Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

I0HVA8

- I0HVA8_RUBGI

UniProt

I0HVA8 - I0HVA8_RUBGI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Rubrivivax gelatinosus (strain NBRC 100245 / IL144)
Status
Unreviewed - 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 sitei132 – 1321Substrate; in homodimeric partnerUniRule annotation
Binding sitei182 – 1821SubstrateUniRule annotation
Active sitei184 – 1841Proton acceptorUniRule annotation
Binding sitei186 – 1861SubstrateUniRule annotation
Metal bindingi210 – 2101Magnesium; via carbamate groupUniRule annotation
Metal bindingi212 – 2121MagnesiumUniRule annotation
Metal bindingi213 – 2131MagnesiumUniRule annotation
Active sitei302 – 3021Proton acceptorUniRule annotation
Binding sitei303 – 3031SubstrateUniRule annotation
Binding sitei335 – 3351SubstrateUniRule annotation
Sitei342 – 3421Transition state stabilizerUniRule annotation
Binding sitei387 – 3871SubstrateUniRule 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

LyaseUniRule annotationImported, MonooxygenaseUniRule annotation, Oxidoreductase

Keywords - Biological processi

Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation, PhotosynthesisUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciRGEL983917:GLJR-3646-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 annotationImported
Ordered Locus Names:RGE_36060Imported
OrganismiRubrivivax gelatinosus (strain NBRC 100245 / IL144)Imported
Taxonomic identifieri983917 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesRubrivivax
ProteomesiUP000007883: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei210 – 2101N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

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

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

KOiK01601.

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.

I0HVA8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNKPHEPGAT GDQILDKKQR YSAGVLKYRQ MGYWDSDYVP KATDVVCLFR
60 70 80 90 100
ITPQEGVDPI EAAAAVAGES STATWTVVWT DRLTACDSYR AKAYKVEPVP
110 120 130 140 150
GRPGEYFAWV AYDLILFEEG SIANMTASLI GNVFSFKPLK AARLEDIQIP
160 170 180 190 200
VAYVKTFKGP PTGLIVERER LDKFGRPLLG ATTKPKLGLS GRNYGRVIYE
210 220 230 240 250
GLKGGLDFMK DDENINSQPF MHWRDRFLYV MDGVNKASAA TGEVKGSYLN
260 270 280 290 300
VTGATMEDIY ERAEFAKELG SVVIMVDLII GWSAIQSIAN WARKNDMIVH
310 320 330 340 350
MHRAGHGTYT RQKNHGVSFR VMAKWLRLAG VDHLHTGTAV GKLEGDPLTV
360 370 380 390 400
QGYYNVCRDA YTKQDLPRGL FFDQDWADLR KVMPVASGGI HAGQMHQLID
410 420 430 440 450
LFGDDVILQF GGGTIGHPAG IQAGAVANRV ALEAMVKARN EGRDIKNEGP
460 470 480 490
EILQKAAQFC TPLKQALDTW KDVSFNYAST DQSDYAVTPA TSA
Length:493
Mass (Da):54,372
Last modified:June 13, 2012 - v1
Checksum:i780F4633E7415C06
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP012320 Genomic DNA. Translation: BAL96945.1.
RefSeqiYP_005438444.1. NC_017075.1.

Genome annotation databases

EnsemblBacteriaiBAL96945; BAL96945; RGE_36060.
GeneIDi12027736.
KEGGirge:RGE_36060.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP012320 Genomic DNA. Translation: BAL96945.1 .
RefSeqi YP_005438444.1. NC_017075.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAL96945 ; BAL96945 ; RGE_36060 .
GeneIDi 12027736.
KEGGi rge:RGE_36060.

Phylogenomic databases

KOi K01601.

Enzyme and pathway databases

BioCyci RGEL983917:GLJR-3646-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. "Complete genome sequence of phototrophic betaproteobacterium Rubrivivax gelatinosus IL144."
    Nagashima S., Sekine M., Takami A., Shimizu T., Nakamura S., Aono E., Sakamoto K., Nakazawa H., Yamazaki S., Fujita N., Shimada K., Hanada S., Nagashima K.
    Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NBRC 100245 / IL144Imported.

Entry informationi

Entry nameiI0HVA8_RUBGI
AccessioniPrimary (citable) accession number: I0HVA8
Entry historyi
Integrated into UniProtKB/TrEMBL: June 13, 2012
Last sequence update: June 13, 2012
Last modified: October 29, 2014
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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, Reference proteomeImported

External Data

Dasty 3