ID   C7RNN3_ACCRE            Unreviewed;       459 AA.
AC   C7RNN3;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000256|ARBA:ARBA00019702};
DE            EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287};
GN   OrderedLocusNames=CAP2UW1_0825 {ECO:0000313|EMBL:ACV34169.1};
OS   Accumulibacter regalis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=522306 {ECO:0000313|EMBL:ACV34169.1};
RN   [1] {ECO:0000313|EMBL:ACV34169.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UW-1 {ECO:0000313|EMBL:ACV34169.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Barry K., Pitluck S., Lowry S., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., McMahon K.D., Hugenholtz P.;
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACV34169.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UW-1 {ECO:0000313|EMBL:ACV34169.1};
RG   US DOE Joint Genome Institute;
RA   Martin H.G., Ivanova N., Kunin V., Warnecke F., Barry K., He S.,
RA   Salamov A., Szeto E., Dalin E., Pangilinan J.L., Lapidus A., Lowry S.,
RA   Kyrpides N.C., McMahon K.D., Hugenholtz P.;
RT   "Complete sequence of chromosome of Candidatus Accumulibacter phosphatis
RT   clade IIA str. UW-1.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC       ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC       fixation, as well as the oxidative fragmentation of the pentose
CC       substrate. Both reactions occur simultaneously and in competition at
CC       the same active site. {ECO:0000256|ARBA:ARBA00003617}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type II
CC       subfamily. {ECO:0000256|ARBA:ARBA00005475}.
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DR   EMBL; CP001715; ACV34169.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7RNN3; -.
DR   STRING; 522306.CAP2UW1_0825; -.
DR   KEGG; app:CAP2UW1_0825; -.
DR   eggNOG; COG1850; Bacteria.
DR   HOGENOM; CLU_031450_3_1_4; -.
DR   OrthoDB; 9770811at2; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR   CDD; cd08211; RuBisCO_large_II; 1.
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_01339; RuBisCO_L_type2; 1.
DR   InterPro; IPR033966; RuBisCO.
DR   InterPro; IPR020878; RuBisCo_large_chain_AS.
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   InterPro; IPR020871; RuBisCO_lsuII.
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   SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR   SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1.
DR   PROSITE; PS00157; RUBISCO_LARGE; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:ACV34169.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          12..130
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          143..440
FT                   /note="Ribulose bisphosphate carboxylase large subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00016"
SQ   SEQUENCE   459 AA;  50767 MW;  50263104D5959E2E CRC64;
     MDQSNRYADL SLKEEDLIKG GKHILVAYKM KPKAGYDYLP AAAHFAAESS TGTNVEVCTT
     DDFTRGVDAL VYHIDEATEE MRIAYPLDLF DRNVTDGRMM IVSFLTLVIG NNQGMGDIEH
     AKIYDFYMPE RAIQLFDGPA KDISDMWRVL GRPVKDGGYI AGTIIKPKLG LRPEPFAKAA
     YQFWLGGDFI KNDEPQGNQV FAPMKKVMPL VYDAMKRAQD ETGQAKLFSA NITADDHYEM
     CARADYILET FGPDADKVAF LVDGYVGGPG MVTTARRQYP NQYLHYHRAG HGAVTSPSSR
     RGYDAYVLAK MSRLQGASGI HVGTMGYGKM EGSADDRAIA YVIERDEYQG PAYYQKWYGM
     KPTTPIISGG MNALRLPGFF ANLGHGNVIN TSGGGSYGHI DSPAAGAISL RQAYECWKAG
     ADPIAWAREH KEFARAFESF PGDADTLYPG WREKLGVHR
//