GenomeNet

Database: UniProt/SWISS-PROT
Entry: RBL_METJA
LinkDB: RBL_METJA
Original site: RBL_METJA 
ID   RBL_METJA               Reviewed;         425 AA.
AC   Q58632;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 2.
DT   10-OCT-2018, entry version 119.
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=MJ1235;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 /
OS   JCM 10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci;
OC   Methanococcales; Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D.,
RA   Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D.,
RA   Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I.,
RA   Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A.,
RA   Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D.,
RA   Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C.,
RA   Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M.,
RA   Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBUNIT.
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=10049390;
RA   Watson G.M.F., Yu J.-P., Tabita F.R.;
RT   "Unusual ribulose 1,5-bisphosphate carboxylase/oxygenase of anoxic
RT   Archaea.";
RL   J. Bacteriol. 181:1569-1575(1999).
RN   [3]
RP   ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=12730164; DOI=10.1128/JB.185.10.3049-3059.2003;
RA   Finn M.W., Tabita F.R.;
RT   "Synthesis of catalytically active form III ribulose 1,5-bisphosphate
RT   carboxylase/oxygenase in archaea.";
RL   J. Bacteriol. 185:3049-3059(2003).
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: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose
CC       1,5-bisphosphate + CO(2) + H(2)O. {ECO:0000255|HAMAP-
CC       Rule:MF_01133, ECO:0000269|PubMed:10049390}.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
CC       D-ribulose 1,5-bisphosphate + O(2). {ECO:0000255|HAMAP-
CC       Rule:MF_01133, ECO:0000269|PubMed:10049390}.
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   -!- ACTIVITY REGULATION: Reversibly inhibited by O(2).
CC       {ECO:0000269|PubMed:10049390, ECO:0000269|PubMed:12730164}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 65 degrees Celsius. Highly thermostable.
CC         {ECO:0000269|PubMed:12730164};
CC   -!- SUBUNIT: Homodimer. In contrast to form I RuBisCO, the form III
CC       RuBisCO is composed solely of large subunits.
CC       {ECO:0000269|PubMed:10049390, ECO:0000269|PubMed:12730164}.
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; L77117; AAB99239.1; -; Genomic_DNA.
DR   RefSeq; WP_010870747.1; NC_000909.1.
DR   ProteinModelPortal; Q58632; -.
DR   SMR; Q58632; -.
DR   STRING; 243232.MJ_1235; -.
DR   EnsemblBacteria; AAB99239; AAB99239; MJ_1235.
DR   GeneID; 1452131; -.
DR   KEGG; mja:MJ_1235; -.
DR   eggNOG; arCOG04443; Archaea.
DR   eggNOG; COG1850; LUCA.
DR   InParanoid; Q58632; -.
DR   KO; K01601; -.
DR   OMA; HRAMHAA; -.
DR   OrthoDB; POG093Z02MJ; -.
DR   PhylomeDB; Q58632; -.
DR   BioCyc; MJAN243232:G1GKE-1340-MONOMER; -.
DR   BRENDA; 4.1.1.39; 3260.
DR   Proteomes; UP000000805; 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; 1.
DR   SUPFAM; SSF51649; SSF51649; 1.
DR   SUPFAM; SSF54966; SSF54966; 1.
DR   TIGRFAMs; TIGR03326; rubisco_III; 1.
PE   1: Evidence at protein level;
KW   Carbon dioxide fixation; Complete proteome; Lyase; Magnesium;
KW   Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN         1    425       Ribulose bisphosphate carboxylase.
FT                                /FTId=PRO_0000062673.
FT   REGION      353    355       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   REGION      375    378       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   ACT_SITE    153    153       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   ACT_SITE    269    269       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   METAL       179    179       Magnesium; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01133}.
FT   METAL       181    181       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   METAL       182    182       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   BINDING     155    155       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   BINDING     270    270       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   BINDING     302    302       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   SITE        309    309       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01133}.
FT   MOD_RES     179    179       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
SQ   SEQUENCE   425 AA;  47859 MW;  C6F9F1653BA76039 CRC64;
     MDYINLNYRP NEGDLLSCMV IKGENLEKLA NEIAGESSIG TWTKVQTMKS DIYEKLRPKV
     YEIKEIGEEN GYKVGLIKIA YPLYDFEINN MPGVLAGIAG NIFGMKIAKG LRILDFRFPA
     EFVKAYKGPR FGIEGVRETL KIKERPLLGT IVKPKVGLKT EEHAKVAYEA WVGGVDLVKD
     DENLTSQEFN KFEDRIYKTL EMRDKAEEET GERKAYMPNI TAPYREMIRR AEIAEDAGSE
     YVMIDVVVCG FSAVQSFREE DFKFIIHAHR AMHAAMTRSR DFGISMLALA KIYRLLGVDQ
     LHIGTVVGKM EGGEKEVKAI RDEIVYDKVE ADNENKFFNQ DWFDIKPVFP VSSGGVHPRL
     VPKIVEILGR DLIIQAGGGV HGHPDGTRAG AKAMRAAIEA IIEGKSLEEK AEEVAELKKA
     LEYWK
//
DBGET integrated database retrieval system