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Database: UniProt/TrEMBL
Entry: A0A0G3G5C2_9GAMM
LinkDB: A0A0G3G5C2_9GAMM
Original site: A0A0G3G5C2_9GAMM 
ID   A0A0G3G5C2_9GAMM        Unreviewed;       474 AA.
AC   A0A0G3G5C2;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   25-OCT-2017, entry version 15.
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:AKJ95574.1};
GN   Synonyms=cbbL {ECO:0000256|HAMAP-Rule:MF_01338};
GN   ORFNames=TVD_09485 {ECO:0000313|EMBL:AKJ95574.1};
OS   Thioalkalivibrio versutus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=106634 {ECO:0000313|EMBL:AKJ95574.1, ECO:0000313|Proteomes:UP000064201};
RN   [1] {ECO:0000313|EMBL:AKJ95574.1, ECO:0000313|Proteomes:UP000064201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D301 {ECO:0000313|EMBL:AKJ95574.1,
RC   ECO:0000313|Proteomes:UP000064201};
RA   Mu T., Zhou J., Xu X.;
RT   "Complete Sequence for the Genome of the Thioalkalivibrio versutus
RT   D301.";
RL   Submitted (APR-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; CP011367; AKJ95574.1; -; Genomic_DNA.
DR   RefSeq; WP_018144355.1; NZ_CP011367.1.
DR   EnsemblBacteria; AKJ95574; AKJ95574; TVD_09485.
DR   GeneID; 29523696; -.
DR   KEGG; tvr:TVD_09485; -.
DR   PATRIC; fig|106634.4.peg.1943; -.
DR   KO; K01601; -.
DR   Proteomes; UP000064201; 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   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   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:UP000064201};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000313|EMBL:AKJ95574.1};
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       18    138       RuBisCO_large_N. {ECO:0000259|Pfam:
FT                                PF02788}.
FT   DOMAIN      148    456       RuBisCO_large. {ECO:0000259|Pfam:
FT                                PF00016}.
FT   ACT_SITE    169    169       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   ACT_SITE    288    288       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   METAL       195    195       Magnesium; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   METAL       197    197       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   METAL       198    198       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     117    117       Substrate; in homodimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   BINDING     167    167       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     171    171       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     289    289       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     321    321       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     373    373       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   SITE        328    328       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   MOD_RES     195    195       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01338}.
SQ   SEQUENCE   474 AA;  53065 MW;  6F1AA2266F2448C2 CRC64;
     MSAAKKYSAG VKDYRETYWM PEYTPLDTDL LACFKITPQP GIDREEAAAA VAAESSTGTW
     TTVWTDLLTD MDYYKGRAYM IEDVPGDDES FYAFIAYPID LFEEGSMVNV FTSLVGNVFG
     FKAIRMLRLE DVRFPIAYVK TCGGPPMGIQ VERDRLNKYG RPMLGCTIKP KLGLSAKNYG
     RAVYECLRGG LDFTKDDENI NSQPFMRWRD RFDFVQEATE KAEAETGERK GHYLNVTAPT
     PEEMYKRAEY AKEIGAPIIM HDYITGGFCA NTGLANWCRD NGMLLHIHRA MHAVIDRHPK
     HGIHFRVLAK ILRLSGGDHL HTGTVVGKLE GDRAATLGWI DLLRESFIPE DRSRGIFFDQ
     DWGSMPGVFA VASGGIHVWH MPALVAIFGD DSVLQFGGGT LGHPWGNAPG ATANRVAVEA
     CVQARNEGRE IEKEGKEILT QAAQHSPELK IAMETWKEIK FEFDTTDKLD VQHK
//
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