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Q11BE3 (MASZ_CHESB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 63. 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:Meso_3915
OrganismChelativorans sp. (strain BNC1) [Complete proteome] [HAMAP]
Taxonomic identifier266779 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeChelativorans

Protein attributes

Sequence length732 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 – 732732Malate synthase G HAMAP-Rule MF_00641
PRO_1000130891

Regions

Region124 – 1252Acetyl-CoA binding By similarity
Region455 – 4584Glyoxylate binding By similarity

Sites

Active site3381Proton acceptor By similarity
Active site6291Proton donor By similarity
Metal binding4301Magnesium By similarity
Metal binding4581Magnesium By similarity
Binding site1171Acetyl-CoA; via carbonyl oxygen By similarity
Binding site2741Acetyl-CoA By similarity
Binding site3111Acetyl-CoA By similarity
Binding site3381Glyoxylate By similarity
Binding site4301Glyoxylate By similarity
Binding site5391Acetyl-CoA; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue6151Cysteine sulfenic acid (-SOH) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q11BE3 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 7B62E9807F370B74

FASTA73280,279
        10         20         30         40         50         60 
MTDRVEINGL KIARELHDFA MNEVLPGTGV DAETFWHSLS QIVHTLSPRN RALLSKRDDL 

        70         80         90        100        110        120 
QAKIDAWHRA NRAPSDLQAY EAFLREIGYL LPEGPDFKVT TSDVDPEISQ IAGPQLVVPV 

       130        140        150        160        170        180 
MNARYALNAA NARWGSLYDA LYGTDAIPET AGAERGKGFN PQRGEKVIAW ARKFLDESIP 

       190        200        210        220        230        240 
LRNASWADAA RLSVKDGKLA VDFDGAAADL ADPAQFTGYS GEADSPREVV LARNGLHVRI 

       250        260        270        280        290        300 
IIDRNHPIGS TDRAGIADVV MEAALTTIMD CEDSVAAVDA EDKVLAYRNW LGLMKGDLEE 

       310        320        330        340        350        360 
TFQKGGTTVT RKLNQDIRLT APDGSPIKLP GRSLMLVRNV GHLMTNPAIL DRDGKEVPEG 

       370        380        390        400        410        420 
IMDAMFTALI ALHDIGPNGR RMNSRAGSMY VVKPKMHGPE EVAFAVELFG SVEDALGMRP 

       430        440        450        460        470        480 
NTIKMGIMDE ERRTTVNLKE CIRAASERVV FINTGFLDRT GDEIHTSMEA GPMIRKGDMK 

       490        500        510        520        530        540 
QSTWIAAYEN WNVDIGLLCG LSGRAQIGKG MWAMPDLMAA MLDQKIAHPK AGANTAWVPS 

       550        560        570        580        590        600 
PTAATLHATH YHQVDVKAVQ EGLKSRTRAK LGDILSIPVA VRPNWSPEDI RQELDNNAQG 

       610        620        630        640        650        660 
ILGYVVRWID QGVGCSKVPD INNVGLMEDR ATLRISSQHI ANWLHHGVVT PEQVMETMKR 

       670        680        690        700        710        720 
MAEVVDSQNA GDPDYEPIAP NFEDSIAFQA ACDLVFKGRE QPNGYTEPVL HARRLQKKAQ 

       730 
DRKGAAADSS RG 

« Hide

References

[1]"Complete sequence of chromosome of Mesorhizobium sp. BNC1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BNC1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000390 Genomic DNA. Translation: ABG65282.1.
RefSeqYP_676447.1. NC_008254.1.

3D structure databases

ProteinModelPortalQ11BE3.
SMRQ11BE3. Positions 2-720.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266779.Meso_3915.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG65282; ABG65282; Meso_3915.
GeneID4181887.
KEGGmes:Meso_3915.
PATRIC21348220. VBICheSp72577_4708.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2225.
HOGENOMHOG000220740.
KOK01638.
OMASQFIENE.
OrthoDBEOG6HJ286.

Enzyme and pathway databases

BioCycCSP266779:GI09-3980-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_CHESB
AccessionPrimary (citable) accession number: Q11BE3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: August 22, 2006
Last modified: June 11, 2014
This is version 63 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