EMBL; L13929; AAB01594.1; -; Genomic_DNA.
DR   EMBL; DQ383815; ABD47154.1; -; Genomic_DNA.
DR   RefSeq; YP_588125.1; NC_007977.1.
DR   ProteinModelPortal; P45738; -.
DR   SMR; P45738; -.
DR   EnsemblPlants; OTG37585; OTG37585; HannXRQ_Chr01g0020381.
DR   GeneID; 4055709; -.
DR   Gramene; OTG37585; OTG37585; HannXRQ_Chr01g0020381.
DR   KEGG; han:4055709; -.
DR   KO; K01601; -.
DR   BRENDA; 4.1.1.39; 2597.
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: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; -; 1.
DR   Gene3D; 3.30.70.150; -; 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   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SFLD; SFLDS00014; RuBisCO; 1.
DR   SUPFAM; SSF51649; SSF51649; 1.
DR   SUPFAM; SSF54966; SSF54966; 1.
DR   PROSITE; PS00157; RUBISCO_LARGE; 1.
PE   3: Inferred from homology;
KW   Acetylation; Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW   Disulfide bond; Lyase; Magnesium; Metal-binding; Methylation;
KW   Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis;
KW   Plastid.
FT   PROPEP        1      2       {ECO:0000255|HAMAP-Rule:MF_01338}.
FT                                /FTId=PRO_0000031247.
FT   CHAIN         3    485       Ribulose bisphosphate carboxylase large
FT                                chain.
FT                                /FTId=PRO_0000031248.
FT   ACT_SITE    175    175       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   ACT_SITE    294    294       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   METAL       201    201       Magnesium; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   METAL       203    203       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   METAL       204    204       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     123    123       Substrate; in homodimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   BINDING     173    173       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     177    177       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     295    295       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     327    327       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     379    379       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   SITE        334    334       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   MOD_RES       3      3       N-acetylproline. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   MOD_RES      14     14       N6,N6,N6-trimethyllysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   MOD_RES     201    201       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   DISULFID    247    247       Interchain; in linked form.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   CONFLICT    225    225       I -> L (in Ref. 2; AAB01594).
FT                                {ECO:0000305}.
FT   CONFLICT    244    244       A -> T (in Ref. 2; AAB01594).
FT                                {ECO:0000305}.
FT   CONFLICT    412    412       G -> E (in Ref. 2; AAB01594).
FT                                {ECO:0000305}.
FT   CONFLICT    416    417       GA -> VV (in Ref. 2; AAB01594).
FT                                {ECO:0000305}.
FT   CONFLICT    448    449       AT -> HS (in Ref. 2; AAB01594).
FT                                {ECO:0000305}.
FT   CONFLICT    474    474       T -> P (in Ref. 2; AAB01594).
FT                                {ECO:0000305}.
SQ   SEQUENCE   485 AA;  53853 MW;  F654C6474D56BD2A CRC64;
     MSPQTETKAS VGFKAGVKDY KLTYYTPEYE TKDTDILAAF RVTPQPGVPP EEAGAAVAAE
     SSTGTWTTVW TDGLTSLDRY KGRCYGLEPV PGEDNQFIAY VAYPLDLFEE GSVTNMFTSI
     VGNVFGFKAL RALRLEDLRI PTAYVKTFDG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
     SAKNYGRACY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIYKAQA ETGEIKGHYL
     NATAGNCEDM MKRAVFAREL GVPIVMHDYL TGGFTANTSL SQYCRDNGLL LHIHRAMHAV
     IDRQKNHGMH FRVLAKALRM SGGDHIHSGT VVGKLEGERE ITLGFVDLLR DDFIEKDRSR
     GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
     RVALEACVQA RNEGRDLATE GNEIIREATK WSPELAAACE VWKEIKFEFQ AMDTLDTDKD
     KDKKR
//
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