GenomeNet

Database: UniProt
Entry: A0A0A6PQL9_9GAMM
LinkDB: A0A0A6PQL9_9GAMM
Original site: A0A0A6PQL9_9GAMM 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system