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Protein

Citrate lyase subunit beta-like protein

Gene

DR_1240

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May play a role in fatty acid biosynthesis.Curated

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei74Substrate1 Publication1
Metal bindingi129Magnesium1 Publication1
Binding sitei129Substrate1 Publication1
Metal bindingi155Magnesium1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciDRAD243230:GH46-1266-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate lyase subunit beta-like protein (EC:4.1.-.-)
Gene namesi
Ordered Locus Names:DR_1240
OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Taxonomic identifieri243230 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
Proteomesi
  • UP000002524 Componenti: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002863871 – 284Citrate lyase subunit beta-like proteinAdd BLAST284

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

STRINGi243230.DR_1240.

Structurei

Secondary structure

1284
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 15Combined sources7
Helixi19 – 24Combined sources6
Turni25 – 28Combined sources4
Beta strandi31 – 38Combined sources8
Helixi45 – 65Combined sources21
Beta strandi69 – 74Combined sources6
Helixi83 – 86Combined sources4
Helixi87 – 89Combined sources3
Beta strandi94 – 99Combined sources6
Helixi105 – 117Combined sources13
Beta strandi124 – 128Combined sources5
Helixi131 – 135Combined sources5
Helixi137 – 141Combined sources5
Beta strandi146 – 151Combined sources6
Helixi153 – 160Combined sources8
Helixi169 – 171Combined sources3
Helixi172 – 185Combined sources14
Beta strandi188 – 191Combined sources4
Helixi200 – 212Combined sources13
Beta strandi216 – 222Combined sources7
Helixi223 – 230Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SGJX-ray1.84A/B/C1-284[»]
ProteinModelPortaliQ9RUZ0.
SMRiQ9RUZ0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9RUZ0.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CI0. Bacteria.
COG2301. LUCA.
HOGENOMiHOG000242281.
InParanoidiQ9RUZ0.
KOiK01644.
OMAiWAYFGAE.
OrthoDBiPOG091H08ZB.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
InterProiIPR005000. Aldolase/citrate-lyase_domain.
IPR011206. Citrate_lyase_beta/mcl1/mcl2.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERiPTHR32308. PTHR32308. 1 hit.
PfamiPF03328. HpcH_HpaI. 1 hit.
[Graphical view]
PIRSFiPIRSF015582. Cit_lyase_B. 1 hit.
SUPFAMiSSF51621. SSF51621. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9RUZ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAPPALLRS VLFAPGNRAD LIAKLPRSAP DAVVIDLEDA VPGTAEAKAA
60 70 80 90 100
ARPVAHDAAR DLIAAAPHLA VFVRVNALHS PYFEDDLSVL TPELSGVVVP
110 120 130 140 150
KLEMGAEARQ VAQMLQERSL PLPILAGLET GAGVWNAREI MEVPEVAWAY
160 170 180 190 200
FGAEDYTTDL GGKRTPGGLE VLYARSQVAL AARLTGVAAL DIVVTALNDP
210 220 230 240 250
ETFRADAEQG RALGYSGKLC IHPAQVALAH EYFGPTEADR ARARALLDAA
260 270 280
AAAAQRGHGA FSFEGQMVDE PMLAKARTLL SHEA
Length:284
Mass (Da):29,980
Last modified:May 1, 2000 - v1
Checksum:iF95B6C9B20F89EC5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF10813.1.
PIRiF75418.
RefSeqiNP_294964.1. NC_001263.1.
WP_010887883.1. NZ_CP015081.1.

Genome annotation databases

EnsemblBacteriaiAAF10813; AAF10813; DR_1240.
GeneIDi1798759.
KEGGidra:DR_1240.
PATRICi21630068. VBIDeiRad64572_1435.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF10813.1.
PIRiF75418.
RefSeqiNP_294964.1. NC_001263.1.
WP_010887883.1. NZ_CP015081.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SGJX-ray1.84A/B/C1-284[»]
ProteinModelPortaliQ9RUZ0.
SMRiQ9RUZ0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243230.DR_1240.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF10813; AAF10813; DR_1240.
GeneIDi1798759.
KEGGidra:DR_1240.
PATRICi21630068. VBIDeiRad64572_1435.

Phylogenomic databases

eggNOGiENOG4105CI0. Bacteria.
COG2301. LUCA.
HOGENOMiHOG000242281.
InParanoidiQ9RUZ0.
KOiK01644.
OMAiWAYFGAE.
OrthoDBiPOG091H08ZB.

Enzyme and pathway databases

BioCyciDRAD243230:GH46-1266-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9RUZ0.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
InterProiIPR005000. Aldolase/citrate-lyase_domain.
IPR011206. Citrate_lyase_beta/mcl1/mcl2.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERiPTHR32308. PTHR32308. 1 hit.
PfamiPF03328. HpcH_HpaI. 1 hit.
[Graphical view]
PIRSFiPIRSF015582. Cit_lyase_B. 1 hit.
SUPFAMiSSF51621. SSF51621. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCITEL_DEIRA
AccessioniPrimary (citable) accession number: Q9RUZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2000
Last modified: November 2, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

This organism lacks the other subunits that are necessary for ATP-independent citrate lyase activity. Even though this protein has clear similarity to citrate lyase beta subunit, it is expected to have a somewhat different enzyme activity.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.