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Q9ZI34

- RBL_BRADU

UniProt

Q9ZI34 - RBL_BRADU

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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Status
Reviewed - Annotation score: 4 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.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

Kineticsi

The CO2/O2 specificity factor (tau) is 75.

  1. KM=55 µM for ribulose 1,5-bisphosphate1 Publication
  2. KM=66 µM for CO21 Publication

Vmax=2.8 µmol/min/mg enzyme with CO2 as substrate1 Publication

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

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciBJAP224911:GJEJ-2608-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chainUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCO large subunitUniRule annotation
Gene namesi
Name:cbbLUniRule annotation
Ordered Locus Names:blr2585
OrganismiBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Taxonomic identifieri224911 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium
ProteomesiUP000002526: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 486486Ribulose bisphosphate carboxylase large chainPRO_0000062620Add
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

STRINGi224911.blr2585.

Structurei

3D structure databases

ProteinModelPortaliQ9ZI34.
SMRiQ9ZI34. Positions 13-479.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
InParanoidiQ9ZI34.
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.

Q9ZI34-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNAHTGTVRG KERYRSGVME YKRMGYWEPD YTPKDTDVIA LFRVTPQEGV
60 70 80 90 100
DPIEASAAVA GESSTATWTV VWTDRLTAAE KYRAKCHRVD PVPGTPGSYF
110 120 130 140 150
AYIAYDLDLF EPGSIANLSA SIIGNVFGFK PLKALRLEDM RFPVAYVKTF
160 170 180 190 200
QGPATGIVVE RERLDKFGRP LLGATVKPKL GLSGRNYGRV VYEALKGGLD
210 220 230 240 250
FTKDDENINS QPFMHWRDRF LYCIEAVNRA QAASGEVKGT YLNITAGTME
260 270 280 290 300
DMYERAEFAK ELGSCIVMID LVIGYTAIQS MAKWARRNDM ILHLHRAGHS
310 320 330 340 350
TYTRQKSHGV SFRVIAKWMR LAGVDHIHAG TVVGKLEGDP NTTRGYYDVC
360 370 380 390 400
REDFNPTKLE HGLFFDQSWA SLNKMMPVAS GGIHAGQMHQ LLDLLGEDVV
410 420 430 440 450
LQFGGGTIGH PMGIAAGAIA NRVALEAMIL ARNEGRDYVH EGPEILAKAA
460 470 480
QTCTPLKSAL EVWKDVTFNY QSTDTPDFVP TALETV
Length:486
Mass (Da):53,818
Last modified:May 1, 1999 - v1
Checksum:i4E949E13F57FDCE7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 871H → Y in AAN61148. (PubMed:9882445)Curated
Sequence conflicti87 – 871H → Y in BAC47850. (PubMed:9882445)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF041820 Genomic DNA. Translation: AAD05386.1.
AY150332 Genomic DNA. Translation: AAN61148.1.
BA000040 Genomic DNA. Translation: BAC47850.1.
RefSeqiNP_769225.1. NC_004463.1.

Genome annotation databases

EnsemblBacteriaiBAC47850; BAC47850; BAC47850.
GeneIDi1049510.
KEGGibja:blr2585.
PATRICi21188584. VBIBraJap65052_2551.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF041820 Genomic DNA. Translation: AAD05386.1 .
AY150332 Genomic DNA. Translation: AAN61148.1 .
BA000040 Genomic DNA. Translation: BAC47850.1 .
RefSeqi NP_769225.1. NC_004463.1.

3D structure databases

ProteinModelPortali Q9ZI34.
SMRi Q9ZI34. Positions 13-479.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224911.blr2585.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC47850 ; BAC47850 ; BAC47850 .
GeneIDi 1049510.
KEGGi bja:blr2585.
PATRICi 21188584. VBIBraJap65052_2551.

Phylogenomic databases

eggNOGi COG1850.
HOGENOMi HOG000230831.
InParanoidi Q9ZI34.
KOi K01601.
OrthoDBi EOG6ZKXMS.

Enzyme and pathway databases

BioCyci BJAP224911:GJEJ-2608-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

« Hide 'large scale' publications
  1. "Closely related form I ribulose bisphosphate carboxylase/oxygenase molecules that possess different CO2/O2 substrate specificities."
    Horken K.M., Tabita F.R.
    Arch. Biochem. Biophys. 361:183-194(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], KINETIC PARAMETERS.
    Strain: BJ110.
  2. "The Bradyrhizobium japonicum cbb locus."
    Fischer H.-M., Bauer E., Hennecke H.
    Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.

Entry informationi

Entry nameiRBL_BRADU
AccessioniPrimary (citable) accession number: Q9ZI34
Secondary accession number(s): Q79UA8, Q8GKR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: May 1, 1999
Last modified: November 26, 2014
This is version 83 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 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