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Q9ZHZ4 (RBL2_HALNC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase

Short name=RuBisCO
EC=4.1.1.39
Gene names
Name:cbbM
Ordered Locus Names:Hneap_1095
OrganismHalothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus neapolitanus) [Complete proteome] [HAMAP]
Taxonomic identifier555778 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesHalothiobacillaceaeHalothiobacillus

Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_01339

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01339

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01339

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01339

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01339

Induction

Form II RuBisCO is expressed in the presence of form I, when grown in air with or without 5% CO2, although it is not the major activity. When the form I gene is disrupted the RuBisCO form II activity increases but is not found in carboxysomes. HAMAP-Rule MF_01339

Miscellaneous

The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits By similarity.

Sequence similarities

Belongs to the RuBisCO large chain family. Type II subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 459459Ribulose bisphosphate carboxylase HAMAP-Rule MF_01339
PRO_0000062670

Sites

Active site1661Proton acceptor By similarity
Active site2871Proton acceptor By similarity
Metal binding1911Magnesium; via carbamate group By similarity
Metal binding1931Magnesium By similarity
Metal binding1941Magnesium By similarity
Binding site1111Substrate; in homodimeric partner By similarity
Binding site1681Substrate By similarity
Binding site2881Substrate By similarity
Binding site3211Substrate By similarity
Binding site3681Substrate By similarity
Site3291Transition state stabilizer By similarity

Amino acid modifications

Modified residue1911N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZHZ4 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 84101EDB69A063FF

FASTA45950,573
        10         20         30         40         50         60 
MDQSARYADL SLKEEDLIAG GKHILVAYKM KPKAGHGYLE ASAHFAAESS TGTNVEVSTT 

        70         80         90        100        110        120 
DDFTKGVDAL VYYIDEATED MRIAYPMDLF DRNVTDGRMM LVSVLTLIIG NNQGMGDIEH 

       130        140        150        160        170        180 
AKIHDIYFPE RAIQLFDGPS KDISDMWRIL GRPIENGGYI AGTIIKPKLG LRPEPFAAAA 

       190        200        210        220        230        240 
YQFWLGGDFI KNDEPQGNQV FCPLKKVLPL VYDSMKRAQD ETGQAKLFSM NITADDHYEM 

       250        260        270        280        290        300 
MARADFGLET FGPDADKLAF LVDGFVGGPG MITTARRQYP NQYLHYHRAG HGMITSPSAK 

       310        320        330        340        350        360 
RGYTAFVLAK ISRLQGASGI HVGTMGYGKM EGEGDDRNIA YMIERDEAQG PVYFQKWYGM 

       370        380        390        400        410        420 
KPTTPIISGG MNALRLPGFF ENLGHGNVIN TAGGGSYGHI DSPAAGAISL KQAYECWKAG 

       430        440        450 
ADPIEFAKEH KEFARAFESF PKDADAIFPG WREKLGVHK 

« Hide

References

« Hide 'large scale' references
[1]"A form II Rubisco gene and associated genes in Thiobacillus neapolitanus."
Shively J.M.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of Halothiobacillus neapolitanus c2."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Kerfeld C., Cannon G., Heinhort S.
Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 23641 / c2.
[3]"Insertion mutation of the form I cbbL gene encoding ribulose bisphosphate carboxylase/oxygenase (RuBisCO) in Thiobacillus neapolitanus results in expression of form II RuBisCO, loss of carboxysomes, and an increased CO2 requirement for growth."
Baker S.H., Jin S., Aldrich H.C., Howard G.T., Shively J.M.
J. Bacteriol. 180:4133-4139(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: DETECTION OF EXPRESSION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF046932 Genomic DNA. Translation: AAD02442.1.
CP001801 Genomic DNA. Translation: ACX95931.1.
RefSeqYP_003262978.1. NC_013422.1.

3D structure databases

ProteinModelPortalQ9ZHZ4.
SMRQ9ZHZ4. Positions 2-457.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING555778.Hneap_1095.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACX95931; ACX95931; Hneap_1095.
GeneID8534243.
KEGGhna:Hneap_1095.
PATRIC32206056. VBIHalNea120669_1103.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMANQYLHYH.
OrthoDBEOG66QKT8.
ProtClustDBPRK13475.

Enzyme and pathway databases

BioCycHNEA555778:GIVV-1131-MONOMER.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01339. RuBisCO_L_type2.
InterProIPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRBL2_HALNC
AccessionPrimary (citable) accession number: Q9ZHZ4
Secondary accession number(s): D0KZQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: May 1, 1999
Last modified: February 19, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families