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Database: UniProt
Entry: A0A0F8VFA8_9ARCH
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ID   A0A0F8VFA8_9ARCH        Unreviewed;       424 AA.
AC   A0A0F8VFA8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   12-SEP-2018, entry version 14.
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   ECO:0000313|EMBL:KKK43062.1};
GN   ORFNames=Lokiarch_30170 {ECO:0000313|EMBL:KKK43062.1};
OS   Lokiarchaeum sp. GC14_75.
OC   Archaea; Asgard group; Candidatus Lokiarchaeota; Lokiarchaeum.
OX   NCBI_TaxID=1538547 {ECO:0000313|EMBL:KKK43062.1, ECO:0000313|Proteomes:UP000034722};
RN   [1] {ECO:0000313|EMBL:KKK43062.1, ECO:0000313|Proteomes:UP000034722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GC14-75 {ECO:0000313|EMBL:KKK43062.1};
RX   PubMed=25945739; DOI=10.1038/nature14447;
RA   Spang A., Saw J.H., Jorgensen S.L., Zaremba-Niedzwiedzka K.,
RA   Martijn J., Lind A.E., van Eijk R., Schleper C., Guy L., Ettema T.J.;
RT   "Complex archaea that bridge the gap between prokaryotes and
RT   eukaryotes.";
RL   Nature 521:173-179(2015).
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: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose
CC       1,5-bisphosphate + CO(2) + H(2)O. {ECO:0000256|HAMAP-
CC       Rule:MF_01133}.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
CC       D-ribulose 1,5-bisphosphate + O(2). {ECO:0000256|HAMAP-
CC       Rule:MF_01133}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01133};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01133};
CC   -!- SUBUNIT: Homodimer or homodecamer. In contrast to form I RuBisCO,
CC       the 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
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:0000256|HAMAP-
CC       Rule:MF_01133}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type III
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01133}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KKK43062.1}.
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DR   EMBL; JYIM01000282; KKK43062.1; -; Genomic_DNA.
DR   KEGG; loki:Lokiarch_30170; -.
DR   PATRIC; fig|1538547.4.peg.3168; -.
DR   KO; K01601; -.
DR   Proteomes; UP000034722; Unassembled WGS sequence.
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; -; 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   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01133};
KW   Complete proteome {ECO:0000313|Proteomes:UP000034722};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01133};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034722}.
FT   DOMAIN        4    119       RuBisCO_large_N. {ECO:0000259|Pfam:
FT                                PF02788}.
FT   DOMAIN      130    423       RuBisCO_large. {ECO:0000259|Pfam:
FT                                PF00016}.
FT   REGION      352    354       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01133}.
FT   REGION      374    377       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01133}.
FT   ACT_SITE    151    151       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01133}.
FT   ACT_SITE    269    269       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01133}.
FT   METAL       177    177       Magnesium; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01133}.
FT   METAL       179    179       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01133}.
FT   METAL       180    180       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01133}.
FT   BINDING     153    153       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01133}.
FT   BINDING     270    270       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01133}.
FT   BINDING     302    302       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01133}.
FT   SITE        309    309       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01133}.
FT   MOD_RES     177    177       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01133}.
SQ   SEQUENCE   424 AA;  47500 MW;  28BF3D5B0840FC21 CRC64;
     MIHYVNLDYV PDENDLIVMY YVEKAPDCRD LEQACEEIAK ESSIGTWTEI ATLSADIADR
     LKPSAFYIDH ENNIVKIAYN KELFEAENIP QILSAIAGNI YGMKVLKYLR LLDISFPKDI
     VKKYKGPKFG IKGIRNLTKI NNRPLLGTIV KPKVGLNEID HAKVCGEAWM GGLDLVKDDE
     NLTNMIFNKF EKRIIETLKI RDKVENATGE RKFYMPNITA PLSIMKDRAD FVLGNGGEYV
     MIDVLTVGFS ALQEIRNYLD NEKVIIHAHR AMHAALTRNK KHGMSMISIA KLMRLIGMDQ
     LHSGTIVGKM QGDRQEVLET NKVITKSKIV GNNLTLLDQN WENIKPILPV ASGGLSPLQI
     PELIENLGKD IVLQFGGGCH GHPDGTLAGA QAIRQAVNAV LENIELKEYA KTHRELARAI
     DKWG
//
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