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A4WW35

- RBL1_RHOS5

UniProt

A4WW35 - RBL1_RHOS5

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Protein

Ribulose bisphosphate carboxylase large chain 1

Gene

cbbL1

Organism
Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
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

BioCyciRSPH349102:GHE1-4039-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:Rsph17025_2712
OrganismiRhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
Taxonomic identifieri349102 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
ProteomesiUP000000234: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 486486Ribulose bisphosphate carboxylase large chain 1PRO_0000355752Add
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

STRINGi349102.Rsph17025_2712.

Structurei

3D structure databases

ProteinModelPortaliA4WW35.
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.

A4WW35-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDTKNTEIKG KERYKAGVLK YAQMGYWDGD YQPKDTDVLA LFRITPQEGV
60 70 80 90 100
DPIEAAAAVA GESSTATWTV VWTDRLTACD SYRAKAYKVE PVPGTPGQYF
110 120 130 140 150
CYVAYDLILF EEGSIANLTA SIIGNVFSFK PLKAARLEDM RFPVAYVKTY
160 170 180 190 200
KGPPTGIIVE RERLDKFGKP LLGATTKPKL GLSGKNYGRV VYEGLKGGLD
210 220 230 240 250
FMKDDENINS QPFMHWRDRF LYVMEAVNLA SAQTGEVKGH YLNITAGTME
260 270 280 290 300
EMYRRAEFAK SLGSVIVMVD LIIGYTAIQS ISEWCRQNDM ILHMHRAGHG
310 320 330 340 350
TYTRQKNHGI SFRVIAKWLR LAGVDHLHCG TAVGKLEGDP PTVQGYYNVC
360 370 380 390 400
REPFNTVDLQ RGLFFEQDWA DLKKVMPVAS GGIHAGQMHQ LLSLFGDDVV
410 420 430 440 450
LQFGGGTIGH PMGIQAGATA NRVALEAMVL ARNEGRNIDV EGPEILRAAA
460 470 480
KWCKPLEAAL DTWGNITFNY TSTDTSDFVP TPSVSM
Length:486
Mass (Da):53,799
Last modified:May 29, 2007 - v1
Checksum:iC283647E569C73A6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000661 Genomic DNA. Translation: ABP71599.1.
RefSeqiYP_001168904.1. NC_009428.1.

Genome annotation databases

EnsemblBacteriaiABP71599; ABP71599; Rsph17025_2712.
GeneIDi5085290.
KEGGirsq:Rsph17025_2712.
PATRICi23163772. VBIRhoSph94549_2799.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000661 Genomic DNA. Translation: ABP71599.1 .
RefSeqi YP_001168904.1. NC_009428.1.

3D structure databases

ProteinModelPortali A4WW35.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 349102.Rsph17025_2712.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABP71599 ; ABP71599 ; Rsph17025_2712 .
GeneIDi 5085290.
KEGGi rsq:Rsph17025_2712.
PATRICi 23163772. VBIRhoSph94549_2799.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci RSPH349102:GHE1-4039-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: ATCC 17025 / ATH 2.4.3.

Entry informationi

Entry nameiRBL1_RHOS5
AccessioniPrimary (citable) accession number: A4WW35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: May 29, 2007
Last modified: November 26, 2014
This is version 49 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