ID W9H4Q3_9PROT Unreviewed; 422 AA.
AC W9H4Q3;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Ribulose bisphosphate carboxylase {ECO:0000313|EMBL:EWY41039.1};
GN ORFNames=N825_30620 {ECO:0000313|EMBL:EWY41039.1};
OS Skermanella stibiiresistens SB22.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Skermanella.
OX NCBI_TaxID=1385369 {ECO:0000313|EMBL:EWY41039.1, ECO:0000313|Proteomes:UP000019486};
RN [1] {ECO:0000313|EMBL:EWY41039.1, ECO:0000313|Proteomes:UP000019486}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB22 {ECO:0000313|EMBL:EWY41039.1,
RC ECO:0000313|Proteomes:UP000019486};
RA Zhu W., Wang G.;
RT "The genome sequence of Skermanella stibiiresistens.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|RuleBase:RU003834}.
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:EWY41039.1}.
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DR EMBL; AVFL01000005; EWY41039.1; -; Genomic_DNA.
DR RefSeq; WP_037449805.1; NZ_AVFL01000005.1.
DR AlphaFoldDB; W9H4Q3; -.
DR STRING; 1385369.N825_30620; -.
DR PATRIC; fig|1385369.3.peg.1761; -.
DR OrthoDB; 9764279at2; -.
DR Proteomes; UP000019486; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:InterPro.
DR GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR CDD; cd08207; RLP_NonPhot; 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 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 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000019486}.
FT DOMAIN 6..130
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 140..419
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
SQ SEQUENCE 422 AA; 45450 MW; 0364B9D77006B292 CRC64;
MTAQRITATY RIETAYPLQE AAETMAGEQS TGTFIRLPGE TDEMRELYGA HIERLTELGE
VEEPSLPGAG VPKGSGGKPV WRRAEVELSW SLDNFGPSLP NLVATVAGNL FELRPFSGLR
LLDIGLPEAF AARYPGPKFG VEGTRRLSGV EGRPLIGTII KPSVGMGPEA TAEVARVLCE
AGIDFIKDDE LQADGAHCPF EARARAVMRV IEDQAQRTGK KTMFAFNITG DLDEMRRRHD
LVLELGGTCV MASLNSVGVV GMVELGRFSQ LPIHAHRNGW GYLSRSQELG WSYVAWQKIW
RLAGADHMHV NGLQNKFCES DESVIASAKA CLTPMFESKP CTVMPVFSSG QSARQAPGTY
AALGSSDLIF AAGGGIMGHP DGPAAGFASL RESWEAALKG IPLDEYARDH PALAKALTAY
AS
//