RBS_BRADU
ID RBS_BRADU Reviewed; 134 AA.
AC Q9ZI33;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Ribulose bisphosphate carboxylase small subunit {ECO:0000255|HAMAP-Rule:MF_00859};
DE Short=RuBisCO small subunit {ECO:0000255|HAMAP-Rule:MF_00859};
GN Name=cbbS {ECO:0000255|HAMAP-Rule:MF_00859}; OrderedLocusNames=blr2586;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=BJ110;
RX PubMed=9882445; DOI=10.1006/abbi.1998.0979;
RA Horken K.M., Tabita F.R.;
RT "Closely related form I ribulose bisphosphate carboxylase/oxygenase
RT molecules that possess different CO2/O2 substrate specificities.";
RL Arch. Biochem. Biophys. 361:183-194(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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:0000255|HAMAP-Rule:MF_00859,
CC ECO:0000269|PubMed:9882445}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=55 uM for ribulose 1,5-bisphosphate {ECO:0000269|PubMed:9882445};
CC KM=66 uM for CO(2) {ECO:0000269|PubMed:9882445};
CC Vmax=2.8 umol/min/mg enzyme with CO(2) as substrate
CC {ECO:0000269|PubMed:9882445};
CC Note=The CO(2)/O(2) specificity factor (tau) is 75.;
CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00859, ECO:0000305|PubMed:9882445}.
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:0000255|HAMAP-Rule:MF_00859}.
CC -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00859}.
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DR EMBL; AF041820; AAD05387.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC47851.1; -; Genomic_DNA.
DR RefSeq; NP_769226.1; NC_004463.1.
DR RefSeq; WP_011085372.1; NZ_CP011360.1.
DR AlphaFoldDB; Q9ZI33; -.
DR SMR; Q9ZI33; -.
DR STRING; 224911.27350842; -.
DR PRIDE; Q9ZI33; -.
DR EnsemblBacteria; BAC47851; BAC47851; BAC47851.
DR GeneID; 64022337; -.
DR KEGG; bja:blr2586; -.
DR PATRIC; fig|224911.44.peg.2175; -.
DR eggNOG; COG4451; Bacteria.
DR HOGENOM; CLU_098114_2_0_5; -.
DR InParanoid; Q9ZI33; -.
DR OMA; KQCQVLS; -.
DR PhylomeDB; Q9ZI33; -.
DR SABIO-RK; Q9ZI33; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR CDD; cd03527; RuBisCO_small; 1.
DR Gene3D; 3.30.190.10; -; 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; PTHR31262; 1.
DR Pfam; PF00101; RuBisCO_small; 1.
DR SMART; SM00961; RuBisCO_small; 1.
DR SUPFAM; SSF55239; SSF55239; 1.
PE 1: Evidence at protein level;
KW Calvin cycle; Carbon dioxide fixation; Reference proteome.
FT CHAIN 1..134
FT /note="Ribulose bisphosphate carboxylase small subunit"
FT /id="PRO_0000198611"
SQ SEQUENCE 134 AA; 15515 MW; 68301DC185F479FB CRC64;
MKLTQGCFSF LPDLTDDQIY KQVQYCLAKG WAVNIEFTDD PHPRNTYWEM WGLPMFDLQD
AAGVMMELAE CRRVYGDRYI RISGFDSSPG WESVRISFLV NRPPQEAEFE LVRQEVGGRA
IRYTTVRKAP AHVS
