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Q9ZHZ4

- RBL2_HALNC

UniProt

Q9ZHZ4 - RBL2_HALNC

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Protein

Ribulose bisphosphate carboxylase

Gene
cbbM, Hneap_1095
Organism
Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus neapolitanus)
Status
Reviewed - 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 By similarity.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 By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei111 – 1111Substrate; in homodimeric partner By similarity
Active sitei166 – 1661Proton acceptor By similarity
Binding sitei168 – 1681Substrate By similarity
Metal bindingi191 – 1911Magnesium; via carbamate group By similarity
Metal bindingi193 – 1931Magnesium By similarity
Metal bindingi194 – 1941Magnesium By similarity
Active sitei287 – 2871Proton acceptor By similarity
Binding sitei288 – 2881Substrate By similarity
Binding sitei321 – 3211Substrate By similarity
Sitei329 – 3291Transition state stabilizer By similarity
Binding sitei368 – 3681Substrate By similarity

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

BioCyciHNEA555778:GIVV-1131-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase (EC:4.1.1.39)
Short name:
RuBisCO
Gene namesi
Name:cbbM
Ordered Locus Names:Hneap_1095
OrganismiHalothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus neapolitanus)
Taxonomic identifieri555778 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesHalothiobacillaceaeHalothiobacillus
ProteomesiUP000009102: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 459459Ribulose bisphosphate carboxylaseUniRule annotationPRO_0000062670Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei191 – 1911N6-carboxylysine By similarity

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.UniRule annotation

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi555778.Hneap_1095.

Structurei

3D structure databases

ProteinModelPortaliQ9ZHZ4.
SMRiQ9ZHZ4. Positions 2-457.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiDYARDHP.
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

MDQSARYADL SLKEEDLIAG GKHILVAYKM KPKAGHGYLE ASAHFAAESS    50
TGTNVEVSTT DDFTKGVDAL VYYIDEATED MRIAYPMDLF DRNVTDGRMM 100
LVSVLTLIIG NNQGMGDIEH AKIHDIYFPE RAIQLFDGPS KDISDMWRIL 150
GRPIENGGYI AGTIIKPKLG LRPEPFAAAA YQFWLGGDFI KNDEPQGNQV 200
FCPLKKVLPL VYDSMKRAQD ETGQAKLFSM NITADDHYEM MARADFGLET 250
FGPDADKLAF LVDGFVGGPG MITTARRQYP NQYLHYHRAG HGMITSPSAK 300
RGYTAFVLAK ISRLQGASGI HVGTMGYGKM EGEGDDRNIA YMIERDEAQG 350
PVYFQKWYGM KPTTPIISGG MNALRLPGFF ENLGHGNVIN TAGGGSYGHI 400
DSPAAGAISL KQAYECWKAG ADPIEFAKEH KEFARAFESF PKDADAIFPG 450
WREKLGVHK 459
Length:459
Mass (Da):50,573
Last modified:May 1, 1999 - v1
Checksum:i84101EDB69A063FF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
GeneIDi8534243.
KEGGihna:Hneap_1095.
PATRICi32206056. VBIHalNea120669_1103.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF046932 Genomic DNA. Translation: AAD02442.1 .
CP001801 Genomic DNA. Translation: ACX95931.1 .
RefSeqi WP_012823967.1. NC_013422.1.
YP_003262978.1. NC_013422.1.

3D structure databases

ProteinModelPortali Q9ZHZ4.
SMRi Q9ZHZ4. Positions 2-457.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 555778.Hneap_1095.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACX95931 ; ACX95931 ; Hneap_1095 .
GeneIDi 8534243.
KEGGi hna:Hneap_1095.
PATRICi 32206056. VBIHalNea120669_1103.

Phylogenomic databases

eggNOGi COG1850.
HOGENOMi HOG000230831.
KOi K01601.
OMAi DYARDHP.
OrthoDBi EOG66QKT8.

Enzyme and pathway databases

BioCyci HNEA555778:GIVV-1131-MONOMER.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01339. RuBisCO_L_type2.
InterProi IPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
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

« 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: September 3, 2014
This is version 70 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 By similarity.

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi