ID D7A343_STAND Unreviewed; 489 AA. AC D7A343; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAR-2024, entry version 79. 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 OrderedLocusNames=Snov_0428 {ECO:0000313|EMBL:ADH87761.1}; OS Starkeya novella (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM OS 12100 / NBRC 12443 / NCIMB 10456). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Xanthobacteraceae; Ancylobacter. OX NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH87761.1, ECO:0000313|Proteomes:UP000006633}; RN [1] {ECO:0000313|EMBL:ADH87761.1, ECO:0000313|Proteomes:UP000006633} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC RC 12443 / NCIMB 10456 {ECO:0000313|Proteomes:UP000006633}; RX PubMed=23450099; DOI=10.4056/sigs.3006378; RA Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A., Copeland A., RA Berry K.W., Glavina Del Rio T., Hammon N., Dalin E., Tice H., Pitluck S., RA Richardson P., Bruce D., Goodwin L.A., Han C., Tapia R., Detter J.C., RA Chang Y.J., Jeffries C.D., Land M., Hauser L., Kyrpides N.C., Goker M., RA Ivanova N., Klenk H.P., Woyke T.; RT "Complete genome sequence of the facultatively chemolithoautotrophic and RT methylotrophic alpha Proteobacterium Starkeya novella type strain (ATCC RT 8093(T))."; RL Stand. Genomic Sci. 7:44-58(2012). 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 at CC the same active site. {ECO:0000256|HAMAP-Rule:MF_01338}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5- CC bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870, CC ChEBI:CHEBI:58272; EC=4.1.1.39; CC Evidence={ECO:0000256|ARBA:ARBA00001067, ECO:0000256|HAMAP- CC Rule:MF_01338}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate + CC 2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033, CC ChEBI:CHEBI:58272; Evidence={ECO:0000256|HAMAP-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-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 RuBisCO CC this homodimer is arranged in a barrel-like tetramer with the small CC subunits forming a tetrameric 'cap' on each end of the 'barrel'. CC {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 of CC 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 (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP002026; ADH87761.1; -; Genomic_DNA. DR RefSeq; WP_013165266.1; NC_014217.1. DR AlphaFoldDB; D7A343; -. DR STRING; 639283.Snov_0428; -. DR KEGG; sno:Snov_0428; -. DR eggNOG; COG1850; Bacteria. DR HOGENOM; CLU_031450_2_0_5; -. DR OrthoDB; 9764279at2; -. DR Proteomes; UP000006633; 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-UniRule. DR CDD; cd08212; RuBisCO_large_I; 1. DR Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1. DR Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 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 PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1. DR PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1. DR Pfam; PF00016; RuBisCO_large; 1. DR Pfam; PF02788; RuBisCO_large_N; 1. DR SFLD; SFLDG01052; RuBisCO; 1. DR SFLD; SFLDS00014; RuBisCO; 1. DR SFLD; SFLDG00301; RuBisCO-like_proteins; 1. DR SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1. DR SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1. DR PROSITE; PS00157; RUBISCO_LARGE; 1. PE 3: Inferred from homology; KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567, ECO:0000256|HAMAP- KW Rule:MF_01338}; KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP- KW Rule:MF_01338}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01338}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01338}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01338}; KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000256|HAMAP- KW Rule:MF_01338}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01338}. FT DOMAIN 29..149 FT /note="Ribulose bisphosphate carboxylase large subunit FT ferrodoxin-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF02788" FT DOMAIN 159..466 FT /note="Ribulose bisphosphate carboxylase large subunit C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF00016" FT ACT_SITE 180 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT ACT_SITE 298 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 128 FT /ligand="substrate" FT /note="in homodimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 178 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 182 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 206 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="via carbamate group" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 208 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 209 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 299 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 331 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 383 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT SITE 338 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT MOD_RES 206 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" SQ SEQUENCE 489 AA; 54138 MW; F62FCB0F0878F040 CRC64; MNAIDKTASA DKPRSRYSAG VMEYRKMGYW QPDYEPKDTD VIALFRVTPQ DGVDPIEASA AVAGESSTAT WTVVWTDRLT ACDKYRAKCY RVDPVPNSPG SWFAYIAYDL DLFEPGSISN LSASIIGNVF GFKPLKALRL EDMRLPVAYV KTFDGPATGI VVERERLDKF GRPLLGATVK PKLGLSGRNY GRVVYEALKG GLDFTKDDEN INSQPFMHWR ERFLYCMEAV NKAQASTGEI KGTYLNVTAG TMEDMYERAD FAKSLGSNIV MIDLVIGYTA IQSMAKWARR NDMILHLHRA GHSTYTRQKS HGVSFRVIAK WMRLAGVDHI HAGTVVGKLE GDPHTTKGYY DICRDDFVPQ NLAHGVFFDQ DWASTRKLMP VASGGIHAGQ MHQLIDLLGE DVVLQFGGGT IGHPMGIQAG ATANRVALEC MILARNEGRD ILAEGPDILN EAARHCMPLK QALETWKDVT FNYSSTDTPD FVPQATAAE //