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Ribulose bisphosphate carboxylase (RuBisCO) (EC 4.1.1.39)

 B7R258_9EURY            Unreviewed;       444 AA.
B7R258;
10-FEB-2009, integrated into UniProtKB/TrEMBL.
10-FEB-2009, sequence version 1.
12-SEP-2018, entry version 52.
RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000256|HAMAP-Rule:MF_01133};
Short=RuBisCO {ECO:0000256|HAMAP-Rule:MF_01133};
EC=4.1.1.39 {ECO:0000256|HAMAP-Rule:MF_01133};
Name=rbcL {ECO:0000256|HAMAP-Rule:MF_01133};
ORFNames=TAM4_1764 {ECO:0000313|EMBL:EEB74397.1};
Thermococcus sp. AM4.
Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
Thermococcus.
NCBI_TaxID=246969 {ECO:0000313|EMBL:EEB74397.1, ECO:0000313|Proteomes:UP000009277};
[1] {ECO:0000313|EMBL:EEB74397.1, ECO:0000313|Proteomes:UP000009277}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AM4 {ECO:0000313|EMBL:EEB74397.1};
PubMed=22123768; DOI=10.1128/JB.06259-11;
Oger P., Sokolova T.G., Kozhevnikova D.A., Chernyh N.A.,
Bartlett D.H., Bonch-Osmolovskaya E.A., Lebedinsky A.V.;
"Complete Genome Sequence of the Hyperthermophilic Archaeon
Thermococcus sp. Strain AM4, Capable of Organotrophic Growth and
Growth at the Expense of Hydrogenogenic or Sulfidogenic Oxidation of
Carbon Monoxide.";
J. Bacteriol. 193:7019-7020(2011).
-!- FUNCTION: Catalyzes the addition of molecular CO(2) and H(2)O to
ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3-
phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation
pathway, together with AMP phosphorylase and R15P isomerase.
{ECO:0000256|HAMAP-Rule:MF_01133}.
-!- CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose
1,5-bisphosphate + CO(2) + H(2)O. {ECO:0000256|HAMAP-
Rule:MF_01133}.
-!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
D-ribulose 1,5-bisphosphate + O(2). {ECO:0000256|HAMAP-
Rule:MF_01133}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_01133};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_01133};
-!- SUBUNIT: Homodimer or homodecamer. In contrast to form I RuBisCO,
the form III RuBisCO is composed solely of large subunits.
{ECO:0000256|HAMAP-Rule:MF_01133}.
-!- MISCELLANEOUS: Because the Archaea possessing a type III RuBisCO
are all anaerobic, it is most likely that only the carboxylase
activity of RuBisCO, and not the competitive oxygenase activity
(by which RuBP reacts with O(2) to form one molecule of 3-
phosphoglycerate and one molecule of 2-phosphoglycolate), is
biologically relevant in these strains. {ECO:0000256|HAMAP-
Rule:MF_01133}.
-!- SIMILARITY: Belongs to the RuBisCO large chain family. Type III
subfamily. {ECO:0000256|HAMAP-Rule:MF_01133}.
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EMBL; CP002952; EEB74397.1; -; Genomic_DNA.
RefSeq; WP_014122283.1; NC_016051.1.
ProteinModelPortal; B7R258; -.
STRING; 246969.TAM4_1764; -.
EnsemblBacteria; EEB74397; EEB74397; TAM4_1764.
GeneID; 7419691; -.
KEGG; tha:TAM4_1764; -.
eggNOG; arCOG04443; Archaea.
eggNOG; COG1850; LUCA.
KO; K01601; -.
OrthoDB; POG093Z02MJ; -.
BioCyc; TSP246969:G1GNJ-1127-MONOMER; -.
Proteomes; UP000009277; Chromosome.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
GO; GO:0006196; P:AMP catabolic process; IEA:UniProtKB-UniRule.
GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
CDD; cd08213; RuBisCO_large_III; 1.
Gene3D; 3.20.20.110; -; 1.
Gene3D; 3.30.70.150; -; 1.
HAMAP; MF_01133; RuBisCO_L_type3; 1.
InterPro; IPR033966; RuBisCO.
InterPro; IPR017712; RuBisCO_III.
InterPro; IPR000685; RuBisCO_lsu_C.
InterPro; IPR036376; RuBisCO_lsu_C_sf.
InterPro; IPR017443; RuBisCO_lsu_fd_N.
InterPro; IPR036422; RuBisCO_lsu_N_sf.
PANTHER; PTHR42704; PTHR42704; 1.
Pfam; PF00016; RuBisCO_large; 1.
Pfam; PF02788; RuBisCO_large_N; 1.
SFLD; SFLDS00014; RuBisCO; 1.
SUPFAM; SSF51649; SSF51649; 1.
SUPFAM; SSF54966; SSF54966; 1.
TIGRFAMs; TIGR03326; rubisco_III; 1.
3: Inferred from homology;
Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01133};
Complete proteome {ECO:0000313|Proteomes:UP000009277};
Lyase {ECO:0000256|HAMAP-Rule:MF_01133};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01133};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01133};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01133}.
DOMAIN 12 130 RuBisCO_large_N.
{ECO:0000259|Pfam:PF02788}.
DOMAIN 142 438 RuBisCO_large.
{ECO:0000259|Pfam:PF00016}.
REGION 367 369 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01133}.
REGION 389 392 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01133}.
ACT_SITE 163 163 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01133}.
ACT_SITE 281 281 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01133}.
METAL 189 189 Magnesium; via carbamate group.
{ECO:0000256|HAMAP-Rule:MF_01133}.
METAL 191 191 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01133}.
METAL 192 192 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01133}.
BINDING 165 165 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01133}.
BINDING 282 282 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01133}.
BINDING 314 314 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01133}.
SITE 322 322 Transition state stabilizer.
{ECO:0000256|HAMAP-Rule:MF_01133}.
MOD_RES 189 189 N6-carboxylysine. {ECO:0000256|HAMAP-
Rule:MF_01133}.
SEQUENCE 444 AA; 49807 MW; 8BD0A123C21ED7CB CRC64;
MVEKFDKIYD YYVDKGYEPN KKRDIIAVFR VTPAEGYTIE AAAGAVAAES STGTWTTLYP
WYEQERWADL SAKAYDFIDM GDGSWIVRIA YPFHAFEEWN LPGLLASIAG NVFGMKRVKG
LRLEDLYIPE IVLRNFNGPA FGIEGVRKML EIYDRPLYGV VPKPKVGYSP EEFEKLAYEL
LSNGADYMKD DENLTSPWYN RFDERAEIVA RVIDKVENET GEKKTWFANI TADVREMERR
LEILADLGLK HAMVDVVITG WGALEYIRDL AADYGLAIHG HRAMHAAFTR NKYHGISMFV
LAKLYRIIGI DQLHVGTAGA GKLEGGKWDV IQNARILREE TYTPDENDVF HLEQKFYGMK
PAFPTSSGGL HPGNIEPVIE ALGKDIVLQL GGGTLGHPDG PGAGARAVRQ AIDAIMQGIP
LDEYAKTHKE LARALEKWGH VTPV


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