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Database: UniProt/SWISS-PROT
Entry: RBS_HALNC
LinkDB: RBS_HALNC
Original site: RBS_HALNC 
ID   RBS_HALNC               Reviewed;         110 AA.
AC   P45686; D0KZ91;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   28-FEB-2018, entry version 93.
DE   RecName: Full=Ribulose bisphosphate carboxylase small chain;
DE            Short=RuBisCO small subunit;
DE            EC=4.1.1.39;
GN   Name=cbbS; Synonyms=rbcS; OrderedLocusNames=Hneap_0921;
OS   Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus
OS   neapolitanus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Halothiobacillaceae; Halothiobacillus.
OX   NCBI_TaxID=555778;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9696760;
RA   Baker S.H., Jin S., Aldrich H.C., Howard G.T., Shively J.M.;
RT   "Insertion mutation of the form I cbbL gene encoding ribulose
RT   bisphosphate carboxylase/oxygenase (RuBisCO) in Thiobacillus
RT   neapolitanus results in expression of form II RuBisCO, loss of
RT   carboxysomes, and an increased CO2 requirement for growth.";
RL   J. Bacteriol. 180:4133-4139(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23641 / c2;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Davenport K., Brettin T.,
RA   Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Kerfeld C., Cannon G., Heinhort S.;
RT   "Complete sequence of Halothiobacillus neapolitanus c2.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RA   Kerfeld C.A., Sawaya M.R., Pashkov I., Cannon G., Williams E.,
RA   Tran K., Yeates T.O.;
RT   "The structure of Halothiobacillus neapolitanus Rubisco.";
RL   Submitted (APR-2005) to the PDB data bank.
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
CC       at the same active site.
CC   -!- CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose
CC       1,5-bisphosphate + CO(2) + H(2)O.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
CC       D-ribulose 1,5-bisphosphate + O(2).
CC   -!- SUBUNIT: 8 large chains + 8 small chains.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000305}.
DR   EMBL; AF038430; AAC32550.1; -; Genomic_DNA.
DR   EMBL; CP001801; ACX95764.1; -; Genomic_DNA.
DR   RefSeq; WP_012823800.1; NC_013422.1.
DR   PDB; 1SVD; X-ray; 1.80 A; M=1-110.
DR   PDBsum; 1SVD; -.
DR   ProteinModelPortal; P45686; -.
DR   SMR; P45686; -.
DR   STRING; 555778.Hneap_0921; -.
DR   EnsemblBacteria; ACX95764; ACX95764; Hneap_0921.
DR   KEGG; hna:Hneap_0921; -.
DR   eggNOG; ENOG4108VFZ; Bacteria.
DR   eggNOG; COG4451; LUCA.
DR   HOGENOM; HOG000141332; -.
DR   KO; K01602; -.
DR   OMA; WNPAIEH; -.
DR   OrthoDB; POG091H13LH; -.
DR   BRENDA; 4.1.1.39; 6349.
DR   EvolutionaryTrace; P45686; -.
DR   Proteomes; UP000009102; Chromosome.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.190.10; -; 1.
DR   InterPro; IPR000894; RuBisCO_sc_dom.
DR   InterPro; IPR036385; RuBisCO_ssu_sf.
DR   Pfam; PF00101; RuBisCO_small; 1.
DR   SMART; SM00961; RuBisCO_small; 1.
DR   SUPFAM; SSF55239; SSF55239; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calvin cycle; Carbon dioxide fixation;
KW   Complete proteome; Lyase; Monooxygenase; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    110       Ribulose bisphosphate carboxylase small
FT                                chain.
FT                                /FTId=PRO_0000198631.
FT   TURN         15     18       {ECO:0000244|PDB:1SVD}.
FT   HELIX        24     36       {ECO:0000244|PDB:1SVD}.
FT   STRAND       40     46       {ECO:0000244|PDB:1SVD}.
FT   HELIX        48     50       {ECO:0000244|PDB:1SVD}.
FT   STRAND       57     60       {ECO:0000244|PDB:1SVD}.
FT   HELIX        69     82       {ECO:0000244|PDB:1SVD}.
FT   STRAND       86     94       {ECO:0000244|PDB:1SVD}.
FT   TURN         95     98       {ECO:0000244|PDB:1SVD}.
FT   STRAND       99    107       {ECO:0000244|PDB:1SVD}.
SQ   SEQUENCE   110 AA;  12855 MW;  9C4F1AB8D29B104D CRC64;
     MAEMQDYKQS LKYETFSYLP PMNAERIRAQ IKYAIAQGWS PGIEHVEVKN SMNQYWYMWK
     LPFFGEQNVD NVLAEIEACR SAYPTHQVKL VAYDNYAQSL GLAFVVYRGN
//
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