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Q8FNB3 (MASZ_COREF) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 75. 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:masZ
Ordered Locus Names:CE2231
OrganismCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) [Complete proteome] [HAMAP]
Taxonomic identifier196164 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length748 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 – 748748Malate synthase G HAMAP-Rule MF_00641
PRO_0000166884

Regions

Region148 – 1492Acetyl-CoA binding By similarity
Region478 – 4814Glyoxylate binding By similarity

Sites

Active site3621Proton acceptor By similarity
Active site6531Proton donor By similarity
Metal binding4531Magnesium By similarity
Metal binding4811Magnesium By similarity
Binding site1411Acetyl-CoA; via carbonyl oxygen By similarity
Binding site2981Acetyl-CoA By similarity
Binding site3351Acetyl-CoA By similarity
Binding site3621Glyoxylate By similarity
Binding site4531Glyoxylate By similarity
Binding site5621Acetyl-CoA; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue6391Cysteine sulfenic acid (-SOH) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FNB3 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: F9550473EC4E9A09

FASTA74883,491
        10         20         30         40         50         60 
MPAHTRSLAS KELCMNHQQI DAADKTERVT VGGMQVAKVL RDFLTESVLP RVGVDAERFW 

        70         80         90        100        110        120 
NGFGDIVRDM TPRNRELLAR RDELQAQLDE YYRENPGKPD PEKYEAFLRE IGYLVDEPAP 

       130        140        150        160        170        180 
AEIRTQNIDS EIATTAGPQL VVPILNARFA LNAANARWGS LYDALYGTNA IPDEDGAERG 

       190        200        210        220        230        240 
AEYNPVRGQK VIQWGRDFLD AVLPLDGASH ADVEKYNITD GKLAAHVNDG IYRLKDRDAY 

       250        260        270        280        290        300 
LGFTGYFEDP TSILLQNNGL HIELQIDPTH PIGKEDKTGL KDIILESAIT TIMDFEDSVA 

       310        320        330        340        350        360 
AVDAEDKTLG YRNWFLLNTG ELTEEVAKGD RTFTRKLNDD RVFIGKNGAE LTLHGRSLLF 

       370        380        390        400        410        420 
VRNVGHLMTN PAILVDGEEI YEGIMDAIIT TVCAIPGIAP QNKKKNSRKG SIYIVKPKQH 

       430        440        450        460        470        480 
GPEEVAFTNE LFARVEDLLD LPRHTLKVGV MDEERRTSVN LDACIMEVAD RLAFINTGFL 

       490        500        510        520        530        540 
DRTGDEIHTS MEAGAMVRKA DMQTAPWKQA YEDNNVDAGI QRGLPGKAQI GKGMWAMTEL 

       550        560        570        580        590        600 
MGEMLEKKIG QLREGANTAW VPSPTGATLH ATHYHRVDVF KVQDELRAAG RRDSLGKILD 

       610        620        630        640        650        660 
VPVAPDTNWT DAEKREELDN NCQSILGYVV RWVEQGVGCS KVPDIHDIDL MEDRATLRIS 

       670        680        690        700        710        720 
SQILANWLRH GVVTEEQVIE SLERMAVVVD EQNAGDPNYL NMAPNFTESV AFQAARDLIL 

       730        740 
KGTESPAGYT EPILHARRRE FKELHGIK 

« Hide

References

[1]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000035 Genomic DNA. Translation: BAC19041.1.
RefSeqNP_738841.1. NC_004369.1.

3D structure databases

ProteinModelPortalQ8FNB3.
SMRQ8FNB3. Positions 26-742.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196164.CE2231.

Proteomic databases

PRIDEQ8FNB3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC19041; BAC19041; BAC19041.
GeneID1032082.
KEGGcef:CE2231.
PATRIC21490591. VBICorEff9312_2207.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000220740.
KOK01638.
OMAPKMHGPD.
OrthoDBEOG6HJ286.
ProtClustDBPRK02999.

Enzyme and pathway databases

BioCycCEFF196164:GJW8-2270-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_COREF
AccessionPrimary (citable) accession number: Q8FNB3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 75 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