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Q8KBL4 (RBLL_CHLTE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase-like protein
Short name=RuBisCO-like protein
Gene names
Ordered Locus Names:CT1772
OrganismChlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS) [Reference proteome] [HAMAP]
Taxonomic identifier194439 [NCBI]
Taxonomic lineageBacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobaculum ›

Protein attributes

Sequence length435 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in sulfur metabolism and oxidative stress response. Does not show RuBisCO activity. Ref.2 Ref.3

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Subunit structure

Homodimer. Ref.3

Sequence similarities

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

Caution

Although strongly related to RuBisCO family, it lacks the conserved Lys active site in position 327, which is replaced by an Arg residue, suggesting that it may catalyze enolization but not carboxylation.

Ontologies

Keywords
   LigandMagnesium
Metal-binding
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbon fixation

Inferred from electronic annotation. Source: InterPro

   Molecular_functionmagnesium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 435435Ribulose bisphosphate carboxylase-like protein
PRO_0000062679

Sites

Metal binding1981Magnesium; via carbamate group Potential
Metal binding2001Magnesium By similarity
Metal binding2011Magnesium By similarity

Amino acid modifications

Modified residue1981N6-carboxylysine Potential

Secondary structure

1 ............................................................................. 435
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8KBL4 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 41C282555ED2ECB0

FASTA43548,003
        10         20         30         40         50         60 
MNAEDVKGFF ASRESLDMEQ YLVLDYYLES VGDIETALAH FCSEQSTAQW KRVGVDEDFR 

        70         80         90        100        110        120 
LVHAAKVIDY EVIEELEQLS YPVKHSETGK IHACRVTIAH PHCNFGPKIP NLLTAVCGEG 

       130        140        150        160        170        180 
TYFTPGVPVV KLMDIHFPDT YLADFEGPKF GIEGLRDILN AHGRPIFFGV VKPNIGLSPG 

       190        200        210        220        230        240 
EFAEIAYQSW LGGLDIAKDD EMLADVTWSS IEERAAHLGK ARRKAEAETG EPKIYLANIT 

       250        260        270        280        290        300 
DEVDSLMEKH DVAVRNGANA LLINALPVGL SAVRMLSNYT QVPLIGHFPF IASFSRMEKY 

       310        320        330        340        350        360 
GIHSKVMTKL QRLAGLDAVI MPGFGDRMMT PEEEVLENVI ECTKPMGRIK PCLPVPGGSD 

       370        380        390        400        410        420 
SALTLQTVYE KVGNVDFGFV PGRGVFGHPM GPKAGAKSIR QAWEAIEQGI SIETWAETHP 

       430 
ELQAMVDQSL LKKQD

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium."
Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M. expand/collapse author list , Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49652 / DSM 12025 / TLS.
[2]"A ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO)-like protein from Chlorobium tepidum that is involved with sulfur metabolism and the response to oxidative stress."
Hanson T.E., Tabita F.R.
Proc. Natl. Acad. Sci. U.S.A. 98:4397-4402(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: WT2321.
[3]"Crystal structure of a RuBisCO-like protein from the green sulfur bacterium Chlorobium tepidum."
Li H., Sawaya M.R., Tabita F.R., Eisenberg D.
Structure 13:779-789(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), FUNCTION, SUBUNIT.
Strain: WT2321.
[4]"Crystal structure of a RuBisCO-like protein from Chlorobium tepidum."
Fedorov A.A., Fedorov E.V., Imker H.J., Gerlt J.A., Almo S.C.
Submitted (MAY-2004) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
Strain: ATCC 49652 / DSM 12025 / TLS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE006470 Genomic DNA. Translation: AAM72993.1.
RefSeqNP_662651.1. NC_002932.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TELX-ray2.70A/B1-435[»]
1YKWX-ray2.00A/B1-435[»]
ProteinModelPortalQ8KBL4.
SMRQ8KBL4. Positions 1-428.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-48441N.
STRING194439.CT1772.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM72993; AAM72993; CT1772.
GeneID1008092.
KEGGcte:CT1772.
PATRIC21401403. VBIChlTep116050_1606.

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMANITDEVD.
ProtClustDBCLSK637929.

Enzyme and pathway databases

BioCycCTEP194439:GHN0-1766-MONOMER.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
InterProIPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
[Graphical view]
PfamPF00016. RuBisCO_large. 1 hit.
[Graphical view]
SUPFAMSSF51649. RuBisCO_large. 1 hit.
SSF54966. RuBisCO_large. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. False negative.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8KBL4.

Entry information

Entry nameRBLL_CHLTE
AccessionPrimary (citable) accession number: Q8KBL4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: October 1, 2002
Last modified: May 1, 2013
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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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