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A5E993

- RBL1A_BRASB

UniProt

A5E993 - RBL1A_BRASB

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Protein

Ribulose bisphosphate carboxylase large chain 1

Gene

cbbL1

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 sitei127 – 1271Substrate; in homodimeric partnerUniRule annotation
Binding sitei177 – 1771SubstrateUniRule annotation
Active sitei179 – 1791Proton acceptorUniRule annotation
Binding sitei181 – 1811SubstrateUniRule annotation
Metal bindingi205 – 2051Magnesium; via carbamate groupUniRule annotation
Metal bindingi207 – 2071MagnesiumUniRule annotation
Metal bindingi208 – 2081MagnesiumUniRule annotation
Active sitei297 – 2971Proton acceptorUniRule annotation
Binding sitei298 – 2981SubstrateUniRule annotation
Binding sitei330 – 3301SubstrateUniRule annotation
Sitei337 – 3371Transition state stabilizerUniRule annotation
Binding sitei382 – 3821SubstrateUniRule 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-438-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain 1UniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCO large subunit 1UniRule annotation
Gene namesi
Name:cbbL1UniRule annotation
Ordered Locus Names:BBta_0451
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 – 488488Ribulose bisphosphate carboxylase large chain 1PRO_0000299958Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei205 – 2051N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi288000.BBta_0451.

Structurei

3D structure databases

ProteinModelPortaliA5E993.
SMRiA5E993. Positions 15-481.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiCTPLKQA.
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.

A5E993-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNEALKSLTV TGKERYKSGV LEYKRMGYWE PDYEPKDTDV IALFRVTPQN
60 70 80 90 100
GVDPIEASAA VAGESSTATW TVVWTDRLTA AEKYRAKCYR VDPVPNTPGS
110 120 130 140 150
YFAYIAYDLD LFEPGSIANL SASIIGNVFG FKPLKALRLE DMRFPVAYVK
160 170 180 190 200
TFQGPATGIV VERERLDKFG RPLLGATVKP KLGLSGRNYG RVVYEALKGG
210 220 230 240 250
LDFTKDDENT NSQPFMHWRD RFLYCMEAVN KAQAATGEVK GTYLNVTAAT
260 270 280 290 300
MEDMYERAEF AKELGSVIIM IDLVIGYTAI QSMAKWARRN DMILHLHRAG
310 320 330 340 350
HGTYTRQKSH GVSFRVIAKW MRLAGVDHIH AGTVVGKLEG DPNTTRGYYD
360 370 380 390 400
ICREDHNPMA LEYGLFFEQH WASLNKLMPV ASGGIHAGQM HQLLNYLGED
410 420 430 440 450
VVLQFGGGTI GHPLGIQAGA TANRVALEAM ILARNEGRDY VHEGPEILAK
460 470 480
AAATCTPLKQ ALDVWKNVTF NYDSTDTPDF VPTAAVTA
Length:488
Mass (Da):54,042
Last modified:June 12, 2007 - v1
Checksum:i04A753A5D99867E3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000494 Genomic DNA. Translation: ABQ32737.1.
RefSeqiWP_012040789.1. NC_009485.1.
YP_001236643.1. NC_009485.1.

Genome annotation databases

EnsemblBacteriaiABQ32737; ABQ32737; BBta_0451.
GeneIDi5154513.
KEGGibbt:BBta_0451.
PATRICi21201912. VBIBraSp29847_0655.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000494 Genomic DNA. Translation: ABQ32737.1 .
RefSeqi WP_012040789.1. NC_009485.1.
YP_001236643.1. NC_009485.1.

3D structure databases

ProteinModelPortali A5E993.
SMRi A5E993. Positions 15-481.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 288000.BBta_0451.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABQ32737 ; ABQ32737 ; BBta_0451 .
GeneIDi 5154513.
KEGGi bbt:BBta_0451.
PATRICi 21201912. VBIBraSp29847_0655.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci BSP288000:GJBR-438-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 nameiRBL1A_BRASB
AccessioniPrimary (citable) accession number: A5E993
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