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Database: UniProt/SWISS-PROT
Entry: RBL_PYRHO
LinkDB: RBL_PYRHO
Original site: RBL_PYRHO 
ID   RBL_PYRHO               Reviewed;         430 AA.
AC   O58677;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   05-DEC-2018, entry version 125.
DE   RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000255|HAMAP-Rule:MF_01133};
DE            Short=RuBisCO {ECO:0000255|HAMAP-Rule:MF_01133};
DE            EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01133};
GN   Name=rbcL {ECO:0000255|HAMAP-Rule:MF_01133}; OrderedLocusNames=PH0939;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 /
OS   NBRC 100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y.,
RA   Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y.,
RA   Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K.,
RA   Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RG   RIKEN structural genomics initiative (RSGI);
RT   "Crystal structure of octameric ribulose-1,5-bisphosphate
RT   carboxylase/oxygenase (Rubisco) from Pyrococcus horikoshii OT3 (form-1
RT   crystal).";
RL   Submitted (JUN-2005) to the PDB data bank.
CC   -!- FUNCTION: Catalyzes the addition of molecular CO(2) and H(2)O to
CC       ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3-
CC       phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation
CC       pathway, together with AMP phosphorylase and R15P isomerase.
CC       {ECO:0000255|HAMAP-Rule:MF_01133}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 3-phospho-D-glycerate + 2 H(+) = CO2 + D-ribulose 1,5-
CC         bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870,
CC         ChEBI:CHEBI:58272; EC=4.1.1.39; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01133};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose 1,5-bisphosphate + O2 = 2-phosphoglycolate +
CC         3-phospho-D-glycerate + 2 H(+); Xref=Rhea:RHEA:36631,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57870,
CC         ChEBI:CHEBI:58033, ChEBI:CHEBI:58272;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01133};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01133};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01133};
CC   -!- SUBUNIT: Homodimer or homodecamer. In contrast to form I RuBisCO,
CC       the form III RuBisCO is composed solely of large subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_01133}.
CC   -!- MISCELLANEOUS: Because the Archaea possessing a type III RuBisCO
CC       are all anaerobic, it is most likely that only the carboxylase
CC       activity of RuBisCO, and not the competitive oxygenase activity
CC       (by which RuBP reacts with O(2) to form one molecule of 3-
CC       phosphoglycerate and one molecule of 2-phosphoglycolate), is
CC       biologically relevant in these strains. {ECO:0000255|HAMAP-
CC       Rule:MF_01133}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type III
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01133}.
DR   EMBL; BA000001; BAA30036.1; -; Genomic_DNA.
DR   PIR; F71084; F71084.
DR   PDB; 2CWX; X-ray; 2.00 A; A/E=1-430.
DR   PDB; 2CXE; X-ray; 3.00 A; A/B/C/D=1-430.
DR   PDB; 2D69; X-ray; 1.90 A; A/B/D/E=1-430.
DR   PDBsum; 2CWX; -.
DR   PDBsum; 2CXE; -.
DR   PDBsum; 2D69; -.
DR   ProteinModelPortal; O58677; -.
DR   SMR; O58677; -.
DR   STRING; 70601.PH0939; -.
DR   EnsemblBacteria; BAA30036; BAA30036; BAA30036.
DR   KEGG; pho:PH0939; -.
DR   eggNOG; arCOG04443; Archaea.
DR   eggNOG; COG1850; LUCA.
DR   HOGENOM; HOG000230831; -.
DR   KO; K01601; -.
DR   OMA; FTQDWAS; -.
DR   OrthoDB; POG093Z02MJ; -.
DR   BRENDA; 4.1.1.39; 5244.
DR   EvolutionaryTrace; O58677; -.
DR   Proteomes; UP000000752; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006196; P:AMP catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   CDD; cd08213; RuBisCO_large_III; 1.
DR   Gene3D; 3.20.20.110; -; 1.
DR   Gene3D; 3.30.70.150; -; 1.
DR   HAMAP; MF_01133; RuBisCO_L_type3; 1.
DR   InterPro; IPR033966; RuBisCO.
DR   InterPro; IPR017712; RuBisCO_III.
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   PANTHER; PTHR42704; PTHR42704; 1.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SFLD; SFLDS00014; RuBisCO; 2.
DR   SUPFAM; SSF51649; SSF51649; 1.
DR   SUPFAM; SSF54966; SSF54966; 1.
DR   TIGRFAMs; TIGR03326; rubisco_III; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbon dioxide fixation; Complete proteome; Lyase;
KW   Magnesium; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN         1    430       Ribulose bisphosphate carboxylase.
FT                                /FTId=PRO_0000062677.
FT   REGION      348    350       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   REGION      370    373       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   ACT_SITE    160    160       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   ACT_SITE    278    278       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   METAL       186    186       Magnesium; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01133}.
FT   METAL       188    188       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   METAL       189    189       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   BINDING     162    162       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   BINDING     279    279       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   BINDING     311    311       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   SITE        318    318       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01133}.
FT   MOD_RES     186    186       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   STRAND        7      9       {ECO:0000244|PDB:2D69}.
FT   HELIX        11     14       {ECO:0000244|PDB:2D69}.
FT   STRAND       25     37       {ECO:0000244|PDB:2D69}.
FT   HELIX        39     49       {ECO:0000244|PDB:2D69}.
FT   TURN         50     52       {ECO:0000244|PDB:2D69}.
FT   STRAND       55     59       {ECO:0000244|PDB:2D69}.
FT   HELIX        63     65       {ECO:0000244|PDB:2CXE}.
FT   HELIX        66     68       {ECO:0000244|PDB:2D69}.
FT   STRAND       71     78       {ECO:0000244|PDB:2D69}.
FT   STRAND       81     88       {ECO:0000244|PDB:2D69}.
FT   HELIX        90     92       {ECO:0000244|PDB:2D69}.
FT   HELIX        98    105       {ECO:0000244|PDB:2D69}.
FT   HELIX       108    111       {ECO:0000244|PDB:2D69}.
FT   STRAND      115    124       {ECO:0000244|PDB:2D69}.
FT   HELIX       127    130       {ECO:0000244|PDB:2D69}.
FT   HELIX       139    147       {ECO:0000244|PDB:2D69}.
FT   STRAND      150    152       {ECO:0000244|PDB:2CXE}.
FT   STRAND      154    157       {ECO:0000244|PDB:2D69}.
FT   STRAND      160    163       {ECO:0000244|PDB:2D69}.
FT   HELIX       167    179       {ECO:0000244|PDB:2D69}.
FT   STRAND      183    186       {ECO:0000244|PDB:2D69}.
FT   HELIX       199    217       {ECO:0000244|PDB:2D69}.
FT   STRAND      222    224       {ECO:0000244|PDB:2D69}.
FT   HELIX       231    243       {ECO:0000244|PDB:2D69}.
FT   STRAND      248    252       {ECO:0000244|PDB:2D69}.
FT   HELIX       253    256       {ECO:0000244|PDB:2D69}.
FT   HELIX       258    271       {ECO:0000244|PDB:2D69}.
FT   STRAND      274    278       {ECO:0000244|PDB:2D69}.
FT   TURN        280    282       {ECO:0000244|PDB:2D69}.
FT   HELIX       283    286       {ECO:0000244|PDB:2D69}.
FT   STRAND      291    293       {ECO:0000244|PDB:2D69}.
FT   HELIX       295    305       {ECO:0000244|PDB:2D69}.
FT   STRAND      308    311       {ECO:0000244|PDB:2D69}.
FT   STRAND      317    319       {ECO:0000244|PDB:2D69}.
FT   HELIX       323    334       {ECO:0000244|PDB:2D69}.
FT   STRAND      344    350       {ECO:0000244|PDB:2D69}.
FT   HELIX       353    355       {ECO:0000244|PDB:2D69}.
FT   HELIX       356    363       {ECO:0000244|PDB:2D69}.
FT   STRAND      368    370       {ECO:0000244|PDB:2D69}.
FT   HELIX       372    376       {ECO:0000244|PDB:2D69}.
FT   HELIX       382    398       {ECO:0000244|PDB:2D69}.
FT   HELIX       402    405       {ECO:0000244|PDB:2D69}.
FT   TURN        406    408       {ECO:0000244|PDB:2CXE}.
FT   HELIX       410    422       {ECO:0000244|PDB:2D69}.
SQ   SEQUENCE   430 AA;  48247 MW;  1068CA138F019AD9 CRC64;
     MMVLRMKVEW YLDFVDLNYE PGRDELIVEY YFEPNGVSPE EAAGRIASES SIGTWTTLWK
     LPEMAKRSMA KVFYLEKHGE GYIAKIAYPL TLFEEGSLVQ LFSAVAGNVF GMKALKNLRL
     LDFHPPYEYL RHFKGPQFGV QGIREFMGVK DRPLTATVPK PKMGWSVEEY AEIAYELWSG
     GIDLLKDDEN FTSFPFNRFE ERVRKLYRVR DRVEAETGET KEYLINITGP VNIMEKRAEM
     VANEGGQYVM IDIVVAGWSA LQYMREVTED LGLAIHAHRA MHAAFTRNPR HGITMLALAK
     AARMIGVDQI HTGTAVGKMA GNYEEIKRIN DFLLSKWEHI RPVFPVASGG LHPGLMPELI
     RLFGKDLVIQ AGGGVMGHPD GPRAGAKALR DAIDAAIEGV DLDEKAKSSP ELKKSLREVG
     LSKAKVGVQH
//
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