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C0ZZZ0 (MASZ_RHOE4) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 36. 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:RER_32170
OrganismRhodococcus erythropolis (strain PR4 / NBRC 100887) [Complete proteome] [HAMAP]
Taxonomic identifier234621 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length727 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 – 727727Malate synthase G HAMAP-Rule MF_00641
PRO_1000212377

Regions

Region125 – 1262Acetyl-CoA binding By similarity
Region460 – 4634Glyoxylate binding By similarity

Sites

Active site3401Proton acceptor By similarity
Active site6341Proton donor By similarity
Metal binding4351Magnesium By similarity
Metal binding4631Magnesium By similarity
Binding site1181Acetyl-CoA; via carbonyl oxygen By similarity
Binding site2761Acetyl-CoA By similarity
Binding site3131Acetyl-CoA By similarity
Binding site3401Glyoxylate By similarity
Binding site4351Glyoxylate By similarity
Binding site5441Acetyl-CoA; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue6201Cysteine sulfenic acid (-SOH) By similarity

Sequences

Sequence LengthMass (Da)Tools
C0ZZZ0 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: BD7F5753677FE3C1

FASTA72778,695
        10         20         30         40         50         60 
MTERVQVGSL QVAKVLYDFV VEEALPGTGV DAETFWAGAD KVITELAPKN RDLLAKRDDL 

        70         80         90        100        110        120 
QAQIDQWHRD HAGAPIDAAA YKAFLQEIGY LLPTPAEFSV TTANVDTEIT STAGPQLVVP 

       130        140        150        160        170        180 
ILNARFALNA SNARWGSLYD ALYGTNAISE ENGAEKGSGY NKVRGDKVIA WAREFLDAAA 

       190        200        210        220        230        240 
PLASGSHADS TKYVIDGSEL KITLADGTVT TLAQPEKFVG YLGAKDAPTS ILLLNNGLHA 

       250        260        270        280        290        300 
EIQIDASSPI GSTDAAGVKD VVLESAVTTI MDFEDSVAAV DADDKVVGYR NWLGLNRGDL 

       310        320        330        340        350        360 
SEEIKKGAKS FTRTLNGDRK YTAVDGSELS LHGRSLLFVR NVGHLMTNPA ILDADGNEVP 

       370        380        390        400        410        420 
EGILDALITS TCAVHGLSIS DANGPLDNSR TGSIYIVKPK QHGPEEVAFT TELFGRVEQV 

       430        440        450        460        470        480 
LGLPENTLKV GIMDEERRTT VNLAACIKEA VDRVVFINTG FLDRTGDEIH TSMEAGAMVR 

       490        500        510        520        530        540 
KAEMKKQKWI GAYEDWNVDT GLACGLQGKA QIGKGMWAMT ELMADMLEQK IGHPKAGANT 

       550        560        570        580        590        600 
AWVPSPTGAT LHATHYHRVD VFAVQDSLKG KPRASVDDIL TIPLAPSTDW TDAEKKEELD 

       610        620        630        640        650        660 
NNCQSILGYV VRWIDAGVGC SKVPDIHDVA LMEDRATLRI SSQLLANWLR HGIVSESDVV 

       670        680        690        700        710        720 
SALERMAPVV DRQNEGDAEY RNMAPDFDSN IAFQAAKELI LEGAKQPSGY TEPILHRRRR 


EYKAANA 

« Hide

References

[1]"Comparison of the complete genome sequences of Rhodococcus erythropolis PR4 and Rhodococcus opacus B4."
Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PR4 / NBRC 100887.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008957 Genomic DNA. Translation: BAH33925.1.
RefSeqYP_002766664.1. NC_012490.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING234621.RER_32170.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH33925; BAH33925; RER_32170.
GeneID7709397.
KEGGrer:RER_32170.
PATRIC23192880. VBIRhoEry66701_3723.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2225.
HOGENOMHOG000220740.
KOK01638.
OMAPKMHGPD.
OrthoDBEOG6HJ286.
ProtClustDBPRK02999.

Enzyme and pathway databases

BioCycRERY234621:GHDE-3253-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_RHOE4
AccessionPrimary (citable) accession number: C0ZZZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 26, 2009
Last modified: February 19, 2014
This is version 36 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