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

Q89UE3 (MASZ_BRADU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 72. 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:bll1474
OrganismBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110) [Reference proteome] [HAMAP]
Taxonomic identifier224911 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length721 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
Reference 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 – 721721Malate synthase G HAMAP-Rule MF_00641
PRO_0000166881

Regions

Region124 – 1252Acetyl-CoA binding By similarity
Region456 – 4594Glyoxylate binding By similarity

Sites

Active site3391Proton acceptor By similarity
Active site6301Proton donor By similarity
Metal binding4311Magnesium By similarity
Metal binding4591Magnesium By similarity
Binding site1171Acetyl-CoA; via carbonyl oxygen By similarity
Binding site2741Acetyl-CoA By similarity
Binding site3111Acetyl-CoA By similarity
Binding site3391Glyoxylate By similarity
Binding site4311Glyoxylate By similarity
Binding site5401Acetyl-CoA; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue6161Cysteine sulfenic acid (-SOH) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q89UE3 [UniParc].

Last modified April 30, 2003. Version 1.
Checksum: B34A9EBCEDA1422E

FASTA72177,928
        10         20         30         40         50         60 
MKRVDAHGLK IAPVLFDFIA KEAAPKTGIA PDAFWAGVAA IIKDLGPKNR ALLALRDALQ 

        70         80         90        100        110        120 
AKIDDWHRAN KGKAFDLNAY TAFLKEIGYL VPEPATQKVE TANVDEEIGK ICGPQLVVPL 

       130        140        150        160        170        180 
TNARYALNAA NARWGSLYDA FYGTDAIPHD PSESGKGYNK ARGDKVIAKA KAFLDAAVPL 

       190        200        210        220        230        240 
ATGSHTDVTA YSIVAGQLAV KLKSGNATAL KNAAQFAGFQ GDAAAPSAVL LVNNGLHVEV 

       250        260        270        280        290        300 
TINRNSAIGK DDPAGVADMV MEAAVSTILD MEDSVAAVDA EDKVLVYRNT LGLMNGTLSA 

       310        320        330        340        350        360 
DFEKGGKTLT RSLNADRSYK TPDGKGEVKL HGRSLLLMRN CGHHMFTDAV LDERGEEVPE 

       370        380        390        400        410        420 
GLLDAAVSGL LAIHDLKGNS KVKNSRTGSA YIVKPKMHGP DEVSFTCEIF DRVEKMLGLP 

       430        440        450        460        470        480 
ENTLKVGIMD EERRTTVNLK ACIQRASKRI MFINTGFLDR TGDEIHTSME AGPMIRKNEM 

       490        500        510        520        530        540 
KAQAWIKAYE DWNVDMGLID GLPGHAQIGK GMWAAPDKMA DMLAQKLAHP QAGATTAWVP 

       550        560        570        580        590        600 
SPTAATLHAL HYHQVNVIAR QEELTKGGPR AKLSDILTIP VSKSNWAPDD VKQEIDNNCQ 

       610        620        630        640        650        660 
GILGYVVRWI DQGVGCSKVP DIHDVGLMED RATLRISSQH LANWLHQGVI TEAQVMESLK 

       670        680        690        700        710        720 
RMAVVVDKQN AGDAIYKPMA PAFDGVAFKA ACDLIFKGRE QPNGYTEYIL TARRREAKAA 


G 

« Hide

References

[1]"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110."
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.
DNA Res. 9:189-197(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000040 Genomic DNA. Translation: BAC46739.1.
RefSeqNP_768114.1. NC_004463.1.

3D structure databases

ProteinModelPortalQ89UE3.
SMRQ89UE3. Positions 3-719.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224911.bll1474.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC46739; BAC46739; BAC46739.
GeneID1055224.
KEGGbja:bll1474.
PATRIC21186546. VBIBraJap65052_1535.

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBJAP224911:GJEJ-1492-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_BRADU
AccessionPrimary (citable) accession number: Q89UE3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 30, 2003
Last modified: February 19, 2014
This is version 72 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