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Protein

Ribulose bisphosphate carboxylase-like protein

Gene

CT1772

Organism
Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi198Magnesium; via carbamate groupSequence analysis1
Metal bindingi200MagnesiumBy similarity1
Metal bindingi201MagnesiumBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Magnesium, Metal-binding

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 / NBRC 103806 / TLS)
Taxonomic identifieri194439 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum
Proteomesi
  • UP000001007 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000626791 – 435Ribulose bisphosphate carboxylase-like proteinAdd BLAST435

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei198N6-carboxylysineSequence analysis1

Proteomic databases

PRIDEiQ8KBL4.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

DIPiDIP-48441N.
STRINGi194439.CT1772.

Structurei

Secondary structure

1435
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 9Combined sources4
Helixi13 – 15Combined sources3
Helixi18 – 20Combined sources3
Beta strandi21 – 32Combined sources12
Helixi34 – 44Combined sources11
Turni61 – 63Combined sources3
Beta strandi66 – 78Combined sources13
Beta strandi91 – 101Combined sources11
Helixi102 – 104Combined sources3
Helixi109 – 116Combined sources8
Helixi119 – 122Combined sources4
Beta strandi129 – 136Combined sources8
Helixi139 – 142Combined sources4
Helixi151 – 159Combined sources9
Beta strandi166 – 170Combined sources5
Helixi179 – 191Combined sources13
Beta strandi195 – 198Combined sources4
Beta strandi204 – 206Combined sources3
Helixi211 – 229Combined sources19
Beta strandi234 – 238Combined sources5
Helixi243 – 245Combined sources3
Helixi246 – 256Combined sources11
Beta strandi260 – 264Combined sources5
Helixi265 – 268Combined sources4
Helixi270 – 279Combined sources10
Beta strandi284 – 287Combined sources4
Turni289 – 291Combined sources3
Helixi292 – 295Combined sources4
Beta strandi300 – 302Combined sources3
Helixi304 – 314Combined sources11
Beta strandi317 – 322Combined sources6
Beta strandi328 – 330Combined sources3
Helixi332 – 343Combined sources12
Beta strandi353 – 357Combined sources5
Turni362 – 364Combined sources3
Helixi365 – 372Combined sources8
Beta strandi377 – 379Combined sources3
Beta strandi381 – 387Combined sources7
Helixi392 – 407Combined sources16
Helixi412 – 416Combined sources5
Helixi420 – 427Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TELX-ray2.70A/B1-435[»]
1YKWX-ray2.00A/B1-435[»]
ProteinModelPortaliQ8KBL4.
SMRiQ8KBL4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8KBL4.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105DT1. Bacteria.
COG1850. LUCA.
HOGENOMiHOG000230831.
KOiK01601.
OMAiKDDEIFF.
OrthoDBiPOG091H0DKL.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
InterProiIPR033966. RuBisCO.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8KBL4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAEDVKGFF ASRESLDMEQ YLVLDYYLES VGDIETALAH FCSEQSTAQW
60 70 80 90 100
KRVGVDEDFR LVHAAKVIDY EVIEELEQLS YPVKHSETGK IHACRVTIAH
110 120 130 140 150
PHCNFGPKIP NLLTAVCGEG TYFTPGVPVV KLMDIHFPDT YLADFEGPKF
160 170 180 190 200
GIEGLRDILN AHGRPIFFGV VKPNIGLSPG EFAEIAYQSW LGGLDIAKDD
210 220 230 240 250
EMLADVTWSS IEERAAHLGK ARRKAEAETG EPKIYLANIT DEVDSLMEKH
260 270 280 290 300
DVAVRNGANA LLINALPVGL SAVRMLSNYT QVPLIGHFPF IASFSRMEKY
310 320 330 340 350
GIHSKVMTKL QRLAGLDAVI MPGFGDRMMT PEEEVLENVI ECTKPMGRIK
360 370 380 390 400
PCLPVPGGSD SALTLQTVYE KVGNVDFGFV PGRGVFGHPM GPKAGAKSIR
410 420 430
QAWEAIEQGI SIETWAETHP ELQAMVDQSL LKKQD
Length:435
Mass (Da):48,003
Last modified:October 1, 2002 - v1
Checksum:i41C282555ED2ECB0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006470 Genomic DNA. Translation: AAM72993.1.
RefSeqiNP_662651.1. NC_002932.3.
WP_010933432.1. NC_002932.3.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006470 Genomic DNA. Translation: AAM72993.1.
RefSeqiNP_662651.1. NC_002932.3.
WP_010933432.1. NC_002932.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TELX-ray2.70A/B1-435[»]
1YKWX-ray2.00A/B1-435[»]
ProteinModelPortaliQ8KBL4.
SMRiQ8KBL4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48441N.
STRINGi194439.CT1772.

Proteomic databases

PRIDEiQ8KBL4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4105DT1. Bacteria.
COG1850. LUCA.
HOGENOMiHOG000230831.
KOiK01601.
OMAiKDDEIFF.
OrthoDBiPOG091H0DKL.

Miscellaneous databases

EvolutionaryTraceiQ8KBL4.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
InterProiIPR033966. RuBisCO.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
ProtoNetiSearch...

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: November 30, 2016
This is version 84 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

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 one 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.