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Q8KBL4

- RBLL_CHLTE

UniProt

Q8KBL4 - RBLL_CHLTE

Protein

Ribulose bisphosphate carboxylase-like protein

Gene

CT1772

Organism
Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    Functioni

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

    Cofactori

    Binds 1 magnesium ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi198 – 1981Magnesium; via carbamate groupSequence Analysis
    Metal bindingi200 – 2001MagnesiumBy similarity
    Metal bindingi201 – 2011MagnesiumBy similarity

    GO - Molecular functioni

    1. magnesium ion binding Source: InterPro

    GO - Biological processi

    1. carbon fixation Source: InterPro

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciCTEP194439:GHN0-1811-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylase-like protein
    Short name:
    RuBisCO-like protein
    Gene namesi
    Ordered Locus Names:CT1772
    OrganismiChlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS)
    Taxonomic identifieri194439 [NCBI]
    Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum
    ProteomesiUP000001007: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 435435Ribulose bisphosphate carboxylase-like proteinPRO_0000062679Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei198 – 1981N6-carboxylysineSequence Analysis

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    DIPiDIP-48441N.
    STRINGi194439.CT1772.

    Structurei

    Secondary structure

    1
    435
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 94
    Helixi13 – 153
    Helixi18 – 203
    Beta strandi21 – 3212
    Helixi34 – 4411
    Turni61 – 633
    Beta strandi66 – 7813
    Beta strandi91 – 10111
    Helixi102 – 1043
    Helixi109 – 1168
    Helixi119 – 1224
    Beta strandi129 – 1368
    Helixi139 – 1424
    Helixi151 – 1599
    Beta strandi166 – 1705
    Helixi179 – 19113
    Beta strandi195 – 1984
    Beta strandi204 – 2063
    Helixi211 – 22919
    Beta strandi234 – 2385
    Helixi243 – 2453
    Helixi246 – 25611
    Beta strandi260 – 2645
    Helixi265 – 2684
    Helixi270 – 27910
    Beta strandi284 – 2874
    Turni289 – 2913
    Helixi292 – 2954
    Beta strandi300 – 3023
    Helixi304 – 31411
    Beta strandi317 – 3226
    Beta strandi328 – 3303
    Helixi332 – 34312
    Beta strandi353 – 3575
    Turni362 – 3643
    Helixi365 – 3728
    Beta strandi377 – 3793
    Beta strandi381 – 3877
    Helixi392 – 40716
    Helixi412 – 4165
    Helixi420 – 4278

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TELX-ray2.70A/B1-435[»]
    1YKWX-ray2.00A/B1-435[»]
    ProteinModelPortaliQ8KBL4.
    SMRiQ8KBL4. Positions 1-428.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8KBL4.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiMSIFKGV.
    OrthoDBiEOG62K1SK.

    Family and domain databases

    Gene3Di3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    InterProiIPR000685. RuBisCO_lsu_C.
    IPR017443. RuBisCO_lsu_fd_N.
    [Graphical view]
    PfamiPF00016. RuBisCO_large. 1 hit.
    [Graphical view]
    SUPFAMiSSF51649. SSF51649. 1 hit.
    SSF54966. SSF54966. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q8KBL4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNAEDVKGFF ASRESLDMEQ YLVLDYYLES VGDIETALAH FCSEQSTAQW    50
    KRVGVDEDFR LVHAAKVIDY EVIEELEQLS YPVKHSETGK IHACRVTIAH 100
    PHCNFGPKIP NLLTAVCGEG TYFTPGVPVV KLMDIHFPDT YLADFEGPKF 150
    GIEGLRDILN AHGRPIFFGV VKPNIGLSPG EFAEIAYQSW LGGLDIAKDD 200
    EMLADVTWSS IEERAAHLGK ARRKAEAETG EPKIYLANIT DEVDSLMEKH 250
    DVAVRNGANA LLINALPVGL SAVRMLSNYT QVPLIGHFPF IASFSRMEKY 300
    GIHSKVMTKL QRLAGLDAVI MPGFGDRMMT PEEEVLENVI ECTKPMGRIK 350
    PCLPVPGGSD SALTLQTVYE KVGNVDFGFV PGRGVFGHPM GPKAGAKSIR 400
    QAWEAIEQGI SIETWAETHP ELQAMVDQSL LKKQD 435
    Length:435
    Mass (Da):48,003
    Last modified:October 1, 2002 - v1
    Checksum:i41C282555ED2ECB0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE006470 Genomic DNA. Translation: AAM72993.1.
    RefSeqiNP_662651.1. NC_002932.3.

    Genome annotation databases

    EnsemblBacteriaiAAM72993; AAM72993; CT1772.
    GeneIDi1008092.
    KEGGicte:CT1772.
    PATRICi21401403. VBIChlTep116050_1606.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE006470 Genomic DNA. Translation: AAM72993.1 .
    RefSeqi NP_662651.1. NC_002932.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TEL X-ray 2.70 A/B 1-435 [» ]
    1YKW X-ray 2.00 A/B 1-435 [» ]
    ProteinModelPortali Q8KBL4.
    SMRi Q8KBL4. Positions 1-428.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48441N.
    STRINGi 194439.CT1772.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAM72993 ; AAM72993 ; CT1772 .
    GeneIDi 1008092.
    KEGGi cte:CT1772.
    PATRICi 21401403. VBIChlTep116050_1606.

    Phylogenomic databases

    eggNOGi COG1850.
    HOGENOMi HOG000230831.
    KOi K01601.
    OMAi MSIFKGV.
    OrthoDBi EOG62K1SK.

    Enzyme and pathway databases

    BioCyci CTEP194439:GHN0-1811-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q8KBL4.

    Family and domain databases

    Gene3Di 3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    InterProi IPR000685. RuBisCO_lsu_C.
    IPR017443. RuBisCO_lsu_fd_N.
    [Graphical view ]
    Pfami PF00016. RuBisCO_large. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51649. SSF51649. 1 hit.
    SSF54966. SSF54966. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. 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: WT23211 Publication.
    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: WT23211 Publication.
    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.

    Entry informationi

    Entry nameiRBLL_CHLTE
    AccessioniPrimary (citable) accession number: Q8KBL4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2005
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    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

    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.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3