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Q37BZ5

- RBL1A_RHOPS

UniProt

Q37BZ5 - RBL1A_RHOPS

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Protein

Ribulose bisphosphate carboxylase large chain 1

Gene

cbbL1

Organism
Rhodopseudomonas palustris (strain BisB5)
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

Binds 1 magnesium ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei115 – 1151Substrate; in homodimeric partnerUniRule annotation
Binding sitei165 – 1651SubstrateUniRule annotation
Active sitei167 – 1671Proton acceptorUniRule annotation
Binding sitei169 – 1691SubstrateUniRule annotation
Metal bindingi193 – 1931Magnesium; via carbamate groupUniRule annotation
Metal bindingi195 – 1951MagnesiumUniRule annotation
Metal bindingi196 – 1961MagnesiumUniRule annotation
Active sitei286 – 2861Proton acceptorUniRule annotation
Binding sitei287 – 2871SubstrateUniRule annotation
Binding sitei319 – 3191SubstrateUniRule annotation
Sitei326 – 3261Transition state stabilizerUniRule annotation
Binding sitei371 – 3711SubstrateUniRule 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

BioCyciRPAL316057:GHDC-1575-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:RPD_1549
OrganismiRhodopseudomonas palustris (strain BisB5)
Taxonomic identifieri316057 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas
ProteomesiUP000001818: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 472472Ribulose bisphosphate carboxylase large chain 1PRO_0000251458Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei193 – 1931N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi316057.RPD_1549.

Structurei

3D structure databases

ProteinModelPortaliQ37BZ5.
SMRiQ37BZ5. Positions 15-459.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiMFKRAEY.
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.

Q37BZ5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLKSYQAGVR EYRETYWDPH YTPKDSDILA VFKVIPQAGV PREEAAAAVC
60 70 80 90 100
AESSTATWTT VWTDLLTDLD YYKGRAYAIE DVPGDDEAFY AFVAYPMGLF
110 120 130 140 150
EEGSIVNVFT SLVGNVFGFK AVRALRLEDV RFPLWFVTTC DGPPHGIQVE
160 170 180 190 200
RDKLDKYGRP MLGCTIKPKL GLSAKNYGRA VYECLRGGLD FTKDDENVNS
210 220 230 240 250
QPFMRWRDRF EFCQEAIEKA EQETGERKGH YLNVTAPNME EIYRRAEFAK
260 270 280 290 300
EIGSPIIMSD YLTIGWAAHS SLSRWCRANG MLLHVHRAMH GVIDRNPRHG
310 320 330 340 350
INFRVLAKLL RLLGGDHLHS GTVVGKLEGD RAATLGWVDL MRERHVKEDR
360 370 380 390 400
SRGLFFDQPW GHMAPVMPVA SGGIHVWHMP ALLAIFGDDA VFQFGGGTLG
410 420 430 440 450
HPWGNAAGAA ANRVALEACV RARNEGRDVE REGKDILTAA AQSSPELKVA
460 470
METWREIKFE FDVVDKLDAP HR
Length:472
Mass (Da):53,009
Last modified:December 6, 2005 - v1
Checksum:i2C224B243490441D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000283 Genomic DNA. Translation: ABE38786.1.
RefSeqiWP_011501970.1. NC_007958.1.
YP_568687.1. NC_007958.1.

Genome annotation databases

EnsemblBacteriaiABE38786; ABE38786; RPD_1549.
GeneIDi4022029.
KEGGirpd:RPD_1549.
PATRICi23278049. VBIRhoPal120395_1602.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000283 Genomic DNA. Translation: ABE38786.1 .
RefSeqi WP_011501970.1. NC_007958.1.
YP_568687.1. NC_007958.1.

3D structure databases

ProteinModelPortali Q37BZ5.
SMRi Q37BZ5. Positions 15-459.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 316057.RPD_1549.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABE38786 ; ABE38786 ; RPD_1549 .
GeneIDi 4022029.
KEGGi rpd:RPD_1549.
PATRICi 23278049. VBIRhoPal120395_1602.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci RPAL316057:GHDC-1575-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: BisB5.

Entry informationi

Entry nameiRBL1A_RHOPS
AccessioniPrimary (citable) accession number: Q37BZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: December 6, 2005
Last modified: October 1, 2014
This is version 57 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