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Protein

Ribulose bisphosphate carboxylase

Gene

cbbM

Organism
Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus neapolitanus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

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 Mg2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei111 – 1111Substrate; in homodimeric partnerUniRule annotation
Active sitei166 – 1661Proton acceptorUniRule annotation
Binding sitei168 – 1681SubstrateUniRule annotation
Metal bindingi191 – 1911Magnesium; via carbamate groupUniRule annotation
Metal bindingi193 – 1931MagnesiumUniRule annotation
Metal bindingi194 – 1941MagnesiumUniRule annotation
Active sitei287 – 2871Proton acceptorUniRule annotation
Binding sitei288 – 2881SubstrateUniRule annotation
Binding sitei321 – 3211SubstrateUniRule annotation
Sitei329 – 3291Transition state stabilizerUniRule annotation
Binding sitei368 – 3681SubstrateUniRule annotation

GO - Molecular functioni

GO - Biological processi

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

BioCyciHNEA555778:GIVV-1131-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylaseUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCOUniRule annotation
Gene namesi
Name:cbbMUniRule annotation
Ordered Locus Names:Hneap_1095
OrganismiHalothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus neapolitanus)
Taxonomic identifieri555778 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesHalothiobacillaceaeHalothiobacillus
ProteomesiUP000009102 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 459459Ribulose bisphosphate carboxylasePRO_0000062670Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei191 – 1911N6-carboxylysineUniRule annotation

Expressioni

Inductioni

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.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi555778.Hneap_1095.

Structurei

3D structure databases

ProteinModelPortaliQ9ZHZ4.
SMRiQ9ZHZ4. Positions 2-457.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiNQYLHYH.
OrthoDBiEOG66QKT8.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01339. RuBisCO_L_type2.
InterProiIPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
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.

Q9ZHZ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDQSARYADL SLKEEDLIAG GKHILVAYKM KPKAGHGYLE ASAHFAAESS
60 70 80 90 100
TGTNVEVSTT DDFTKGVDAL VYYIDEATED MRIAYPMDLF DRNVTDGRMM
110 120 130 140 150
LVSVLTLIIG NNQGMGDIEH AKIHDIYFPE RAIQLFDGPS KDISDMWRIL
160 170 180 190 200
GRPIENGGYI AGTIIKPKLG LRPEPFAAAA YQFWLGGDFI KNDEPQGNQV
210 220 230 240 250
FCPLKKVLPL VYDSMKRAQD ETGQAKLFSM NITADDHYEM MARADFGLET
260 270 280 290 300
FGPDADKLAF LVDGFVGGPG MITTARRQYP NQYLHYHRAG HGMITSPSAK
310 320 330 340 350
RGYTAFVLAK ISRLQGASGI HVGTMGYGKM EGEGDDRNIA YMIERDEAQG
360 370 380 390 400
PVYFQKWYGM KPTTPIISGG MNALRLPGFF ENLGHGNVIN TAGGGSYGHI
410 420 430 440 450
DSPAAGAISL KQAYECWKAG ADPIEFAKEH KEFARAFESF PKDADAIFPG

WREKLGVHK
Length:459
Mass (Da):50,573
Last modified:May 1, 1999 - v1
Checksum:i84101EDB69A063FF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF046932 Genomic DNA. Translation: AAD02442.1.
CP001801 Genomic DNA. Translation: ACX95931.1.
RefSeqiWP_012823967.1. NC_013422.1.
YP_003262978.1. NC_013422.1.

Genome annotation databases

EnsemblBacteriaiACX95931; ACX95931; Hneap_1095.
KEGGihna:Hneap_1095.
PATRICi32206056. VBIHalNea120669_1103.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF046932 Genomic DNA. Translation: AAD02442.1.
CP001801 Genomic DNA. Translation: ACX95931.1.
RefSeqiWP_012823967.1. NC_013422.1.
YP_003262978.1. NC_013422.1.

3D structure databases

ProteinModelPortaliQ9ZHZ4.
SMRiQ9ZHZ4. Positions 2-457.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi555778.Hneap_1095.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACX95931; ACX95931; Hneap_1095.
KEGGihna:Hneap_1095.
PATRICi32206056. VBIHalNea120669_1103.

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiNQYLHYH.
OrthoDBiEOG66QKT8.

Enzyme and pathway databases

BioCyciHNEA555778:GIVV-1131-MONOMER.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01339. RuBisCO_L_type2.
InterProiIPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiRBL2_HALNC
AccessioniPrimary (citable) accession number: Q9ZHZ4
Secondary accession number(s): D0KZQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: May 1, 1999
Last modified: April 1, 2015
This is version 74 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 contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits.UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.