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Q8FZ50 (MASZ_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BR1648, BS1330_I1642
OrganismBrucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]
Taxonomic identifier204722 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length728 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 – 728728Malate synthase G HAMAP-Rule MF_00641
PRO_0000166883

Regions

Region130 – 1312Acetyl-CoA binding By similarity
Region462 – 4654Glyoxylate binding By similarity

Sites

Active site3451Proton acceptor By similarity
Active site6361Proton donor By similarity
Metal binding4371Magnesium By similarity
Metal binding4651Magnesium By similarity
Binding site1231Acetyl-CoA; via carbonyl oxygen By similarity
Binding site2811Acetyl-CoA By similarity
Binding site3181Acetyl-CoA By similarity
Binding site3451Glyoxylate By similarity
Binding site4371Glyoxylate By similarity
Binding site5461Acetyl-CoA; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue6221Cysteine sulfenic acid (-SOH) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FZ50 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: F95669D002A14EDE

FASTA72879,967
        10         20         30         40         50         60 
MGSAEKRNYV EIEGLAVAPE LVEFLAKEAA PGTGVEPEKF WKGFAAIIRD LAPKNRALLA 

        70         80         90        100        110        120 
KRDELQARID AWYKENRDKG YSQADYQQFL KDIGYLLPEG GAFSVSTTNV DPEITHIAGP 

       130        140        150        160        170        180 
QLVVPVMNAR YALNAANARW GSLYDALYGT DAISEADGAE KGKGYNPKRG EKVIAWAKNF 

       190        200        210        220        230        240 
LDESAPLSTG KWADVAGLAV NDGKLEIRLT DGSATTLKDE SQFKGYNGDA ASPTNVLLAK 

       250        260        270        280        290        300 
HNMHVDIVIN ADHPIGKTDP AHIADVVLES AISTIQDCED SIAAVDAEDK VAVYRNWLGL 

       310        320        330        340        350        360 
MNGKLEDTFE KNGKQMTRRL NGDRTYTAPD GSTLTLKGHS LMLVRNVGHL MTNPAILDAE 

       370        380        390        400        410        420 
GNEVPEGIMD AAFTSLIALH DIGPNGRHMN SREGSVYIVK PKMHGPEEVA FANEIFTRTE 

       430        440        450        460        470        480 
EMLGMKPNTL KIGIMDEERR TTVNLKEAIR AAKDRVVFIN TGFLDRTGDE IHTSMEAGPM 

       490        500        510        520        530        540 
IRKGDMKQAA WIGAYEQWNV DIGLECGLSG HAQIGKGMWA MPDMMAAMLE QKIAHPKAGA 

       550        560        570        580        590        600 
NTAWVPSPTA ATLHATHYHK IDVAAVQEKL KSRPRAKLDD ILSVPVAVRP NWTPDDIQHE 

       610        620        630        640        650        660 
IDNNAQGILG YVVRWIDQGV GCSKVPDINN VGLMEDRATL RISAQHIANW LYHGVVSEAQ 

       670        680        690        700        710        720 
VMETMKRMAA IVDKQNEGDP LYRPMAADFD KSIAFQAACD LVFKGREQPN GYTEPVLHRR 


RLELKQAS 

« Hide

References

[1]"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts."
Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. expand/collapse author list , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.
[2]"Revised genome sequence of Brucella suis 1330."
Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.
J. Bacteriol. 193:6410-6410(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014291 Genomic DNA. Translation: AAN30550.1.
CP002997 Genomic DNA. Translation: AEM18966.1.
RefSeqNP_698635.1. NC_004310.3.
YP_005616458.1. NC_017251.1.

3D structure databases

ProteinModelPortalQ8FZ50.
SMRQ8FZ50. Positions 10-725.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING204722.BR1648.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN30550; AAN30550; BR1648.
AEM18966; AEM18966; BS1330_I1642.
GeneID1167340.
12137411.
KEGGbms:BR1648.
bsi:BS1330_I1642.
PATRIC17791682. VBIBruSui107850_1675.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

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_BRUSU
AccessionPrimary (citable) accession number: Q8FZ50
Secondary accession number(s): G0K6I2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 73 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

Brucella suis

Brucella suis (strain 1330): entries and gene names