ID   RBS1_HYDMR              Reviewed;         117 AA.
AC   Q59459;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Ribulose bisphosphate carboxylase small subunit 1 {ECO:0000255|HAMAP-Rule:MF_00859};
DE            Short=RuBisCO small subunit 1 {ECO:0000255|HAMAP-Rule:MF_00859};
GN   Name=cbbS1 {ECO:0000255|HAMAP-Rule:MF_00859};
GN   Synonyms=cbbS-1 {ECO:0000303|PubMed:9531639};
OS   Hydrogenovibrio marinus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Hydrogenovibrio.
OX   NCBI_TaxID=28885;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND EXPRESSION IN E.COLI.
RC   STRAIN=DSM 11271 / JCM 7688 / MH-110;
RX   PubMed=9531639; DOI=10.1007/s002030050584;
RA   Nishihara H., Yaguchi T., Chung S.-Y., Suzuki K., Yanagi M., Yamasato K.,
RA   Kodama T., Igarashi Y.;
RT   "Phylogenetic position of an obligately chemoautotrophic, marine hydrogen-
RT   oxidizing bacterium, Hydrogenovibrio marinus, on the basis of 16S rRNA gene
RT   sequences and two form I RuBisCO gene sequences.";
RL   Arch. Microbiol. 169:364-368(1998).
RN   [2]
RP   CHARACTERIZATION IN E.COLI, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBUNIT.
RC   STRAIN=DSM 11271 / JCM 7688 / MH-110;
RX   DOI=10.1016/S0922-338X(97)86759-1;
RA   Hayashi N.R., Oguni A., Yaguchi T., Chung S.-Y., Nishihara H., Kodama T.,
RA   Igarashi Y.;
RT   "Different properties of gene products of three sets ribulose 1,5-
RT   bisphosphate carboxylase/oxygenase from a marine obligately autotrophic
RT   hydrogen-oxidizing bacterium, Hydrogenovibrio marinus strain MH-110.";
RL   J. Ferment. Bioeng. 85:150-155(1998).
RN   [3]
RP   INDUCTION OF EXPRESSION BY CO(2) IN H.MARINUS.
RC   STRAIN=DSM 11271 / JCM 7688 / MH-110;
RX   PubMed=15317772; DOI=10.1128/jb.186.17.5685-5691.2004;
RA   Yoshizawa Y., Toyoda K., Arai H., Ishii M., Igarashi Y.;
RT   "CO2-responsive expression and gene organization of three ribulose-1,5-
RT   bisphosphate carboxylase/oxygenase enzymes and carboxysomes in
RT   Hydrogenovibrio marinus strain MH-110.";
RL   J. Bacteriol. 186:5685-5691(2004).
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|Ref.2}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=1.2 umol/min/mg enzyme with CO(2) as substrate, expressed in
CC         E.coli {ECO:0000269|Ref.2};
CC         Note=The CO(2)/O(2) specificity factor (tau) is 26.6.
CC         {ECO:0000269|Ref.2};
CC   -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00859, ECO:0000269|Ref.2}.
CC   -!- INDUCTION: Both mRNA and protein accumulate at 2% and 0.03% CO(2), but
CC       not at 15% or 0.15% CO(2) (at protein level).
CC       {ECO:0000269|PubMed:15317772}.
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; D43621; BAA07730.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59459; -.
DR   SMR; Q59459; -.
DR   STRING; 28885.EI16_08845; -.
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.
FT   CHAIN           1..117
FT                   /note="Ribulose bisphosphate carboxylase small subunit 1"
FT                   /id="PRO_0000198614"
SQ   SEQUENCE   117 AA;  13306 MW;  60D35A401A0C9694 CRC64;
     MSQELDYPSS LSAPTSRKAE TFSYLPKMTT DQIKAQVEYI ISKGWNPAIE HSEPENAFSY
     YWYMWKLPMF GDTDANVVLA EVDACIKANP NNHVRLIGYD NYAQSQGANM LVKRGDM