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Database: UniProt
Entry: D2REY6_ARCPA
LinkDB: D2REY6_ARCPA
Original site: D2REY6_ARCPA 
ID   D2REY6_ARCPA            Unreviewed;       447 AA.
AC   D2REY6;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   12-SEP-2018, entry version 56.
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=Arcpr_1634 {ECO:0000313|EMBL:ADB58680.1};
OS   Archaeoglobus profundus (strain DSM 5631 / JCM 9629 / NBRC 100127 /
OS   Av18).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
OC   Archaeoglobaceae; Archaeoglobus.
OX   NCBI_TaxID=572546 {ECO:0000313|EMBL:ADB58680.1, ECO:0000313|Proteomes:UP000001901};
RN   [1] {ECO:0000313|EMBL:ADB58680.1, ECO:0000313|Proteomes:UP000001901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5631 / JCM 9629 / NBRC 100127 / Av18
RC   {ECO:0000313|Proteomes:UP000001901};
RX   PubMed=21304717;
RA   von Jan M., Lapidus A., Del Rio T.G., Copeland A., Tice H.,
RA   Cheng J.F., Lucas S., Chen F., Nolan M., Goodwin L., Han C.,
RA   Pitluck S., Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA   Chertkov O., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Saunders E., Brettin T., Detter J.C.,
RA   Chain P., Eichinger K., Huber H., Spring S., Rohde M., Goker M.,
RA   Wirth R., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Archaeoglobus profundus type strain
RT   (AV18).";
RL   Stand. Genomic Sci. 2:327-346(2010).
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}.
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DR   EMBL; CP001857; ADB58680.1; -; Genomic_DNA.
DR   ProteinModelPortal; D2REY6; -.
DR   STRING; 572546.Arcpr_1634; -.
DR   EnsemblBacteria; ADB58680; ADB58680; Arcpr_1634.
DR   KEGG; apo:Arcpr_1634; -.
DR   eggNOG; arCOG04443; Archaea.
DR   eggNOG; COG1850; LUCA.
DR   HOGENOM; HOG000230831; -.
DR   KO; K01601; -.
DR   OMA; HRAMHAA; -.
DR   OrthoDB; POG093Z02MJ; -.
DR   Proteomes; UP000001901; 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   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01133};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001901};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01133, ECO:0000313|EMBL:ADB58680.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001901}.
FT   DOMAIN       16    136       RuBisCO_large_N. {ECO:0000259|Pfam:
FT                                PF02788}.
FT   DOMAIN      149    441       RuBisCO_large. {ECO:0000259|Pfam:
FT                                PF00016}.
FT   REGION      370    372       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01133}.
FT   REGION      392    395       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01133}.
FT   ACT_SITE    166    166       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01133}.
FT   ACT_SITE    284    284       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01133}.
FT   METAL       192    192       Magnesium; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01133}.
FT   METAL       194    194       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01133}.
FT   METAL       195    195       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01133}.
FT   BINDING     168    168       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01133}.
FT   BINDING     285    285       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01133}.
FT   BINDING     317    317       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01133}.
FT   SITE        325    325       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01133}.
FT   MOD_RES     192    192       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01133}.
SQ   SEQUENCE   447 AA;  50333 MW;  1C59F7CBE3BCBA72 CRC64;
     MLHRTRVMPD FEMYFEYVDK SYEPSERDLI AVFRVKPSEG FKIEDVAGAI ASESSTGTWT
     TLYDWCDKDR IKKLSAKAYE FIDLEDGSWI VKIAYPVELF ERGSITCLLA SIAGNIFGMK
     RVAGLRLEDV YLPKEFLKYF EGPNFGKDVR KIFKVYDRPI VGTVPKPKVG YTPDEVEKLA
     YELLSGGMDY IKDDENLTSQ DFCKFEERAK AIMKAIDKAE SDTGEKKVWF ANITGDVKEM
     EKRMKIVADY GNPYVMIDVV IAGWSVLKYM RELANDYGLA IHAHRAMHSA FTRNRYHGIS
     MFVLAKLYRV IGVDQLHIGT AGYGKLEGGM WEVVQYAKIL RESSYVPDEK DIFHIKQEFH
     HIKPAMPVSS GGLHPGNVAG VIDALGEDII IQVGGGVMGH PDGPKAGAKA VRQALEAIKL
     GIPLDEYAKD HKELAKALEK WGYVKPV
//
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