Ribulose bisphosphate carboxylase large chain

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O98949 (O98949_9RHOD) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 69. History...

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

Third-party data

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

Names and origin

Protein names

Recommended name:
Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
Short name=RuBisCO large subunit HAMAP-Rule MF_01338
EC=4.1.1.39 HAMAP-Rule MF_01338

Gene names

Name:

rbcL HAMAP-Rule MF_01338

Encoded on

Plastid; Chloroplast EMBL BAA75796.1

Organism

Galdieria partita EMBL BAA75796.1

Taxonomic identifier

83374 [NCBI]

Taxonomic lineage

Eukaryota › Rhodophyta › Bangiophyceae › Cyanidiales › Cyanidiaceae › Galdieria

Protein attributes

Sequence length	493 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. HAMAP-Rule MF_01338
Subunit structure	Heterohexadecamer of 8 large chains and 8 small chains By similarity. HAMAP-Rule MF_01338
Subcellular location	Plastid › chloroplast By similarity HAMAP-Rule MF_01338 RuleBase RU000303.
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. HAMAP-Rule MF_01338

Ontologies

Keywords
Biological process	Calvin cycle HAMAP-Rule MF_01338 Carbon dioxide fixation HAMAP-Rule MF_01338 Photorespiration HAMAP-Rule MF_01338 Photosynthesis HAMAP-Rule MF_01338 RuleBase RU004237
Cellular component	Chloroplast RuleBase RU000303 EMBL BAA75796.1 Plastid
Ligand	Magnesium HAMAP-Rule MF_01338 PDB 1BWV Metal-binding HAMAP-Rule MF_01338 PDB 1BWV
Molecular function	Lyase HAMAP-Rule MF_01338 Monooxygenase HAMAP-Rule MF_01338 Oxidoreductase
Technical term	3D-structure PDB 1BWV PDB 1IWA
Gene Ontology (GO)
Biological_process	photorespiration Inferred from electronic annotation. Source: UniProtKB-KW reductive pentose-phosphate cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
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

Sites

Active site

184

Proton acceptor By similarity HAMAP-Rule MF_01338

Active site

302

Proton acceptor By similarity HAMAP-Rule MF_01338

Metal binding

210

Magnesium PDB 1BWV

Metal binding

210

Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338

Metal binding

212

Magnesium PDB 1BWV

Metal binding

212

Magnesium By similarity HAMAP-Rule MF_01338

Metal binding

213

Magnesium PDB 1BWV

Metal binding

213

Magnesium By similarity HAMAP-Rule MF_01338

Binding site

132

Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338

Binding site

182

Substrate By similarity HAMAP-Rule MF_01338

Binding site

186

Substrate By similarity HAMAP-Rule MF_01338

Binding site

303

Substrate By similarity HAMAP-Rule MF_01338

Binding site

335

Substrate By similarity HAMAP-Rule MF_01338

Binding site

387

Substrate By similarity HAMAP-Rule MF_01338

Site

342

Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue

210

N6-carboxylysine PDB 1BWV

Modified residue

210

N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence

Length

Mass (Da)

Tools

O98949 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: FF86E3FF8C68C937
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FASTA

493

54,994

        10         20         30         40         50         60 
MSQSIEEKSV QERTRIKNSR YESGVIPYAK MGYWNPDYQV KDTDVLALFR VTPQPGVDPI 

        70         80         90        100        110        120 
EAAAAVAGES STATWTVVWT DLLTAADLYR AKAYKVDQVP NNPEQYFAYI AYELDLFEEG 

       130        140        150        160        170        180 
SIANLTASII GNVFGFKAVK ALRLEDMRLP LAYLKTFQGP ATGVILERER LDKFGRPLLG 

       190        200        210        220        230        240 
CTTKPKLGLS GKNYGRVVYE ALKGGLDFVK DDENINSQPF MRWRERYLFT MEAVNKASAA 

       250        260        270        280        290        300 
TGEVKGHYLN VTAATMEEMY ARANFAKELG SVIIMIDLVI GYTAIQTMAK WARDNDMILH 

       310        320        330        340        350        360 
LHRAGNSTYS RQKNHGMNFR VICKWMRMAG VDHIHAGTVV GKLEGDPIIT RGFYKTLLLP 

       370        380        390        400        410        420 
KLERNLQEGL FFDMEWASLR KVMPVASGGI HAGQMHQLIH YLGEDVVLQF GGGTIGHPDG 

       430        440        450        460        470        480 
IQAGATANRV ALEAMILARN ENRDYLTEGP EILREAAKTC GALRTALDLW KDITFNYTST 

       490 
DTSDFVETPT ANI

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References

[1]	"Structure and function study of ribulose-1,5-bisphosphate carboxylase/oxygenase of the red algae, Galdieria partita Tokara." Tomizawa K. Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[2]	"Crystal structure of carboxylase reaction-oriented ribulose 1, 5-bisphosphate carboxylase/oxygenase from a thermophilic red alga, Galdieria partita." Sugawara H., Yamamoto H., Shibata N., Inoue T., Okada S., Miyake C., Yokota A., Kai Y. J. Biol. Chem. 274:15655-15661(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, CARBOXYLATION AT LYS-210.
[3]	"X-ray structure of Galdieria Rubisco complexed with one sulfate ion per active site." Okano Y., Mizohata E., Xie Y., Matsumura H., Sugawara H., Inoue T., Yokota A., Kai Y. FEBS Lett. 527:33-36(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB018008 Genomic DNA. Translation: BAA75796.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BWV	X-ray	2.40	A/C/E/G	1-493	[»]
1IWA	X-ray	2.60	A/C/E/G/I/K/M/O	1-493	[»]

ProteinModelPortal

O98949.

SMR

O98949. Positions 14-486.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

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...

Other

EvolutionaryTrace

O98949.

Entry information

Entry name

O98949_9RHOD

Accession

Primary (citable) accession number: O98949

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 1999
Last sequence update:	May 1, 1999
Last modified:	April 3, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Family and domain databases

Other

Entry information