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B8ZSN3 (MASZ_MYCLB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 37. 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:MLBr02069
OrganismMycobacterium leprae (strain Br4923) [Complete proteome] [HAMAP]
Taxonomic identifier561304 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length731 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Pathway

Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. HAMAP-Rule MF_00641

Subunit structure

Homodimer. Ref.2

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 term3D-structure
Complete 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_1000147426

Regions

Region125 – 1262Acetyl-CoA binding By similarity
Region464 – 4674Glyoxylate binding By similarity

Sites

Active site3401Proton acceptor By similarity
Active site6381Proton donor By similarity
Metal binding4391Magnesium
Metal binding4671Magnesium
Binding site1181Acetyl-CoA; via carbonyl oxygen By similarity
Binding site2761Acetyl-CoA By similarity
Binding site3131Acetyl-CoA By similarity
Binding site3401Glyoxylate By similarity
Binding site4391Glyoxylate By similarity
Binding site5481Acetyl-CoA; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue6241Cysteine sulfenic acid (-SOH) By similarity

Secondary structure

.................................................................................................................. 731
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
B8ZSN3 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 3878C0DAE26DECDA

FASTA73180,143
        10         20         30         40         50         60 
MTDRVSAGNL RVARVLYDFV NNEALPGTDI NPNSFWSGVA KVVADLTPQN QSLLNSRDEL 

        70         80         90        100        110        120 
QAQIDKWHRH RVIEPFDVDA YRQFLIDIGY LLPEPDDFTI STSGVDDEIT MTAGPQLVVP 

       130        140        150        160        170        180 
VLNARFALNA ANARWGSLYD ALYGTDTIPE TEGAEKGSEY NKIRGDKVIA YARKFMDQAV 

       190        200        210        220        230        240 
PLASDSWTNA TGVSIFDGQL QIAIGTNSTG LASPEKFVGY NRQLRSSNWS VLLANHGLHI 

       250        260        270        280        290        300 
EVLIDPESPI GKTDPVGIKD VILESAITTI MDFEDSVTAV DADDKVRGYR NWLGLNKGDL 

       310        320        330        340        350        360 
TEEVNKDGKT FTRVLNADRS YTTPDGGELT LPGRSLLFVR NVGHLTTSDA ILVDGGDGQE 

       370        380        390        400        410        420 
KEVFEGIIDA VFTGLAAIHG LKTGEANGPL TNSRTGSIYI VKPKMHGPAE VAFTCELFSR 

       430        440        450        460        470        480 
VEDVLGLPQG TLKVGIMDEE RRTTLNLKAC IKAAADRVVF INTGFLDRTG DEIHTSMEAG 

       490        500        510        520        530        540 
PMIRKGAMKN STWIKAYEDA NVDIGLAAGF KGKAQIGKGM WAMTELMADM VEQKIGQPKA 

       550        560        570        580        590        600 
GATTAWVPSP TAATLHAMHY HQVDVAAVQQ ELTGQRRATV DQLLTIPLAK ELAWAPEEIR 

       610        620        630        640        650        660 
EEVDNDCQSI LGYVVRWVDQ GIGCSKVPDI HNVALMEDRA TLRISSQLLA NWLRHGVITS 

       670        680        690        700        710        720 
EDVRASLERM APLVDQQNAE DPAYRPMAPN FDDSIAFLAA QELILSGAQQ PNGYTEPILH 

       730 
RRRREFKAQN R 

« Hide

References

« Hide 'large scale' references
[1]"Comparative genomic and phylogeographic analysis of Mycobacterium leprae."
Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A., Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C., Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H., Vera-Cabrera L. expand/collapse author list , Stefani M.M., Banu S., Macdonald M., Sapkota B.R., Spencer J.S., Thomas J., Harshman K., Singh P., Busso P., Gattiker A., Rougemont J., Brennan P.J., Cole S.T.
Nat. Genet. 41:1282-1289(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Br4923.
[2]"The structure of glcb from mycobacterium leprae."
Seattle StructuraL Genomics Center for Infectious Disease (SSGCID)
Submitted (APR-2012) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH MAGNESIUM ION, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM211192 Genomic DNA. Translation: CAR72166.1.
RefSeqYP_002504009.1. NC_011896.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4EX4X-ray2.10A/B1-731[»]
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING561304.MLBr_02069.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR72166; CAR72166; MLBr02069.
GeneID7325139.
KEGGmlb:MLBr_02069.
PATRIC18047419. VBIMycLep121698_3918.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2225.
KOK01638.
OMASTIMDFE.
OrthoDBEOG6HJ286.

Enzyme and pathway databases

BioCycMLEP561304:GJP6-2112-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_MYCLB
AccessionPrimary (citable) accession number: B8ZSN3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: May 14, 2014
This is version 37 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways