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A1T9P9 (MASZ_MYCVP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. 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:Mvan_3097
OrganismMycobacterium vanbaalenii (strain DSM 7251 / PYR-1) [Complete proteome] [HAMAP]
Taxonomic identifier350058 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length734 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 – 734734Malate synthase G HAMAP-Rule MF_00641
PRO_1000056912

Regions

Region125 – 1262Acetyl-CoA binding By similarity
Region465 – 4684Glyoxylate binding By similarity

Sites

Active site3451Proton acceptor By similarity
Active site6391Proton donor By similarity
Metal binding4401Magnesium By similarity
Metal binding4681Magnesium By similarity
Binding site1181Acetyl-CoA; via carbonyl oxygen By similarity
Binding site2761Acetyl-CoA By similarity
Binding site3131Acetyl-CoA By similarity
Binding site3451Glyoxylate By similarity
Binding site4401Glyoxylate By similarity
Binding site5491Acetyl-CoA; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue6251Cysteine sulfenic acid (-SOH) By similarity

Sequences

Sequence LengthMass (Da)Tools
A1T9P9 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 8A57EC7050B20332

FASTA73479,327
        10         20         30         40         50         60 
MTDRVTVGNL RVAPVLYDFI NNEALPGTDI DPDTFWSGVD KVVADLTPRN QDLLARRDDL 

        70         80         90        100        110        120 
QAQIDRWHRA RVIGGFEPED YKQFLTDIGY LEPEPADFSI TTAGVDDEIT TTAGPQLVVP 

       130        140        150        160        170        180 
ILNARFALNA ANARWGSLYD ALYGTDVISD EGGAEAGSGY NPVRGDKVIA YARRFLDGAV 

       190        200        210        220        230        240 
PLASGSWSDI TGLKLDEGQL AATLDDGGTV GLGTPEQFVG YLGDAEAPTA VLLVNNGLHI 

       250        260        270        280        290        300 
EILIDAEAPI GATDKAGIKD VVLESAITTI MDFEDSVAAV DADDKVLGYR NWLGLNRGDL 

       310        320        330        340        350        360 
AEEVSKGGKT FTRVLNSDRT YTAANPGPDG ATELTLPGRS LLFVRNVGHL MTNDAIVDAQ 

       370        380        390        400        410        420 
GNEIPEGIQD ALFTSLIGIH GLRTGDGNGP LVNSRTGSIY IVKPKMHGPD EVAFTCELFS 

       430        440        450        460        470        480 
RVEDVLGLPQ NTLKVGIMDE ERRTTLNLKA CIKAAADRVV FINTGFLDRT GDEIHTSMDA 

       490        500        510        520        530        540 
GPMIRKGAMK STEWIAAYEN QNVDIGLETG FSGRAQIGKG MWAMTDLMAD MVEQKIGQPR 

       550        560        570        580        590        600 
AGATTAWVPS PTAATLHAMH YHEVDVFAVH NELAGTRRGT VDQLLTIPLA KELAWAPEEI 

       610        620        630        640        650        660 
REEVDNNCQS ILGYVVRWID AGVGCSKVPD IHDVALMEDR ATLRISSQLL ANWLRHGVIT 

       670        680        690        700        710        720 
EEDVKASLRR MAAVVDEQNA ADPDFRPMAP DPDGSIAFQA AQELILSGAD QPNGYTEPIL 

       730 
HRRRREFKAA SNVG 

« Hide

References

[1]"Complete sequence of Mycobacterium vanbaalenii PYR-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.J., Miller C., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 7251 / PYR-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000511 Genomic DNA. Translation: ABM13899.1.
RefSeqYP_953905.1. NC_008726.1.

3D structure databases

ProteinModelPortalA1T9P9.
SMRA1T9P9. Positions 5-729.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING350058.Mvan_3097.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM13899; ABM13899; Mvan_3097.
GeneID4646853.
KEGGmva:Mvan_3097.
PATRIC18184465. VBIMycVan31953_3154.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycMVAN350058:GIWR-3116-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_MYCVP
AccessionPrimary (citable) accession number: A1T9P9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: February 19, 2014
This is version 51 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