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P04718

- RBL2_RHORU

UniProt

P04718 - RBL2_RHORU

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Protein

Ribulose bisphosphate carboxylase

Gene

cbbM

Organism
Rhodospirillum rubrum
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.
3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.

Cofactori

Binds 1 magnesium ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei111 – 1111Substrate; in homodimeric partner
Active sitei166 – 1661Proton acceptor
Binding sitei168 – 1681Substrate
Metal bindingi191 – 1911Magnesium; via carbamate group
Metal bindingi193 – 1931Magnesium
Metal bindingi194 – 1941Magnesium
Active sitei287 – 2871Proton acceptor
Binding sitei288 – 2881Substrate
Binding sitei321 – 3211Substrate
Sitei329 – 3291Transition state stabilizer
Binding sitei368 – 3681Substrate

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. monooxygenase activity Source: UniProtKB-KW
  3. ribulose-bisphosphate carboxylase activity Source: CACAO

GO - Biological processi

  1. reductive pentose-phosphate cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation, Photosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13280.
SABIO-RKP04718.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase (EC:4.1.1.39)
Short name:
RuBisCO
Gene namesi
Name:cbbM
Synonyms:cbbL2, rbpL
OrganismiRhodospirillum rubrum
Taxonomic identifieri1085 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 466466Ribulose bisphosphate carboxylasePRO_0000062666Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei191 – 1911N6-carboxylysine1 Publication

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

IntActiP04718. 1 interaction.
MINTiMINT-8090212.

Structurei

Secondary structure

1
466
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 63
Helixi14 – 207
Beta strandi23 – 3210
Beta strandi34 – 363
Helixi38 – 4811
Turni49 – 513
Beta strandi70 – 756
Turni76 – 794
Beta strandi80 – 867
Helixi87 – 893
Turni94 – 963
Helixi101 – 1099
Helixi111 – 1133
Beta strandi116 – 12712
Helixi130 – 1334
Helixi143 – 1508
Beta strandi154 – 1563
Beta strandi160 – 1645
Beta strandi166 – 1694
Helixi173 – 18311
Turni184 – 1863
Beta strandi188 – 1914
Beta strandi197 – 1993
Helixi204 – 22219
Beta strandi227 – 2315
Helixi237 – 25115
Helixi252 – 2576
Beta strandi258 – 2636
Turni264 – 2663
Helixi269 – 27810
Beta strandi284 – 2874
Turni289 – 2913
Helixi292 – 2954
Beta strandi301 – 3033
Helixi305 – 31511
Beta strandi318 – 3214
Helixi336 – 3449
Beta strandi346 – 3494
Beta strandi354 – 3563
Beta strandi364 – 3696
Turni373 – 3753
Helixi376 – 3838
Beta strandi389 – 3924
Turni394 – 3974
Helixi403 – 41917
Helixi423 – 4286
Helixi431 – 4399
Helixi441 – 4477
Helixi451 – 4555

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RBAX-ray2.60A/B1-466[»]
1RUSX-ray2.90A/B1-466[»]
2RUSX-ray2.30A/B1-466[»]
5RUBX-ray1.70A/B1-466[»]
9RUBX-ray2.60A/B1-466[»]
ProteinModelPortaliP04718.
SMRiP04718. Positions 2-460.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04718.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01339. RuBisCO_L_type2.
InterProiIPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04718-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDQSSRYVNL ALKEEDLIAG GEHVLCAYIM KPKAGYGYVA TAAHFAAESS
60 70 80 90 100
TGTNVEVCTT DDFTRGVDAL VYEVDEAREL TKIAYPVALF HRNITDGKAM
110 120 130 140 150
IASFLTLTMG NNQGMGDVEY AKMHDFYVPE AYRALFDGPS VNISALWKVL
160 170 180 190 200
GRPEVDGGLV VGTIIKPKLG LRPKPFAEAC HAFWLGGDFI KNDEPQGNQP
210 220 230 240 250
FAPLRDTIAL VADAMRRAQD ETGEAKLFSA NITADDPFEI IARGEYVLET
260 270 280 290 300
FGENASHVAL LVDGYVAGAA AITTARRRFP DNFLHYHRAG HGAVTSPQSK
310 320 330 340 350
RGYTAFVHCK MARLQGASGI HTGTMGFGKM EGESSDRAIA YMLTQDEAQG
360 370 380 390 400
PFYRQSWGGM KACTPIISGG MNALRMPGFF ENLGNANVIL TAGGGAFGHI
410 420 430 440 450
DGPVAGARSL RQAWQAWRDG VPVLDYAREH KELARAFESF PGDADQIYPG
460
WRKALGVEDT RSALPA
Length:466
Mass (Da):50,504
Last modified:August 13, 1987 - v1
Checksum:i37D8C0076CAF7D54
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X00286 Genomic DNA. Translation: CAA25080.1.
PIRiS07295.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X00286 Genomic DNA. Translation: CAA25080.1 .
PIRi S07295.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RBA X-ray 2.60 A/B 1-466 [» ]
1RUS X-ray 2.90 A/B 1-466 [» ]
2RUS X-ray 2.30 A/B 1-466 [» ]
5RUB X-ray 1.70 A/B 1-466 [» ]
9RUB X-ray 2.60 A/B 1-466 [» ]
ProteinModelPortali P04718.
SMRi P04718. Positions 2-460.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P04718. 1 interaction.
MINTi MINT-8090212.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-13280.
SABIO-RK P04718.

Miscellaneous databases

EvolutionaryTracei P04718.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01339. RuBisCO_L_type2.
InterProi IPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view ]
Pfami PF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view ]
SUPFAMi SSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEi PS00157. RUBISCO_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Nucleotide sequence of the ribulosebisphosphate carboxylase gene from Rhodospirillum rubrum."
    Nargang F., McIntosh L., Somerville C.R.
    Mol. Gen. Genet. 193:220-224(1984)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Isolation and sequencing of an active-site peptide from Rhodospirillum rubrum ribulosebisphosphate carboxylase/oxygenase after affinity labeling with 2-[(bromoacetyl)amino]pentitol 1,5-bisphosphate."
    Fraij B., Hartman F.C.
    Biochemistry 22:1515-1520(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 314-337.
  3. "Three-dimensional structure of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum at 2.9-A resolution."
    Schneider G., Lindqvist Y., Braenden C.-I., Lorimer G.
    EMBO J. 5:3409-3415(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
  4. "Crystal structure of the active site of ribulose-bisphosphate carboxylase."
    Andersson I., Knight S., Schneider G., Lindqvist Y., Lundqvist T., Braenden C.-I., Lorimer G.H.
    Nature 337:229-234(1989)
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
  5. "Crystallographic refinement and structure of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum at 1.7-A resolution."
    Schneider G., Lindqvist Y., Lundqvist T.
    J. Mol. Biol. 211:989-1008(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
  6. "Crystal structure of the ternary complex of ribulose-1,5-bisphosphate carboxylase, Mg(II), and activator CO2 at 2.3-A resolution."
    Lundqvist T., Schneider G.
    Biochemistry 30:904-908(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), COFACTOR, SUBUNIT, CARBAMYLATION AT LYS-191.

Entry informationi

Entry nameiRBL2_RHORU
AccessioniPrimary (citable) accession number: P04718
Secondary accession number(s): P19365, P72313
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: October 1, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits (By similarity).By similarity

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3