ID A0A076HNC8_9SYNE Unreviewed; 471 AA.
AC A0A076HNC8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 25-OCT-2017, entry version 22.
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 Synonyms=rbcL {ECO:0000256|HAMAP-Rule:MF_01338};
GN ORFNames=KR52_13200 {ECO:0000313|EMBL:AII50082.1};
OS Synechococcus sp. KORDI-52.
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=585425 {ECO:0000313|EMBL:AII50082.1, ECO:0000313|Proteomes:UP000028593};
RN [1] {ECO:0000313|EMBL:AII50082.1, ECO:0000313|Proteomes:UP000028593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KORDI-52 {ECO:0000313|EMBL:AII50082.1,
RC ECO:0000313|Proteomes:UP000028593};
RA Choi D.H., Kwon K.-K., Lee J.-H., Noh J.H.;
RT "Genome sequence of Synechococcus sp. KORDI-52.";
RL Submitted (JUN-2013) 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 in the photorespiration process. Both reactions occur
CC simultaneously and in competition at the same active site.
CC {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 https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP006271; AII50082.1; -; Genomic_DNA.
DR RefSeq; WP_011363747.1; NZ_CP006271.1.
DR ProteinModelPortal; A0A076HNC8; -.
DR SMR; A0A076HNC8; -.
DR EnsemblBacteria; AII50082; AII50082; KR52_13200.
DR KEGG; synd:KR52_13200; -.
DR KO; K01601; -.
DR Proteomes; UP000028593; 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: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; 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:UP000028593};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000313|EMBL:AII50082.1};
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 Photorespiration {ECO:0000256|HAMAP-Rule:MF_01338}.
FT DOMAIN 15 136 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 471 AA; 52832 MW; C9D5CF9DAFD6B97D CRC64;
MSKKYDAGVK EYRDTYWTPD YVPLDTDLLA CFKCTGQEGV PKEEVAAAVA AESSTGTWST
VWSELLTDLD FYKGRCYRIE DVPGDKESFY AFIAYPLDLF EEGSITNVLT SLVGNVFGFK
ALRHLRLEDI RFPMAFIKSC YGPPNGIQVE RDRMNKYGRP LLGCTIKPKL GLSGKNYGRV
VYECLRGGLD FTKDDENINS QPFQRWQNRF EFVAEAIKLS EQETGERKGH YLNVTANTPE
EMYERAEFAK ELGMPIIMHD FITGGFTANT GLSKWCRKNG MLLHIHRAMH AVIDRHPKHG
IHFRVLAKCL RLSGGDQLHT GTVVGKLEGD RQTTLGYIDQ LRESFVPEDR SRGNFFDQDW
GSMPGVFAVA SGGIHVWHMP ALVTIFGDDS VLQFGGGTHG HPWGSAAGAA ANRVALEACV
KARNAGRHLE KESRDILTEA AKHSPELAIA LETWKEIKFE FDTVDKLDVQ N
//
