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Database: UniProt/SWISS-PROT
Entry: RBL_ARCFU
LinkDB: RBL_ARCFU
Original site: RBL_ARCFU 
ID   RBL_ARCFU               Reviewed;         441 AA.
AC   O28635;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   10-OCT-2018, entry version 118.
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};
GN   OrderedLocusNames=AF_1638;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM
OS   9628 / NBRC 100126).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
OC   Archaeoglobaceae; Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E.,
RA   Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D.,
RA   Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C.,
RA   Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R.,
RA   Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J.,
RA   Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A.,
RA   Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A.,
RA   Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P.,
RA   Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C.,
RA   Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O.,
RA   Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-
RT   reducing archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
RN   [2]
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RC   STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
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:12730164}.
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:12730164}.
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:12730164}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Active over a broad temperature range.
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: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; AE000782; AAB89603.1; -; Genomic_DNA.
DR   PIR; E69454; E69454.
DR   RefSeq; WP_010879134.1; NC_000917.1.
DR   ProteinModelPortal; O28635; -.
DR   SMR; O28635; -.
DR   STRING; 224325.AF1638; -.
DR   EnsemblBacteria; AAB89603; AAB89603; AF_1638.
DR   GeneID; 24795382; -.
DR   KEGG; afu:AF_1638; -.
DR   eggNOG; arCOG04443; Archaea.
DR   eggNOG; COG1850; LUCA.
DR   KO; K01601; -.
DR   OMA; HRAMHAA; -.
DR   OrthoDB; POG093Z02MJ; -.
DR   BRENDA; 4.1.1.39; 414.
DR   Proteomes; UP000002199; 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    441       Ribulose bisphosphate carboxylase.
FT                                /FTId=PRO_0000062671.
FT   REGION      364    366       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   REGION      386    389       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        319    319       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01133}.
FT   MOD_RES     186    186       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
SQ   SEQUENCE   441 AA;  48557 MW;  F191B4A83F36F3FD CRC64;
     MAEFEIYREY VDKSYEPQKD DIVAVFRITP AEGFTIEDAA GAVAAESSTG TWTSLHPWYD
     EERVKGLSAK AYDFVDLGDG SSIVRIAYPS ELFEPHNMPG LLASIAGNVF GMKRVKGLRL
     EDLQLPKSFL KDFKGPSKGK EGVKKIFGVA DRPIVGTVPK PKVGYSAEEV EKLAYELLSG
     GMDYIKDDEN LTSPAYCRFE ERAERIMKVI EKVEAETGEK KSWFANITAD VREMERRLKL
     VAELGNPHVM VDVVITGWGA LEYIRDLAED YDLAIHGHRA MHAAFTRNAK HGISMFVLAK
     LYRIIGIDQL HIGTAGAGKL EGQKWDTVQN ARIFSEVEYT PDEGDAFHLS QNFHHIKPAM
     PVSSGGLHPG NLEPVIDALG KEIVIQVGGG VLGHPMGAKA GAKAVRQALD AIISAIPLEE
     HAKQHPELQA ALEKWGRVTP I
//
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