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A2SJJ7

- RBL1B_METPP

UniProt

A2SJJ7 - RBL1B_METPP

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Protein

Ribulose bisphosphate carboxylase large chain 2

Gene

cbbL2

Organism
Methylibium petroleiphilum (strain PM1)
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

Binds 1 magnesium ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei125 – 1251Substrate; in homodimeric partnerUniRule annotation
Binding sitei175 – 1751SubstrateUniRule annotation
Active sitei177 – 1771Proton acceptorUniRule annotation
Binding sitei179 – 1791SubstrateUniRule annotation
Metal bindingi203 – 2031Magnesium; via carbamate groupUniRule annotation
Metal bindingi205 – 2051MagnesiumUniRule annotation
Metal bindingi206 – 2061MagnesiumUniRule annotation
Active sitei295 – 2951Proton acceptorUniRule annotation
Binding sitei296 – 2961SubstrateUniRule annotation
Binding sitei328 – 3281SubstrateUniRule annotation
Sitei335 – 3351Transition state stabilizerUniRule annotation
Binding sitei380 – 3801SubstrateUniRule 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, Photosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMPET420662:GHBE-2816-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain 2UniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCO large subunit 2UniRule annotation
Gene namesi
Name:cbbL2UniRule annotation
Ordered Locus Names:Mpe_A2782
OrganismiMethylibium petroleiphilum (strain PM1)
Taxonomic identifieri420662 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesMethylibium
ProteomesiUP000000366: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 485485Ribulose bisphosphate carboxylase large chain 2PRO_0000299965Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei203 – 2031N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains.UniRule annotation

Protein-protein interaction databases

STRINGi420662.Mpe_A2782.

Structurei

3D structure databases

ProteinModelPortaliA2SJJ7.
SMRiA2SJJ7. Positions 23-466.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OrthoDBiEOG6ZKXMS.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1.
InterProiIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
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.

A2SJJ7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNEPTQITDT KKRYAAGVLK YAQMGYWNGD YVPKDTDILA LFRITPQDGV
60 70 80 90 100
DPIEAAAAVA GESSTATWTV VWTDRLTACD MYRAKAYKVE PVPNNPGQYF
110 120 130 140 150
CYVAYDLSLF EEGSIANVTA SIIGNVFSFK PLKAARLEDM KFPVSYVKTF
160 170 180 190 200
AGPPTGIVVE RERLDKFGRP LLGATTKPKL GLSGRNYGRV VYEGLKGGLD
210 220 230 240 250
FMKDDENINS QPFMHWRDRF LFVMDAVNKA SAATGEVKGS YLNVTAGTME
260 270 280 290 300
EMYRRAEFAK ELGSVIIMID LVVGYTAIQS MSNWARQNDM VLHMHRAGHG
310 320 330 340 350
TYTRQKNHGV SFRVIAKWLR MAGVDHLHTG TAVGKLEGDP LTVQGYYNVC
360 370 380 390 400
RDTHTKVDLP RGIFFDQDWG ALKKVMPVAS GGIHAGQMHQ LIDLFGDDVV
410 420 430 440 450
LQFGGGTIGH PQGIQAGATA NRVALEAMVL ARNEGRDIKN EGPQILRDAA
460 470 480
KSCTPLAAAL DTWGDITFNY TSTDTSDYVP TPSVA
Length:485
Mass (Da):53,310
Last modified:September 11, 2007 - v2
Checksum:i3B36C71F79F2FCAD
GO

Sequence cautioni

The sequence ABM95736.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000555 Genomic DNA. Translation: ABM95736.1. Different initiation.
RefSeqiYP_001021971.1. NC_008825.1.

Genome annotation databases

EnsemblBacteriaiABM95736; ABM95736; Mpe_A2782.
GeneIDi4785032.
KEGGimpt:Mpe_A2782.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000555 Genomic DNA. Translation: ABM95736.1 . Different initiation.
RefSeqi YP_001021971.1. NC_008825.1.

3D structure databases

ProteinModelPortali A2SJJ7.
SMRi A2SJJ7. Positions 23-466.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 420662.Mpe_A2782.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABM95736 ; ABM95736 ; Mpe_A2782 .
GeneIDi 4785032.
KEGGi mpt:Mpe_A2782.

Phylogenomic databases

eggNOGi COG1850.
HOGENOMi HOG000230831.
KOi K01601.
OrthoDBi EOG6ZKXMS.

Enzyme and pathway databases

BioCyci MPET420662:GHBE-2816-MONOMER.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01338. RuBisCO_L_type1.
InterProi IPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
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. "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-proteobacterium Methylibium petroleiphilum PM1."
    Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., Hristova K.R.
    J. Bacteriol. 189:1931-1945(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PM1.

Entry informationi

Entry nameiRBL1B_METPP
AccessioniPrimary (citable) accession number: A2SJJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: October 1, 2014
This is version 48 of the entry and version 2 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 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".UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3