GenomeNet

Database: UniProt/TrEMBL
Entry: S6B5M5_9PROT
LinkDB: S6B5M5_9PROT
Original site: S6B5M5_9PROT 
ID   S6B5M5_9PROT            Unreviewed;       473 AA.
AC   S6B5M5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   25-OCT-2017, entry version 33.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|HAMAP-Rule:MF_01338};
DE            Short=RuBisCO large subunit {ECO:0000256|HAMAP-Rule:MF_01338};
DE            EC=4.1.1.39 {ECO:0000256|HAMAP-Rule:MF_01338};
GN   Name=cbbL {ECO:0000256|HAMAP-Rule:MF_01338,
GN   ECO:0000313|EMBL:BAN35842.1};
GN   ORFNames=SCD_n02031 {ECO:0000313|EMBL:BAN35842.1};
OS   Sulfuricella denitrificans skB26.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Gallionellaceae; Sulfuricella.
OX   NCBI_TaxID=1163617 {ECO:0000313|EMBL:BAN35842.1, ECO:0000313|Proteomes:UP000015559};
RN   [1] {ECO:0000313|EMBL:BAN35842.1, ECO:0000313|Proteomes:UP000015559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SkB26 {ECO:0000313|EMBL:BAN35842.1};
RX   PubMed=22773644; DOI=10.1128/AEM.01349-12;
RA   Watanabe T., Kojima H., Fukui M.;
RT   "Draft genome sequence of a psychrotolerant sulfur-oxidizing
RT   bacterium, Sulfuricella denitrificans skB26, and proteomic insights
RT   into cold adaptation.";
RL   Appl. Environ. Microbiol. 78:6545-6549(2012).
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:0000256|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:0000256|HAMAP-
CC       Rule:MF_01338}.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
CC       D-ribulose 1,5-bisphosphate + O(2). {ECO:0000256|HAMAP-
CC       Rule:MF_01338}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01338};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01338};
CC   -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC       {ECO:0000256|HAMAP-Rule:MF_01338}.
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:0000256|HAMAP-Rule:MF_01338}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01338}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01338}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AP013066; BAN35842.1; -; Genomic_DNA.
DR   RefSeq; WP_009205037.1; NC_022357.1.
DR   ProteinModelPortal; S6B5M5; -.
DR   EnsemblBacteria; BAN35842; BAN35842; SCD_n02031.
DR   KEGG; sdr:SCD_n02031; -.
DR   KO; K01601; -.
DR   OrthoDB; POG091H14UZ; -.
DR   Proteomes; UP000015559; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Calvin cycle {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Complete proteome {ECO:0000313|Proteomes:UP000015559};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000313|EMBL:BAN35842.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Monooxygenase {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015559}.
FT   DOMAIN       16    137       RuBisCO_large_N. {ECO:0000259|Pfam:
FT                                PF02788}.
FT   DOMAIN      147    455       RuBisCO_large. {ECO:0000259|Pfam:
FT                                PF00016}.
FT   ACT_SITE    168    168       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   ACT_SITE    287    287       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   METAL       194    194       Magnesium; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   METAL       196    196       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   METAL       197    197       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     116    116       Substrate; in homodimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   BINDING     166    166       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     170    170       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     288    288       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     320    320       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     372    372       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   SITE        327    327       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   MOD_RES     194    194       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01338}.
SQ   SEQUENCE   473 AA;  52710 MW;  19897BCB514100A0 CRC64;
     MAVKTYNAGV KEYRQTYWTP EYTPLDTDIL ACFKITPQAG VPREEVAAAV AAESSTGTWT
     TVWTDLLTDL DYYKGRAYRI EDVPGDDTCF YAFVAYPIDL FEEGSVVNVL TSLVGNVFGF
     KALRALRLED IRFPIAYVKT CGGPPQGIQV ERDKMNKYGR PMLGCTIKPK LGLSAKNYGR
     AVYECLRGGL DFTKDDENVN SQPFMRWRDR FEFVHEATMK AQRETGERKG HYLNVTAPTP
     EMMYERAEFA KEIGAPIIMH DYLTGGLTAN TGLANWCRKN GMLLHIHRAM HAVLDRNPHH
     GIHFRVLTKV LRLSGGDHLH SGTVVGKLEG DREATLGWID TMRDEFIKED RSRGLFFDQD
     WGSMPGVIPV ASGGIHVWHM PALVNIFGDD SVLQFGGGTL GHPWGNAAGA AANRVALEAS
     VAARNEGRNI EKEGKDILTK AAASSPELKI AMETWKEIKF EFDTVDKLDV AHK
//
DBGET integrated database retrieval system