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Q7WR61 (MASZ_BORBR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 63. 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:BB0095
OrganismBordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]
Taxonomic identifier257310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length725 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 – 725725Malate synthase G HAMAP-Rule MF_00641
PRO_1000056893

Regions

Region125 – 1262Acetyl-CoA binding By similarity
Region453 – 4564Glyoxylate binding By similarity

Sites

Active site3391Proton acceptor By similarity
Active site6321Proton donor By similarity
Metal binding4281Magnesium By similarity
Metal binding4561Magnesium By similarity
Binding site1181Acetyl-CoA; via carbonyl oxygen By similarity
Binding site2751Acetyl-CoA By similarity
Binding site3121Acetyl-CoA By similarity
Binding site3391Glyoxylate By similarity
Binding site4281Glyoxylate By similarity
Binding site5371Acetyl-CoA; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue6181Cysteine sulfenic acid (-SOH) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7WR61 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 56CFA5BAAD16127C

FASTA72578,547
        10         20         30         40         50         60 
MTERIPHHGL QVAASLHRFI EDEALSGSGL APDEFWAGFA ALVRDLAPRN RELLAERDRL 

        70         80         90        100        110        120 
QGEIDAWHRA HPGPVRDSAG YQALLERIGY LQPQPAQVTA STRDVDSEIA SQAGPQLVVP 

       130        140        150        160        170        180 
VSNARYALNA ANARWGSLYD ALYGTDAIPP VAGDDGKGYN PARGEAVIAR ARAFLDEAAP 

       190        200        210        220        230        240 
LAQGSHADAT AYAIEGGKLA VTLGAGQRTG LRNPAQLAGY QGDASQPAAV LLANNGLHFE 

       250        260        270        280        290        300 
IQIDRQHQIG ATDAAGVKDV LLEAALTTIM DCEDSVAAVD ADDKVLIYRN WLGLMKGDLS 

       310        320        330        340        350        360 
ESVTKGGKTF TRRLNADRQY HKPDGGTLTL HGRSLMFVRN VGHLMTNPAI LDEQGNEVPE 

       370        380        390        400        410        420 
GILDAVITSL AALPDRANRL NSRTGSIYIV KPKMHGPAEA AFANELFDRV EDLLKLPRHT 

       430        440        450        460        470        480 
IKMGIMDEER RTSVNLKACI AAAAARVAFI NTGFLDRTGD EMHTGMEAGP MLRKGDMKSS 

       490        500        510        520        530        540 
AWITAYERNN VLVGLDCGLR GRAQIGKGMW AMPDMMAAML EQKIGHPKAG ANTAWVPSPT 

       550        560        570        580        590        600 
AATLHAMHYH QVDVAAVQQA LEQTRYDSVR DELLAGLLTV PVGDPAAWSA DDIQRELDNN 

       610        620        630        640        650        660 
AQGILGYVVR WIDQGVGCSK VPDINNVGLM EDRATLRISS QHIANWLRHG IVDRAQVNAT 

       670        680        690        700        710        720 
FERMAKVVDQ QNAGDPNYLP MAGHFDTSFA YRAACALVFE GLTQPNGYTE PLLHEYRQAF 


KAAQR 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX640437 Genomic DNA. Translation: CAE30597.1.
RefSeqNP_886648.1. NC_002927.3.

3D structure databases

ProteinModelPortalQ7WR61.
SMRQ7WR61. Positions 10-717.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257310.BB0095.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE30597; CAE30597; BB0095.
GeneID2662908.
KEGGbbr:BB0095.
PATRIC21133398. VBIBorBro124907_0101.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2225.
HOGENOMHOG000220740.
KOK01638.
OMASQFIENE.
OrthoDBEOG6HJ286.

Enzyme and pathway databases

BioCycBBRO257310:BB0095-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_BORBR
AccessionPrimary (citable) accession number: Q7WR61
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 63 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