Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B3QKU1 (MASZ_RHOPT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Malate synthase G

EC=2.3.3.9
Gene names
Name:glcB
Ordered Locus Names:Rpal_4697
OrganismRhodopseudomonas palustris (strain TIE-1) [Complete proteome] [HAMAP]
Taxonomic identifier395960 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas

Protein attributes

Sequence length724 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA By similarity. HAMAP-Rule MF_00641

Catalytic activity

Acetyl-CoA + H2O + glyoxylate = (S)-malate + CoA. HAMAP-Rule MF_00641

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00641

Pathway

Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. HAMAP-Rule MF_00641

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00641

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00641.

Sequence similarities

Belongs to the malate synthase family. GlcB subfamily.

Ontologies

Keywords
   Biological processGlyoxylate bypass
Tricarboxylic acid cycle
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionTransferase
   PTMOxidation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglyoxylate cycle

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmalate synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 724724Malate synthase G HAMAP-Rule MF_00641
PRO_1000130897

Regions

Region124 – 1252Acetyl-CoA binding By similarity
Region454 – 4574Glyoxylate binding By similarity

Sites

Active site3371Proton acceptor By similarity
Active site6281Proton donor By similarity
Metal binding4291Magnesium By similarity
Metal binding4571Magnesium By similarity
Binding site1171Acetyl-CoA; via carbonyl oxygen By similarity
Binding site2731Acetyl-CoA By similarity
Binding site3101Acetyl-CoA By similarity
Binding site3371Glyoxylate By similarity
Binding site4291Glyoxylate By similarity
Binding site5381Acetyl-CoA; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue6141Cysteine sulfenic acid (-SOH) By similarity

Sequences

Sequence LengthMass (Da)Tools
B3QKU1 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 0102198CFF95EEFC

FASTA72478,535
        10         20         30         40         50         60 
MNRIDAHGLK IAPVLFDFIA KEAAPKTGIA PDVFWAGLAA IVRDLAPKTR ALLKTRDDLQ 

        70         80         90        100        110        120 
AKIDAWHLAN KGKKQDMAAY TAFLKEIGYL LPEPPTVPVE TANIDEEIGK LCGPQLVVPL 

       130        140        150        160        170        180 
SNARYALNAA NARWGSLYDA FYGTDAIPQE ATQAKGYDKA RGDKVIAKAK AFLDQAAPLA 

       190        200        210        220        230        240 
TGSHSDVTGY SVIAGQLSAK LKSGNATGLK KPAQFAGFRG DAANPSAVLL VNNGLHIEIK 

       250        260        270        280        290        300 
IDRANTIGKD DPAGVADLVI ESAVSTILDM EDSVAAVDAD DKVLIYRNTL GLMDGTLSES 

       310        320        330        340        350        360 
FEKGGKTVTR ALNGDRTYTA PDGKEISLHG RSLLLMRNVG HHMWTDAVLD SDGQEIPEGF 

       370        380        390        400        410        420 
LDAAVSGLIA IHDLKHLGKT RNSRTGSVYI VKPKMHGPDE VALTVELFGR VETMLGLTAN 

       430        440        450        460        470        480 
TLKVGIMDEE RRTTVNLKAC IQNASKRIVF INTGFLDRTG DEIHTSMEAG PMIRKNEMKA 

       490        500        510        520        530        540 
QPWIKAYEDW NVDTGLVDGL PGHAQIGKGM WAAPDKMADM LAQKIGHPQA GATTAWVPSP 

       550        560        570        580        590        600 
TAATLHALHY HQVDVIARQQ ELAKGGPRAK LEDILTIPVS NSNWAPDDVR QEIDNNCQGI 

       610        620        630        640        650        660 
LGYVVRWIDQ GVGCSKVPDI HDVGLMEDRA TLRISSQHLA NWLHHGVVTK DQVLDSLKRM 

       670        680        690        700        710        720 
AVIVDKQNEG DALYRPIAPD FDGVAFEAAC DLIFKGRAQP NGYTEYILHE RRREAKAAHL 


ESAR 

« Hide

References

[1]"Complete sequence of Rhodopseudomonas palustris TIE-1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Emerson D., Newman D.K., Roden E., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TIE-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001096 Genomic DNA. Translation: ACF03188.1.
RefSeqYP_001993663.1. NC_011004.1.

3D structure databases

ProteinModelPortalB3QKU1.
SMRB3QKU1. Positions 9-721.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING395960.Rpal_4697.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF03188; ACF03188; Rpal_4697.
GeneID6412383.
KEGGrpt:Rpal_4697.
PATRIC23313936. VBIRhoPal88240_4755.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2225.
HOGENOMHOG000220740.
KOK01638.
OMASQFIENE.
OrthoDBEOG6HJ286.

Enzyme and pathway databases

BioCycRPAL395960:GHPC-4742-MONOMER.
UniPathwayUPA00703; UER00720.

Family and domain databases

Gene3D2.170.170.11. 2 hits.
HAMAPMF_00641. Malate_synth_G.
InterProIPR011076. Malate_synth-like.
IPR023310. Malate_synth_G_beta_sub_dom.
IPR001465. Malate_synthase.
IPR006253. Malate_synthG.
[Graphical view]
PfamPF01274. Malate_synthase. 1 hit.
[Graphical view]
SUPFAMSSF51645. SSF51645. 1 hit.
TIGRFAMsTIGR01345. malate_syn_G. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMASZ_RHOPT
AccessionPrimary (citable) accession number: B3QKU1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 2, 2008
Last modified: May 14, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways