ID RBL_PROMM Reviewed; 470 AA.
AC Q7V6F8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 28-FEB-2018, entry version 88.
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 Synonyms=rbcL {ECO:0000255|HAMAP-Rule:MF_01338};
GN OrderedLocusNames=PMT_1205;
OS Prochlorococcus marinus (strain MIT 9313).
OC Bacteria; Cyanobacteria; Synechococcales; Prochloraceae;
OC Prochlorococcus.
OX NCBI_TaxID=74547;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9313;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P.,
RA Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R.,
RA Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M.,
RA Shaw S.L., Steglich C., Sullivan M.B., Ting C.S., Tolonen A.,
RA Webb E.A., Zinser E.R., Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic
RT niche differentiation.";
RL Nature 424:1042-1047(2003).
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 in the photorespiration process. Both reactions occur
CC simultaneously and in competition at the same active site.
CC {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 -!- 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; BX548175; CAE21380.1; -; Genomic_DNA.
DR RefSeq; WP_011130576.1; NC_005071.1.
DR ProteinModelPortal; Q7V6F8; -.
DR SMR; Q7V6F8; -.
DR STRING; 74547.PMT1205; -.
DR EnsemblBacteria; CAE21380; CAE21380; PMT_1205.
DR KEGG; pmt:PMT_1205; -.
DR eggNOG; ENOG4105DT1; Bacteria.
DR eggNOG; COG1850; LUCA.
DR KO; K01601; -.
DR OMA; HRAMHAA; -.
DR OrthoDB; POG091H14UZ; -.
DR BioCyc; PMAR74547:G1G3N-1314-MONOMER; -.
DR Proteomes; UP000001423; 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:0009853; P:photorespiration; IEA:UniProtKB-KW.
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; 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.
PE 3: Inferred from homology;
KW Calvin cycle; Carbon dioxide fixation; Complete proteome; Lyase;
KW Magnesium; Metal-binding; Monooxygenase; Oxidoreductase;
KW Photorespiration; Photosynthesis; Reference proteome.
FT CHAIN 1 470 Ribulose bisphosphate carboxylase large
FT chain.
FT /FTId=PRO_0000062638.
FT ACT_SITE 167 167 Proton acceptor. {ECO:0000255|HAMAP-
FT Rule:MF_01338}.
FT ACT_SITE 286 286 Proton acceptor. {ECO:0000255|HAMAP-
FT Rule:MF_01338}.
FT METAL 193 193 Magnesium; via carbamate group.
FT {ECO:0000255|HAMAP-Rule:MF_01338}.
FT METAL 195 195 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_01338}.
FT METAL 196 196 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_01338}.
FT BINDING 115 115 Substrate; in homodimeric partner.
FT {ECO:0000255|HAMAP-Rule:MF_01338}.
FT BINDING 165 165 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_01338}.
FT BINDING 169 169 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_01338}.
FT BINDING 287 287 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_01338}.
FT BINDING 319 319 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_01338}.
FT BINDING 371 371 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_01338}.
FT SITE 326 326 Transition state stabilizer.
FT {ECO:0000255|HAMAP-Rule:MF_01338}.
FT MOD_RES 193 193 N6-carboxylysine. {ECO:0000255|HAMAP-
FT Rule:MF_01338}.
SQ SEQUENCE 470 AA; 52573 MW; 341368654FDD59C3 CRC64;
MSKKYDAGVK EYRDTYWTPD YVPLDTDLLA CFKCTGQEGV PREEVAAAVA AESSTGTWST
VWSELLTDLE FYKGRCYRIE DVPGDKESFY AFIAYPLDLF EEGSITNVLT SLVGNVFGFK
ALRHLRLEDI RFPMAFIKTC GGPPNGIVVE RDRLNKYGRP LLGCTIKPKL GLSGKNYGRV
VYECLRGGLD LTKDDENINS QPFQRWRERF EFVAEAVKLA QQETGEVKGH YLNCTATTPE
EMYERAEFAK ELDMPIIMHD YITGGFTANT GLANWCRKNG MLLHIHRAMH AVIDRHPKHG
IHFRVLAKCL RLSGGDQLHT GTVVGKLEGD RQTTLGYIDN LRESFVPEDR SRGNFFDQDW
GSMPGVFAVA SGGIHVWHMP ALLAIFGDDS CLQFGGGTHG HPWGSAAGAA ANRVALEACV
KARNAGREIE KESRDILMEA AKHSPELAIA LETWKEIKFE FDTVDKLDVQ
//
