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A0PSI5 (MASZ_MYCUA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:MUL_3055
OrganismMycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]
Taxonomic identifier362242 [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_1000056911

Regions

Region125 – 1262Acetyl-CoA binding By similarity
Region463 – 4664Glyoxylate binding By similarity

Sites

Active site3391Proton acceptor By similarity
Active site6371Proton donor By similarity
Metal binding4381Magnesium By similarity
Metal binding4661Magnesium By similarity
Binding site1181Acetyl-CoA; via carbonyl oxygen By similarity
Binding site2751Acetyl-CoA By similarity
Binding site3121Acetyl-CoA By similarity
Binding site3391Glyoxylate By similarity
Binding site4381Glyoxylate By similarity
Binding site5471Acetyl-CoA; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue6231Cysteine sulfenic acid (-SOH) By similarity

Sequences

Sequence LengthMass (Da)Tools
A0PSI5 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: BB2A4320CAA7264F

FASTA73179,479
        10         20         30         40         50         60 
MTDRVSAGNL RVARVLYDFV NNEALPGTDI DQDSFWAGVD KVVTDLTPQN QDLLKTRDDL 

        70         80         90        100        110        120 
QAQIDKWHRH RVIEPLDPQA YREFLTEIGY LLPAPEDFTI TTSGVDDEIT TTAGPQLVVP 

       130        140        150        160        170        180 
ILNARFALNA ANARWGSLYD ALYGTDVISE SDGAEKGRGY NKVRGDKVIA YARQFLDDSV 

       190        200        210        220        230        240 
PLAGASYTDA TGFKVEDGQL VVSLADTSAA LADPGQFAGY TGTAENPKSI LLANHGLHIE 

       250        260        270        280        290        300 
ILIDPESQIG ATDGAGVKDV ILESAITTIM DFEDSVAAVD ADDKALGYRN WLGLNRGDLS 

       310        320        330        340        350        360 
EDVTKDDKTF TRVLNTDRTY TAPHGGELTL PGRSLLFVRN VGHLMTNDAI VSDAEGAEGA 

       370        380        390        400        410        420 
PVFEGIMDAL FTGLIAIHGL RSTDANGLLT NSRTGSIYIV KPKMHGPAEV AFTCELFSRV 

       430        440        450        460        470        480 
EDVLGLPQGT MKVGIMDEER RTTLNLKACI KAAADRVVFI NTGFLDRTGD EIHTSMEAGP 

       490        500        510        520        530        540 
MIRKGAMKNT AWIKAYEDAN VDTGLAAGFS GKAQIGKGMW AMTELMADMV EQKIAQPKAG 

       550        560        570        580        590        600 
ATTAWVPSPT AATLHAMHYH KVDVFAVQKE LQGKTRTSVD ELLTIPLAKE LAWAPEEIRE 

       610        620        630        640        650        660 
EVDNNCQSIL GYVVRWIDQG VGCSKVPDIH NVALMEDRAT LRISSQLLAN WLRHGVITSE 

       670        680        690        700        710        720 
DVRASLERMA PLVDKQNAGD PEYHAMAPNF DDSIAFLAAQ DLILSGAQQP NGYTEPILHR 

       730 
RRRELKARAG A 

« Hide

References

[1]"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer."
Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. expand/collapse author list , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.
Genome Res. 17:192-200(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Agy99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000325 Genomic DNA. Translation: ABL05304.1.
RefSeqYP_906775.1. NC_008611.1.

3D structure databases

ProteinModelPortalA0PSI5.
SMRA0PSI5. Positions 5-730.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING362242.MUL_3055.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL05304; ABL05304; MUL_3055.
GeneID4553683.
KEGGmul:MUL_3055.
PATRIC18173441. VBIMycUlc37413_3556.

Organism-specific databases

GenoListMUL_3055.
CMRSearch...

Phylogenomic databases

eggNOGCOG2225.
HOGENOMHOG000220740.
KOK01638.
OMASQFIENE.
OrthoDBEOG6HJ286.

Enzyme and pathway databases

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_MYCUA
AccessionPrimary (citable) accession number: A0PSI5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 9, 2007
Last modified: May 14, 2014
This is version 52 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