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Q1QGD4

- RBL1B_NITHX

UniProt

Q1QGD4 - RBL1B_NITHX

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Protein

Ribulose bisphosphate carboxylase large chain 2

Gene

cbbL2

Organism
Nitrobacter hamburgensis (strain X14 / DSM 10229)
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 sitei128 – 1281Substrate; in homodimeric partnerUniRule annotation
Binding sitei178 – 1781SubstrateUniRule annotation
Active sitei180 – 1801Proton acceptorUniRule annotation
Binding sitei182 – 1821SubstrateUniRule annotation
Metal bindingi206 – 2061Magnesium; via carbamate groupUniRule annotation
Metal bindingi208 – 2081MagnesiumUniRule annotation
Metal bindingi209 – 2091MagnesiumUniRule annotation
Active sitei298 – 2981Proton acceptorUniRule annotation
Binding sitei299 – 2991SubstrateUniRule annotation
Binding sitei331 – 3311SubstrateUniRule annotation
Sitei338 – 3381Transition state stabilizerUniRule annotation
Binding sitei383 – 3831SubstrateUniRule 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

BioCyciNHAM323097:GHP7-4115-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain 2UniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCO large subunit 2UniRule annotation
Gene namesi
Name:cbbL2UniRule annotation
Ordered Locus Names:Nham_4049
Encoded oniPlasmid 10 Publication
OrganismiNitrobacter hamburgensis (strain X14 / DSM 10229)
Taxonomic identifieri323097 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter
ProteomesiUP000001953: Plasmid pNITHX1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 488488Ribulose bisphosphate carboxylase large chain 2PRO_0000251447Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei206 – 2061N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi323097.Nham_4049.

Structurei

3D structure databases

ProteinModelPortaliQ1QGD4.
SMRiQ1QGD4. Positions 26-469.
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.

Q1QGD4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNVLNEKSLT VRGKDRYKSG VMSYKKMGYW EPDYTPKDTD IICLFRVTPQ
60 70 80 90 100
DGVDPIEAAA AVAGESSTAT WTVVWTDRLT AAEKYRAKCY RVDPVPGAEG
110 120 130 140 150
QYFAYIAYDL DLFEPGSISN LTASVIGNVF GFKPLKALRL EDMRLPVAYV
160 170 180 190 200
KTFKGPPTGI VVERERLDKF GRPLLGATVK PKLGLSGRNY GRVVYEALKG
210 220 230 240 250
GLDFTKDDEN INSQPFMHWR ERFLYCMEAV NRAQAATGEI KGSYLNVTAA
260 270 280 290 300
TMEDMYERAE FAKELGSVVV MIDLVIGYTA IQSMSNWARK NDMILHLHRA
310 320 330 340 350
GHSTYTRQRN HGVSFRVISK WMRLAGVDHI HAGTVVGKLE GDPLTTRGYY
360 370 380 390 400
DICREEHNPM QLEHGIFFDQ NWASLNKMMP VASGGIHAGQ MHQLIQHLGE
410 420 430 440 450
DVVLQFGGGT IGHPMGIQAG ATANRVALEA MILARNEGRD YVSEGPDILA
460 470 480
KAAASCTPLK QALEVWKDVT FNYQSTDAPD YVTTPAVA
Length:488
Mass (Da):54,167
Last modified:May 16, 2006 - v1
Checksum:iD9BE53686D953C91
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000320 Genomic DNA. Translation: ABE64713.1.
RefSeqiYP_571545.1. NC_007959.1.

Genome annotation databases

EnsemblBacteriaiABE64713; ABE64713; Nham_4049.
GeneIDi4025375.
KEGGinha:Nham_4049.
PATRICi22685933. VBINitHam61822_0013.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000320 Genomic DNA. Translation: ABE64713.1 .
RefSeqi YP_571545.1. NC_007959.1.

3D structure databases

ProteinModelPortali Q1QGD4.
SMRi Q1QGD4. Positions 26-469.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 323097.Nham_4049.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABE64713 ; ABE64713 ; Nham_4049 .
GeneIDi 4025375.
KEGGi nha:Nham_4049.
PATRICi 22685933. VBINitHam61822_0013.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci NHAM323097:GHP7-4115-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: X14 / DSM 10229.

Entry informationi

Entry nameiRBL1B_NITHX
AccessioniPrimary (citable) accession number: Q1QGD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: May 16, 2006
Last modified: November 26, 2014
This is version 54 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