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Q2W3S5

- RBL2_MAGSA

UniProt

Q2W3S5 - RBL2_MAGSA

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Protein

Ribulose bisphosphate carboxylase

Gene

cbbM

Organism
Magnetospirillum magneticum (strain AMB-1 / ATCC 700264)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

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.UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg(2+) ion per subunit.UniRule annotation

Sites

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

GO - Molecular functioni

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

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

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMMAG342108:GJNU-2726-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylaseUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCOUniRule annotation
Gene namesi
Name:cbbMUniRule annotation
Ordered Locus Names:amb2696
OrganismiMagnetospirillum magneticum (strain AMB-1 / ATCC 700264)
Taxonomic identifieri342108 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeMagnetospirillum
ProteomesiUP000007058: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 459459Ribulose bisphosphate carboxylasePRO_0000251407Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei191 – 1911N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi342108.amb2696.

Structurei

3D structure databases

ProteinModelPortaliQ2W3S5.
SMRiQ2W3S5. Positions 2-457.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO large chain family. Type II subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiAKEHREF.
OrthoDBiEOG66QKT8.

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.

Q2W3S5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDQSKRYVNL GLREADLIKG GRHVLCAYRM RPRPGHGYVE TAAHFAAESS
60 70 80 90 100
TGTNVEVCTT DDFTRGVDAL VYEVDEAEGL MKIAYPVELF DRNIIDGKAM
110 120 130 140 150
IASFLTLTVG NNQGMSDVEN AKMEDFYVPP DFLTLFDGPA RNIAHMWKVL
160 170 180 190 200
GRPEVNGGMV VGTIIKPKLG LRPKPFADAC HQFWLGGDFI KNDEPQGNQV
210 220 230 240 250
FAPFKDTMRL VADSMRRAQD ETGQAKLFSA NITADDPAEM IARGQFILDT
260 270 280 290 300
FGENASHVAF LVDGFVAGPT AVTTCRRNFP DTFLHYHRAG HGAITSRQSK
310 320 330 340 350
RGYSVLVHMK MARLLGASGI HTGTMGYGKM EGAPDEKVVA YMLERPTAEG
360 370 380 390 400
PHYRQDWGDM RACTPIISGG MNALRLPGFF DNLGHSNVIQ TSGGGAFGHK
410 420 430 440 450
DGPVAGALSL RQAHEAWMRG ISLVEYAQGH PELRGAFESF ASDADRLYPG

WRDRLRIAA
Length:459
Mass (Da):50,349
Last modified:January 10, 2006 - v1
Checksum:i3A16B2EE0C3BABBB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007255 Genomic DNA. Translation: BAE51500.1.
RefSeqiYP_422059.1. NC_007626.1.

Genome annotation databases

EnsemblBacteriaiBAE51500; BAE51500; amb2696.
GeneIDi3802793.
KEGGimag:amb2696.
PATRICi22439648. VBIMagMag129836_2663.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007255 Genomic DNA. Translation: BAE51500.1 .
RefSeqi YP_422059.1. NC_007626.1.

3D structure databases

ProteinModelPortali Q2W3S5.
SMRi Q2W3S5. Positions 2-457.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 342108.amb2696.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAE51500 ; BAE51500 ; amb2696 .
GeneIDi 3802793.
KEGGi mag:amb2696.
PATRICi 22439648. VBIMagMag129836_2663.

Phylogenomic databases

eggNOGi COG1850.
HOGENOMi HOG000230831.
KOi K01601.
OMAi AKEHREF.
OrthoDBi EOG66QKT8.

Enzyme and pathway databases

BioCyci MMAG342108:GJNU-2726-MONOMER.

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. "Complete genome sequence of the facultative anaerobic magnetotactic bacterium Magnetospirillum sp. strain AMB-1."
    Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.
    DNA Res. 12:157-166(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AMB-1 / ATCC 700264.

Entry informationi

Entry nameiRBL2_MAGSA
AccessioniPrimary (citable) accession number: Q2W3S5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: January 10, 2006
Last modified: November 26, 2014
This is version 63 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.UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3