RBLL_ALLVD
ID RBLL_ALLVD Reviewed; 457 AA.
AC Q93UZ0; D3RP65;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Ribulose bisphosphate carboxylase-like protein;
DE Short=RuBisCO-like protein;
GN OrderedLocusNames=Alvin_2545; ORFNames=ORF457;
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16245138; DOI=10.1023/a:1021280104053;
RA Nagashima S., Shimada K., Matsuura K., Nagashima K.V.P.;
RT "Transcription of three sets of genes coding for the core light-harvesting
RT proteins in the purple sulfur bacterium, Allochromatium vinosum.";
RL Photosyn. Res. 74:269-280(2002).
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).
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 -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type IV
CC subfamily. {ECO:0000305}.
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DR EMBL; AB050620; BAB44150.1; -; Genomic_DNA.
DR EMBL; CP001896; ADC63455.1; -; Genomic_DNA.
DR RefSeq; WP_012971724.1; NC_013851.1.
DR AlphaFoldDB; Q93UZ0; -.
DR SMR; Q93UZ0; -.
DR STRING; 572477.Alvin_2545; -.
DR EnsemblBacteria; ADC63455; ADC63455; Alvin_2545.
DR KEGG; alv:Alvin_2545; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_3_1_6; -.
DR OMA; AHFPFIA; -.
DR OrthoDB; 848380at2; -.
DR Proteomes; UP000001441; 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; IPR036422; RuBisCO_lsu_N_sf.
DR PANTHER; PTHR42704; PTHR42704; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR SFLD; SFLDS00014; RuBisCO; 1.
DR SUPFAM; SSF51649; SSF51649; 1.
DR SUPFAM; SSF54966; SSF54966; 1.
PE 3: Inferred from homology;
KW Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..457
FT /note="Ribulose bisphosphate carboxylase-like protein"
FT /id="PRO_0000062681"
FT REGION 426..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 199
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 199
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 457 AA; 49562 MW; 42CD47B503185D38 CRC64;
MTASDWAGFF ADEASLDREA YLFLDYYLEC SGDPELAAAH FCSEQSTAQW RRVGSDEDLR
PRFGARVVDL QILDGARPEF SYGVGSGSDA PVTACRLRIA HPHGNFGPRL PNLLSAICGE
GTFFSPGAPI VKLLDIEFPE SYLACFQGPQ FGVAGLRERL QVHDRPIFFG VIKPNIGLPP
EAFSELGHES WLGGLDIAKD DEMLADTDWC PLDRRAELLG EARRRAEAAT GVPKIYLANI
TDEVDRLVEL HDRAVERGAN ALLINAMPTG LSAVRMLRKH AQVPLMAHFP FIAPFARLER
FGVHTRVFTK LQRLAGYDVI IMPGFGPRMH MTDDEVRACA TACLEPMGPI KPSLPVPGGS
DWAGTLRPLY EKLGTVDFGF VPGRGVFGHP MGPRAGAASI RQAWEAIVAG ETLEERAKRH
PELSAAIAAF GKPAHGQAAS PQPSEQASEP DAAGGDS