RBLL2_RHOPA
ID RBLL2_RHOPA Reviewed; 432 AA.
AC Q6ND47;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Ribulose bisphosphate carboxylase-like protein 2;
DE Short=RuBisCO-like protein;
GN Name=rlp2; OrderedLocusNames=RPA0262;
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=258594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009;
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA Harrison F.H., Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
CC -!- FUNCTION: May be involved in sulfur metabolism and oxidative stress
CC response. Does not show RuBisCO activity (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type IV
CC subfamily. {ECO:0000305}.
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; BX572593; CAE25706.1; -; Genomic_DNA.
DR RefSeq; WP_011155830.1; NC_005296.1.
DR PDB; 2QYG; X-ray; 3.30 A; A/B/C/D=1-432.
DR PDBsum; 2QYG; -.
DR AlphaFoldDB; Q6ND47; -.
DR SMR; Q6ND47; -.
DR STRING; 258594.RPA0262; -.
DR PRIDE; Q6ND47; -.
DR EnsemblBacteria; CAE25706; CAE25706; RPA0262.
DR GeneID; 66891271; -.
DR KEGG; rpa:RPA0262; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_3_0_5; -.
DR OMA; AHFPFIA; -.
DR PhylomeDB; Q6ND47; -.
DR BioCyc; RPAL258594:TX73_RS01360-MON; -.
DR EvolutionaryTrace; Q6ND47; -.
DR Proteomes; UP000001426; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:InterPro.
DR GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR Gene3D; 3.20.20.110; -; 1.
DR Gene3D; 3.30.70.150; -; 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 PANTHER; PTHR42704; PTHR42704; 1.
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 1: Evidence at protein level;
KW 3D-structure; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..432
FT /note="Ribulose bisphosphate carboxylase-like protein 2"
FT /id="PRO_0000062683"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255"
FT BINDING 200
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 198
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255"
FT HELIX 4..9
FT /evidence="ECO:0007829|PDB:2QYG"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:2QYG"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:2QYG"
FT STRAND 21..32
FT /evidence="ECO:0007829|PDB:2QYG"
FT HELIX 34..45
FT /evidence="ECO:0007829|PDB:2QYG"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:2QYG"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:2QYG"
FT STRAND 91..101
FT /evidence="ECO:0007829|PDB:2QYG"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:2QYG"
FT HELIX 109..116
FT /evidence="ECO:0007829|PDB:2QYG"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:2QYG"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:2QYG"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:2QYG"
FT HELIX 151..159
FT /evidence="ECO:0007829|PDB:2QYG"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:2QYG"
FT HELIX 180..192
FT /evidence="ECO:0007829|PDB:2QYG"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:2QYG"
FT HELIX 211..229
FT /evidence="ECO:0007829|PDB:2QYG"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:2QYG"
FT HELIX 245..255
FT /evidence="ECO:0007829|PDB:2QYG"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:2QYG"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:2QYG"
FT HELIX 270..277
FT /evidence="ECO:0007829|PDB:2QYG"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:2QYG"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:2QYG"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:2QYG"
FT HELIX 304..314
FT /evidence="ECO:0007829|PDB:2QYG"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:2QYG"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:2QYG"
FT HELIX 332..343
FT /evidence="ECO:0007829|PDB:2QYG"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:2QYG"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:2QYG"
FT HELIX 365..372
FT /evidence="ECO:0007829|PDB:2QYG"
FT TURN 383..387
FT /evidence="ECO:0007829|PDB:2QYG"
FT HELIX 392..407
FT /evidence="ECO:0007829|PDB:2QYG"
FT HELIX 412..416
FT /evidence="ECO:0007829|PDB:2QYG"
FT HELIX 420..428
FT /evidence="ECO:0007829|PDB:2QYG"
SQ SEQUENCE 432 AA; 46464 MW; 1C02E95D7430C620 CRC64;
MTPDDIAGFY AKRADLDLDN YIELDFDFEC AGDPHEAAAH LCSEQSTAQW RRVGFDEDFR
PRFAAKVLEL SAEPRPSGFS VPVECAARGP VHACRVTIAH PHGNFGAKIP NLLSAVCGEG
VFFSPGIPLI RLQDIRFPEP YLAAFDGPRF GIAGVRERLQ AFDRPIFFGV IKPNIGLPPQ
PFAELGYQSW TGGLDIAKDD EMLADVDWCP LAERAALLGD ACRRASAETG VPKIYLANIT
DEVDRLTELH DVAVANGAGA LLINAMPVGL SAVRMLRKHA TVPLIAHFPF IAAFSRLANY
GIHSRVMTRL QRLAGFDVVI MPGFGPRMMT PEHEVLDCIR ACLEPMGPIK PCLPVPGGSD
SAATLENVYR KVGSADFGFV PGRGVFGHPM GPAAGATSIR QAWDAIAAGI PVPDHAASHP
ELAAALRAFG GR
