Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B1MB69 (MASZ_MYCA9) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. 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:MAB_2409c
OrganismMycobacterium abscessus (strain ATCC 19977 / DSM 44196) [Complete proteome] [HAMAP]
Taxonomic identifier561007 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium abscessus

Protein attributes

Sequence length735 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 – 735735Malate synthase G HAMAP-Rule MF_00641
PRO_1000130892

Regions

Region125 – 1262Acetyl-CoA binding By similarity
Region466 – 4694Glyoxylate binding By similarity

Sites

Active site3461Proton acceptor By similarity
Active site6411Proton donor By similarity
Metal binding4411Magnesium By similarity
Metal binding4691Magnesium By similarity
Binding site1181Acetyl-CoA; via carbonyl oxygen By similarity
Binding site2811Acetyl-CoA By similarity
Binding site3181Acetyl-CoA By similarity
Binding site3461Glyoxylate By similarity
Binding site4411Glyoxylate By similarity
Binding site5501Acetyl-CoA; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue6271Cysteine sulfenic acid (-SOH) By similarity

Sequences

Sequence LengthMass (Da)Tools
B1MB69 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 29D2078E5D4D336E

FASTA73580,389
        10         20         30         40         50         60 
MSDRVDVGNL RVARVLYDFI TNEALPGTGV DADAFWAGVD KVVTDLAPRN RELLERRDDL 

        70         80         90        100        110        120 
QTQVDRWHRQ RAIEPLDGAA YQDFLTEIGY LVPEPEDFTI TTANVDDEIT TTAGPQLVVP 

       130        140        150        160        170        180 
ILNARFALNA ANARWGSLYD ALYGTDVIPE ADGAEKASAD TGGYNKVRGD KVIAYAREVL 

       190        200        210        220        230        240 
DGAAPLASGS WKDAVGLKID DGQLLVELGD EFSTGLQNPD QFVGYTGKLG KPQWSVLLIN 

       250        260        270        280        290        300 
HGLHIEVLID PDSPIGSTDK AGIKDVVLES AITTIMDFED SVAAVDAEDK VLGYRNWLGL 

       310        320        330        340        350        360 
NKGDLSEEVS KGGKTFTRVL NEDRVFTTPD GKGELTLPGR SLLFVRNVGH LMTNDAIVDA 

       370        380        390        400        410        420 
AGNEMPEGIQ DALFTSLIAI HGLRSGKKNG PLKNSRTGSI YIVKPKMHGP EEVAFTAELF 

       430        440        450        460        470        480 
GRVEEVLGLP HATLKVGIMD EERRTTVNLK AAIKAASDRV VFINTGFLDR TGDEIHTSME 

       490        500        510        520        530        540 
AGPMCRKAVM KSQPWILAYE DHNVDTGLGA GLAGKAQIGK GMWAMPDLMA DMVAQKIAQP 

       550        560        570        580        590        600 
RAGATTAWVP SPTAATLHAL HYHQVDVKAV DQELAGKHRA KLESLLTIPL AESRHDWTAE 

       610        620        630        640        650        660 
DIREEIDNNC QSILGYVVRW IDQGVGCSKV PDIHDVALME DRATLRISSQ LLANWLRHDV 

       670        680        690        700        710        720 
ITEDEVVEGL KRMAPVVDRQ NAGDKEYRPM APDFDSNIAF QAAKELILEG KDQPNGYTEP 

       730 
ILHRRRREYK AAAAK 

« Hide

References

[1]"Acquisition of foreign virulence genes by the cystic fibrosis pathogen Mycobacterium abscessus."
Genoscope
Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L., Gaillard J.L.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19977 / DSM 44196.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU458896 Genomic DNA. Translation: CAM62490.1.
RefSeqYP_001703144.1. NC_010397.1.

3D structure databases

ProteinModelPortalB1MB69.
SMRB1MB69. Positions 5-735.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING561007.MAB_2409c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM62490; CAM62490; MAB_2409c.
GeneID5964919.
KEGGmab:MAB_2409c.
PATRIC17976552. VBIMycAbs55940_2453.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycMABS561007:GJTG-2423-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_MYCA9
AccessionPrimary (citable) accession number: B1MB69
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: February 19, 2014
This is version 48 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