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A3Q0E7 (MASZ_MYCSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 51. 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:Mjls_2844
OrganismMycobacterium sp. (strain JLS) [Complete proteome] [HAMAP]
Taxonomic identifier164757 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length731 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 – 731731Malate synthase G HAMAP-Rule MF_00641
PRO_1000056907

Regions

Region125 – 1262Acetyl-CoA binding By similarity
Region462 – 4654Glyoxylate binding By similarity

Sites

Active site3421Proton acceptor By similarity
Active site6361Proton donor By similarity
Metal binding4371Magnesium By similarity
Metal binding4651Magnesium By similarity
Binding site1181Acetyl-CoA; via carbonyl oxygen By similarity
Binding site2771Acetyl-CoA By similarity
Binding site3141Acetyl-CoA By similarity
Binding site3421Glyoxylate 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
A3Q0E7 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: FB2D4F7132115B6C

FASTA73179,879
        10         20         30         40         50         60 
MTDRVTVGNL RVARALYDFI TDEALAGTDL DPDSFWSGVD KVVTDLTPRN QELLARRDDL 

        70         80         90        100        110        120 
QAQIDKWHRQ RAIGPHDADE YKQFLTEIGY LEPDPGDFTI TTAGVDDEIT TTAGPQLVVP 

       130        140        150        160        170        180 
VLNARFALNA ANARWGSLYD ALYGTDVISD EDGAEKGTSY NRVRGDKVIA YAREFLDGAA 

       190        200        210        220        230        240 
PLASGSYADA TGFRIEDGQV QVELGDDQWV GLAGPDQFVG YTGELGSPQW SILLRNNGLH 

       250        260        270        280        290        300 
IEILIDPDSP VGSTDKAGVK DVVLESAVTT IMDFEDSVAA VDAEDKVLGY RNWLGLNRGD 

       310        320        330        340        350        360 
LSEEVSKGDK TFTRVLNPDR TYTTPDGSGE LTLPGRSLLF VRNVGHLMTN DAITDAEGNE 

       370        380        390        400        410        420 
VFEGIQDALF TGLIAMHGLK ESDANGPLRN SRTGSVYIVK PKMHGPAEVA YTVDLFSRVE 

       430        440        450        460        470        480 
DVLGLPQNTL KVGIMDEERR TTLNLKACIK AAADRVVFIN TGFLDRTGDE IHTSMEAGPM 

       490        500        510        520        530        540 
IRKGAMKSQP WIKAYEDQNV DVGLATGFSG RAQIGKGMWA MTDLMADMVE QKIGQPKAGA 

       550        560        570        580        590        600 
TTAWVPSPTA ATLHAMHYHQ VDVYAVHKEL EGKQRASLDD LLTIPLAKEL AWAPEEIREE 

       610        620        630        640        650        660 
VDNNCQSILG YVVRWIDAGV GCSKVPDIHD IALMEDRATL RISSQLLANW LRHGVITEED 

       670        680        690        700        710        720 
VKTSLRRMAA VVDEQNAKDP DFKPMATDPD SSIAFQAAQE LILAGGTQPS GYTEPILHRR 

       730 
RREYKASVAG A 

« Hide

References

[1]"Complete sequence of Mycobacterium sp. JLS."
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J., Sims R.C., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JLS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000580 Genomic DNA. Translation: ABN98624.1.
RefSeqYP_001071115.1. NC_009077.1.

3D structure databases

ProteinModelPortalA3Q0E7.
SMRA3Q0E7. Positions 5-729.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING164757.Mjls_2844.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN98624; ABN98624; Mjls_2844.
GeneID4878558.
KEGGmjl:Mjls_2844.
PATRIC18091857. VBIMycSp51234_2864.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2225.
HOGENOMHOG000220740.
KOK01638.
OMASQFIENE.
OrthoDBEOG6HJ286.

Enzyme and pathway databases

BioCycMSP164757:GHV3-2858-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_MYCSJ
AccessionPrimary (citable) accession number: A3Q0E7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 3, 2007
Last modified: May 14, 2014
This is version 51 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