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Database: UniProt/SWISS-PROT
Entry: RBL_SYNP6
LinkDB: RBL_SYNP6
Original site: RBL_SYNP6 
ID   RBL_SYNP6               Reviewed;         472 AA.
AC   P00880;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   10-OCT-2018, entry version 145.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain;
DE            Short=RuBisCO large subunit;
DE            EC=4.1.1.39 {ECO:0000269|PubMed:7922027, ECO:0000269|PubMed:9882445};
GN   Name=cbbL; Synonyms=rbcA, rbcL; OrderedLocusNames=syc0130_c;
OS   Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
OS   (Anacystis nidulans).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=269084;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6307620; DOI=10.1089/dna.1983.2.121;
RA   Reichelt B.Y., Delaney S.F.;
RT   "The nucleotide sequence for the large subunit of ribulose 1,5-
RT   bisphosphate carboxylase from a unicellular cyanobacterium,
RT   Synechococcus PCC6301.";
RL   DNA 2:121-129(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CARBAMYLATION AT LYS-198.
RX   PubMed=16593333; DOI=10.1073/pnas.80.13.4050;
RA   Shinozaki K., Yamada C., Takahata N., Sugiura M.;
RT   "Molecular cloning and sequence analysis of the cyanobacterial gene
RT   for the large subunit of ribulose-1,5-bisphosphate
RT   carboxylase/oxygenase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:4050-4054(1983).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Shinozaki K., Sugiura M.;
RT   "Genes for the large and small subunits of ribulose-1,5-bisphosphate
RT   carboxylase/oxygenase constitute a single operon in a cyanobacterium
RT   Anacystis nidulans 6301.";
RL   Mol. Gen. Genet. 200:27-32(1985).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX   PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA   Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA   Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT   "Complete nucleotide sequence of the freshwater unicellular
RT   cyanobacterium Synechococcus elongatus PCC 6301 chromosome: gene
RT   content and organization.";
RL   Photosyn. Res. 93:55-67(2007).
RN   [5]
RP   PROTEIN SEQUENCE OF 333-342.
RX   PubMed=8031129; DOI=10.1006/abbi.1994.1301;
RA   Read B.A., Tabita F.R.;
RT   "High substrate specificity factor ribulose bisphosphate
RT   carboxylase/oxygenase from eukaryotic marine algae and properties of
RT   recombinant cyanobacterial RubiSCO containing 'algal' residue
RT   modifications.";
RL   Arch. Biochem. Biophys. 312:210-218(1994).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=9882445; DOI=10.1006/abbi.1998.0979;
RA   Horken K.M., Tabita F.R.;
RT   "Closely related form I ribulose bisphosphate carboxylase/oxygenase
RT   molecules that possess different CO2/O2 substrate specificities.";
RL   Arch. Biochem. Biophys. 361:183-194(1999).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 6-472 OF ACTIVATED HOLOENZYME
RP   IN COMPLEX WITH TRANSITION-STATE ANALOG 2-CABP AND MAGNESIUM, SUBUNIT,
RP   AND DISULFIDE BOND.
RX   PubMed=8245022;
RA   Newman J., Gutteridge S.;
RT   "The X-ray structure of Synechococcus ribulose-bisphosphate
RT   carboxylase/oxygenase-activated quaternary complex at 2.2-A
RT   resolution.";
RL   J. Biol. Chem. 268:25876-25886(1993).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF INACTIVATED HOLOENZYME IN
RP   COMPLEX WITH PRODUCT ANALOG, FUNCTION, CATALYTIC ACTIVITY, AND
RP   SUBUNIT.
RX   PubMed=7922027; DOI=10.1016/S0969-2126(00)00050-2;
RA   Newman J., Gutteridge S.;
RT   "Structure of an effector-induced inactivated state of ribulose 1,5-
RT   bisphosphate carboxylase/oxygenase: the binary complex between enzyme
RT   and xylulose 1,5-bisphosphate.";
RL   Structure 2:495-502(1994).
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:0000269|PubMed:7922027, ECO:0000269|PubMed:9882445}.
CC   -!- CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose
CC       1,5-bisphosphate + CO(2) + H(2)O. {ECO:0000269|PubMed:7922027,
CC       ECO:0000269|PubMed:9882445}.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
CC       D-ribulose 1,5-bisphosphate + O(2). {ECO:0000269|PubMed:9882445}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:8245022};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:8245022};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=39 uM for ribulose 1,5-bisphosphate
CC         {ECO:0000269|PubMed:9882445};
CC         KM=173 uM for CO(2) {ECO:0000269|PubMed:9882445};
CC         Vmax=2.5 umol/min/mg enzyme with CO(2) as substrate
CC         {ECO:0000269|PubMed:9882445};
CC         Note=The CO(2)/O(2) specificity factor (tau) is 39.;
CC   -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains
CC       (PubMed:9882445, PubMed:7922027); disulfide-linked
CC       (PubMed:8245022). The disulfide link is formed within the large
CC       subunit homodimers (PubMed:8245022). {ECO:0000269|PubMed:7922027,
CC       ECO:0000269|PubMed:8245022, ECO:0000305|PubMed:9882445}.
CC   -!- INTERACTION:
CC       A0A0H3K9R3:rbcX; NbExp=3; IntAct=EBI-9023246, EBI-15936812;
CC       Q44212:rbcX (xeno); NbExp=3; IntAct=EBI-9023246, EBI-9023244;
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.
CC       {ECO:0000305|PubMed:8245022}.
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:0000269|PubMed:8245022}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000305}.
DR   EMBL; K00486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X03220; CAA26972.1; -; Genomic_DNA.
DR   EMBL; AP008231; BAD78320.1; -; Genomic_DNA.
DR   PIR; A90941; RKYCL.
DR   RefSeq; WP_011242444.1; NC_006576.1.
DR   PDB; 1RBL; X-ray; 2.20 A; A/B/C/D/E/F/G/H=6-472.
DR   PDB; 1RSC; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-472.
DR   PDB; 2WVW; EM; 9.00 A; A/B/C/D/E/F/G/H=1-472.
DR   PDB; 3RG6; X-ray; 3.20 A; A/B=1-472.
DR   PDBsum; 1RBL; -.
DR   PDBsum; 1RSC; -.
DR   PDBsum; 2WVW; -.
DR   PDBsum; 3RG6; -.
DR   ProteinModelPortal; P00880; -.
DR   SMR; P00880; -.
DR   DIP; DIP-6210N; -.
DR   IntAct; P00880; 2.
DR   STRING; 269084.syc0130_c; -.
DR   EnsemblBacteria; BAD78320; BAD78320; syc0130_c.
DR   KEGG; syc:syc0130_c; -.
DR   eggNOG; ENOG4105DT1; Bacteria.
DR   eggNOG; COG1850; LUCA.
DR   HOGENOM; HOG000230831; -.
DR   KO; K01601; -.
DR   OMA; HRAMHAA; -.
DR   OrthoDB; POG091H14UZ; -.
DR   SABIO-RK; P00880; -.
DR   EvolutionaryTrace; P00880; -.
DR   Proteomes; UP000001175; Chromosome.
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   1: Evidence at protein level;
KW   3D-structure; Calvin cycle; Carbon dioxide fixation;
KW   Complete proteome; Direct protein sequencing; Disulfide bond; Lyase;
KW   Magnesium; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Photorespiration; Photosynthesis.
FT   CHAIN         1    472       Ribulose bisphosphate carboxylase large
FT                                chain.
FT                                /FTId=PRO_0000062651.
FT   ACT_SITE    172    172       Proton acceptor.
FT   ACT_SITE    291    291       Proton acceptor.
FT   METAL       198    198       Magnesium; via carbamate group.
FT                                {ECO:0000269|PubMed:8245022}.
FT   METAL       200    200       Magnesium. {ECO:0000269|PubMed:8245022}.
FT   METAL       201    201       Magnesium. {ECO:0000269|PubMed:8245022}.
FT   BINDING     120    120       Substrate; in homodimeric partner.
FT   BINDING     170    170       Substrate.
FT   BINDING     174    174       Substrate.
FT   BINDING     292    292       Substrate.
FT   BINDING     324    324       Substrate.
FT   BINDING     376    376       Substrate.
FT   SITE        331    331       Transition state stabilizer.
FT   MOD_RES     198    198       N6-carboxylysine.
FT                                {ECO:0000269|PubMed:16593333}.
FT   DISULFID    244    244       Interchain; in linked form.
FT                                {ECO:0000269|PubMed:8245022}.
FT   CONFLICT     38     39       RF -> PV (in Ref. 1; K00486).
FT                                {ECO:0000305}.
FT   CONFLICT    353    353       A -> R (in Ref. 1; K00486).
FT                                {ECO:0000305}.
FT   HELIX        18     21       {ECO:0000244|PDB:1RBL}.
FT   STRAND       32     41       {ECO:0000244|PDB:1RBL}.
FT   HELIX        47     57       {ECO:0000244|PDB:1RBL}.
FT   TURN         58     60       {ECO:0000244|PDB:1RBL}.
FT   STRAND       63     65       {ECO:0000244|PDB:1RBL}.
FT   HELIX        67     71       {ECO:0000244|PDB:1RBL}.
FT   HELIX        74     77       {ECO:0000244|PDB:1RBL}.
FT   STRAND       80     86       {ECO:0000244|PDB:1RBL}.
FT   STRAND       94    100       {ECO:0000244|PDB:1RBL}.
FT   HELIX       102    104       {ECO:0000244|PDB:1RBL}.
FT   HELIX       110    118       {ECO:0000244|PDB:1RBL}.
FT   HELIX       121    123       {ECO:0000244|PDB:1RBL}.
FT   STRAND      127    136       {ECO:0000244|PDB:1RBL}.
FT   HELIX       139    142       {ECO:0000244|PDB:1RBL}.
FT   HELIX       152    159       {ECO:0000244|PDB:1RBL}.
FT   STRAND      166    168       {ECO:0000244|PDB:1RBL}.
FT   STRAND      172    175       {ECO:0000244|PDB:1RBL}.
FT   HELIX       179    191       {ECO:0000244|PDB:1RBL}.
FT   STRAND      195    198       {ECO:0000244|PDB:1RBL}.
FT   STRAND      204    206       {ECO:0000244|PDB:1RBL}.
FT   HELIX       211    229       {ECO:0000244|PDB:1RBL}.
FT   STRAND      234    238       {ECO:0000244|PDB:1RBL}.
FT   HELIX       244    256       {ECO:0000244|PDB:1RBL}.
FT   STRAND      260    265       {ECO:0000244|PDB:1RBL}.
FT   HELIX       266    269       {ECO:0000244|PDB:1RBL}.
FT   HELIX       271    284       {ECO:0000244|PDB:1RBL}.
FT   STRAND      287    291       {ECO:0000244|PDB:1RBL}.
FT   HELIX       295    299       {ECO:0000244|PDB:1RBL}.
FT   STRAND      302    306       {ECO:0000244|PDB:1RBL}.
FT   HELIX       308    318       {ECO:0000244|PDB:1RBL}.
FT   STRAND      321    324       {ECO:0000244|PDB:1RBL}.
FT   STRAND      328    332       {ECO:0000244|PDB:1RBL}.
FT   HELIX       336    347       {ECO:0000244|PDB:1RBL}.
FT   STRAND      349    351       {ECO:0000244|PDB:1RBL}.
FT   HELIX       355    357       {ECO:0000244|PDB:1RBL}.
FT   STRAND      372    378       {ECO:0000244|PDB:1RBL}.
FT   HELIX       381    383       {ECO:0000244|PDB:1RBL}.
FT   HELIX       384    391       {ECO:0000244|PDB:1RBL}.
FT   STRAND      396    398       {ECO:0000244|PDB:1RBL}.
FT   HELIX       401    404       {ECO:0000244|PDB:1RBL}.
FT   HELIX       410    430       {ECO:0000244|PDB:1RBL}.
FT   HELIX       434    448       {ECO:0000244|PDB:1RBL}.
FT   HELIX       450    459       {ECO:0000244|PDB:1RBL}.
SQ   SEQUENCE   472 AA;  52448 MW;  CDD8519AA9D493C9 CRC64;
     MPKTQSAAGY KAGVKDYKLT YYTPDYTPKD TDLLAAFRFS PQPGVPADEA GAAIAAESST
     GTWTTVWTDL LTDMDRYKGK CYHIEPVQGE ENSYFAFIAY PLDLFEEGSV TNILTSIVGN
     VFGFKAIRSL RLEDIRFPVA LVKTFQGPPH GIQVERDLLN KYGRPMLGCT IKPKLGLSAK
     NYGRAVYECL RGGLDFTKDD ENINSQPFQR WRDRFLFVAD AIHKSQAETG EIKGHYLNVT
     APTCEEMMKR AEFAKELGMP IIMHDFLTAG FTANTTLAKW CRDNGVLLHI HRAMHAVIDR
     QRNHGIHFRV LAKCLRLSGG DHLHSGTVVG KLEGDKASTL GFVDLMREDH IEADRSRGVF
     FTQDWASMPG VLPVASGGIH VWHMPALVEI FGDDSVLQFG GGTLGHPWGN APGATANRVA
     LEACVQARNE GRDLYREGGD ILREAGKWSP ELAAALDLWK EIKFEFETMD KL
//
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