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Entry: F8AM17_METOI
LinkDB: F8AM17_METOI
Original site: F8AM17_METOI 
ID   F8AM17_METOI            Unreviewed;       425 AA.
AC   F8AM17;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000256|HAMAP-Rule:MF_01133};
DE            Short=RuBisCO {ECO:0000256|HAMAP-Rule:MF_01133};
DE            EC=4.1.1.39 {ECO:0000256|HAMAP-Rule:MF_01133};
GN   Name=rbcL {ECO:0000256|HAMAP-Rule:MF_01133};
GN   OrderedLocusNames=Metok_0719 {ECO:0000313|EMBL:AEH06696.1};
OS   Methanothermococcus okinawensis (strain DSM 14208 / JCM 11175 / IH1).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanothermococcus.
OX   NCBI_TaxID=647113 {ECO:0000313|EMBL:AEH06696.1, ECO:0000313|Proteomes:UP000009296};
RN   [1] {ECO:0000313|EMBL:AEH06696.1, ECO:0000313|Proteomes:UP000009296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14208 / JCM 11175 / IH1
RC   {ECO:0000313|Proteomes:UP000009296};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Held B., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Sieprawska-Lupa M., Takai K.,
RA   Miyazaki J., Whitman W., Woyke T.;
RT   "Complete sequence of chromosome of Methanothermococcus okinawensis IH1.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEH06696.1, ECO:0000313|Proteomes:UP000009296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14208 / JCM 11175 / IH1
RC   {ECO:0000313|Proteomes:UP000009296};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Held B., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Sieprawska-Lupa M., Takai K.,
RA   Miyazaki J., Whitman W., Woyke T.;
RT   "Complete sequence of chromosome of Methanothermococcus okinawensis IH1.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01133}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (2R)-3-phosphoglycerate + 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:0000256|HAMAP-
CC         Rule:MF_01133};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate +
CC         2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033,
CC         ChEBI:CHEBI:58272; Evidence={ECO:0000256|HAMAP-Rule:MF_01133};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01133};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01133};
CC   -!- SUBUNIT: Homodimer or homodecamer. In contrast to form I RuBisCO, the
CC       form III RuBisCO is composed solely of large subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_01133}.
CC   -!- MISCELLANEOUS: Because the Archaea possessing a type III RuBisCO are
CC       all anaerobic, it is most likely that only the carboxylase activity of
CC       RuBisCO, and not the competitive oxygenase activity (by which RuBP
CC       reacts with O(2) to form one molecule of 3-phosphoglycerate and one
CC       molecule of 2-phosphoglycolate), is biologically relevant in these
CC       strains. {ECO:0000256|HAMAP-Rule:MF_01133}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type III
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01133}.
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DR   EMBL; CP002792; AEH06696.1; -; Genomic_DNA.
DR   RefSeq; WP_013866882.1; NC_015636.1.
DR   AlphaFoldDB; F8AM17; -.
DR   STRING; 647113.Metok_0719; -.
DR   GeneID; 10772860; -.
DR   KEGG; mok:Metok_0719; -.
DR   eggNOG; arCOG04443; Archaea.
DR   HOGENOM; CLU_031450_3_1_2; -.
DR   OMA; IHGHPDG; -.
DR   OrthoDB; 52787at2157; -.
DR   Proteomes; UP000009296; 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   Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 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   NCBIfam; TIGR03326; rubisco_III; 1.
DR   PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR   PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SFLD; SFLDS00014; RuBisCO; 1.
DR   SFLD; SFLDG00301; RuBisCO-like_proteins; 1.
DR   SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR   SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01133};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01133, ECO:0000313|EMBL:AEH06696.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01133};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01133};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01133}.
FT   DOMAIN          2..122
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          132..424
FT                   /note="Ribulose bisphosphate carboxylase large subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00016"
FT   ACT_SITE        153
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   ACT_SITE        269
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   BINDING         179
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   BINDING         181
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   BINDING         182
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   BINDING         270
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   BINDING         302
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   BINDING         353..355
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   BINDING         375..378
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   SITE            309
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   MOD_RES         179
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
SQ   SEQUENCE   425 AA;  47362 MW;  E2A1A4B6BF3F5829 CRC64;
     MDYLELGYEP KDNELLSCMV VKAENLKKAA NDIAGESSIG TWTELKTMKS EIYKKLKPRV
     YEINEMGKEG DTNIGLIKIA YPLDTFEPNN MPGTLAGIAG NIFGMKSLNG LRILDFRFPK
     EFIKCYSGPK YGIKGIRKLL NVMERPLVGT IVKPKVGLNS EEHAKVAYNS WIGGCDIVKD
     DENLVSQDFN KFEGRLHKVL ECRDKAESET GEKKIYMPNI TAPYREMVRR AELVEDAGCE
     YAMIDVVVLG FSAVQQIREE GFNFAIHAHR AMHAAITRSR EWGISMLALA KIYRLLGVDQ
     LHIGTVVGKM EGGKDEVCSI RDEIVLEDVK EDNKNKFFNQ KWHGLNNTFP VSSGGVYPKL
     VPEIVNIFGK DVIIQAGGGI HGHPEGTVAG ARAMRASVEA SIEGIPLSEK AEEVSELKKA
     LEYWK
//
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