Ribulose bisphosphate carboxylase large chain 1 - Nitrobacter winogradskyi (strain Nb-255 / ATCC 25391)

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Reviewed, UniProtKB/Swiss-Prot Q3SR45 (RBL1A_NITWN)

Last modified January 19, 2010. Version 33. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Ribulose bisphosphate carboxylase large chain 1
      Short name=RuBisCO large subunit 1
    EC=4.1.1.39

Gene names

Name:	cbbL1
Ordered Locus Names:	Nwi_1987

Organism

Nitrobacter winogradskyi (strain Nb-255 / ATCC 25391) [Complete proteome] [HAMAP]

Taxonomic identifier

323098 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Nitrobacter

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Protein attributes

Sequence length	473 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

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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. HAMAP 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 MF_01338
Sequence similarities	Belongs to the RuBisCO large chain family. Type I subfamily.

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Ontologies

Keywords
Biological process	Calvin cycle Carbon dioxide fixation
Ligand	Magnesium Metal-binding
Molecular function	Lyase Monooxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW 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: UniProtKB-KW monooxygenase activity Inferred from electronic annotation. Source: UniProtKB-KW ribulose-bisphosphate carboxylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 473

473

Ribulose bisphosphate carboxylase large chain 1 HAMAP MF_01338

PRO_0000251451

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

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Sequences

Sequence

Length

Mass (Da)

Tools

Q3SR45-1 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: DF83FC650BCEFA82
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FASTA

473

52,677

        10         20         30         40         50         60 
MAVKSYQAGV TQYRQSYWQP DYMPLDTDIL ACFKITPQPG VDREEAAAAV AAESSCGTWT 

        70         80         90        100        110        120 
TVWTDLLTDL DYYKGRAYRL EDVPGDDTCY YAFIAYPIDL FEEGSVVNVF TSLVGNVFGF 

       130        140        150        160        170        180 
KAVRALRLED LRFPIAYVKT CGGPPHGIQV ERDKLNKYGR PLLGCTIKPK LGLSAKNYGR 

       190        200        210        220        230        240 
ACYEALRGGL DFTKDDENIN SQPFMRWRDR FDFVMEAVQK AEQETGERKG HYLNVTAPTP 

       250        260        270        280        290        300 
EEMYKRAEYA KEIRAPIIMH DYLAGGLCAN AGLANWCRNN GMLLHIHRAM HAVIDRNPHH 

       310        320        330        340        350        360 
GIHFRVLTKI LRLSGGDHLH TGTVVGKLEG DRASTLGWID LLRESFVPED RSRGIFFDQD 

       370        380        390        400        410        420 
WGSMPGGFAV ASGGIHVWHM PALVTIFGDD SVLQFGGGTL GHPWGNAAGA HANRVALEAC 

       430        440        450        460        470 
VQARGEGRHL EKEGKDILTA AAAHSPELKI AMETWKEIKF EFETMDKLAI ANK

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References

[1]

"Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium Nitrobacter winogradskyi Nb-255."
Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L., Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J., Hickey W.J.
Appl. Environ. Microbiol. 72:2050-2063(2006) [PubMed: 16517654] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000115 Genomic DNA. Translation: ABA05246.1.
RefSeq	YP_318598.1.
3D structure databases
HSSP	HSSP built from PDB template 1SVD based on UniProtKB O85040.
SMR	Q3SR45. Positions 16-460.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3SR45.
Genome annotation databases
GeneID	3674251.
GenomeReviews	Gene locus Nwi_1987 in contig CP000115_GR.
KEGG	nwi:Nwi_1987.
NMPDR	fig\|323098.3.peg.1324.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1850.
HOGENOM	HBG405441.
OMA	YTPDYTP.
Enzyme and pathway databases
BioCyc	NWIN323098:NWI_1987-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.
Pfam	PF00016. RuBisCO_large. 1 hit. PF02788. RuBisCO_large_N. 1 hit. [Graphical view]
PROSITE	PS00157. RUBISCO_LARGE. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

RBL1A_NITWN

Accession

Primary (citable) accession number: Q3SR45

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	October 11, 2005
Last modified:	January 19, 2010
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

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

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents