ID A0A0S7ZKM7_9SPIR Unreviewed; 411 AA.
AC A0A0S7ZKM7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE RecName: Full=Ribulose 1,5-bisphosphate carboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMS17_10495 {ECO:0000313|EMBL:KPJ86892.1};
OS Spirochaetes bacterium DG_61.
OC Bacteria; Spirochaetota.
OX NCBI_TaxID=1704237 {ECO:0000313|EMBL:KPJ86892.1, ECO:0000313|Proteomes:UP000050987};
RN [1] {ECO:0000313|EMBL:KPJ86892.1, ECO:0000313|Proteomes:UP000050987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_61 {ECO:0000313|EMBL:KPJ86892.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPJ86892.1}.
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DR EMBL; LJNB01000137; KPJ86892.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7ZKM7; -.
DR Proteomes; UP000050987; 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; cd08205; RuBisCO_IV_RLP; 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; 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.
PE 3: Inferred from homology;
FT DOMAIN 20..135
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 145..410
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
SQ SEQUENCE 411 AA; 46224 MW; 9BFBD7980DB7F9C5 CRC64;
MERVHDPVIF QHAIDGIDMK NNIIATYYMS DRLPGVDFID HFKLIESIAI EGSTGSWQRV
EEESTEVREM LSGKLVGYYE IPTEDEYRKS AVIQLAFPIN AWHDNVPMML LSIAGNCFAY
SQRIRLLDVV FPENMVKNFR GPKFGVEGTR ELLGIPERPL SLHIIKPKMG MTPKQTGDQV
YQTAIGGADM AKDDEMTSDT YNNNFRDRLK YVMDAIDRAE KRTGKRMIYF CSITDEVSKL
HEKAREAVEI GANGLLITYS VGLSAIREVT SDPDINIPVM VHNSHMIASM DTISWPVFTK
LIRLCGADQT LTPTYWSSIP MVSLEEGIRC QHVAQAPFYG FKKMWSMPAA GTYPGLTPIL
MSEYGKDIII PSGGGMLGHP DGYTAGAQAW QQAIASVMED VPIDEYRRTR R
//
