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A4IN50 (MASZ_GEOTN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 49. 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:GTNG_1384
OrganismGeobacillus thermodenitrificans (strain NG80-2) [Complete proteome] [HAMAP]
Taxonomic identifier420246 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

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_1000056903

Regions

Region124 – 1252Acetyl-CoA binding By similarity
Region456 – 4594Glyoxylate binding By similarity

Sites

Active site3391Proton acceptor By similarity
Active site6301Proton donor By similarity
Metal binding4311Magnesium By similarity
Metal binding4591Magnesium By similarity
Binding site1171Acetyl-CoA; via carbonyl oxygen By similarity
Binding site2751Acetyl-CoA By similarity
Binding site3121Acetyl-CoA By similarity
Binding site3391Glyoxylate By similarity
Binding site4311Glyoxylate By similarity
Binding site5401Acetyl-CoA; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue6161Cysteine sulfenic acid (-SOH) By similarity

Sequences

Sequence LengthMass (Da)Tools
A4IN50 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: 37B1B2D489B3ADA2

FASTA72781,200
        10         20         30         40         50         60 
MIEYVQAGTI QVAKVLYEFV NEELLPNSGL DQDKFWSDFA ALIADLTPRN KELLARRDEI 

        70         80         90        100        110        120 
QEKLNEWYKE HRGRFDFHEY KAFLTDIGYL EPEVEDFEIT TDNVDEEIAV QAGPQLVVPL 

       130        140        150        160        170        180 
TNARYALNAA NARWGSLYDA LYGTDAISEE DGAERGSSYN PVRGAKVIAY GRQFLDEAVP 

       190        200        210        220        230        240 
LVEHSHKDAV QYAIVDGKLV VTTEGGATTG LKEPEKLIGF QGEPQNPTAV LLKNNGLHIE 

       250        260        270        280        290        300 
IQIDREHPVG KTDKAGIKDI VLEAAVTTIM DGEDSVAAVD AEDKVVVYRN LFGLIKGDLT 

       310        320        330        340        350        360 
ATFEKNGKRL TRTLNPDREY KTPDGGELVL PGRSLMFVRN VGHLMTNNAI LDANGEEVYE 

       370        380        390        400        410        420 
GIIDAVVTSL IMKHSLIGNT RYLNSRKGSI YIVKPKMHGS AEVAFANELF DRVEDMLGLE 

       430        440        450        460        470        480 
RNTIKIGVMD EERRTSLNLK NCIYEVRDRI VFINTGFLDR TGDEIHTSME AGPMRRKNDM 

       490        500        510        520        530        540 
KSSTWLAGYE KSNVAVGLAA GFRGRAQIGK GMWAMPDLMA EMLKQKGAQL KAGANTAWVP 

       550        560        570        580        590        600 
SPTAATLHAL HYHQVNVAAV QNELANDRND YRDDILQIPV VDNPQWTADE IQEELDNNCQ 

       610        620        630        640        650        660 
SILGYVVRWI DQGIGCSKVP DIHNIGLMED RATLRISSQI LANWLHHGIC TKEQVLETFK 

       670        680        690        700        710        720 
RMAKVVDEQN AGDPNYRPMA PNYDDSVAFQ AACDLVFLGY EQPNGYTEPI LHRRRQEAKA 


KFAAVQQ 

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References

[1]"Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir."
Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X., Han W., Peng X., Liu R., Wang L.
Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NG80-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000557 Genomic DNA. Translation: ABO66754.1.
RefSeqYP_001125499.1. NC_009328.1.

3D structure databases

ProteinModelPortalA4IN50.
SMRA4IN50. Positions 5-723.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING420246.GTNG_1384.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO66754; ABO66754; GTNG_1384.
GeneID4966323.
KEGGgtn:GTNG_1384.
PATRIC21979151. VBIGeoThe136879_1455.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycGTHE420246:GIXT-1456-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_GEOTN
AccessionPrimary (citable) accession number: A4IN50
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 1, 2007
Last modified: February 19, 2014
This is version 49 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