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Database: UniProt/TrEMBL
Entry: H2B943_GOSRA
LinkDB: H2B943_GOSRA
Original site: H2B943_GOSRA 
ID   H2B943_GOSRA            Unreviewed;       479 AA.
AC   H2B943;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   25-OCT-2017, entry version 34.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302};
DE            Short=RuBisCO large subunit {ECO:0000256|HAMAP-Rule:MF_01338};
DE            EC=4.1.1.39 {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302};
GN   Name=rbcL {ECO:0000256|HAMAP-Rule:MF_01338,
GN   ECO:0000313|EMBL:ADV39129.1};
GN   ORFNames=GoraCp029 {ECO:0000313|EMBL:ADV39129.1};
OS   Gossypium raimondii (New World cotton).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:ADV39129.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Malvales; Malvaceae; Malvoideae;
OC   Gossypium.
OX   NCBI_TaxID=29730 {ECO:0000313|EMBL:ADV39129.1};
RN   [1] {ECO:0000313|EMBL:ADV39129.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=22876273; DOI=10.1371/journal.pone.0037128;
RA   Xu Q., Xiong G., Li P., He F., Huang Y., Wang K., Li Z., Hua J.;
RT   "Analysis of complete nucleotide sequences of 12 gossypium chloroplast
RT   genomes: origin and evolution of allotetraploids.";
RL   PLoS ONE 7:E37128-E37128(2012).
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:0000256|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:0000256|HAMAP-
CC       Rule:MF_01338, ECO:0000256|RuleBase:RU000302}.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
CC       D-ribulose 1,5-bisphosphate + O(2). {ECO:0000256|HAMAP-
CC       Rule:MF_01338, ECO:0000256|RuleBase:RU000302}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01338, ECO:0000256|RuleBase:RU000302};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01338, ECO:0000256|RuleBase:RU000302};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC       Rule:MF_01338, ECO:0000256|RuleBase:RU000302}.
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:0000256|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:0000256|HAMAP-Rule:MF_01338}.
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DR   EMBL; HQ325744; ADV39129.1; -; Genomic_DNA.
DR   RefSeq; YP_005087701.1; NC_016668.1.
DR   PRIDE; H2B943; -.
DR   GeneID; 11538595; -.
DR   KEGG; gra:11538595; -.
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   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   Calvin cycle {ECO:0000256|HAMAP-Rule:MF_01338,
KW   ECO:0000256|RuleBase:RU000302};
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01338,
KW   ECO:0000256|RuleBase:RU000302};
KW   Chloroplast {ECO:0000256|RuleBase:RU000302,
KW   ECO:0000313|EMBL:ADV39129.1};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01338,
KW   ECO:0000256|RuleBase:RU000302};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01338,
KW   ECO:0000256|RuleBase:RU000302};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01338,
KW   ECO:0000256|RuleBase:RU000302};
KW   Methylation {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Monooxygenase {ECO:0000256|HAMAP-Rule:MF_01338,
KW   ECO:0000256|RuleBase:RU000302};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01338,
KW   ECO:0000256|RuleBase:RU000302};
KW   Photorespiration {ECO:0000256|HAMAP-Rule:MF_01338,
KW   ECO:0000256|RuleBase:RU000302};
KW   Photosynthesis {ECO:0000256|HAMAP-Rule:MF_01338,
KW   ECO:0000256|RuleBase:RU000302};
KW   Plastid {ECO:0000313|EMBL:ADV39129.1}.
FT   DOMAIN       24    144       RuBisCO_large_N. {ECO:0000259|Pfam:
FT                                PF02788}.
FT   DOMAIN      154    462       RuBisCO_large. {ECO:0000259|Pfam:
FT                                PF00016}.
FT   ACT_SITE    175    175       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   ACT_SITE    294    294       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   METAL       201    201       Magnesium; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   METAL       203    203       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   METAL       204    204       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     123    123       Substrate; in homodimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   BINDING     173    173       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     177    177       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     295    295       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     327    327       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     379    379       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   SITE        334    334       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   MOD_RES      14     14       N6,N6,N6-trimethyllysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   MOD_RES     201    201       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01338}.
FT   DISULFID    247    247       Interchain; in linked form.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
SQ   SEQUENCE   479 AA;  53117 MW;  4A5D056985F77E83 CRC64;
     MSPQTETKAS VGFKAGVKEY KLTYYTPQYE VKDTDILAAF RVTPQPGVPP EEAGAAVAAE
     SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV PGEEDQYICY VAYPLDLFEE GSVTNMFTSI
     VGNVFGFKAL RALRLEDLRI PTAYVKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
     SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIYKSQA ETGEIKGHYL
     NATAGTCEEM IKRAVCAREL GVPIVMHDYL TGGFTANTSL ARYCRDNGLL LHIHRAMHAV
     IDRQKNHGMH FRVLAKALRM SGGDHIHAGT VVGKLEGERD ITLGFVDLLR DDFIEKDRSR
     GIYFTQDWVS MPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
     RVALEACVQA RNEGRDLARE GNEIIREASK WSPELAAACE VWKAIKFEFD AVDKLDKPA
//
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