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P58348

- RBL1_RHIME

UniProt

P58348 - RBL1_RHIME

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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
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 sitei126 – 1261Substrate; in homodimeric partnerUniRule annotation
Binding sitei176 – 1761SubstrateUniRule annotation
Active sitei178 – 1781Proton acceptorUniRule annotation
Binding sitei180 – 1801SubstrateUniRule annotation
Metal bindingi204 – 2041Magnesium; via carbamate groupUniRule annotation
Metal bindingi206 – 2061MagnesiumUniRule annotation
Metal bindingi207 – 2071MagnesiumUniRule annotation
Active sitei296 – 2961Proton acceptorUniRule annotation
Binding sitei297 – 2971SubstrateUniRule annotation
Binding sitei329 – 3291SubstrateUniRule annotation
Sitei336 – 3361Transition state stabilizerUniRule annotation
Binding sitei381 – 3811SubstrateUniRule 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

BioCyciSMEL266834:GJF6-3624-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:RB0191
ORF Names:SMb20198
Encoded oniPlasmid pSymB (megaplasmid 2)0 Publication
OrganismiRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Taxonomic identifieri266834 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
ProteomesiUP000001976: Plasmid pSymB

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 486486Ribulose bisphosphate carboxylase large chainPRO_0000062643Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei204 – 2041N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi266834.SM_b20198.

Structurei

3D structure databases

ProteinModelPortaliP58348.
SMRiP58348. Positions 7-480.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1850.
KOiK01601.
OMAiFTQDWAS.
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.

P58348-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNADAKTEIK GRERYKAGVL KYAQMGYWNG DYEPKDTDLI ALFRITPQDG
60 70 80 90 100
VDPIEAAAAV AGESSTATWT VVWTDRLTAC DQYRAKAYRV DPVPGTPGQY
110 120 130 140 150
FCYVAYDLIL FEEGSIANLT ASIIGNVFSF KPLKAARLED MRLPVAYVKT
160 170 180 190 200
FRGPPTGIVV ERERLDKFGK PLLGATTKPK LGLSGKNYGR VVYEGLKGGL
210 220 230 240 250
DFMKDDENIN SQPFMHWRDR YLYCMEAVNH ASAVTGEVKG HYLNITAGTM
260 270 280 290 300
EEMYRRAEFA KELGSVIVMV DLIVGWTAIQ SISEWCRQND MILHMHRAGH
310 320 330 340 350
GTYTRQKNHG ISFRVIAKWL RLAGVDHLHA GTAVGKLEGD PPTVQGYYNV
360 370 380 390 400
CREMKNEVDL PRGLFFEQDW ADLKKVMPVA SGGIHAGQMH QLLDLFGDDV
410 420 430 440 450
VLQFGGGTIG HPMGIQAGAT ANRVALEAMV LARNEGRDIA HEGPEILRAA
460 470 480
AKWCKPLEAA LDIWGNISFN YTPTDTSDFV PSVTAA
Length:486
Mass (Da):53,791
Last modified:November 16, 2001 - v1
Checksum:i4386CA656929EC5F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591985 Genomic DNA. Translation: CAC48591.1.
PIRiG95865.
RefSeqiNP_436731.1. NC_003078.1.

Genome annotation databases

EnsemblBacteriaiCAC48591; CAC48591; SM_b20198.
GeneIDi1236522.
KEGGisme:SM_b20198.
PATRICi23636771. VBISinMel96828_5107.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591985 Genomic DNA. Translation: CAC48591.1 .
PIRi G95865.
RefSeqi NP_436731.1. NC_003078.1.

3D structure databases

ProteinModelPortali P58348.
SMRi P58348. Positions 7-480.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 266834.SM_b20198.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAC48591 ; CAC48591 ; SM_b20198 .
GeneIDi 1236522.
KEGGi sme:SM_b20198.
PATRICi 23636771. VBISinMel96828_5107.

Phylogenomic databases

eggNOGi COG1850.
KOi K01601.
OMAi FTQDWAS.
OrthoDBi EOG6ZKXMS.

Enzyme and pathway databases

BioCyci SMEL266834:GJF6-3624-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. "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing endosymbiont Sinorhizobium meliloti."
    Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J., Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.
    Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1021.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1021.

Entry informationi

Entry nameiRBL1_RHIME
AccessioniPrimary (citable) accession number: P58348
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 16, 2001
Last modified: November 26, 2014
This is version 88 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, Plasmid, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3