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A9IHH4 (MASZ_BORPD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:Bpet4866
OrganismBordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) [Complete proteome] [HAMAP]
Taxonomic identifier340100 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length726 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 – 726726Malate synthase G HAMAP-Rule MF_00641
PRO_1000130887

Regions

Region125 – 1262Acetyl-CoA binding By similarity
Region452 – 4554Glyoxylate binding By similarity

Sites

Active site3381Proton acceptor By similarity
Active site6311Proton donor By similarity
Metal binding4271Magnesium By similarity
Metal binding4551Magnesium By similarity
Binding site1181Acetyl-CoA; via carbonyl oxygen By similarity
Binding site2741Acetyl-CoA By similarity
Binding site3111Acetyl-CoA By similarity
Binding site3381Glyoxylate By similarity
Binding site4271Glyoxylate By similarity
Binding site5361Acetyl-CoA; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue6171Cysteine sulfenic acid (-SOH) By similarity

Sequences

Sequence LengthMass (Da)Tools
A9IHH4 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 9248C75C6A1258C5

FASTA72678,962
        10         20         30         40         50         60 
MTERIQQDGL QVAAVLHRFI QDEALPAGGI DAPRFWAGFA ALVRDLAPRN RALLAERDRL 

        70         80         90        100        110        120 
QRELDTWHRA HPGPVRDLRA YRAFLEQIGY LQPVPGTVRV ETANVDAEIA EQAGPQLVVP 

       130        140        150        160        170        180 
MSNARYALNA ANARWGSLYD ALYGTDAIPP TPGDTGRGYH PQRGQAVIAR ARAFLDEAVP 

       190        200        210        220        230        240 
LAQGSHADAT GYSVDNGQLR VALAQGSTGL AQPEQFAGYQ GDAQAPQAIL LKHHGLHIEI 

       250        260        270        280        290        300 
QIDRAHSIGA TDAAGIKDVV VEAALTTIMD CEDSVAAVDA EDKVQVYRNW LGLMKGDLAE 

       310        320        330        340        350        360 
QVTKGGQTFT RRLNADRVYH APGGGTLTLH GRSLMFVRNV GHLMTNPAVL DADGNEIPEG 

       370        380        390        400        410        420 
ILDAVVTTLA ALPDRASRRN SRAGSIYIVK PKMHGPAEAA FANELFDRVE DLLGLPRHTV 

       430        440        450        460        470        480 
KMGIMDEERR TSVNLKACIQ AAAGRVAFIN TGFLDRTGDE MHSSMEAGPM MRKGDMKSSA 

       490        500        510        520        530        540 
WIAAYERSNV LVGLDCGLRG RAQIGKGMWA MPDLMAAMLE QKIGHPKAGA NTAWVPSPTA 

       550        560        570        580        590        600 
ATLHALHYHQ VDVPAVQQQL ESTRLASVQD ELLDGLLTVP VGNPADWSPD DIRHELENNA 

       610        620        630        640        650        660 
QGILGYVVRW IDQGVGCSKV PDINNVGLME DRATLRISSQ HIANWMRHGI ATREQVRDTF 

       670        680        690        700        710        720 
ERMAAVVDRQ NAGDPLYQPM AGHFDTSIAF QAACALVFEG LAQPNGYTEP LLHQYRLAFK 


ARHNKG 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM902716 Genomic DNA. Translation: CAP45218.1.
RefSeqYP_001633485.1. NC_010170.1.

3D structure databases

ProteinModelPortalA9IHH4.
SMRA9IHH4. Positions 2-722.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING340100.Bpet4866.

Proteomic databases

PRIDEA9IHH4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAP45218; CAP45218; Bpet4866.
GeneID5819865.
KEGGbpt:Bpet4866.
PATRIC21171336. VBIBorPet31633_4894.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2225.
HOGENOMHOG000220740.
KOK01638.
OMASQFIENE.
OrthoDBEOG6HJ286.

Enzyme and pathway databases

BioCycBPET340100:GJBO-4937-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_BORPD
AccessionPrimary (citable) accession number: A9IHH4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 5, 2008
Last modified: May 14, 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