Ribulose bisphosphate carboxylase large chain - Nostoc sp. (strain PCC 7120 / UTEX 2576)

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P00879 (RBL_NOSS1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 103. 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
Short name=RuBisCO large subunit
EC=4.1.1.39

Gene names

Name:	cbbL
Synonyms:	rbc, rbcA, rbcL
Ordered Locus Names:	alr1524

Organism

Nostoc sp. (strain PCC 7120 / UTEX 2576) [Complete proteome] [HAMAP]

Taxonomic identifier

103690 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Nostoc

Protein attributes

Sequence length	476 AA.
Sequence status	Complete.
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 in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site By similarity. 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.
Mass spectrometry	Molecular mass is 53411 Da from positions 1 - 476. Determined by MALDI. Ref.4

Ontologies

Keywords
Biological process	Calvin cycle Carbon dioxide fixation Photorespiration 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	photorespiration Inferred from electronic annotation. Source: UniProtKB-KW 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

Chain

1 – 476

476

Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338

PRO_0000062619

Sites

Active site

176

Proton acceptor By similarity

Active site

295

Proton acceptor By similarity

Metal binding

202

Magnesium; via carbamate group By similarity

Metal binding

204

Magnesium By similarity

Metal binding

205

Magnesium By similarity

Binding site

124

Substrate; in homodimeric partner By similarity

Binding site

174

Substrate By similarity

Binding site

178

Substrate By similarity

Binding site

296

Substrate By similarity

Binding site

328

Substrate By similarity

Binding site

380

Substrate By similarity

Site

335

Transition state stabilizer By similarity

Amino acid modifications

Modified residue

202

N6-carboxylysine By similarity

Disulfide bond

248

Interchain; in linked form By similarity

Experimental info

Sequence conflict

V → G in AAA22041. Ref.1

Sequence conflict

V → G in AAA22024. Ref.2

Sequence conflict

V → G in AAA22027. Ref.2

Sequence conflict

V → G in AAA22028. Ref.2

Sequence conflict

F → S in AAA22041. Ref.1

Sequence conflict

F → S in AAA22024. Ref.2

Sequence conflict

F → S in AAA22027. Ref.2

Sequence conflict

F → S in AAA22028. Ref.2

Sequence conflict

120

S → Y in AAA22041. Ref.1

Sequence conflict

120

S → Y in AAA22024. Ref.2

Sequence conflict

120

S → Y in AAA22027. Ref.2

Sequence conflict

120

S → Y in AAA22028. Ref.2

Sequence conflict

127

G → V in AAA22041. Ref.1

Sequence conflict

127

G → V in AAA22024. Ref.2

Sequence conflict

127

G → V in AAA22027. Ref.2

Sequence conflict

127

G → V in AAA22028. Ref.2

Sequence conflict

279

T → N in AAA22041. Ref.1

Sequence conflict

279

T → N in AAA22024. Ref.2

Sequence conflict

279

T → N in AAA22027. Ref.2

Sequence conflict

279

T → N in AAA22028. Ref.2

Sequence conflict

290

V → L in AAA22041. Ref.1

Sequence conflict

290

V → L in AAA22024. Ref.2

Sequence conflict

290

V → L in AAA22027. Ref.2

Sequence conflict

290

V → L in AAA22028. Ref.2

Sequence conflict

399

S → F in AAA22041. Ref.1

Sequence conflict

399

S → F in AAA22024. Ref.2

Sequence conflict

399

S → F in AAA22027. Ref.2

Sequence conflict

399

S → F in AAA22028. Ref.2

Sequence conflict

416

P → R in AAA22041. Ref.1

Sequence conflict

416

P → R in AAA22024. Ref.2

Sequence conflict

416

P → R in AAA22027. Ref.2

Sequence conflict

416

P → R in AAA22028. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P00879 [UniParc].

Last modified January 23, 2002. Version 3.
Checksum: ABEDB246FA2E6A01
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FASTA

476

53,045

        10         20         30         40         50         60 
MSYAQTKTQT KSGYKAGVQD YRLTYYTPDY TPKDTDILAA FRVTPQPGVP FEEAAAAVAA 

        70         80         90        100        110        120 
ESSTGTWTTV WTDLLTDLDR YKGRCYDIEP VPGEDNQFIA YIAYPLDLFE EGSITNVLTS 

       130        140        150        160        170        180 
IVGNVFGFKA LRALRLEDIR FPVAYIKTFQ GPPHGIQVER DKLNKYGRPL LGCTIKPKLG 

       190        200        210        220        230        240 
LSAKNYGRAV YECLRGGLDF TKDDENINSA PFQRWRDRFL FVADAITKAQ AETGEIKGHY 

       250        260        270        280        290        300 
LNVTAPTCEE MLKRAEYAKE LKQPIIMHDY LTAGFTANTT LARWCRDNGV LLHIHRAMHA 

       310        320        330        340        350        360 
VIDRQKNHGI HFRVLAKALR LSGGDHIHTG TVVGKLEGER GITMGFVDLL RENYVEQDKS 

       370        380        390        400        410        420 
RGIYFTQDWA SLPGVMAVAS GGIHVWHMPA LVEIFGDDSV LQFGGGTLGH PWGNAPGATA 

       430        440        450        460        470 
NRVALEACVQ ARNEGRNLAR EGNDVIREAA KWSPELAVAC ELWKEIKFEF EAMDTV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and sequence of the gene for the large subunit of ribulose-1,5-bisphosphate carboxylase from the cyanobacterium Anabaena 7120." Curtis S.E., Haselkorn R. Proc. Natl. Acad. Sci. U.S.A. 80:1835-1839(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Cotranscription of genes encoding the small and large subunits of ribulose-1,5-bisphosphate carboxylase in the cyanobacterium Anabaena 7120." Nierzwicki-Bauer S.A., Curtis S.E., Haselkorn R. Proc. Natl. Acad. Sci. U.S.A. 81:5961-5965(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
[3]	"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120." Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. , Takazawa M., Yamada M., Yasuda M., Tabata S. DNA Res. 8:205-213(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 7120 / UTEX 2576.
[4]	Singh H., Rajaram H., Apte S.K. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 16-22, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J01540 Genomic DNA. Translation: AAA22041.1. L02520 Genomic DNA. Translation: AAA22024.1. L02521 Genomic DNA. Translation: AAA22027.1. L02522 Genomic DNA. Translation: AAA22028.1. BA000019 Genomic DNA. Translation: BAB77890.1.
PIR	RKAIL7. A01099. AF1996.
RefSeq	NP_485564.1. NC_003272.1.
3D structure databases
ProteinModelPortal	P00879.
SMR	P00879. Positions 13-470.
ModBase	Search...
Protein-protein interaction databases
STRING	103690.alr1524.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB77890; BAB77890; BAB77890.
GeneID	1105116.
KEGG	ana:alr1524.
PATRIC	22773054. VBINosSp37423_2010.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1850.
HOGENOM	HOG000230831.
KO	K01601.
OMA	FTQDWAS.
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

RBL_NOSS1

Accession

Primary (citable) accession number: P00879
Secondary accession number(s): Q60124

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2002
Last modified:	May 1, 2013
This is version 103 of the entry and version 3 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

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents