Ribulose bisphosphate carboxylase large chain - Rhizobium meliloti (strain 1021) (Ensifer meliloti)

Contribute

Send feedback

Read comments (?) or add your own

P58348 (RBL1_RHIME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 75. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ribulose bisphosphate carboxylase large chain
Short name=RuBisCO large subunit
EC=4.1.1.39

Gene names

Name:	cbbL
Ordered Locus Names:	RB0191
ORF Names:	SMb20198

Encoded on

Plasmid pSymB (megaplasmid 2)

Organism

Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

266834 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

Protein attributes

Sequence length	486 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site By similarity. HAMAP MF_01338
Catalytic activity	2 3-phospho-D-glycerate + 2 H⁺ = D-ribulose 1,5-bisphosphate + CO₂ + H₂O. HAMAP MF_01338 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O₂. HAMAP MF_01338
Cofactor	Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01338
Subunit structure	Heterohexadecamer of 8 large chains and 8 small chains By similarity.
Miscellaneous	The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric "cap" on each end of the "barrel" By similarity. HAMAP MF_01338
Sequence similarities	Belongs to the RuBisCO large chain family. Type I subfamily.

Ontologies

Keywords
Biological process	Calvin cycle Carbon dioxide fixation
Ligand	Magnesium Metal-binding
Molecular function	Lyase Monooxygenase Oxidoreductase
Technical term	Complete proteome Plasmid
Gene Ontology (GO)
Biological process	reductive pentose-phosphate cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	plastid Inferred from electronic annotation. Source: InterPro
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: InterPro monooxygenase activity Inferred from electronic annotation. Source: UniProtKB-KW ribulose-bisphosphate carboxylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 486

486

Ribulose bisphosphate carboxylase large chain HAMAP MF_01338

PRO_0000062643

Sites

Active site

178

Proton acceptor By similarity

Active site

296

Proton acceptor By similarity

Metal binding

204

Magnesium; via carbamate group By similarity

Metal binding

206

Magnesium By similarity

Metal binding

207

Magnesium By similarity

Binding site

126

Substrate; in homodimeric partner By similarity

Binding site

176

Substrate By similarity

Binding site

180

Substrate By similarity

Binding site

297

Substrate By similarity

Binding site

329

Substrate By similarity

Binding site

381

Substrate By similarity

Site

336

Transition state stabilizer By similarity

Amino acid modifications

Modified residue

204

N6-carboxylysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P58348 [UniParc].

Last modified November 16, 2001. Version 1.
Checksum: 4386CA656929EC5F
Show »

FASTA

486

53,791

        10         20         30         40         50         60 
MNADAKTEIK GRERYKAGVL KYAQMGYWNG DYEPKDTDLI ALFRITPQDG VDPIEAAAAV 

        70         80         90        100        110        120 
AGESSTATWT VVWTDRLTAC DQYRAKAYRV DPVPGTPGQY FCYVAYDLIL FEEGSIANLT 

       130        140        150        160        170        180 
ASIIGNVFSF KPLKAARLED MRLPVAYVKT FRGPPTGIVV ERERLDKFGK PLLGATTKPK 

       190        200        210        220        230        240 
LGLSGKNYGR VVYEGLKGGL DFMKDDENIN SQPFMHWRDR YLYCMEAVNH ASAVTGEVKG 

       250        260        270        280        290        300 
HYLNITAGTM EEMYRRAEFA KELGSVIVMV DLIVGWTAIQ SISEWCRQND MILHMHRAGH 

       310        320        330        340        350        360 
GTYTRQKNHG ISFRVIAKWL RLAGVDHLHA GTAVGKLEGD PPTVQGYYNV CREMKNEVDL 

       370        380        390        400        410        420 
PRGLFFEQDW ADLKKVMPVA SGGIHAGQMH QLLDLFGDDV VLQFGGGTIG HPMGIQAGAT 

       430        440        450        460        470        480 
ANRVALEAMV LARNEGRDIA HEGPEILRAA AKWCKPLEAA LDIWGNISFN YTPTDTSDFV 


PSVTAA

« Hide

References

[1]	"The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing endosymbiont Sinorhizobium meliloti." Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J., Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A. Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001) [PubMed: 11481431] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.
[2]	"The composite genome of the legume symbiont Sinorhizobium meliloti." Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. Batut J. Science 293:668-672(2001) [PubMed: 11474104] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591985 Genomic DNA. Translation: CAC48591.1.
PIR	G95865.
RefSeq	NP_436731.1. NC_003078.1.
3D structure databases
ProteinModelPortal	P58348.
SMR	P58348. Positions 7-480.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1236522.
GenomeReviews	Gene locus RB0191 in contig AL591985_GR.
KEGG	sme:SM_b20198.
NMPDR	fig\|266834.1.peg.4826.
PATRIC	23636771. VBISinMel96828_5107.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG405441.
OMA	HRAMHAA.
ProtClustDB	PRK04208.
Enzyme and pathway databases
BioCyc	SMEL266834:SMB20198-MONOMER.
Family and domain databases
HAMAP	MF_01338. RuBisCO_L_type1. [Tree]
InterPro	IPR020878. RuBisCo_large_chain_AS. IPR020888. RuBisCO_lsu. IPR000685. RuBisCO_lsu_C. IPR017443. RuBisCO_lsu_fd_N. IPR017444. RuBisCO_lsu_N. [Graphical view]
Gene3D	G3DSA:3.20.20.110. RuBisCO_large. 1 hit. G3DSA:3.30.70.150. RuBisCO_large. 1 hit.
KO	K01601.
Pfam	PF00016. RuBisCO_large. 1 hit. PF02788. RuBisCO_large_N. 1 hit. [Graphical view]
SUPFAM	SSF51649. RuBisCO_large. 1 hit. SSF54966. RuBisCO_large. 1 hit.
PROSITE	PS00157. RUBISCO_LARGE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RBL1_RHIME

Accession

Primary (citable) accession number: P58348

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 16, 2001
Last sequence update:	November 16, 2001
Last modified:	January 25, 2012
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents