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Database: UniProt/SWISS-PROT
Entry: RBL1B_ALLVD
LinkDB: RBL1B_ALLVD
Original site: RBL1B_ALLVD 
ID   RBL1B_ALLVD             Reviewed;         471 AA.
AC   P22859; D3RQ48;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 4.
DT   28-FEB-2018, entry version 114.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain 2 {ECO:0000255|HAMAP-Rule:MF_01338};
DE            Short=RuBisCO large subunit 2 {ECO:0000255|HAMAP-Rule:MF_01338};
DE            EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338};
GN   Name=cbbL2 {ECO:0000255|HAMAP-Rule:MF_01338};
GN   Synonyms=rbcL {ECO:0000255|HAMAP-Rule:MF_01338};
GN   OrderedLocusNames=Alvin_2750;
OS   Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 /
OS   NCIMB 10441 / D) (Chromatium vinosum).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Chromatiaceae; Allochromatium.
OX   NCBI_TaxID=572477;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1899846; DOI=10.1016/0378-1119(91)90009-Z;
RA   Kobayashi H., Viale A.M., Takabe T., Akazawa T., Wada K.,
RA   Shinozaki K., Kobayashi K., Sugiura M.;
RT   "Sequence and expression of genes encoding the large and small
RT   subunits of ribulose 1,5-bisphosphate carboxylase/oxygenase from
RT   Chromatium vinosum.";
RL   Gene 97:55-62(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX   PubMed=22675582; DOI=10.4056/sigs.2335270;
RA   Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA   Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT   "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL   Stand. Genomic Sci. 5:311-330(2011).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-26.
RX   PubMed=2211708;
RA   Viale A.M., Kobayashi H., Akazawa T.;
RT   "Distinct properties of Escherichia coli products of plant-type
RT   ribulose-1,5-bisphosphate carboxylase/oxygenase directed by two sets
RT   of genes from the photosynthetic bacterium Chromatium vinosum.";
RL   J. Biol. Chem. 265:18386-18392(1990).
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. {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       disulfide-linked. The disulfide link is formed within the large
CC       subunit homodimers. {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- PTM: The disulfide bond which can form in the large chain dimeric
CC       partners within the hexadecamer appears to be associated with
CC       oxidative stress and protein turnover. {ECO:0000255|HAMAP-
CC       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:0000255|HAMAP-Rule:MF_01338}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- CAUTION: In C.vinosum two similar set of genes code for RuBisCO
CC       large and small chains: the RbcL-RbcS and the RbcA-RbcB sets.
CC       Under standard photoautotrophic culture conditions only the latter
CC       set seems active, the former probably being cryptic.
CC       {ECO:0000305}.
DR   EMBL; D90204; BAA14229.1; -; Genomic_DNA.
DR   EMBL; CP001896; ADC63659.1; -; Genomic_DNA.
DR   PIR; JQ0586; RKKRL2.
DR   RefSeq; WP_012971927.1; NC_013851.1.
DR   ProteinModelPortal; P22859; -.
DR   SMR; P22859; -.
DR   STRING; 572477.Alvin_2750; -.
DR   EnsemblBacteria; ADC63659; ADC63659; Alvin_2750.
DR   KEGG; alv:Alvin_2750; -.
DR   eggNOG; ENOG4105DT1; Bacteria.
DR   eggNOG; COG1850; LUCA.
DR   HOGENOM; HOG000230831; -.
DR   KO; K01601; -.
DR   OMA; GGGTQGH; -.
DR   OrthoDB; POG091H14UZ; -.
DR   BioCyc; AVIN572477:G1GHE-2784-MONOMER; -.
DR   Proteomes; UP000001441; 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   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   Calvin cycle; Carbon dioxide fixation; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; Lyase; Magnesium;
KW   Metal-binding; Monooxygenase; Oxidoreductase; Photosynthesis;
KW   Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:2211708}.
FT   CHAIN         2    471       Ribulose bisphosphate carboxylase large
FT                                chain 2.
FT                                /FTId=PRO_0000062622.
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   DISULFID    240    240       Interchain; in linked form.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   CONFLICT    145    145       P -> R (in Ref. 1; BAA14229).
FT                                {ECO:0000305}.
FT   CONFLICT    222    222       Q -> R (in Ref. 1; BAA14229).
FT                                {ECO:0000305}.
FT   CONFLICT    297    297       N -> H (in Ref. 1; BAA14229).
FT                                {ECO:0000305}.
SQ   SEQUENCE   471 AA;  52284 MW;  08A26940B6458D97 CRC64;
     MSTKTYDAGV KDYALTYWTP DYVPLDSDLL ACFKVTPQAK VSREEAAAAV AAESSTGTWT
     TVWSDLLTDL DYYKGRAYRI EDVPGDKESF YAFIAYPLDL FEEGSIVNVL TSLVGNVFGF
     KAVRALRLED IRFPLHYVKT CGGPPNGIQV ERDRMDKYGR PFLGATVKPK LGLSAKNYGR
     AVYEMLRGGL DFTKDDENVN SQPFMRWQNR FEFVSEAVRK AQEETGERKG HYLNVTAPTC
     EEMFKRAEFA KECGAPIIMH DFLTGGFTAN TSLANWCRDN GMLLHIHRAM HAVIDRNPKH
     GIHFRVLAKC LRLSGGDHLH TGTVVGKLEG DRQSTLGFVD QLRESFIPED RSRGLFFDQD
     WGGMPGVMAV ASGGIHVWHI PALVTIFGDD SVLQFGGGTQ GHPWGNAAGA AANRVATEAC
     VKARNEGVEI EKHAREVLSD AARHSPELAV AMETWKEIKF EFDVVDKLDA A
//
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