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Entry: A0A167A533_9GAMM
LinkDB: A0A167A533_9GAMM
Original site: A0A167A533_9GAMM 
ID   A0A167A533_9GAMM        Unreviewed;       470 AA.
AC   A0A167A533;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-SEP-2017, entry version 9.
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=rbcL {ECO:0000313|EMBL:ANB01502.1};
GN   Synonyms=cbbL {ECO:0000256|HAMAP-Rule:MF_01338};
GN   ORFNames=ECTOBSL9_0621 {ECO:0000313|EMBL:ANB01502.1};
OS   Ectothiorhodospira sp. BSL-9.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Ectothiorhodospira.
OX   NCBI_TaxID=1442136 {ECO:0000313|EMBL:ANB01502.1, ECO:0000313|Proteomes:UP000076772};
RN   [1] {ECO:0000313|EMBL:ANB01502.1, ECO:0000313|Proteomes:UP000076772}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSL-9 {ECO:0000313|EMBL:ANB01502.1,
RC   ECO:0000313|Proteomes:UP000076772};
RA   Saltikov C., Conrad A., Hernandez J., Stoneburner B., Oremland R.,
RA   Rosen M., Miller L., McCann-Hoeft S., Pourmand N., Bernick D.;
RT   "The arx anaerobic arsenite-oxidization pathway is conserved in
RT   Halomonas and Ectothiorhodospira strains isolated from Big Soda Lake,
RT   Nevada.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP011994; ANB01502.1; -; Genomic_DNA.
DR   RefSeq; WP_063463833.1; NZ_CP011994.1.
DR   EnsemblBacteria; ANB01502; ANB01502; ECTOBSL9_0621.
DR   KEGG; ebs:ECTOBSL9_0621; -.
DR   PATRIC; fig|1442136.6.peg.634; -.
DR   KO; K01601; -.
DR   Proteomes; UP000076772; 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; IPR017443; RuBisCO_lsu_fd_N.
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:UP000076772};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000313|EMBL:ANB01502.1};
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}.
FT   DOMAIN       16    136       RuBisCO_large_N. {ECO:0000259|Pfam:
FT                                PF02788}.
FT   DOMAIN      146    454       RuBisCO_large. {ECO:0000259|Pfam:
FT                                PF00016}.
FT   ACT_SITE    167    167       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   ACT_SITE    286    286       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   METAL       193    193       Magnesium; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   METAL       195    195       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   METAL       196    196       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     115    115       Substrate; in homodimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   BINDING     165    165       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     169    169       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     287    287       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     319    319       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     371    371       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   SITE        326    326       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   MOD_RES     193    193       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01338}.
SQ   SEQUENCE   470 AA;  52378 MW;  CFFB2E0DAB4B2FEC CRC64;
     MSKTYDAGVK EYRDMYWTPD YVPLDTDLLA CFKVTGQPGV PREEVAAAVA AESSTGTWST
     VWSELLTDLE YYKGRAYRIE DVPGDKESFY TFIAYPIDLF EEGSIVNVLT SLVGNVFGFK
     ALRHLRLEDI RFPIAYVKTC MGPPSGIQVE RDKLNKYGRP LLGCTIKPKL GLSAKNYGRA
     VYECLRGGLD FTKDDENVNS QPFMRWQNRF EFVAEAVAAS QQETGERKGH YLNVTAPDPE
     EMYARAEFAK ELGQPIIMHD YITGGFCANT GLAKWCRKNG MLLHIHRAMH AVIDRHPKHG
     IHFRVLAKCL RLSGGDHLHT GTVVGKLEGD RGSTLGFVDL LRESFIPEDR SRGIFFDQDW
     GSMPGVFAVA SGGIHVWHMP ALVTIFGDDS VLQFGGGTQG HPWGNAAGAA ANRVALEACV
     KARNEGREIE KEARDVLTEA ARHSPELAIA METWKEIKFE FETVDKLDQG
//
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