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Q9AE55 (MASZ_RHOFA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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
Synonyms:vicA
OrganismRhodococcus fascians
Taxonomic identifier1828 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length724 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
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 – 724724Malate synthase G HAMAP-Rule MF_00641
PRO_0000166899

Regions

Region125 – 1262Acetyl-CoA binding By similarity
Region457 – 4604Glyoxylate binding By similarity

Sites

Active site3401Proton acceptor By similarity
Active site6311Proton donor By similarity
Metal binding4321Magnesium By similarity
Metal binding4601Magnesium 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 site4321Glyoxylate By similarity
Binding site5411Acetyl-CoA; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue6171Cysteine sulfenic acid (-SOH) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9AE55 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: F889FE883890995E

FASTA72478,610
        10         20         30         40         50         60 
MTDRVQAGGL QVAKVLFDFV EKEALPGTDL DSEAFWAGAA SVIADLAPKN KALLAVRDEI 

        70         80         90        100        110        120 
QGKVDAWHGE HAGAEYDRAA YKAFLKEIGY LLDEPADFQI HTSGVDTEIT TTAGPQLVVP 

       130        140        150        160        170        180 
VLNARFAINA SNARWGSLYD ALYGTDAIPE TDGAEKGTSY NKVRGDKVIA FARDFLDEAL 

       190        200        210        220        230        240 
PLSSGSHVGT TGYVVDAASL TVTLADGSTV GLKDPSQLLG YQGTPDAPTA ILFVHNGLHF 

       250        260        270        280        290        300 
EIQIDPESPI GKTDGAGVKD VLLESAVTTI MDFEDSVAAV DADDKVLGYR NWLGLMKGDL 

       310        320        330        340        350        360 
TEEVSKGGKT FTRAMNKDRT YTSVDGSELT LHGRSLLFVR NVGHLMTSDA ILDADGNEVP 

       370        380        390        400        410        420 
EGILDALFTS LAGLHSLTPD NVLSNSRTGS LYIVKPKMHG PDEVAFTAEL FGRVEQVLGL 

       430        440        450        460        470        480 
PTNTLKVGIM DEERRTTVNL KACIQAASER VVFINTGFLD RTGDEIHTSM EAGPVVRKGA 

       490        500        510        520        530        540 
MKGEKWIAAY EDFNVDTGLA AGLQGKAQIG KGMWAMPDLM HDMLEQKIGH PKAGANTAWV 

       550        560        570        580        590        600 
PSPTAATLHA LHYHKVDVFA RQHEIAKAKR ATVDEILEIP LAPSTDWTDE EKQNELDNNS 

       610        620        630        640        650        660 
QSILGYVVRW IDHGVGCSKV PDINDIALME DRATLRISSQ FIANWLRHGI VTEEQVRESL 

       670        680        690        700        710        720 
KRMAPVVDRQ NASDPTYKPL APDFDTNIAF QAASDLIFQG TSQPNGYTEP ILHRRRREYK 


AVNA 

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References

[1]"Characterization of a chromosomal locus that affects pathogenicity in Rhodococcus fascians."
Vereecke D.M., Cornelis K., Van Montagu M., El Jaziri M., Holsters M., Goethals K.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: D188.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ301559 Genomic DNA. Translation: CAC35701.1.

3D structure databases

ProteinModelPortalQ9AE55.
SMRQ9AE55. Positions 2-721.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_RHOFA
AccessionPrimary (citable) accession number: Q9AE55
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: June 1, 2001
Last modified: February 19, 2014
This is version 57 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