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A9BRF0 (MASZ_DELAS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. 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:Daci_0665
OrganismDelftia acidovorans (strain DSM 14801 / SPH-1) [Complete proteome] [HAMAP]
Taxonomic identifier398578 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeDelftia

Protein attributes

Sequence length730 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 – 730730Malate synthase G HAMAP-Rule MF_00641
PRO_1000130889

Regions

Region125 – 1262Acetyl-CoA binding By similarity
Region459 – 4624Glyoxylate binding By similarity

Sites

Active site3401Proton acceptor By similarity
Active site6381Proton donor By similarity
Metal binding4341Magnesium By similarity
Metal binding4621Magnesium By similarity
Binding site1181Acetyl-CoA; via carbonyl oxygen By similarity
Binding site2761Acetyl-CoA By similarity
Binding site3131Acetyl-CoA By similarity
Binding site3401Glyoxylate By similarity
Binding site4341Glyoxylate By similarity
Binding site5431Acetyl-CoA; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue6241Cysteine sulfenic acid (-SOH) By similarity

Sequences

Sequence LengthMass (Da)Tools
A9BRF0 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 74351D7228A3262E

FASTA73078,381
        10         20         30         40         50         60 
MTDRTQAHSL QVATELHRFI NEQVLPGTGV APEAFWKGFD AIVNDLAPRN AALLAERDRL 

        70         80         90        100        110        120 
QTELDTWHKA HPGPITDMAG YQQFLTQIGY LVEQPKDAKA TTTNVDAELA IQAGPQLVVP 

       130        140        150        160        170        180 
ILNARYALNA ANARWGSLYD ALYGTDAIGE DGGAEKGKGY NPVRGAKVIA FARDFLDQAA 

       190        200        210        220        230        240 
PLASGSHKDA AGYRVEAGQL VVALKSGGTT GLKNTAQFVG YQGDAAAPSS VLLLNNGLHI 

       250        260        270        280        290        300 
DIRIDKTTAI GQTDAAGVAD VVVEAALSTI LDLEDSVAAV DAEDKVVGYA NWLGILKGTL 

       310        320        330        340        350        360 
TETFDKGGKS MTRGLNADRE YTGADGKPVK LHGRSLMFVR NVGHLMTNPA ILWGNGKEIP 

       370        380        390        400        410        420 
EGILDAMVTT AIAVHDIKGL GANGIRNSRT GSVYIVKPKM HGPAEAAFAS ELFGRVEKVL 

       430        440        450        460        470        480 
GLPENTVKLG IMDEERRTSV NLKACIAAAA SRVAFINTGF LDRTGDEMHT AMYAGPMVRK 

       490        500        510        520        530        540 
ADMKGSAWLA AYERSNVLVG LGLGLRGKAQ IGKGMWAMPD LMKAMLEQKI GHPKAGANTA 

       550        560        570        580        590        600 
WVPSPTAATL HALHYHQVNV AEVQKQLEQT NADAERATIL ADLLQVPVVK EDKWSAAEKQ 

       610        620        630        640        650        660 
QELDNNVQGI LGYVVRWVDQ GVGCSKVPDI HNVGLMEDRA TLRISSQHIA NWLQHGIVTE 

       670        680        690        700        710        720 
AQVRETFERM AAVVDQQNAG DALYKPMAGH FDTSMAYQAA CDLVFKGKEQ PSGYTEPLLH 

       730 
AWRLKVKAAA 

« Hide

References

[1]"Complete sequence of Delftia acidovorans DSM 14801 / SPH-1."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 14801 / SPH-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000884 Genomic DNA. Translation: ABX33311.1.
RefSeqYP_001561696.1. NC_010002.1.

3D structure databases

ProteinModelPortalA9BRF0.
SMRA9BRF0. Positions 10-729.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING398578.Daci_0665.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX33311; ABX33311; Daci_0665.
GeneID5746218.
KEGGdac:Daci_0665.
PATRIC21635185. VBIDelAci41351_0681.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2225.
HOGENOMHOG000220740.
KOK01638.
OMAPKMHGPD.
OrthoDBEOG6HJ286.
ProtClustDBPRK02999.

Enzyme and pathway databases

BioCycDACI398578:GHK3-682-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_DELAS
AccessionPrimary (citable) accession number: A9BRF0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: January 15, 2008
Last modified: February 19, 2014
This is version 47 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