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Database: UniProt/SWISS-PROT
Entry: RBL_NOSS1
LinkDB: RBL_NOSS1
Original site: RBL_NOSS1 
ID   RBL_NOSS1               Reviewed;         476 AA.
AC   P00879; Q60124;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 3.
DT   25-OCT-2017, entry version 127.
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};
GN   Name=cbbL {ECO:0000255|HAMAP-Rule:MF_01338};
GN   Synonyms=rbc, rbcA, rbcL {ECO:0000255|HAMAP-Rule:MF_01338};
GN   OrderedLocusNames=alr1524;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16593300; DOI=10.1073/pnas.80.7.1835;
RA   Curtis S.E., Haselkorn R.;
RT   "Isolation and sequence of the gene for the large subunit of ribulose-
RT   1,5-bisphosphate carboxylase from the cyanobacterium Anabaena 7120.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:1835-1839(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RX   PubMed=6091125; DOI=10.1073/pnas.81.19.5961;
RA   Nierzwicki-Bauer S.A., Curtis S.E., Haselkorn R.;
RT   "Cotranscription of genes encoding the small and large subunits of
RT   ribulose-1,5-bisphosphate carboxylase in the cyanobacterium Anabaena
RT   7120.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:5961-5965(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T.,
RA   Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M.,
RA   Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
RN   [4]
RP   PROTEIN SEQUENCE OF 16-22, AND MASS SPECTROMETRY.
RA   Singh H., Rajaram H., Apte S.K.;
RL   Submitted (DEC-2008) to UniProtKB.
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   -!- 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   -!- MASS SPECTROMETRY: Mass=53411; Method=MALDI; Range=1-476;
CC       Evidence={ECO:0000269|Ref.4};
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; J01540; AAA22041.1; -; Genomic_DNA.
DR   EMBL; L02520; AAA22024.1; -; Genomic_DNA.
DR   EMBL; L02521; AAA22027.1; -; Genomic_DNA.
DR   EMBL; L02522; AAA22028.1; -; Genomic_DNA.
DR   EMBL; BA000019; BAB77890.1; -; Genomic_DNA.
DR   PIR; A01099; RKAIL7.
DR   PIR; AF1996; AF1996.
DR   RefSeq; WP_010995693.1; NC_003272.1.
DR   ProteinModelPortal; P00879; -.
DR   SMR; P00879; -.
DR   STRING; 103690.alr1524; -.
DR   PRIDE; P00879; -.
DR   EnsemblBacteria; BAB77890; BAB77890; BAB77890.
DR   KEGG; ana:alr1524; -.
DR   eggNOG; ENOG4105DT1; Bacteria.
DR   eggNOG; COG1850; LUCA.
DR   HOGENOM; HOG000230831; -.
DR   KO; K01601; -.
DR   OMA; HRAMHAA; -.
DR   OrthoDB; POG091H14UZ; -.
DR   Proteomes; UP000002483; Chromosome.
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   1: Evidence at protein level;
KW   Calvin cycle; Carbon dioxide fixation; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; Lyase; Magnesium;
KW   Metal-binding; Monooxygenase; Oxidoreductase; Photorespiration;
KW   Photosynthesis; Reference proteome.
FT   CHAIN         1    476       Ribulose bisphosphate carboxylase large
FT                                chain.
FT                                /FTId=PRO_0000062619.
FT   ACT_SITE    176    176       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   ACT_SITE    295    295       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   METAL       202    202       Magnesium; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   METAL       204    204       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   METAL       205    205       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     124    124       Substrate; in homodimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   BINDING     174    174       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     178    178       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     296    296       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     328    328       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     380    380       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   SITE        335    335       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   MOD_RES     202    202       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   DISULFID    248    248       Interchain; in linked form.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   CONFLICT     91     91       V -> G (in Ref. 1; AAA22041 and 2;
FT                                AAA22024/AAA22027/AAA22028).
FT                                {ECO:0000305}.
FT   CONFLICT     98     98       F -> S (in Ref. 1; AAA22041 and 2;
FT                                AAA22024/AAA22027/AAA22028).
FT                                {ECO:0000305}.
FT   CONFLICT    120    120       S -> Y (in Ref. 1; AAA22041 and 2;
FT                                AAA22024/AAA22027/AAA22028).
FT                                {ECO:0000305}.
FT   CONFLICT    127    127       G -> V (in Ref. 1; AAA22041 and 2;
FT                                AAA22024/AAA22027/AAA22028).
FT                                {ECO:0000305}.
FT   CONFLICT    279    279       T -> N (in Ref. 1; AAA22041 and 2;
FT                                AAA22024/AAA22027/AAA22028).
FT                                {ECO:0000305}.
FT   CONFLICT    290    290       V -> L (in Ref. 1; AAA22041 and 2;
FT                                AAA22024/AAA22027/AAA22028).
FT                                {ECO:0000305}.
FT   CONFLICT    399    399       S -> F (in Ref. 1; AAA22041 and 2;
FT                                AAA22024/AAA22027/AAA22028).
FT                                {ECO:0000305}.
FT   CONFLICT    416    416       P -> R (in Ref. 1; AAA22041 and 2;
FT                                AAA22024/AAA22027/AAA22028).
FT                                {ECO:0000305}.
SQ   SEQUENCE   476 AA;  53045 MW;  ABEDB246FA2E6A01 CRC64;
     MSYAQTKTQT KSGYKAGVQD YRLTYYTPDY TPKDTDILAA FRVTPQPGVP FEEAAAAVAA
     ESSTGTWTTV WTDLLTDLDR YKGRCYDIEP VPGEDNQFIA YIAYPLDLFE EGSITNVLTS
     IVGNVFGFKA LRALRLEDIR FPVAYIKTFQ GPPHGIQVER DKLNKYGRPL LGCTIKPKLG
     LSAKNYGRAV YECLRGGLDF TKDDENINSA PFQRWRDRFL FVADAITKAQ AETGEIKGHY
     LNVTAPTCEE MLKRAEYAKE LKQPIIMHDY LTAGFTANTT LARWCRDNGV LLHIHRAMHA
     VIDRQKNHGI HFRVLAKALR LSGGDHIHTG TVVGKLEGER GITMGFVDLL RENYVEQDKS
     RGIYFTQDWA SLPGVMAVAS GGIHVWHMPA LVEIFGDDSV LQFGGGTLGH PWGNAPGATA
     NRVALEACVQ ARNEGRNLAR EGNDVIREAA KWSPELAVAC ELWKEIKFEF EAMDTV
//
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