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Database: UniProt/SWISS-PROT
Entry: RBL_GOSHI
LinkDB: RBL_GOSHI
Original site: RBL_GOSHI 
ID   RBL_GOSHI               Reviewed;         475 AA.
AC   P14958; Q2L916; Q42769;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   10-OCT-2018, entry version 113.
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   Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Malvales; Malvaceae; Malvoideae;
OC   Gossypium.
OX   NCBI_TaxID=3635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. 108-F;
RX   PubMed=2308826; DOI=10.1093/nar/18.1.185;
RA   Gulov M.K., Ulmasov T.N., Aliev K.A., Andrianov V.M., Piruzian E.S.;
RT   "Nucleotide sequence of the chloroplast rbcL gene from cotton
RT   Gossypium hirsutum.";
RL   Nucleic Acids Res. 18:185-185(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Coker 310FR;
RX   PubMed=16553962; DOI=10.1186/1471-2164-7-61;
RA   Lee S.-B., Kaittanis C., Jansen R.K., Hostetler J.B., Tallon L.J.,
RA   Town C.D., Daniell H.;
RT   "The complete chloroplast genome sequence of Gossypium hirsutum:
RT   organization and phylogenetic relationships to other angiosperms.";
RL   BMC Genomics 7:61-61(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-469.
RX   AGRICOLA=IND92012379; DOI=10.2307/2419059;
RA   Giannasi D.E., Zurawski G., Learn G.H., Clegg M.T.;
RT   "Evolutionary relationships of the Caryophyllidae based on comparative
RT   rbcL sequences.";
RL   Syst. Bot. 17:1-15(1992).
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; X15886; CAA33896.1; -; Genomic_DNA.
DR   EMBL; DQ345959; ABC73636.1; -; Genomic_DNA.
DR   EMBL; M77700; AAA33068.1; -; Genomic_DNA.
DR   PIR; S07582; RKCNLU.
DR   RefSeq; YP_538943.1; NC_007944.1.
DR   ProteinModelPortal; P14958; -.
DR   SMR; P14958; -.
DR   GeneID; 3989157; -.
DR   KEGG; ghi:3989157; -.
DR   KO; K01601; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
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   PANTHER; PTHR42704; PTHR42704; 1.
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_0000031245.
FT   CHAIN         3    475       Ribulose bisphosphate carboxylase large
FT                                chain.
FT                                /FTId=PRO_0000031246.
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    359    359       S -> R (in Ref. 1; CAA33896).
FT                                {ECO:0000305}.
FT   CONFLICT    470    474       EAMDT -> DAVDKLDKVEK (in Ref. 2;
FT                                ABC73636). {ECO:0000305}.
SQ   SEQUENCE   475 AA;  52701 MW;  F38CEFD0EC2DCD1D CRC64;
     MSPQTETKAS VGFKAGVKEY KLTYYTPEYE VKDTDILAAF RVTPQPGVPP EEAGAAVAAE
     SSTGTWTTVW TDGLTSLDRY KGRCYDIEPV PGEEDQYICY VAYPLDLFEE GSVTNMFTSI
     VGNVFGFKAL RALRLEDLRV PTAYIKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
     SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIFKSQA ETGEIKGHYL
     NATAGTCEEM IKRAMCAREL GVPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV
     IDRQKNHGMH FRVLAKALRM SGGDHIHAGT VVGKLEGERD ITLGFVDLLR DDFIEKDRSR
     GIYFTQDWVS MPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
     RVALEACVQA RNEGRDLARE GNEIIREASK WSPELAAACE VWKAIKFEFE AMDTL
//
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