ID A0A0A6PQL9_9GAMM Unreviewed; 462 AA.
AC A0A0A6PQL9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000256|ARBA:ARBA00019702};
DE EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287};
GN ORFNames=PN36_07480 {ECO:0000313|EMBL:KHD09267.1};
OS Candidatus Thiomargarita nelsonii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thiomargarita.
OX NCBI_TaxID=1003181 {ECO:0000313|EMBL:KHD09267.1, ECO:0000313|Proteomes:UP000030428};
RN [1] {ECO:0000313|EMBL:KHD09267.1, ECO:0000313|Proteomes:UP000030428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hydrate Ridge {ECO:0000313|EMBL:KHD09267.1};
RX PubMed=27199933; DOI=10.3389/fmicb.2016.00603;
RA Flood B.E., Fliss P., Jones D.S., Dick G.J., Jain S., Kaster A.K.,
RA Winkel M., Mussmann M., Bailey J.;
RT "Single-Cell (Meta-)Genomics of a Dimorphic Candidatus Thiomargarita
RT nelsonii Reveals Genomic Plasticity.";
RL Front. Microbiol. 7:603-603(2016).
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:KHD09267.1}.
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DR EMBL; JSZA02000021; KHD09267.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A6PQL9; -.
DR SMR; A0A0A6PQL9; -.
DR Proteomes; UP000030428; 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 SFLD; SFLDS00014; RuBisCO; 1.
DR SFLD; SFLDG00301; RuBisCO-like_proteins; 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:KHD09267.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030428}.
FT DOMAIN 14..135
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 145..443
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
SQ SEQUENCE 462 AA; 51277 MW; 62677067AB03F01E CRC64;
MALDQSNRYA DLSLKEEDLI KGGNHVLCAY LMKPKEGFFD YLGTAAHFAA ESSTGTNVEV
CTTDDFTKGV DALVYEIDEE KELMKIAYPV DLFDRNMKDG RAMIVSFLTL AIGNNQGMGD
IEYGKMLDFY VPPKYLRLFD GPNKNIVDMW RVLGRPLENG GMVVGTIIKP KLGLRPEPFA
KACYQFWLGG DFIKNDEPQG NQVFAPTRKI IPLIVDAMKR AQDETGEAKI FSANITADDP
FEMIHRGEYI LEEFGEFGDH VAFLVDGYVG GPTAITTCRR YFPNQFLHYH RAGHGAVTSQ
QSQRGYSVLV HMKMARMQGA SGIHTGTMGY GKMEGDATEK NLAYNLERDS ADGLYYHQEW
AGMKATTPII SGGMNALRLP GFFDNLGHCN VIQTSGGGAF GHKDGGAAGA TSLRQARDAW
MQGVDVIEYA KEHEELRGAF ETFTADADKI YPNWREKLGV HK
//