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Q1QHK3 (MASZ_NITHX) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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:Nham_3565
OrganismNitrobacter hamburgensis (strain X14 / DSM 10229) [Complete proteome] [HAMAP]
Taxonomic identifier323097 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter

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_1000056913

Regions

Region124 – 1252Acetyl-CoA binding By similarity
Region454 – 4574Glyoxylate binding By similarity

Sites

Active site3371Proton acceptor By similarity
Active site6281Proton donor By similarity
Metal binding4291Magnesium By similarity
Metal binding4571Magnesium By similarity
Binding site1171Acetyl-CoA; via carbonyl oxygen By similarity
Binding site2731Acetyl-CoA By similarity
Binding site3101Acetyl-CoA By similarity
Binding site3371Glyoxylate By similarity
Binding site4291Glyoxylate By similarity
Binding site5381Acetyl-CoA; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue6141Cysteine sulfenic acid (-SOH) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1QHK3 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: BAD4A93C140936FD

FASTA72778,879
        10         20         30         40         50         60 
MTRIDAHGLK IAPVLFDFIA REATPRTGIA PDAFWAGLAA IVRDLGPRNR ELLAVRDTLQ 

        70         80         90        100        110        120 
AQIDGWHRAN KSRPFDMAAY TAFLKEIGYL LPEPATHAVE TANIDDEIGK ICGPQLVVPL 

       130        140        150        160        170        180 
TNARYALNAA NARWGSLYDA LYGTDAIAHE ANEARGYDKA RGDKVIAKAK AFLDSAAPLS 

       190        200        210        220        230        240 
AGSHADVAGY SVVNGHLSAK LRSGDATGLK TIAQFAGYQG AADAPSAILL VNHGLHIDIR 

       250        260        270        280        290        300 
IDRADRIGKD DPAGVADVII EAAISTILDM EDSVAAVDAD DKVLVYRNTL GLMNGTLTDT 

       310        320        330        340        350        360 
FEKGGKTVTR ALNADRIYTS ANGKEIALHG RSLLLMRNVG HHMVTDAVLD ENGAEIPEGM 

       370        380        390        400        410        420 
LDAAVSSLLA IHDLMGISKT RNSRTGSVYI VKPKMHGPDE VALTCELFAR VETMLGLPEN 

       430        440        450        460        470        480 
TLKIGIMDEE RRTTVNLKTC IQNASKRVCF INTGFLDRTG DEIHTSMEAG PMIRKNEMKA 

       490        500        510        520        530        540 
QPWMRAYEDW NVDIGLIDGL PGHAQIGKGM WAAPDRMADM LAQKVDHPQA GATTAWVPSP 

       550        560        570        580        590        600 
TAATLHALHY HQVDVLKQQQ ELKAGGQRAK LSDILTVPVS QSNWAPDDVR LEIDNNCQGI 

       610        620        630        640        650        660 
LGYVVRWIDQ GVGCSKVPDI HDVGLMEDRA TLRISSQHLA NWLHQNVVTS DQVMDSLKRM 

       670        680        690        700        710        720 
AVVVDKQNAG DPLYTPMAPT FDGVAFKAAC DLVFKGREQP NGYTEYILTE RRRQAKAESK 


GESEAAG 

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References

[1]"Complete sequence of chromosome of Nitrobacter hamburgensis X14."
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L., O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T., Gentry M.E., Bruce D., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: X14 / DSM 10229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000319 Genomic DNA. Translation: ABE64294.1.
RefSeqYP_578754.1. NC_007964.1.

3D structure databases

ProteinModelPortalQ1QHK3.
SMRQ1QHK3. Positions 3-719.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323097.Nham_3565.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE64294; ABE64294; Nham_3565.
GeneID4032602.
KEGGnha:Nham_3565.
PATRIC22695181. VBINitHam61822_4585.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2225.
HOGENOMHOG000220740.
KOK01638.
OMASQFIENE.
OrthoDBEOG6HJ286.

Enzyme and pathway databases

BioCycNHAM323097:GHP7-3621-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_NITHX
AccessionPrimary (citable) accession number: Q1QHK3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 16, 2006
Last modified: May 14, 2014
This is version 54 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