ID G1BWI0_9BACT Unreviewed; 138 AA.
AC G1BWI0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Ribulose bisphosphate carboxylase small subunit {ECO:0000256|HAMAP-Rule:MF_00859};
DE Short=RuBisCO small subunit {ECO:0000256|HAMAP-Rule:MF_00859};
GN Name=cbbS {ECO:0000256|HAMAP-Rule:MF_00859,
GN ECO:0000313|EMBL:AEH40984.1};
OS Candidatus Methylacidiphilum fumarolicum.
OC Bacteria; Verrucomicrobiota; Methylacidiphilae; Methylacidiphilales;
OC Methylacidiphilaceae; Methylacidiphilum (ex Ratnadevi et al. 2023).
OX NCBI_TaxID=591154 {ECO:0000313|EMBL:AEH40984.1};
RN [1] {ECO:0000313|EMBL:AEH40984.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SolV {ECO:0000313|EMBL:AEH40984.1};
RX PubMed=21725016; DOI=10.1128/JB.00407-11;
RA Khadem A.F., Pol A., Wieczorek A., Mohammadi S.S., Francoijs K.J.,
RA Stunnenberg H.G., Jetten M.S., Op den Camp H.J.;
RT "Autotrophic methanotrophy in verrucomicrobia: Methylacidiphilum
RT fumariolicum SolV uses the Calvin-Benson-Bassham cycle for carbon dioxide
RT Fixation.";
RL J. Bacteriol. 193:4438-4446(2011).
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. Although the small subunit is not catalytic it is
CC essential for maximal activity. {ECO:0000256|HAMAP-Rule:MF_00859}.
CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC {ECO:0000256|ARBA:ARBA00038826, ECO:0000256|HAMAP-Rule:MF_00859}.
CC -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO
CC this homodimer is arranged in a barrel-like tetramer with the small
CC subunits forming a tetrameric 'cap' on each end of the 'barrel'.
CC {ECO:0000256|HAMAP-Rule:MF_00859}.
CC -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC {ECO:0000256|HAMAP-Rule:MF_00859}.
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DR EMBL; JF706253; AEH40984.1; -; Genomic_DNA.
DR RefSeq; WP_009060224.1; NZ_OX458932.1.
DR AlphaFoldDB; G1BWI0; -.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
DR CDD; cd03527; RuBisCO_small; 1.
DR Gene3D; 3.30.190.10; Ribulose bisphosphate carboxylase, small subunit; 1.
DR HAMAP; MF_00859; RuBisCO_S_bact; 1.
DR InterPro; IPR024681; RuBisCO_ssu.
DR InterPro; IPR000894; RuBisCO_ssu_dom.
DR InterPro; IPR036385; RuBisCO_ssu_sf.
DR PANTHER; PTHR31262; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR31262:SF23; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT; 1.
DR Pfam; PF00101; RuBisCO_small; 1.
DR SMART; SM00961; RuBisCO_small; 1.
DR SUPFAM; SSF55239; RuBisCO, small subunit; 1.
PE 3: Inferred from homology;
KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567, ECO:0000256|HAMAP-
KW Rule:MF_00859};
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW Rule:MF_00859}.
FT DOMAIN 4..103
FT /note="Ribulose bisphosphate carboxylase small subunit"
FT /evidence="ECO:0000259|SMART:SM00961"
SQ SEQUENCE 138 AA; 16561 MW; 15BFC38FE20024B8 CRC64;
MRITQGTFSY LPDFTDEEIA AQVQYIIDQG WSVMIEYTDD PHPRNTYWDM WGLPLFDIKD
SAAVMQELNQ CRKAFPNHYI RISGYNRQQG YQSTMISFIC NRPKEEPGFE LDRTEWEDRQ
QKYRLKPYAL DKPKGQRY
//
