ID A0A0F7K2W9_9GAMM Unreviewed; 461 AA.
AC A0A0F7K2W9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000256|ARBA:ARBA00019702};
DE EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287};
GN ORFNames=AAY24_15645 {ECO:0000313|EMBL:AKH21550.1};
OS Sedimenticola thiotaurini.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Sedimenticola.
OX NCBI_TaxID=1543721 {ECO:0000313|EMBL:AKH21550.1, ECO:0000313|Proteomes:UP000034410};
RN [1] {ECO:0000313|EMBL:AKH21550.1, ECO:0000313|Proteomes:UP000034410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SIP-G1 {ECO:0000313|EMBL:AKH21550.1,
RC ECO:0000313|Proteomes:UP000034410};
RX PubMed=26089430;
RA Flood B.E., Jones D.S., Bailey J.V.;
RT "Complete Genome Sequence of Sedimenticola thiotaurini Strain SIP-G1, a
RT Polyphosphate- and Polyhydroxyalkanoate-Accumulating Sulfur-Oxidizing
RT Gammaproteobacterium Isolated from Salt Marsh Sediments.";
RL Genome Announc. 3:e00671-15(2015).
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; CP011412; AKH21550.1; -; Genomic_DNA.
DR RefSeq; WP_046860475.1; NZ_CP011412.1.
DR AlphaFoldDB; A0A0F7K2W9; -.
DR KEGG; seds:AAY24_15645; -.
DR PATRIC; fig|1543721.4.peg.3224; -.
DR OrthoDB; 9770811at2; -.
DR Proteomes; UP000034410; Chromosome.
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:AKH21550.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000034410}.
FT DOMAIN 15..134
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 145..442
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
SQ SEQUENCE 461 AA; 50649 MW; CB8E83BAC5EECC43 CRC64;
MSLDQTSRYA DLSLNEDKLI ADGNHILVAY TMEPAAGNGY LATAAHFAAE SSTGTNVEVS
TTDDFTKGVD ALVYEIDEAN GIMKIAYPNE LFDRNVTDGR VMLVSFLTLT IGNNQGMGDV
KNAQMQDFYI PPKMLQLFDG PSKDISDLWR ILGRPVQDGG YIAGTIIKPK LGLRPEPFAE
AAYQFWLGGD FIKNDEPQGN QVFCPMKKVM PLVADAMKRA QDETGQAKLF SANITADDHY
EMMARADYIL ETFGENASHV AFLVDGYVGG PGMITTARRQ YPNQYLHYHR AGHGAVTSPS
SKRGYTAFVL AKMARLQGAS GIHVGTMGYG KMEGSRDDKV IAYMIERDSC DGPFYHQEWY
GMKPTTPIIS GGMNALRLPG FFENLGHGNV INTSGGGSYG HIDSPAAGAI SLRQAYECWK
EGADPVEYAK EHKEFARAFE SFPQDADTIY PGWRDRLGVH K
//