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Database: UniProt/SWISS-PROT
Entry: RBL1_HALNC
LinkDB: RBL1_HALNC
Original site: RBL1_HALNC 
ID   RBL1_HALNC              Reviewed;         473 AA.
AC   O85040; D0KZ92;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-OCT-2017, entry version 94.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000255|HAMAP-Rule:MF_01338};
DE            Short=RuBisCO large subunit {ECO:0000255|HAMAP-Rule:MF_01338};
DE            EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338};
GN   Name=cbbL {ECO:0000255|HAMAP-Rule:MF_01338};
GN   OrderedLocusNames=Hneap_0922;
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], AND EXPRESSION.
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. {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose
CC       1,5-bisphosphate + CO(2) + H(2)O. {ECO:0000255|HAMAP-
CC       Rule:MF_01338}.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
CC       D-ribulose 1,5-bisphosphate + O(2). {ECO:0000255|HAMAP-
CC       Rule:MF_01338}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01338};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01338};
CC   -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC       {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- INDUCTION: Produced when grown in air or in air supplemented with
CC       5% CO(2).
CC   -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC       chain homodimer in a "head-to-tail" conformation. In form I
CC       RuBisCO this homodimer is arranged in a barrel-like tetramer with
CC       the small subunits forming a tetrameric "cap" on each end of the
CC       "barrel". {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}.
DR   EMBL; AF038430; AAC32549.1; -; Genomic_DNA.
DR   EMBL; CP001801; ACX95765.1; -; Genomic_DNA.
DR   RefSeq; WP_012823801.1; NC_013422.1.
DR   PDB; 1SVD; X-ray; 1.80 A; A=1-473.
DR   PDBsum; 1SVD; -.
DR   ProteinModelPortal; O85040; -.
DR   SMR; O85040; -.
DR   STRING; 555778.Hneap_0922; -.
DR   EnsemblBacteria; ACX95765; ACX95765; Hneap_0922.
DR   KEGG; hna:Hneap_0922; -.
DR   eggNOG; ENOG4105DT1; Bacteria.
DR   eggNOG; COG1850; LUCA.
DR   HOGENOM; HOG000230831; -.
DR   KO; K01601; -.
DR   OMA; EYRETYW; -.
DR   OrthoDB; POG091H14UZ; -.
DR   BioCyc; HNEA555778:GIVV-951-MONOMER; -.
DR   BRENDA; 4.1.1.39; 6349.
DR   EvolutionaryTrace; O85040; -.
DR   Proteomes; UP000009102; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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   CDD; cd08212; RuBisCO_large_I; 1.
DR   Gene3D; 3.20.20.110; -; 1.
DR   Gene3D; 3.30.70.150; -; 1.
DR   HAMAP; MF_01338; RuBisCO_L_type1; 1.
DR   InterPro; IPR033966; RuBisCO.
DR   InterPro; IPR020878; RuBisCo_large_chain_AS.
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   InterPro; IPR020888; RuBisCO_lsuI.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SFLD; SFLDS00014; RuBisCO; 1.
DR   SUPFAM; SSF51649; SSF51649; 1.
DR   SUPFAM; SSF54966; SSF54966; 1.
DR   PROSITE; PS00157; RUBISCO_LARGE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calvin cycle; Carbon dioxide fixation;
KW   Complete proteome; Lyase; Magnesium; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN         1    473       Ribulose bisphosphate carboxylase large
FT                                chain.
FT                                /FTId=PRO_0000062660.
FT   ACT_SITE    168    168       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   ACT_SITE    287    287       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   METAL       194    194       Magnesium; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   METAL       196    196       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   METAL       197    197       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     116    116       Substrate; in homodimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   BINDING     166    166       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     170    170       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     288    288       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     320    320       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     372    372       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   SITE        327    327       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   MOD_RES     194    194       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   STRAND       28     37       {ECO:0000244|PDB:1SVD}.
FT   HELIX        43     53       {ECO:0000244|PDB:1SVD}.
FT   TURN         54     56       {ECO:0000244|PDB:1SVD}.
FT   HELIX        63     67       {ECO:0000244|PDB:1SVD}.
FT   TURN         70     72       {ECO:0000244|PDB:1SVD}.
FT   STRAND       76     83       {ECO:0000244|PDB:1SVD}.
FT   STRAND       86     96       {ECO:0000244|PDB:1SVD}.
FT   HELIX        98    100       {ECO:0000244|PDB:1SVD}.
FT   HELIX       106    114       {ECO:0000244|PDB:1SVD}.
FT   HELIX       117    119       {ECO:0000244|PDB:1SVD}.
FT   STRAND      123    132       {ECO:0000244|PDB:1SVD}.
FT   HELIX       135    138       {ECO:0000244|PDB:1SVD}.
FT   HELIX       148    155       {ECO:0000244|PDB:1SVD}.
FT   STRAND      162    166       {ECO:0000244|PDB:1SVD}.
FT   STRAND      170    172       {ECO:0000244|PDB:1SVD}.
FT   HELIX       175    187       {ECO:0000244|PDB:1SVD}.
FT   STRAND      191    194       {ECO:0000244|PDB:1SVD}.
FT   STRAND      200    202       {ECO:0000244|PDB:1SVD}.
FT   HELIX       207    225       {ECO:0000244|PDB:1SVD}.
FT   STRAND      230    234       {ECO:0000244|PDB:1SVD}.
FT   HELIX       240    253       {ECO:0000244|PDB:1SVD}.
FT   STRAND      257    261       {ECO:0000244|PDB:1SVD}.
FT   TURN        262    265       {ECO:0000244|PDB:1SVD}.
FT   HELIX       267    280       {ECO:0000244|PDB:1SVD}.
FT   STRAND      283    287       {ECO:0000244|PDB:1SVD}.
FT   HELIX       291    295       {ECO:0000244|PDB:1SVD}.
FT   STRAND      300    302       {ECO:0000244|PDB:1SVD}.
FT   HELIX       304    314       {ECO:0000244|PDB:1SVD}.
FT   STRAND      317    320       {ECO:0000244|PDB:1SVD}.
FT   HELIX       329    331       {ECO:0000244|PDB:1SVD}.
FT   HELIX       333    343       {ECO:0000244|PDB:1SVD}.
FT   STRAND      345    347       {ECO:0000244|PDB:1SVD}.
FT   HELIX       351    353       {ECO:0000244|PDB:1SVD}.
FT   STRAND      368    374       {ECO:0000244|PDB:1SVD}.
FT   HELIX       377    379       {ECO:0000244|PDB:1SVD}.
FT   HELIX       380    387       {ECO:0000244|PDB:1SVD}.
FT   STRAND      389    394       {ECO:0000244|PDB:1SVD}.
FT   HELIX       397    400       {ECO:0000244|PDB:1SVD}.
FT   HELIX       406    425       {ECO:0000244|PDB:1SVD}.
FT   TURN        430    433       {ECO:0000244|PDB:1SVD}.
FT   HELIX       434    442       {ECO:0000244|PDB:1SVD}.
FT   HELIX       446    455       {ECO:0000244|PDB:1SVD}.
SQ   SEQUENCE   473 AA;  52636 MW;  B84D2EDE46CAF7D8 CRC64;
     MAVKKYSAGV KEYRQTYWMP EYTPLDSDIL ACFKITPQPG VDREEAAAAV AAESSTGTWT
     TVWTDLLTDM DYYKGRAYRI EDVPGDDAAF YAFIAYPIDL FEEGSVVNVF TSLVGNVFGF
     KAVRGLRLED VRFPLAYVKT CGGPPHGIQV ERDKMNKYGR PLLGCTIKPK LGLSAKNYGR
     AVYECLRGGL DFTKDDENIN SQPFMRWRDR FLFVQDATET AEAQTGERKG HYLNVTAPTP
     EEMYKRAEFA KEIGAPIIMH DYITGGFTAN TGLAKWCQDN GVLLHIHRAM HAVIDRNPNH
     GIHFRVLTKI LRLSGGDHLH TGTVVGKLEG DRASTLGWID LLRESFIPED RSRGIFFDQD
     WGSMPGVFAV ASGGIHVWHM PALVNIFGDD SVLQFGGGTL GHPWGNAAGA AANRVALEAC
     VEARNQGRDI EKEGKEILTA AAQHSPELKI AMETWKEIKF EFDTVDKLDT QNR
//
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