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Q0A845 (MASZ_ALKEH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. 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:Mlg_1646
OrganismAlkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1) [Complete proteome] [HAMAP]
Taxonomic identifier187272 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeAlkalilimnicola

Protein attributes

Sequence length729 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 – 729729Malate synthase G HAMAP-Rule MF_00641
PRO_1000130886

Regions

Region125 – 1262Acetyl-CoA binding By similarity
Region461 – 4644Glyoxylate binding By similarity

Sites

Active site3441Proton acceptor By similarity
Active site6351Proton donor By similarity
Metal binding4361Magnesium By similarity
Metal binding4641Magnesium By similarity
Binding site1181Acetyl-CoA; via carbonyl oxygen By similarity
Binding site2801Acetyl-CoA By similarity
Binding site3171Acetyl-CoA By similarity
Binding site3441Glyoxylate By similarity
Binding site4361Glyoxylate By similarity
Binding site5451Acetyl-CoA; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue6211Cysteine sulfenic acid (-SOH) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0A845 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 05A52DB21B7F6187

FASTA72980,444
        10         20         30         40         50         60 
MTQRIEVGGL QVAQELYDLV AKEIAPATGV DADGFWTHLG AIVRDLGARN RELLQKRDEI 

        70         80         90        100        110        120 
QQAIDKWHLE RKGQPHDAAA YKTFLEELGY LQPEGEDFEA TTENVDPEIA EVAGPQLVVP 

       130        140        150        160        170        180 
INNARFALNA ANARWGSLYD ALYGSDVLPE DDGAEKGTRY NPVRGKKVME YAGRVLDEVA 

       190        200        210        220        230        240 
PLAQGRHGDV VAYNLVDDNG RKRLQARLSD GSETGLADPE GLAGYNGAED DPTVLLLRHN 

       250        260        270        280        290        300 
GLHVEIQIDR EHLIGKDHPA GVKDVVMEAA VTAIMDCEDS VAAVDAEDKT AVYRNWLGLM 

       310        320        330        340        350        360 
NGDLETSLEK GGKTIQRRLN ADRDYIGADG RALTLPGRSL MLIRNVGHLM TTPAVLDADG 

       370        380        390        400        410        420 
NEIPEGILDG MVTSLIALYD LKGLGRYRNS RSGSMYIVKP KMHGPDEVAF AVELFGRIED 

       430        440        450        460        470        480 
ALGMERNTLK IGVMDEERRT TVNLKACIRE AKERIIFINT GFLDRTGDEM HTSMEAGPMI 

       490        500        510        520        530        540 
RKAEMKSSRW LNAYEDWNVD IGLECGLRGR AQIGKGMWTM PDLMKGMMEA KIGHPKAGAN 

       550        560        570        580        590        600 
CAWVPSPTAA TLHAIHYHQV NVAEVQDRLA GQRRATLDDL LTIPLEPSPS WSAEEIQQEL 

       610        620        630        640        650        660 
DNNCQGILGY VVRWVDQGIG CSKVPDINNV GLMEDRATLR IASQLLANWL HHGICSEEQI 

       670        680        690        700        710        720 
METMKRMAKV VDQQNAGDPN YRPMAADYDG SVAFQAACEL VLKGREQPSG YTEPVLHRRR 


REAKAKFGA 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000453 Genomic DNA. Translation: ABI56992.1.
RefSeqYP_742482.1. NC_008340.1.

3D structure databases

ProteinModelPortalQ0A845.
SMRQ0A845. Positions 2-726.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING187272.Mlg_1646.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI56992; ABI56992; Mlg_1646.
GeneID4270247.
KEGGaeh:Mlg_1646.
PATRIC20862557. VBIAlkEhr114327_1649.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2225.
HOGENOMHOG000220740.
KOK01638.
OrthoDBEOG6HJ286.

Enzyme and pathway databases

BioCycAEHR187272:GHAX-1690-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_ALKEH
AccessionPrimary (citable) accession number: Q0A845
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: October 17, 2006
Last modified: May 14, 2014
This is version 60 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