Ribulose bisphosphate carboxylase large chain 2 - Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / D)

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P22859 (RBL1B_ALLVD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 88. History...

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

Documents (1) |

Third-party data

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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 2
Short name=RuBisCO large subunit 2
EC=4.1.1.39

Gene names

Name:	cbbL2
Synonyms:	rbcL
Ordered Locus Names:	Alvin_2750

Organism

Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / D) (Chromatium vinosum) [Complete proteome] [HAMAP]

Taxonomic identifier

572477 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Chromatiaceae › Allochromatium ›

Protein attributes

Sequence length	471 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

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. HAMAP-Rule MF_01338
Catalytic activity	2 3-phospho-D-glycerate + 2 H⁺ = D-ribulose 1,5-bisphosphate + CO₂ + H₂O. HAMAP-Rule MF_01338 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O₂. HAMAP-Rule MF_01338
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Subunit structure	Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers By similarity.
Post-translational modification	The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover By similarity. HAMAP-Rule MF_01338
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-Rule MF_01338
Sequence similarities	Belongs to the RuBisCO large chain family. Type I subfamily.
Caution	In C.vinosum two similar set of genes code for RuBisCO large and small chains: the RbcL-RbcS and the RbcA-RbcB sets. Under standard photoautotrophic culture conditions only the latter set seems active, the former probably being cryptic.

Ontologies

Keywords
Biological process	Calvin cycle Carbon dioxide fixation Photosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Lyase Monooxygenase Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological_process	reductive pentose-phosphate cycle Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP monooxygenase activity Inferred from electronic annotation. Source: UniProtKB-KW ribulose-bisphosphate carboxylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3

Chain

2 – 471

470

Ribulose bisphosphate carboxylase large chain 2 HAMAP-Rule MF_01338

PRO_0000062622

Sites

Active site

168

Proton acceptor By similarity

Active site

287

Proton acceptor By similarity

Metal binding

194

Magnesium; via carbamate group By similarity

Metal binding

196

Magnesium By similarity

Metal binding

197

Magnesium By similarity

Binding site

116

Substrate; in homodimeric partner By similarity

Binding site

166

Substrate By similarity

Binding site

170

Substrate By similarity

Binding site

288

Substrate By similarity

Binding site

320

Substrate By similarity

Binding site

372

Substrate By similarity

Site

327

Transition state stabilizer By similarity

Amino acid modifications

Modified residue

194

N6-carboxylysine By similarity

Disulfide bond

240

Interchain; in linked form By similarity

Experimental info

Sequence conflict

145

P → R in BAA14229. Ref.1

Sequence conflict

222

Q → R in BAA14229. Ref.1

Sequence conflict

297

N → H in BAA14229. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P22859 [UniParc].

Last modified June 15, 2010. Version 4.
Checksum: 08A26940B6458D97
Show »

FASTA

471

52,284

        10         20         30         40         50         60 
MSTKTYDAGV KDYALTYWTP DYVPLDSDLL ACFKVTPQAK VSREEAAAAV AAESSTGTWT 

        70         80         90        100        110        120 
TVWSDLLTDL DYYKGRAYRI EDVPGDKESF YAFIAYPLDL FEEGSIVNVL TSLVGNVFGF 

       130        140        150        160        170        180 
KAVRALRLED IRFPLHYVKT CGGPPNGIQV ERDRMDKYGR PFLGATVKPK LGLSAKNYGR 

       190        200        210        220        230        240 
AVYEMLRGGL DFTKDDENVN SQPFMRWQNR FEFVSEAVRK AQEETGERKG HYLNVTAPTC 

       250        260        270        280        290        300 
EEMFKRAEFA KECGAPIIMH DFLTGGFTAN TSLANWCRDN GMLLHIHRAM HAVIDRNPKH 

       310        320        330        340        350        360 
GIHFRVLAKC LRLSGGDHLH TGTVVGKLEG DRQSTLGFVD QLRESFIPED RSRGLFFDQD 

       370        380        390        400        410        420 
WGGMPGVMAV ASGGIHVWHI PALVTIFGDD SVLQFGGGTQ GHPWGNAAGA AANRVATEAC 

       430        440        450        460        470 
VKARNEGVEI EKHAREVLSD AARHSPELAV AMETWKEIKF EFDVVDKLDA A

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and expression of genes encoding the large and small subunits of ribulose 1,5-bisphosphate carboxylase/oxygenase from Chromatium vinosum." Kobayashi H., Viale A.M., Takabe T., Akazawa T., Wada K., Shinozaki K., Kobayashi K., Sugiura M. Gene 97:55-62(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete sequence of chromosome of Allochromatium vinosum DSM 180." US DOE Joint Genome Institute Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Zigann R., Dahl C., Woyke T. Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 17899 / DSM 180 / NBRC 103801 / D.
[3]	"Distinct properties of Escherichia coli products of plant-type ribulose-1,5-bisphosphate carboxylase/oxygenase directed by two sets of genes from the photosynthetic bacterium Chromatium vinosum." Viale A.M., Kobayashi H., Akazawa T. J. Biol. Chem. 265:18386-18392(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-26.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D90204 Genomic DNA. Translation: BAA14229.1. CP001896 Genomic DNA. Translation: ADC63659.1.
PIR	RKKRL2. JQ0586.
RefSeq	YP_003444691.1. NC_013851.1.
3D structure databases
ProteinModelPortal	P22859.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ADC63659; ADC63659; Alvin_2750.
GeneID	8788139.
KEGG	alv:Alvin_2750.
PATRIC	31925280. VBIAllVin64954_2712.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000230831.
KO	K01601.
ProtClustDB	PRK04208.
Family and domain databases
Gene3D	3.20.20.110. 1 hit. 3.30.70.150. 1 hit.
HAMAP	MF_01338. RuBisCO_L_type1.
InterPro	IPR020878. RuBisCo_large_chain_AS. IPR020888. RuBisCO_lsu. IPR000685. RuBisCO_lsu_C. IPR017443. RuBisCO_lsu_fd_N. IPR017444. RuBisCO_lsu_N. [Graphical view]
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

RBL1B_ALLVD

Accession

Primary (citable) accession number: P22859
Secondary accession number(s): D3RQ48

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	June 15, 2010
Last modified:	May 1, 2013
This is version 88 of the entry and version 4 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

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents