ID A0A080M7H6_9PROT Unreviewed; 459 AA.
AC A0A080M7H6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000256|ARBA:ARBA00019702};
DE EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287};
GN Name=cbbM {ECO:0000313|EMBL:KFB77227.1};
GN ORFNames=AW06_001641 {ECO:0000313|EMBL:KFB77227.1};
OS Candidatus Accumulibacter cognatus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=2954383 {ECO:0000313|EMBL:KFB77227.1, ECO:0000313|Proteomes:UP000021315};
RN [1] {ECO:0000313|EMBL:KFB77227.1, ECO:0000313|Proteomes:UP000021315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-02 {ECO:0000313|Proteomes:UP000021315};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFB77227.1}.
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DR EMBL; JDST02000031; KFB77227.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A080M7H6; -.
DR STRING; 1453999.AW06_001641; -.
DR Proteomes; UP000021315; Unassembled WGS sequence.
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:KFB77227.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000021315}.
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; 50897 MW; AF9F103263A2018A CRC64;
MDQSNRYADL SLKEEELIKG GKHLLVAYKM KPKAGYGYLE SAAHFAAESS TGTNVETSTT
DDFTKGVDAL VYSIDEATED MRIAYPLDLF DRNMTDGRMM MVSVLTLIIG NNQGMGDIEH
GKIHDIFIPE RAIQLFDGPA KDISDLWRIL GRPLKDGGYI AGTIIKPKLG LRPEPFAKAA
YQFWLGGDFI KNDEPQGNQV FCPARKVYPL VYDAMKRAMD ETGQAKIFSA NITADDHYEM
LHRADFILET FGPDADKVAF LVDGFVGGPG MITTARRQYP NQYLHYHRAG HGMITSPSAK
RGYTAFVLGK MARLQGASGI HVGTMGFGKM EGESSDKNIC YMLERDECQG PVYYQKWYGM
KPTTSIISGG MNALRLPGFF ENLGHGNVIN TSGGGSYGHI DSPAAGALSL RQAYECWKAG
ADPIEWAREH REFARAFESF PGDADRLYPG WREKLGVHR
//
