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A5EQ63

- RBL1C_BRASB

UniProt

A5EQ63 - RBL1C_BRASB

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Protein

Ribulose bisphosphate carboxylase large chain 3

Gene

cbbL3

Organism
Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182)
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 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

BioCyciBSP288000:GJBR-6132-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain 3UniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCO large subunit 3UniRule annotation
Gene namesi
Name:cbbL3UniRule annotation
Ordered Locus Names:BBta_6397
OrganismiBradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182)
Taxonomic identifieri288000 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium
ProteomesiUP000000246: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 486486Ribulose bisphosphate carboxylase large chain 3PRO_0000299960Add
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

STRINGi288000.BBta_6397.

Structurei

3D structure databases

ProteinModelPortaliA5EQ63.
SMRiA5EQ63. 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.
KOiK01601.
OMAiLDYYLEC.
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.

A5EQ63-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNDQSITVRG KDRYKSGVME YKKMGYWEPS YQPKDTDVIA LFRVTPQDGV
60 70 80 90 100
DPVEACAAVA GESSTATWTV VWTDRLTAAE KYRAKCYRVE PVPGSPGSYF
110 120 130 140 150
AYIAYDLDLF EPGSIANLTA SIIGNVFGFK PLKALRLEDM RLPVAYVKTF
160 170 180 190 200
QGPATGIVVE RERLDKFGRP LLGATVKPKL GLSGRNYGRV VYEALKGGLD
210 220 230 240 250
FTKDDENINS QPFMHWRERF LYCMEAVNKA QAATGEIKGT YLNVTAATME
260 270 280 290 300
DMYERAEFAK ELGSTIIMID LVIGYTAIQS MAKWARRNDM ILHLHRAGHS
310 320 330 340 350
TYTRQRAHGV SFRVIAKWMR LAGVDHIHAG TVVGKLEGDP NTTRGYYDIC
360 370 380 390 400
REDFNPMRLE HGVFFDQHWA SLNKLMPVAS GGIHAGQMHQ LLDLLGEDVV
410 420 430 440 450
LQFGGGTIGH PRGIAAGATA NRVALEAMIL ARNEGRDYVH EGPEILAKAA
460 470 480
QTCTPLREAL EIWKDVTFNY ESTDSPDFVP TVTPAA
Length:486
Mass (Da):53,975
Last modified:June 12, 2007 - v1
Checksum:iA62AC32F3DC5ABF7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000494 Genomic DNA. Translation: ABQ38307.1.
RefSeqiWP_012046248.1. NC_009485.1.
YP_001242213.1. NC_009485.1.

Genome annotation databases

EnsemblBacteriaiABQ38307; ABQ38307; BBta_6397.
GeneIDi5154107.
KEGGibbt:BBta_6397.
PATRICi21213477. VBIBraSp29847_6392.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000494 Genomic DNA. Translation: ABQ38307.1 .
RefSeqi WP_012046248.1. NC_009485.1.
YP_001242213.1. NC_009485.1.

3D structure databases

ProteinModelPortali A5EQ63.
SMRi A5EQ63. Positions 13-479.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 288000.BBta_6397.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABQ38307 ; ABQ38307 ; BBta_6397 .
GeneIDi 5154107.
KEGGi bbt:BBta_6397.
PATRICi 21213477. VBIBraSp29847_6392.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci BSP288000:GJBR-6132-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BTAi1 / ATCC BAA-1182.

Entry informationi

Entry nameiRBL1C_BRASB
AccessioniPrimary (citable) accession number: A5EQ63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: June 12, 2007
Last modified: November 26, 2014
This is version 47 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3