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Q13YU3 (MASZ_BURXL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:Bxeno_A2208
ORF Names:Bxe_A2223
OrganismBurkholderia xenovorans (strain LB400) [Complete proteome] [HAMAP]
Taxonomic identifier266265 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

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_1000056900

Regions

Region125 – 1262Acetyl-CoA binding By similarity
Region454 – 4574Glyoxylate binding By similarity

Sites

Active site3401Proton acceptor By similarity
Active site6331Proton donor By similarity
Metal binding4291Magnesium By similarity
Metal binding4571Magnesium By similarity
Binding site1181Acetyl-CoA; via carbonyl oxygen By similarity
Binding site2751Acetyl-CoA By similarity
Binding site3121Acetyl-CoA By similarity
Binding site3401Glyoxylate By similarity
Binding site4291Glyoxylate By similarity
Binding site5381Acetyl-CoA; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue6191Cysteine sulfenic acid (-SOH) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q13YU3 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 342CB47D2034DB90

FASTA72479,450
        10         20         30         40         50         60 
MTQMNPRGGL QVAANLDQFV ETEALPGTGL DSAAFWSGFD ALVHELAPKN RALLAERDRL 

        70         80         90        100        110        120 
QTELDNWHRA NPGPVRDLRA YRAFLEGIGY IVPVPASVKA TTDHVDTEIA EQAGPQLVVP 

       130        140        150        160        170        180 
LSNQRYALNA ANARWGSLYD ALYGTDAIPE ANGAEKQKAF NPVRGAAVIA YARRFLDQAA 

       190        200        210        220        230        240 
PLANGSHADA TRYGVEGGKL VVTLKNGTSE LKTPAQFIGY QGEESAPSAV LLKHNGLHFE 

       250        260        270        280        290        300 
IQIDANDSIG KTDSAHVKDV VVEAAVSTII DCEDSVAAVD ADDKVQLYRN WLGLMNGDLT 

       310        320        330        340        350        360 
EEVTKNGKTF TRRLNADRVY TAANGTAPVV LHGRSLLFIR NVGHLMTNPA VLTKDGHEIP 

       370        380        390        400        410        420 
EGILDAVITS LCALHDRKHK LNSRTGSIYI VKPKMHGPAE VAFASELFAR VEDLLKLPRN 

       430        440        450        460        470        480 
TIKMGIMDEE RRTSVNLLAC INEARERVAF INTGFLDRTG DEMHTAMEAG PMLRKGDMKS 

       490        500        510        520        530        540 
SAWIAAYERS NVLVGLSAGL RGRSQIGKGM WAMPDLMHAM LEQKIAHPKA GANTAWVPSP 

       550        560        570        580        590        600 
TAATLHALHY HQVDVQAVQQ ELERTDYAKV RDELLDGLLT IPVVAEAKWS DDEIRSEIDN 

       610        620        630        640        650        660 
NAQGILGYVV RWIDQGVGCS KVPDIHNVGL MEDRATLRIS SQHIANWLYH GVVKRELVEE 

       670        680        690        700        710        720 
TFRRMARVVD EQNAGDPLYK PMAPGFDTIA FKAAQALVFE GRQQPSGYTE PLLHKFRLEV 


KKEA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000270 Genomic DNA. Translation: ABE30746.1.
RefSeqYP_558798.1. NC_007951.1.

3D structure databases

ProteinModelPortalQ13YU3.
SMRQ13YU3. Positions 10-722.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266265.Bxe_A2223.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE30746; ABE30746; Bxe_A2223.
GeneID4003121.
KEGGbxe:Bxe_A2223.
PATRIC19329978. VBIBurXen52548_2309.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2225.
HOGENOMHOG000220740.
KOK01638.
OMAIQIDAND.
OrthoDBEOG6HJ286.
ProtClustDBPRK02999.

Enzyme and pathway databases

BioCycBXEN266265:GJII-2309-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_BURXL
AccessionPrimary (citable) accession number: Q13YU3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: February 19, 2014
This is version 53 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