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Database: UniProt/SWISS-PROT
Entry: RBL_METAC
LinkDB: RBL_METAC
Original site: RBL_METAC 
ID   RBL_METAC               Reviewed;         428 AA.
AC   Q8THG2;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   28-FEB-2018, entry version 107.
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=MA_4555;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P.,
RA   FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A.,
RA   Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R.,
RA   Linton L., McEwan P., McKernan K., Talamas J., Tirrell A., Ye W.,
RA   Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M.,
RA   Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A.,
RA   Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K.,
RA   Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C.,
RA   Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T.,
RA   Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E.,
RA   Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic
RT   and physiological diversity.";
RL   Genome Res. 12:532-542(2002).
RN   [2]
RP   CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   AND SUBUNIT.
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
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   -!- ENZYME REGULATION: Reversibly inhibited by O(2).
CC       {ECO:0000269|PubMed:12730164}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Active from 25 to 40 degrees Celsius.
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; AE010299; AAM07894.1; -; Genomic_DNA.
DR   RefSeq; WP_011024428.1; NC_003552.1.
DR   ProteinModelPortal; Q8THG2; -.
DR   SMR; Q8THG2; -.
DR   STRING; 188937.MA4555; -.
DR   PRIDE; Q8THG2; -.
DR   EnsemblBacteria; AAM07894; AAM07894; MA_4555.
DR   GeneID; 1476449; -.
DR   KEGG; mac:MA_4555; -.
DR   eggNOG; arCOG04443; Archaea.
DR   eggNOG; COG1850; LUCA.
DR   InParanoid; Q8THG2; -.
DR   KO; K01601; -.
DR   OMA; HRAMHAA; -.
DR   OrthoDB; POG093Z02MJ; -.
DR   PhylomeDB; Q8THG2; -.
DR   BioCyc; MACE188937:G1FZT-4847-MONOMER; -.
DR   BRENDA; 4.1.1.39; 7224.
DR   Proteomes; UP000002487; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC.
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   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    428       Ribulose bisphosphate carboxylase.
FT                                /FTId=PRO_0000062672.
FT   REGION      354    356       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   REGION      376    379       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   ACT_SITE    151    151       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   ACT_SITE    270    270       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   METAL       177    177       Magnesium; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01133}.
FT   METAL       179    179       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   METAL       180    180       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   BINDING     153    153       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   BINDING     271    271       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   BINDING     303    303       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
FT   SITE        310    310       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01133}.
FT   MOD_RES     177    177       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01133}.
SQ   SEQUENCE   428 AA;  46787 MW;  B03BFCBD9E8AFED5 CRC64;
     MRRDYVDPGY SPKDTDLICE FHIEPAAGIS FEEASTHMAG ESSIDSWTEI STLSPELAAR
     LKPHVFYLDA DTQTVRVAYS EDLFELGSVP QVLSAVAGNI FSMKIVDNLR LQDITFPKSM
     LREFEGPNFG LPGVRDIVGV KDRPLVGTIV KPKVGLTSEM HAEVAYNAFA GGCDLVKDDE
     NLTDQKFNGF EKRAELTLKI AEKAEAETGE RKMYLCNITA PTCEEMIRRL HVLKDLGASY
     AMIDIVPTGW TALQTLREAA ADEGLALHAH RCMHSAFTRN PRHGVSMLLV AKLCRLIGLD
     QLHIGTVVGK MHGDKDEVLS IRDECVLDTV PADPEQHVLA QDWGGLKPMF PVASGGLAPT
     MIPDLYSIFG KEVIMQFGGG IHAHPMGTAA GAAACRQALE ASLEGISLQD YAKDHKELEA
     ALGKWLEK
//
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